|
Name |
Accession |
Description |
Interval |
E-value |
| PycA |
COG1038 |
Pyruvate carboxylase [Energy production and conversion]; Pyruvate carboxylase is part of the ... |
6-1145 |
0e+00 |
|
Pyruvate carboxylase [Energy production and conversion]; Pyruvate carboxylase is part of the Pathway/BioSystem: Urea cycle
Pssm-ID: 440660 [Multi-domain] Cd Length: 1144 Bit Score: 2427.14 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 772685243 6 IQKVLVANRGEIAIRIFRACTELNIRTVAVYSKEDSGSYHRYKADEAYLVGEGKKPIDAYLDIEGIIDIAKRNKVDAIHP 85
Cdd:COG1038 4 IKKVLVANRGEIAIRVFRAATELGIRTVAIYSEEDRYSLHRFKADEAYLIGEGKGPVDAYLDIEEIIRVAKEKGVDAIHP 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 772685243 86 GYGFLSENIHFAKRCEEEGIVFIGPKSEHLDMFGDKVKAREQAEKAGIPVIPGSDGPAETLEAVEQFGQTNGYPIIIKAS 165
Cdd:COG1038 84 GYGFLSENPEFARACEEAGITFIGPSPEVLEMLGDKVAARAAAIEAGVPVIPGTEGPVDDLEEALAFAEEIGYPVMLKAA 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 772685243 166 LGGGGRGMRIVRSESEVKEAYERAKSEAKAAFGNDEVYVEKLIENPKHIEVQVIGDKQGNVVHLFERDCSVQRRHQKVIE 245
Cdd:COG1038 164 AGGGGRGMRVVRSEEELEEAFESARREAKAAFGDDEVFLEKYIERPKHIEVQILGDKHGNIVHLFERDCSVQRRHQKVVE 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 772685243 246 VAPSVSLSPELRNQICEAAVALAKNVNYINAGTVEFLV-ANNEFYFIEVNPRVQVEHTITEMITGVDIVQTQILVAQGHT 324
Cdd:COG1038 244 IAPAPNLDEELREAICEAAVKLAKAVGYVNAGTVEFLVdDDGNFYFIEVNPRIQVEHTVTEEVTGIDIVQSQILIAEGYS 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 772685243 325 LHSKKVNIPEQKDISTIGYAIQSRVTTEDPQNDFMPDTGKIMAYRSGGGFGVRLDTGNSFQGAVITPYYDSLLVKLSTWA 404
Cdd:COG1038 324 LDDPEIGIPSQEDIRLNGYAIQCRITTEDPANNFMPDTGRITAYRSAGGFGIRLDGGNAYTGAVITPYYDSLLVKVTAWG 403
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 772685243 405 LTFEQAAAKMVRNLQEFRIRGIKTNIPFLENVAKHEKFLTGQYDTSFIDTTPELFIFPKQKDRGTKMLTYIGNVTVNGFP 484
Cdd:COG1038 404 RTFEEAIRKMRRALREFRIRGVKTNIPFLENVLNHPDFLAGECTTSFIDETPELFDFPKRRDRATKLLTYLGDVTVNGPP 483
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 772685243 485 GIGKKEKPAFDKPINVKVDIDQQPARGTKQILDEKGAEGLANWVKEQKSVLLTDTTFRDAHQSLLATRFRSHDLKKIANP 564
Cdd:COG1038 484 GVKGRPKPDFPKPKLPKVDLGAPPPKGTKQILDELGPEGFAKWLREQKKVLLTDTTFRDAHQSLLATRVRTRDMLKIAPA 563
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 772685243 565 TAALWPELFSMEMWGGATFDVAYRFLKEDPWKRLEELRKEVPNTLFQMLLRSSNAVGYTNYPDNVIQEFVKQSAQSGIDV 644
Cdd:COG1038 564 TARLLPQLFSLEMWGGATFDVAYRFLKEDPWERLAKLREAIPNILFQMLLRGSNAVGYTNYPDNVVRAFVKEAAEAGIDV 643
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 772685243 645 FRIFDSLNWVKGMTLAIDAVRDTGKVAEAAICYTGDILDKNRTKYDLAYYTSMAKELEAAGAHILGIKDMAGLLKPQAAY 724
Cdd:COG1038 644 FRIFDSLNWVENMRVAIDAVRETGKIAEAAICYTGDILDPKRTKYTLDYYVDLAKELEKAGAHILAIKDMAGLLKPYAAY 723
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 772685243 725 ELVSALKETIDIPVHLHTHDTSGNGIYMYAKAVEAGVDIIDVAVSSMAGLTSQPSASGFYHAMEGNARRPEMNVQNVEML 804
Cdd:COG1038 724 KLVKALKEEVDLPIHLHTHDTSGNQLATYLAAIEAGVDIVDVALASMSGLTSQPSLNSLVAALEGTERDTGLDLDALQEL 803
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 772685243 805 SQYWESVRKYYSEFESGMKSPHTEIYEHEMPGGQYSNLQQQAKGVGLGDRWNEVKEMYRRVNDMFGDIVKVTPSSKVVGD 884
Cdd:COG1038 804 SNYWEAVRKYYAPFESGLKAPTAEVYKHEMPGGQYSNLRQQARALGLGDRWEEVKEMYAAVNRLFGDIVKVTPSSKVVGD 883
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 772685243 885 MALYMVQNNLTEKDVYEKGEQLDFPDSVVELFKGNIGQPHGGFPEKLQKLILKGQEPITVRPGELLEPVSFEAIKQEFKE 964
Cdd:COG1038 884 MALFMVQNGLTPEDVYEKGKDLDFPDSVVSFFKGELGQPPGGFPEELQKKVLKGRKPITVRPGELLPPVDFDALRAELEE 963
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 772685243 965 QHNLEISDQDAVAYALYPKVFSDYVKTAESYGDISVLDTPTFFYGMTLGEEIEVEIERGKTLIVKLISIGEPQPDATRVI 1044
Cdd:COG1038 964 KLGREPSDRDVLSYLLYPKVFEDYAKHREEYGDVSVLPTPTFFYGLRPGEEIEVEIEEGKTLIIKLLAIGEPDEDGMRTV 1043
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 772685243 1045 YFELNGQPREVVIKDESIKSSVQERLKADRTNPSHIAASMPGTVIKVLTEAGTKVNKGDHLMINEAMKMETTVQAPFSGT 1124
Cdd:COG1038 1044 FFELNGQPREVRVRDRSVKVTVASREKADPGNPGHIGAPMPGTVVKVLVKEGDEVKKGDPLLTIEAMKMETTITAPRDGT 1123
|
1130 1140
....*....|....*....|.
gi 772685243 1125 IKQVHVKNGEPIQTGDLLLEI 1145
Cdd:COG1038 1124 VKEVLVKEGDQVEAGDLLIEL 1144
|
|
| PRK12999 |
PRK12999 |
pyruvate carboxylase; Reviewed |
2-1147 |
0e+00 |
|
pyruvate carboxylase; Reviewed
Pssm-ID: 237263 [Multi-domain] Cd Length: 1146 Bit Score: 2326.28 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 772685243 2 SQQSIQKVLVANRGEIAIRIFRACTELNIRTVAVYSKEDSGSYHRYKADEAYLVGEGKKPIDAYLDIEGIIDIAKRNKVD 81
Cdd:PRK12999 1 EMKKIKKVLVANRGEIAIRIFRAATELGIRTVAIYSEEDKLSLHRFKADEAYLIGEGKHPVRAYLDIDEIIRVAKQAGVD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 772685243 82 AIHPGYGFLSENIHFAKRCEEEGIVFIGPKSEHLDMFGDKVKAREQAEKAGIPVIPGSDGPAETLEAVEQFGQTNGYPII 161
Cdd:PRK12999 81 AIHPGYGFLSENPEFARACAEAGITFIGPTAEVLRLLGDKVAARNAAIKAGVPVIPGSEGPIDDIEEALEFAEEIGYPIM 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 772685243 162 IKASLGGGGRGMRIVRSESEVKEAYERAKSEAKAAFGNDEVYVEKLIENPKHIEVQVIGDKQGNVVHLFERDCSVQRRHQ 241
Cdd:PRK12999 161 LKASAGGGGRGMRIVRSEEELEEAFERAKREAKAAFGNDEVYLEKYVENPRHIEVQILGDKHGNVVHLYERDCSVQRRHQ 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 772685243 242 KVIEVAPSVSLSPELRNQICEAAVALAKNVNYINAGTVEFLV-ANNEFYFIEVNPRVQVEHTITEMITGVDIVQTQILVA 320
Cdd:PRK12999 241 KVVEIAPAPGLSEELRERICEAAVKLARAVGYVNAGTVEFLVdADGNFYFIEVNPRIQVEHTVTEEVTGIDIVQSQILIA 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 772685243 321 QGHTLHSKKVNIPEQKDISTIGYAIQSRVTTEDPQNDFMPDTGKIMAYRSGGGFGVRLDTGNSFQGAVITPYYDSLLVKL 400
Cdd:PRK12999 321 EGATLHDLEIGIPSQEDIRLRGYAIQCRITTEDPANNFMPDTGRITAYRSPGGFGVRLDGGNAFAGAEITPYYDSLLVKL 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 772685243 401 STWALTFEQAAAKMVRNLQEFRIRGIKTNIPFLENVAKHEKFLTGQYDTSFIDTTPELFIFPKQKDRGTKMLTYIGNVTV 480
Cdd:PRK12999 401 TAWGRTFEQAVARMRRALREFRIRGVKTNIPFLENVLKHPDFRAGDYTTSFIDETPELFDFPKRRDRGTKLLTYIADVTV 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 772685243 481 NGFPGIgKKEKPAFDKPINVKVDIDQQPARGTKQILDEKGAEGLANWVKEQKSVLLTDTTFRDAHQSLLATRFRSHDLKK 560
Cdd:PRK12999 481 NGFPGV-KKKPPVFPDPRLPKVDLSAPPPAGTKQILDELGPEGFADWLRDQKRVLLTDTTFRDAHQSLLATRVRTKDLLR 559
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 772685243 561 IANPTAALWPELFSMEMWGGATFDVAYRFLKEDPWKRLEELRKEVPNTLFQMLLRSSNAVGYTNYPDNVIQEFVKQSAQS 640
Cdd:PRK12999 560 IAPATARLLPNLFSLEMWGGATFDVAYRFLKEDPWERLAELREAAPNVLFQMLLRGSNAVGYTNYPDNVVRAFVREAAAA 639
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 772685243 641 GIDVFRIFDSLNWVKGMTLAIDAVRDTGKVAEAAICYTGDILDKNRTKYDLAYYTSMAKELEAAGAHILGIKDMAGLLKP 720
Cdd:PRK12999 640 GIDVFRIFDSLNWVENMRVAIDAVRETGKIAEAAICYTGDILDPARAKYDLDYYVDLAKELEKAGAHILAIKDMAGLLKP 719
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 772685243 721 QAAYELVSALKETIDIPVHLHTHDTSGNGIYMYAKAVEAGVDIIDVAVSSMAGLTSQPSASGFYHAMEGNARRPEMNVQN 800
Cdd:PRK12999 720 AAAYELVSALKEEVDLPIHLHTHDTSGNGLATYLAAAEAGVDIVDVAVASMSGLTSQPSLNSIVAALEGTERDTGLDLDA 799
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 772685243 801 VEMLSQYWESVRKYYSEFESGMKSPHTEIYEHEMPGGQYSNLQQQAKGVGLGDRWNEVKEMYRRVNDMFGDIVKVTPSSK 880
Cdd:PRK12999 800 IRKLSPYWEAVRPYYAPFESGLKSPTTEVYLHEMPGGQYSNLKQQARALGLGDRFEEVKEMYAAVNRMFGDIVKVTPSSK 879
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 772685243 881 VVGDMALYMVQNNLTEKDVYEKGEQLDFPDSVVELFKGNIGQPHGGFPEKLQKLILKGQEPITVRPGELLEPVSFEAIKQ 960
Cdd:PRK12999 880 VVGDMALFMVQNGLTPEDVYEPGEDLDFPDSVVSFLKGELGQPPGGFPEPLQKKVLKGEEPITVRPGELLEPVDFEAERA 959
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 772685243 961 EFKEQHNLEISDQDAVAYALYPKVFSDYVKTAESYGDISVLDTPTFFYGMTLGEEIEVEIERGKTLIVKLISIGEPQPDA 1040
Cdd:PRK12999 960 ELEEKLGREVTDRDVLSYLLYPKVFEDYIKHREEYGDVSVLPTPTFFYGLRPGEEIEVEIEPGKTLIIKLEAIGEPDEDG 1039
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 772685243 1041 TRVIYFELNGQPREVVIKDESIKSSVQERLKADRTNPSHIAASMPGTVIKVLTEAGTKVNKGDHLMINEAMKMETTVQAP 1120
Cdd:PRK12999 1040 MRTVYFELNGQPREVQVRDRSVKSTVAAREKADPGNPGHVGAPMPGSVVTVLVKEGDEVKAGDPLAVIEAMKMETTITAP 1119
|
1130 1140
....*....|....*....|....*..
gi 772685243 1121 FSGTIKQVHVKNGEPIQTGDLLLEIEK 1147
Cdd:PRK12999 1120 VDGTVKRVLVKAGDQVEAGDLLVELEP 1146
|
|
| pyruv_carbox |
TIGR01235 |
pyruvate carboxylase; This enzyme plays a role in gluconeogensis but not glycolysis. [Energy ... |
8-1146 |
0e+00 |
|
pyruvate carboxylase; This enzyme plays a role in gluconeogensis but not glycolysis. [Energy metabolism, Glycolysis/gluconeogenesis]
Pssm-ID: 130302 [Multi-domain] Cd Length: 1143 Bit Score: 2151.86 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 772685243 8 KVLVANRGEIAIRIFRACTELNIRTVAVYSKEDSGSYHRYKADEAYLVGEG--KKPIDAYLDIEGIIDIAKRNKVDAIHP 85
Cdd:TIGR01235 1 KILVANRGEIAIRVFRAANELGIRTVAIYSEEDKLSLHRQKADESYQVGEGpdLGPIEAYLSIDEIIRVAKLNGVDAIHP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 772685243 86 GYGFLSENIHFAKRCEEEGIVFIGPKSEHLDMFGDKVKAREQAEKAGIPVIPGSDGPAETLEAVEQFGQTNGYPIIIKAS 165
Cdd:TIGR01235 81 GYGFLSENSEFADACNKAGIIFIGPKAEVMDQLGDKVAARNLAIKAGVPVVPGTDGPPETMEEVLDFAAAIGYPVIIKAS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 772685243 166 LGGGGRGMRIVRSESEVKEAYERAKSEAKAAFGNDEVYVEKLIENPKHIEVQVIGDKQGNVVHLFERDCSVQRRHQKVIE 245
Cdd:TIGR01235 161 WGGGGRGMRVVRSEADVADAFQRAKSEAKAAFGNDEVYVEKLIERPRHIEVQLLGDKHGNVVHLFERDCSVQRRHQKVVE 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 772685243 246 VAPSVSLSPELRNQICEAAVALAKNVNYINAGTVEFLVANN-EFYFIEVNPRVQVEHTITEMITGVDIVQTQILVAQGHT 324
Cdd:TIGR01235 241 VAPAPYLSREVRDEIAEYAVKLAKAVNYINAGTVEFLVDNDgKFYFIEVNPRIQVEHTVTEEITGIDIVQAQIHIADGAS 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 772685243 325 LHSKKVNIPEQKDISTIGYAIQSRVTTEDPQNDFMPDTGKIMAYRSGGGFGVRLDTGNSFQGAVITPYYDSLLVKLSTWA 404
Cdd:TIGR01235 321 LPTPQLGVPNQEDIRTNGYAIQCRVTTEDPANNFQPDTGRIEAYRSAGGFGIRLDGGNSYAGAIITPYYDSLLVKVSAWA 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 772685243 405 LTFEQAAAKMVRNLQEFRIRGIKTNIPFLENVAKHEKFLTGQYDTSFIDTTPELFIFPKQKDRGTKMLTYIGNVTVNGFP 484
Cdd:TIGR01235 401 STPEEAAAKMDRALREFRIRGVKTNIPFLENVLGHPKFLDGSYDTRFIDTTPELFQFVKSQDRATKLLTYLADVTVNGHP 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 772685243 485 GIGKKEKPAFDKPINVKVDIDQQP-ARGTKQILDEKGAEGLANWVKEQKSVLLTDTTFRDAHQSLLATRFRSHDLKKIAN 563
Cdd:TIGR01235 481 EAKDKLKPLENAPRVVVLYADQNPvPRGTKQILDEKGPEGFAEWVRNQKRVLLTDTTFRDAHQSLLATRVRTHDLAKIAP 560
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 772685243 564 PTAALWPELFSMEMWGGATFDVAYRFLKEDPWKRLEELRKEVPNTLFQMLLRSSNAVGYTNYPDNVIQEFVKQSAQSGID 643
Cdd:TIGR01235 561 TTSHALPNLFSLECWGGATFDVAMRFLHEDPWERLEDLRKGVPNILFQMLLRGANGVGYTNYPDNVVKYFVKQAAQGGID 640
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 772685243 644 VFRIFDSLNWVKGMTLAIDAVRDTGKVAEAAICYTGDILDKNRTKYDLAYYTSMAKELEAAGAHILGIKDMAGLLKPQAA 723
Cdd:TIGR01235 641 IFRVFDSLNWVENMRVGMDAVAEAGKVVEAAICYTGDILDPARPKYDLKYYTNLAVELEKAGAHILGIKDMAGLLKPAAA 720
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 772685243 724 YELVSALKETIDIPVHLHTHDTSGNGIYMYAKAVEAGVDIIDVAVSSMAGLTSQPSASGFYHAMEGNARRPEMNVQNVEM 803
Cdd:TIGR01235 721 KLLIKALREKTDLPIHFHTHDTSGIAVASMLAAVEAGVDVVDVAVDSMSGLTSQPSLGAIVAALEGSERDPGLNVAWIRE 800
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 772685243 804 LSQYWESVRKYYSEFESGMKSPHTEIYEHEMPGGQYSNLQQQAKGVGLGDRWNEVKEMYRRVNDMFGDIVKVTPSSKVVG 883
Cdd:TIGR01235 801 LSAYWEAVRNLYAAFESDLKGPASEVYLHEMPGGQYTNLQFQARSLGLGDRWHEVKQAYREANQMFGDIVKVTPSSKVVG 880
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 772685243 884 DMALYMVQNNLTEKDVYEKGEQLDFPDSVVELFKGNIGQPHGGFPEKLQKLILKGQEPITVRPGELLEPVSFEAIKQEFK 963
Cdd:TIGR01235 881 DMALFMVSNDLTVDDVVEPAEELSFPDSVVEFLKGDIGQPHGGFPEPLQKKVLKGEKPITVRPGSLLEPADLDAIRKDLQ 960
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 772685243 964 EQHNLEISDQDAVAYALYPKVFSDYVKTAESYGDISVLDTPTFFYGMTLGEEIEVEIERGKTLIVKLISIGEPQPDATRV 1043
Cdd:TIGR01235 961 EKHEREVSDFDVASYAMYPKVFTDFAKARDTYGPVSVLPTPAFFYGLADGEEIEVDIEKGKTLIIKLQAVGATDSQGERE 1040
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 772685243 1044 IYFELNGQPREVVIKDESIKSSVQERLKADRTNPSHIAASMPGTVIKVLTEAGTKVNKGDHLMINEAMKMETTVQAPFSG 1123
Cdd:TIGR01235 1041 VFFELNGQPRRIKVPDRSHKAEAAVRRKADPGNPAHVGAPMPGVIIEVKVSSGQAVNKGDPLVVLEAMKMETAIQAPKDG 1120
|
1130 1140
....*....|....*....|...
gi 772685243 1124 TIKQVHVKNGEPIQTGDLLLEIE 1146
Cdd:TIGR01235 1121 TIKEVLVKAGEQIDAKDLLLVLE 1143
|
|
| PccA |
COG4770 |
Acetyl/propionyl-CoA carboxylase, alpha subunit [Lipid transport and metabolism]; |
6-466 |
0e+00 |
|
Acetyl/propionyl-CoA carboxylase, alpha subunit [Lipid transport and metabolism];
Pssm-ID: 443802 [Multi-domain] Cd Length: 466 Bit Score: 730.28 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 772685243 6 IQKVLVANRGEIAIRIFRACTELNIRTVAVYSKEDSGSYHRYKADEAYLVGeGKKPIDAYLDIEGIIDIAKRNKVDAIHP 85
Cdd:COG4770 2 FKKVLIANRGEIAVRIIRTCRELGIRTVAVYSDADRDALHVRLADEAVCIG-PAPAAESYLNIDAIIAAAKATGADAIHP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 772685243 86 GYGFLSENIHFAKRCEEEGIVFIGPKSEHLDMFGDKVKAREQAEKAGIPVIPGSDGPAETLEAVEQFGQTNGYPIIIKAS 165
Cdd:COG4770 81 GYGFLSENADFAEACEDAGIVFIGPSPEAIRAMGDKIAAKKLMKAAGVPVVPGSDGPVQDAEEALAIAEEIGYPVLIKAS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 772685243 166 LGGGGRGMRIVRSESEVKEAYERAKSEAKAAFGNDEVYVEKLIENPKHIEVQVIGDKQGNVVHLFERDCSVQRRHQKVIE 245
Cdd:COG4770 161 AGGGGKGMRVVRSEEELEEAFESARREAKAAFGDDRVYLEKYIERPRHIEVQVLADKHGNVVHLGERDCSIQRRHQKVIE 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 772685243 246 VAPSVSLSPELRNQICEAAVALAKNVNYINAGTVEFLV-ANNEFYFIEVNPRVQVEHTITEMITGVDIVQTQILVAQGHT 324
Cdd:COG4770 241 EAPSPALTEELRERMGEAAVRAAKAVGYVGAGTVEFLVdADGNFYFLEMNTRLQVEHPVTEMVTGIDLVEEQIRIAAGEP 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 772685243 325 LHskkvniPEQKDISTIGYAIQSRVTTEDPQNDFMPDTGKIMAYRSGGGFGVRLDTGnSFQGAVITPYYDSLLVKLSTWA 404
Cdd:COG4770 321 LP------FTQEDIKLRGHAIECRINAEDPARGFLPSPGTITRLRPPGGPGVRVDSG-VYEGYEIPPYYDSMIAKLIVWG 393
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 772685243 405 LTFEQAAAKMVRNLQEFRIRGIKTNIPFLENVAKHEKFLTGQYDTSFIDTTPELFIFPKQKD 466
Cdd:COG4770 394 PDREEAIARMRRALAEFVIEGVKTNIPFLRALLAHPDFRAGDVDTGFIERELAELLAAAAPE 455
|
|
| PRK08591 |
PRK08591 |
acetyl-CoA carboxylase biotin carboxylase subunit; Validated |
6-453 |
0e+00 |
|
acetyl-CoA carboxylase biotin carboxylase subunit; Validated
Pssm-ID: 236307 [Multi-domain] Cd Length: 451 Bit Score: 634.92 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 772685243 6 IQKVLVANRGEIAIRIFRACTELNIRTVAVYSKEDSGSYHRYKADEAYLVGEgKKPIDAYLDIEGIIDIAKRNKVDAIHP 85
Cdd:PRK08591 2 FDKILIANRGEIALRIIRACKELGIKTVAVHSTADRDALHVQLADEAVCIGP-APSKKSYLNIPAIISAAEITGADAIHP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 772685243 86 GYGFLSENIHFAKRCEEEGIVFIGPKSEHLDMFGDKVKAREQAEKAGIPVIPGSDGPAETLEAVEQFGQTNGYPIIIKAS 165
Cdd:PRK08591 81 GYGFLSENADFAEICEDSGFTFIGPSAETIRLMGDKVTAKATMKKAGVPVVPGSDGPVDDEEEALAIAKEIGYPVIIKAT 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 772685243 166 LGGGGRGMRIVRSESEVKEAYERAKSEAKAAFGNDEVYVEKLIENPKHIEVQVIGDKQGNVVHLFERDCSVQRRHQKVIE 245
Cdd:PRK08591 161 AGGGGRGMRVVRTEAELEKAFSMARAEAKAAFGNPGVYMEKYLENPRHIEIQVLADGHGNAIHLGERDCSLQRRHQKVLE 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 772685243 246 VAPSVSLSPELRNQICEAAVALAKNVNYINAGTVEFLV-ANNEFYFIEVNPRVQVEHTITEMITGVDIVQTQILVAQGHT 324
Cdd:PRK08591 241 EAPSPAITEELRRKIGEAAVKAAKAIGYRGAGTIEFLYeKNGEFYFIEMNTRIQVEHPVTEMITGVDLVKEQIRIAAGEP 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 772685243 325 LHSKkvnipeQKDISTIGYAIQSRVTTEDPQNDFMPDTGKIMAYRSGGGFGVRLDTGnSFQGAVITPYYDSLLVKLSTWA 404
Cdd:PRK08591 321 LSIK------QEDIVFRGHAIECRINAEDPAKNFMPSPGKITRYHPPGGPGVRVDSA-VYTGYTIPPYYDSMIGKLIVHG 393
|
410 420 430 440
....*....|....*....|....*....|....*....|....*....
gi 772685243 405 LTFEQAAAKMVRNLQEFRIRGIKTNIPFLENVAKHEKFLTGQYDTSFID 453
Cdd:PRK08591 394 ETREEAIARMKRALSEFVIDGIKTTIPLHLRLLNDPNFQAGDYNIHYLE 442
|
|
| PRK08654 |
PRK08654 |
acetyl-CoA carboxylase biotin carboxylase subunit; |
8-458 |
0e+00 |
|
acetyl-CoA carboxylase biotin carboxylase subunit;
Pssm-ID: 236325 [Multi-domain] Cd Length: 499 Bit Score: 605.83 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 772685243 8 KVLVANRGEIAIRIFRACTELNIRTVAVYSKEDSGSYHRYKADEAYLVGEGKkPIDAYLDIEGIIDIAKRNKVDAIHPGY 87
Cdd:PRK08654 4 KILIANRGEIAIRVMRACRELGIKTVAVYSEADKNALFVKYADEAYPIGPAP-PSKSYLNIERIIDVAKKAGADAIHPGY 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 772685243 88 GFLSENIHFAKRCEEEGIVFIGPKSEHLDMFGDKVKAREQAEKAGIPVIPGSDGPAETLEAVEQFGQTNGYPIIIKASLG 167
Cdd:PRK08654 83 GFLAENPEFAKACEKAGIVFIGPSSDVIEAMGSKINAKKLMKKAGVPVLPGTEEGIEDIEEAKEIAEEIGYPVIIKASAG 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 772685243 168 GGGRGMRIVRSESEVKEAYERAKSEAKAAFGNDEVYVEKLIENPKHIEVQVIGDKQGNVVHLFERDCSVQRRHQKVIEVA 247
Cdd:PRK08654 163 GGGIGMRVVYSEEELEDAIESTQSIAQSAFGDSTVFIEKYLEKPRHIEIQILADKHGNVIHLGDRECSIQRRHQKLIEEA 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 772685243 248 PSVSLSPELRNQICEAAVALAKNVNYINAGTVEFLVANNEFYFIEVNPRVQVEHTITEMITGVDIVQTQILVAQGHTLHS 327
Cdd:PRK08654 243 PSPIMTPELRERMGEAAVKAAKAINYENAGTVEFLYSNGNFYFLEMNTRLQVEHPITEMVTGIDIVKEQIKIAAGEELSF 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 772685243 328 KkvnipeQKDISTIGYAIQSRVTTEDPQNDFMPDTGKIMAYRSGGGFGVRLDTGnSFQGAVITPYYDSLLVKLSTWALTF 407
Cdd:PRK08654 323 K------QEDITIRGHAIECRINAEDPLNDFAPSPGKIKRYRSPGGPGVRVDSG-VHMGYEIPPYYDSMISKLIVWGRTR 395
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|.
gi 772685243 408 EQAAAKMVRNLQEFRIRGIKTNIPFLENVAKHEKFLTGQYDTSFIDTTPEL 458
Cdd:PRK08654 396 EEAIARMRRALYEYVIVGVKTNIPFHKAVMENENFVRGNLHTHFIEEETTI 446
|
|
| PRK07178 |
PRK07178 |
acetyl-CoA carboxylase biotin carboxylase subunit; |
6-468 |
0e+00 |
|
acetyl-CoA carboxylase biotin carboxylase subunit;
Pssm-ID: 180865 [Multi-domain] Cd Length: 472 Bit Score: 582.06 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 772685243 6 IQKVLVANRGEIAIRIFRACTELNIRTVAVYSKEDSGSYHRYKADEAYLVGEgkKPIDAYLDIEGIIDIAKRNKVDAIHP 85
Cdd:PRK07178 2 IKKILIANRGEIAVRIVRACAEMGIRSVAIYSEADRHALHVKRADEAYSIGA--DPLAGYLNPRRLVNLAVETGCDALHP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 772685243 86 GYGFLSENIHFAKRCEEEGIVFIGPKSEHLDMFGDKVKAREQAEKAGIPVIPGSDGPAETLEAVEQFGQTNGYPIIIKAS 165
Cdd:PRK07178 80 GYGFLSENAELAEICAERGIKFIGPSAEVIRRMGDKTEARRAMIKAGVPVTPGSEGNLADLDEALAEAERIGYPVMLKAT 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 772685243 166 LGGGGRGMRIVRSESEVKEAYERAKSEAKAAFGNDEVYVEKLIENPKHIEVQVIGDKQGNVVHLFERDCSVQRRHQKVIE 245
Cdd:PRK07178 160 SGGGGRGIRRCNSREELEQNFPRVISEATKAFGSAEVFLEKCIVNPKHIEVQILADSHGNVVHLFERDCSIQRRNQKLIE 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 772685243 246 VAPSVSLSPELRNQICEAAVALAKNVNYINAGTVEFLV-ANNEFYFIEVNPRVQVEHTITEMITGVDIVQTQILVAQGHT 324
Cdd:PRK07178 240 IAPSPQLTPEQRAYIGDLAVRAAKAVGYENAGTVEFLLdADGEVYFMEMNTRVQVEHTITEEITGIDIVREQIRIASGLP 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 772685243 325 LHSKkvnipeQKDISTIGYAIQSRVTTEDPQNDFMPDTGKIMAYRSGGGFGVRLDTGnSFQGAVITPYYDSLLVKLSTWA 404
Cdd:PRK07178 320 LSYK------QEDIQHRGFALQFRINAEDPKNDFLPSFGKITRYYAPGGPGVRTDTA-IYTGYTIPPYYDSMCAKLIVWA 392
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 772685243 405 LTFEQAAAKMVRNLQEFRIRGIKTNIPFLENVAKHEKFLTGQYDTSFIDTTPELFIFPKQKDRG 468
Cdd:PRK07178 393 LTWEEALDRGRRALDDMRVQGVKTTIPYYQEILRNPEFRSGQFNTSFVESHPELTNYSIKRKPE 456
|
|
| PRK06111 |
PRK06111 |
acetyl-CoA carboxylase biotin carboxylase subunit; Validated |
6-452 |
0e+00 |
|
acetyl-CoA carboxylase biotin carboxylase subunit; Validated
Pssm-ID: 180406 [Multi-domain] Cd Length: 450 Bit Score: 564.27 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 772685243 6 IQKVLVANRGEIAIRIFRACTELNIRTVAVYSKEDSGSYHRYKADEAYLVGeGKKPIDAYLDIEGIIDIAKRNKVDAIHP 85
Cdd:PRK06111 2 FQKVLIANRGEIAVRIIRTCQKLGIRTVAIYSEADRDALHVKMADEAYLIG-GPRVQESYLNLEKIIEIAKKTGAEAIHP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 772685243 86 GYGFLSENIHFAKRCEEEGIVFIGPKSEHLDMFGDKVKAREQAEKAGIPVIPGSDGPAETLEAVEQFGQTNGYPIIIKAS 165
Cdd:PRK06111 81 GYGLLSENASFAERCKEEGIVFIGPSADIIAKMGSKIEARRAMQAAGVPVVPGITTNLEDAEEAIAIARQIGYPVMLKAS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 772685243 166 LGGGGRGMRIVRSESEVKEAYERAKSEAKAAFGNDEVYVEKLIENPKHIEVQVIGDKQGNVVHLFERDCSVQRRHQKVIE 245
Cdd:PRK06111 161 AGGGGIGMQLVETEQELTKAFESNKKRAANFFGNGEMYIEKYIEDPRHIEIQLLADTHGNTVYLWERECSVQRRHQKVIE 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 772685243 246 VAPSVSLSPELRNQICEAAVALAKNVNYINAGTVEFLVANNE-FYFIEVNPRVQVEHTITEMITGVDIVQTQILVAQGHT 324
Cdd:PRK06111 241 EAPSPFLDEETRKAMGERAVQAAKAIGYTNAGTIEFLVDEQKnFYFLEMNTRLQVEHPVTEEITGIDLVEQQLRIAAGEK 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 772685243 325 LHSKkvnipeQKDISTIGYAIQSRVTTEDPqNDFMPDTGKIMAYRSGGGFGVRLDTGNSfQGAVITPYYDSLLVKLSTWA 404
Cdd:PRK06111 321 LSFT------QDDIKRSGHAIEVRIYAEDP-KTFFPSPGKITDLTLPGGEGVRHDHAVE-NGVTVTPFYDPMIAKLIAHG 392
|
410 420 430 440
....*....|....*....|....*....|....*....|....*...
gi 772685243 405 LTFEQAAAKMVRNLQEFRIRGIKTNIPFLENVAKHEKFLTGQYDTSFI 452
Cdd:PRK06111 393 ETREEAISRLHDALEELKVEGIKTNIPLLLQVLEDPVFKAGGYTTGFL 440
|
|
| accC |
TIGR00514 |
acetyl-CoA carboxylase, biotin carboxylase subunit; This model represents the biotin ... |
6-454 |
0e+00 |
|
acetyl-CoA carboxylase, biotin carboxylase subunit; This model represents the biotin carboxylase subunit found usually as a component of acetyl-CoA carboxylase. Acetyl-CoA carboxylase is designated EC 6.4.1.2 and this component, biotin carboxylase, has its own designation, EC 6.3.4.14. Homologous domains are found in eukaryotic forms of acetyl-CoA carboxylase and in a number of other carboxylases (e.g. pyruvate carboxylase), but seed members and trusted cutoff are selected so as to exclude these. In some systems, the biotin carboxyl carrier protein and this protein (biotin carboxylase) may be shared by different carboxyltransferases. However, this model is not intended to identify the biotin carboxylase domain of propionyl-coA carboxylase. The model should hit the full length of proteins, except for chloroplast transit peptides in plants. If it hits a domain only of a longer protein, there may be a problem with the identification. [Fatty acid and phospholipid metabolism, Biosynthesis]
Pssm-ID: 129605 [Multi-domain] Cd Length: 449 Bit Score: 541.66 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 772685243 6 IQKVLVANRGEIAIRIFRACTELNIRTVAVYSKEDSGSYHRYKADEAYLVGEgKKPIDAYLDIEGIIDIAKRNKVDAIHP 85
Cdd:TIGR00514 2 LDKILIANRGEIALRILRACKELGIKTVAVHSTADRDALHVLLADEAVCIGP-APSAKSYLNIPNIISAAEITGADAIHP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 772685243 86 GYGFLSENIHFAKRCEEEGIVFIGPKSEHLDMFGDKVKAREQAEKAGIPVIPGSDGPAETLEAVEQFGQTNGYPIIIKAS 165
Cdd:TIGR00514 81 GYGFLSENANFAEQCERSGFTFIGPSAESIRLMGDKVSAIETMKKAGVPCVPGSDGLVEDEEENVRIAKRIGYPVIIKAT 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 772685243 166 LGGGGRGMRIVRSESEVKEAYERAKSEAKAAFGNDEVYVEKLIENPKHIEVQVIGDKQGNVVHLFERDCSVQRRHQKVIE 245
Cdd:TIGR00514 161 AGGGGRGMRVVREPDELVKSISMTRAEAKAAFGNDGVYIEKYIENPRHVEIQVLADKYGNAIYLGERDCSIQRRHQKLLE 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 772685243 246 VAPSVSLSPELRNQICEAAVALAKNVNYINAGTVEFLV-ANNEFYFIEVNPRVQVEHTITEMITGVDIVQTQILVAQGHT 324
Cdd:TIGR00514 241 EAPSPALTPELRRKMGDAAVKAAVSIGYRGAGTVEFLLdKNGEFYFMEMNTRIQVEHPVTEMITGVDLIKEQIRIAAGEP 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 772685243 325 LHSKkvnipeQKDISTIGYAIQSRVTTEDPQNDFMPDTGKIMAYRSGGGFGVRLDtGNSFQGAVITPYYDSLLVKLSTWA 404
Cdd:TIGR00514 321 LSLK------QEDVVVRGHAIECRINAEDPIKTFLPSPGRITRYLPPGGPGVRWD-SHVYSGYTVPPYYDSMIGKLITYG 393
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|
gi 772685243 405 LTFEQAAAKMVRNLQEFRIRGIKTNIPFLENVAKHEKFLTGQYDTSFIDT 454
Cdd:TIGR00514 394 KTREVAIARMKRALSEFIIDGIKTTIPFHQRILEDENFQHGGTNIHYLEK 443
|
|
| PRK09282 |
PRK09282 |
pyruvate carboxylase subunit B; Validated |
532-1147 |
3.04e-180 |
|
pyruvate carboxylase subunit B; Validated
Pssm-ID: 236449 [Multi-domain] Cd Length: 592 Bit Score: 540.59 E-value: 3.04e-180
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 772685243 532 KSVLLTDTTFRDAHQSLLATRFRSHDLKKIAnptaalwPEL-----FSMEMWGGATFDVAYRFLKEDPWKRLEELRKEVP 606
Cdd:PRK09282 2 KKVKITDTTLRDAHQSLLATRMRTEDMLPIA-------EKLdkvgfWSLEVWGGATFDVCIRYLNEDPWERLRKLKKALP 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 772685243 607 NTLFQMLLRSSNAVGYTNYPDNVIQEFVKQSAQSGIDVFRIFDSLNWVKGMTLAIDAVRDTGKVAEAAICYTgdildknr 686
Cdd:PRK09282 75 NTPLQMLLRGQNLVGYRHYPDDVVEKFVEKAAENGIDIFRIFDALNDVRNMEVAIKAAKKAGAHVQGTISYT-------- 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 772685243 687 TK--YDLAYYTSMAKELEAAGAHILGIKDMAGLLKPQAAYELVSALKETIDIPVHLHTHDTSGNGIYMYAKAVEAGVDII 764
Cdd:PRK09282 147 TSpvHTIEKYVELAKELEEMGCDSICIKDMAGLLTPYAAYELVKALKEEVDLPVQLHSHCTSGLAPMTYLKAVEAGVDII 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 772685243 765 DVAVSSMAGLTSQPSASGFYHAMEGNARRPEMNVQNVEMLSQYWESVRKYYSEFESGMKSPHTEIYEHEMPGGQYSNLQQ 844
Cdd:PRK09282 227 DTAISPLAFGTSQPPTESMVAALKGTPYDTGLDLELLFEIAEYFREVRKKYKQFESEFTIVDTRVLIHQVPGGMISNLVS 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 772685243 845 QAKGVGLGDRWNEVKEMYRRVNDMFGDIVKVTPSSKVVGDMAlymVQNNLTE---KDVyekgeqldfPDSVVELFKGNIG 921
Cdd:PRK09282 307 QLKEQNALDKLDEVLEEIPRVREDLGYPPLVTPTSQIVGTQA---VLNVLTGeryKVI---------TKEVKDYVKGLYG 374
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 772685243 922 QPHGGFPEKLQKLILKGQEPITVRPGELLEPvSFEAIKQEFKEQHNLEisDQDAVAYALYPKVFSDYVKTAESYGDISVL 1001
Cdd:PRK09282 375 RPPAPINEELRKKIIGDEEPITCRPADLLEP-ELEKARKEAEELGKSE--KEDVLTYALFPQIAKKFLEEREAGELKPEP 451
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 772685243 1002 DTPTFFYGMTLG--EEIEVEIErGKTLIVKLISIGEPQPdatRVIYFELNGQPREVVIKdESIKSSVQERLKAdrTNPSH 1079
Cdd:PRK09282 452 EPKEAAAAGAEGipTEFKVEVD-GEKYEVKIEGVKAEGK---RPFYLRVDGMPEEVVVE-PLKEIVVGGRPRA--SAPGA 524
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 772685243 1080 IAASMPGTVIKVLTEAGTKVNKGDHLMINEAMKMETTVQAPFSGTIKQVHVKNGEPIQTGDLLLEIEK 1147
Cdd:PRK09282 525 VTSPMPGTVVKVKVKEGDKVKAGDTVLVLEAMKMENEIQAPVDGTVKEILVKEGDRVNPGDVLMEIEP 592
|
|
| PRK05586 |
PRK05586 |
acetyl-CoA carboxylase biotin carboxylase subunit; |
6-452 |
6.66e-180 |
|
acetyl-CoA carboxylase biotin carboxylase subunit;
Pssm-ID: 180150 [Multi-domain] Cd Length: 447 Bit Score: 534.29 E-value: 6.66e-180
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 772685243 6 IQKVLVANRGEIAIRIFRACTELNIRTVAVYSKEDSGSYHRYKADEAYLVGEGKkPIDAYLDIEGIIDIAKRNKVDAIHP 85
Cdd:PRK05586 2 FKKILIANRGEIAVRIIRACREMGIETVAVYSEADKDALHVQLADEAVCIGPAS-SKDSYLNIQNIISATVLTGAQAIHP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 772685243 86 GYGFLSENIHFAKRCEEEGIVFIGPKSEHLDMFGDKVKAREQAEKAGIPVIPGSDGPAETLEAVEQFGQTNGYPIIIKAS 165
Cdd:PRK05586 81 GFGFLSENSKFAKMCKECNIVFIGPDSETIELMGNKSNAREIMIKAGVPVVPGSEGEIENEEEALEIAKEIGYPVMVKAS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 772685243 166 LGGGGRGMRIVRSESEVKEAYERAKSEAKAAFGNDEVYVEKLIENPKHIEVQVIGDKQGNVVHLFERDCSVQRRHQKVIE 245
Cdd:PRK05586 161 AGGGGRGIRIVRSEEELIKAFNTAKSEAKAAFGDDSMYIEKFIENPKHIEFQILGDNYGNVVHLGERDCSLQRRNQKVLE 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 772685243 246 VAPSVSLSPELRNQICEAAVALAKNVNYINAGTVEFLV-ANNEFYFIEVNPRVQVEHTITEMITGVDIVQTQILVAQGHT 324
Cdd:PRK05586 241 EAPSPVMTEELRKKMGEIAVKAAKAVNYKNAGTIEFLLdKDGNFYFMEMNTRIQVEHPITEMITGVDLVKEQIKIAYGEK 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 772685243 325 LHSKkvnipeQKDISTIGYAIQSRVTTEDPQNDFMPDTGKIMAYRSGGGFGVRLDTgNSFQGAVITPYYDSLLVKLSTWA 404
Cdd:PRK05586 321 LSIK------QEDIKINGHSIECRINAEDPKNGFMPCPGKIEELYIPGGLGVRVDS-AVYSGYTIPPYYDSMIGKLIVYG 393
|
410 420 430 440
....*....|....*....|....*....|....*....|....*...
gi 772685243 405 LTFEQAAAKMVRNLQEFRIRGIKTNIPFLENVAKHEKFLTGQYDTSFI 452
Cdd:PRK05586 394 KDREEAIQKMKRALGEFIIEGVNTNIDFQFIILEDEEFIKGTYDTSFI 441
|
|
| PRK08463 |
PRK08463 |
acetyl-CoA carboxylase subunit A; Validated |
6-470 |
2.80e-169 |
|
acetyl-CoA carboxylase subunit A; Validated
Pssm-ID: 169452 [Multi-domain] Cd Length: 478 Bit Score: 508.20 E-value: 2.80e-169
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 772685243 6 IQKVLVANRGEIAIRIFRACTELNIRTVAVYSKEDSGSYHRYKADEAYLVGEgkKPIDAYLDIEGIIDIAKRNKVDAIHP 85
Cdd:PRK08463 2 IHKILIANRGEIAVRVIRACRDLHIKSVAIYTEPDRECLHVKIADEAYRIGT--DPIKGYLDVKRIVEIAKACGADAIHP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 772685243 86 GYGFLSENIHFAKRCEEEGIVFIGPKSEHLDMFGDKVKAREQAEKAGIPVIPGSDG-PAETLEAVEQFGQTNGYPIIIKA 164
Cdd:PRK08463 80 GYGFLSENYEFAKAVEDAGIIFIGPKSEVIRKMGNKNIARYLMKKNGIPIVPGTEKlNSESMEEIKIFARKIGYPVILKA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 772685243 165 SLGGGGRGMRIVRSESEVKEAYERAKSEAKAAFGNDEVYVEKLIENPKHIEVQVIGDKQGNVVHLFERDCSVQRRHQKVI 244
Cdd:PRK08463 160 SGGGGGRGIRVVHKEEDLENAFESCKREALAYFNNDEVFMEKYVVNPRHIEFQILGDNYGNIIHLCERDCSIQRRHQKVI 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 772685243 245 EVAPSVSLSPELRNQICEAAVALAKNVNYINAGTVEFLV-ANNEFYFIEVNPRVQVEHTITEMITGVDIVQTQILVAQGH 323
Cdd:PRK08463 240 EIAPCPSISDNLRKTMGVTAVAAAKAVGYTNAGTIEFLLdDYNRFYFMEMNTRIQVEHGVTEEITGIDLIVRQIRIAAGE 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 772685243 324 TLHSkkvnipEQKDISTIGYAIQSRVTTEDPQNDFMPDTGKIMAYRSGGGFGVRLDTgNSFQGAVITPYYDSLLVKLSTW 403
Cdd:PRK08463 320 ILDL------EQSDIKPRGFAIEARITAENVWKNFIPSPGKITEYYPALGPSVRVDS-HIYKDYTIPPYYDSMLAKLIVK 392
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 772685243 404 ALTFEQAAAKMVRNLQEFRIRGIKTNIPFLENVAKHEKFLTGQYDTSFIDTTPELfIFPKQKDRGTK 470
Cdd:PRK08463 393 ATSYDLAVNKLERALKEFVIDGIRTTIPFLIAITKTREFRRGYFDTSYIETHMQE-LLEKTEDRHQE 458
|
|
| DRE_TIM_PC_TC_5S |
cd07937 |
Pyruvate carboxylase and Transcarboxylase 5S, carboxyltransferase domain; This family includes ... |
536-818 |
1.78e-165 |
|
Pyruvate carboxylase and Transcarboxylase 5S, carboxyltransferase domain; This family includes the carboxyltransferase domains of pyruvate carboxylase (PC) and the transcarboxylase (TC) 5S subunit. Transcarboxylase 5S is a cobalt-dependent metalloenzyme subunit of the biotin-dependent transcarboxylase multienzyme complex. Transcarboxylase 5S transfers carbon dioxide from the 1.3S biotin to pyruvate in the second of two carboxylation reactions catalyzed by TC. The first reaction involves the transfer of carbon dioxide from methylmalonyl-CoA to the 1.3S biotin, and is catalyzed by the 12S subunit. These two steps allow a carboxylate group to be transferred from oxaloacetate to propionyl-CoA to yield pyruvate and methylmalonyl-CoA. The catalytic domain of transcarboxylase 5S has a canonical TIM-barrel fold with a large C-terminal extension that forms a funnel leading to the active site. Transcarboxylase 5S forms a homodimer and there are six dimers per complex. In addition to the catalytic domain, transcarboxylase 5S has several other domains including a carbamoyl-phosphate synthase domain, a biotin carboxylase domain, a carboxyltransferase domain, and an ATP-grasp domain. Pyruvate carboxylase, like TC, is a biotin-dependent enzyme that catalyzes the carboxylation of pyruvate to produce oxaloacetate. In mammals, PC has critical roles in gluconeogenesis, lipogenesis, glyceroneogenesis, and insulin secretion. Inherited PC deficiencies are linked to serious diseases in humans such as lactic acidemia, hypoglycemia, psychomotor retardation, and death. PC is a single-chain enzyme and is active only in its homotetrameric form. PC has three domains, an N-terminal biotin carboxylase domain, a carboxyltransferase domain (this alignment model), and a C-terminal biotin-carboxyl carrier protein domain. This family belongs to the DRE-TIM metallolyase superfamily. DRE-TIM metallolyases include 2-isopropylmalate synthase (IPMS), alpha-isopropylmalate synthase (LeuA), 3-hydroxy-3-methylglutaryl-CoA lyase, homocitrate synthase, citramalate synthase, 4-hydroxy-2-oxovalerate aldolase, re-citrate synthase, transcarboxylase 5S, pyruvate carboxylase, AksA, and FrbC. These members all share a conserved triose-phosphate isomerase (TIM) barrel domain consisting of a core beta(8)-alpha(8) motif with the eight parallel beta strands forming an enclosed barrel surrounded by eight alpha helices. The domain has a catalytic center containing a divalent cation-binding site formed by a cluster of invariant residues that cap the core of the barrel. In addition, the catalytic site includes three invariant residues - an aspartate (D), an arginine (R), and a glutamate (E) - which is the basis for the domain name "DRE-TIM".
Pssm-ID: 163675 Cd Length: 275 Bit Score: 490.02 E-value: 1.78e-165
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 772685243 536 LTDTTFRDAHQSLLATRFRSHDLKKIANPTAALWpeLFSMEMWGGATFDVAYRFLKEDPWKRLEELRKEVPNTLFQMLLR 615
Cdd:cd07937 1 ITDTTLRDAHQSLLATRMRTEDMLPIAEALDEAG--FFSLEVWGGATFDVCMRFLNEDPWERLRELRKAMPNTPLQMLLR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 772685243 616 SSNAVGYTNYPDNVIQEFVKQSAQSGIDVFRIFDSLNWVKGMTLAIDAVRDTGKVAEAAICYTGDildknrTKYDLAYYT 695
Cdd:cd07937 79 GQNLVGYRHYPDDVVELFVEKAAKNGIDIFRIFDALNDVRNLEVAIKAVKKAGKHVEGAICYTGS------PVHTLEYYV 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 772685243 696 SMAKELEAAGAHILGIKDMAGLLKPQAAYELVSALKETIDIPVHLHTHDTSGNGIYMYAKAVEAGVDIIDVAVSSMAGLT 775
Cdd:cd07937 153 KLAKELEDMGADSICIKDMAGLLTPYAAYELVKALKKEVGLPIHLHTHDTSGLAVATYLAAAEAGVDIVDTAISPLSGGT 232
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 772685243 776 SQPSASGFYHAMEGNARRPEMNVQNVEMLSQYWESVRKYYSEF 818
Cdd:cd07937 233 SQPSTESMVAALRGTGRDTGLDLEKLEEISEYFEEVRKKYAPF 275
|
|
| PRK12833 |
PRK12833 |
acetyl-CoA carboxylase biotin carboxylase subunit; Provisional |
4-454 |
1.06e-162 |
|
acetyl-CoA carboxylase biotin carboxylase subunit; Provisional
Pssm-ID: 183781 [Multi-domain] Cd Length: 467 Bit Score: 490.42 E-value: 1.06e-162
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 772685243 4 QSIQKVLVANRGEIAIRIFRACTELNIRTVAVYSKEDSGSYHRYKADEAYLVGeGKKPIDAYLDIEGIIDIAKRNKVDAI 83
Cdd:PRK12833 3 SRIRKVLVANRGEIAVRIIRAARELGMRTVAACSDADRDSLAARMADEAVHIG-PSHAAKSYLNPAAILAAARQCGADAI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 772685243 84 HPGYGFLSENIHFAKRCEEEGIVFIGPKSEHLDMFGDKVKAREQAEKAGIPVIPGSDGPAETLEAVEQFGQTNGYPIIIK 163
Cdd:PRK12833 82 HPGYGFLSENAAFAEAVEAAGLIFVGPDAQTIRTMGDKARARRTARRAGVPTVPGSDGVVASLDAALEVAARIGYPLMIK 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 772685243 164 ASLGGGGRGMRIVRSESEVKEAYERAKSEAKAAFGNDEVYVEKLIENPKHIEVQVIGDKQgNVVHLFERDCSVQRRHQKV 243
Cdd:PRK12833 162 AAAGGGGRGIRVAHDAAQLAAELPLAQREAQAAFGDGGVYLERFIARARHIEVQILGDGE-RVVHLFERECSLQRRRQKI 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 772685243 244 IEVAPSVSLSPELRNQICEAAVALAKNVNYINAGTVEFLV--ANNEFYFIEVNPRVQVEHTITEMITGVDIVQTQILVAQ 321
Cdd:PRK12833 241 LEEAPSPSLTPAQRDALCASAVRLARQVGYRGAGTLEYLFddARGEFYFIEMNTRIQVEHPVTEAITGIDLVQEMLRIAD 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 772685243 322 GHTLHSKkvnipeQKDISTIGYAIQSRVTTEDPQNDFMPDTGKIMAYRSGGGFGVRLDTgNSFQGAVITPYYDSLLVKLS 401
Cdd:PRK12833 321 GEPLRFA------QGDIALRGAALECRINAEDPLRDFFPNPGRIDALVWPQGPGVRVDS-LLYPGYRVPPFYDSLLAKLI 393
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|...
gi 772685243 402 TWALTFEQAAAKMVRNLQEFRIRGIKTNIPFLENVAKHEKFLTGQYDTSFIDT 454
Cdd:PRK12833 394 VHGEDRAAALARAARALRELRIDGMKTTAPLHRALLADADVRAGRFHTNFLEA 446
|
|
| PRK08462 |
PRK08462 |
acetyl-CoA carboxylase biotin carboxylase subunit; |
3-454 |
6.64e-156 |
|
acetyl-CoA carboxylase biotin carboxylase subunit;
Pssm-ID: 236269 [Multi-domain] Cd Length: 445 Bit Score: 471.92 E-value: 6.64e-156
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 772685243 3 QQSIQKVLVANRGEIAIRIFRACTELNIRTVAVYSKEDSGSYHRYKADEAYLVGeGKKPIDAYLDIEGIIDIAKRNKVDA 82
Cdd:PRK08462 1 KKEIKRILIANRGEIALRAIRTIQEMGKEAIAIYSTADKDALYLKYADAKICIG-GAKSSESYLNIPAIISAAEIFEADA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 772685243 83 IHPGYGFLSENIHFAKRCEEEGIVFIGPKSEHLDMFGDKVKAREQAEKAGIPVIPGSDGPAETLEAVEQFGQTNGYPIII 162
Cdd:PRK08462 80 IFPGYGFLSENQNFVEICSHHNIKFIGPSVEVMALMSDKSKAKEVMKRAGVPVIPGSDGALKSYEEAKKIAKEIGYPVIL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 772685243 163 KASLGGGGRGMRIVRSESEVKEAYERAKSEAKAAFGNDEVYVEKLIENPKHIEVQVIGDKQGNVVHLFERDCSVQRRHQK 242
Cdd:PRK08462 160 KAAAGGGGRGMRVVEDESDLENLYLAAESEALSAFGDGTMYMEKFINNPRHIEVQILGDKHGNVIHVGERDCSLQRRHQK 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 772685243 243 VIEVAPSVSLSPELRNQICEAAVALAKNVNYINAGTVEFLV-ANNEFYFIEVNPRVQVEHTITEMITGVDIVQTQILVAQ 321
Cdd:PRK08462 240 LIEESPAVVLDEKTRERLHETAIKAAKAIGYEGAGTFEFLLdSNLDFYFMEMNTRLQVEHTVSEMVSGLDLIEWMIKIAE 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 772685243 322 GHTLhskkvniPEQKDISTIGYAIQSRVTTEDPqNDFMPDTGKIMAYRSGGGFGVRLDTgNSFQGAVITPYYDSLLVKLS 401
Cdd:PRK08462 320 GEEL-------PSQESIKLKGHAIECRITAEDP-KKFYPSPGKITKWIAPGGRNVRMDS-HAYAGYVVPPYYDSMIGKLI 390
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|...
gi 772685243 402 TWALTFEQAAAKMVRNLQEFRIRGIKTNIPFLENVAKHEKFLTGQYDTSFIDT 454
Cdd:PRK08462 391 VWGEDRNRAIAKMKRALKEFKVEGIKTTIPFHLEMMENADFINNKYDTKYLEE 443
|
|
| OadA1 |
COG5016 |
Pyruvate/oxaloacetate carboxyltransferase [Energy production and conversion]; Pyruvate ... |
532-990 |
1.43e-153 |
|
Pyruvate/oxaloacetate carboxyltransferase [Energy production and conversion]; Pyruvate/oxaloacetate carboxyltransferase is part of the Pathway/BioSystem: Urea cycle
Pssm-ID: 444040 [Multi-domain] Cd Length: 540 Bit Score: 469.37 E-value: 1.43e-153
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 772685243 532 KSVLLTDTTFRDAHQSLLATRFRSHDLKKIAnptaalwPEL-----FSMEMWGGATFDVAYRFLKEDPWKRLEELRKEVP 606
Cdd:COG5016 2 KKVKITDTTLRDGHQSLFATRMRTEDMLPIA-------EKLdeagfWSLEVWGGATFDSCIRYLNEDPWERLRLLRKAMP 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 772685243 607 NTLFQMLLRSSNAVGYTNYPDNVIQEFVKQSAQSGIDVFRIFDSLNWVKGMTLAIDAVRDTGKVAEAAICYTGDILdknr 686
Cdd:COG5016 75 NTPLQMLLRGQNLVGYRHYPDDVVELFVKRAAENGIDIFRIFDALNDVRNLETAIKAAKKAGAHAQGAISYTISPV---- 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 772685243 687 tkYDLAYYTSMAKELEAAGAHILGIKDMAGLLKPQAAYELVSALKETIDIPVHLHTHDTSGNGIYMYAKAVEAGVDIIDV 766
Cdd:COG5016 151 --HTVEYYVELAKELEDMGADSICIKDMAGLLTPYRAYELVKALKEALDIPIELHTHATSGLAPATYLKAIEAGVDIIDT 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 772685243 767 AVSSMAGLTSQPSASGFYHAMEGNARRPEMNVQNVEMLSQYWESVRKYYSEFESGMKSPHTEIYEHEMPGGQYSNLQQQA 846
Cdd:COG5016 229 AISPLAGGTSQPPTESMVAALKGTGYDTGLDLEALLEIADYFREVRKKYAKFEPEATGVDPRVLVHQVPGGMLSNLVSQL 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 772685243 847 KGVGLGDRWNEV-KEMyRRVNDMFGDIVKVTPSSKVVGDMAlymVQNNLTEKDvYEKgeqldFPDSVVELFKGNIGQPHG 925
Cdd:COG5016 309 KEQGALDRLDEVlEEI-PRVREDLGYPPLVTPTSQIVGTQA---VLNVLTGER-YKM-----ITKEVKDYVLGYYGKTPA 378
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 772685243 926 GFPEKLQKLILKGQEPITVRPGELLEPvSFEAIKQEFkeqhnLEISDQDAVAYALYPKVFSDYVK 990
Cdd:COG5016 379 PIDPEVRKKALGDEEPITCRPADLLEP-ELEKLRKEG-----LAKSDEDVLTYALFPQVAIKFLK 437
|
|
| oadA |
TIGR01108 |
oxaloacetate decarboxylase alpha subunit; This model describes the bacterial oxaloacetate ... |
536-1142 |
1.56e-148 |
|
oxaloacetate decarboxylase alpha subunit; This model describes the bacterial oxaloacetate decarboxylase alpha subunit and its equivalents in archaea. The oxaloacetate decarboxylase Na+ pump is the paradigm of the family of Na+ transport decarboxylases that present in bacteria and archaea. It a multi subunit enzyme consisting of a peripheral alpha-subunit and integral membrane subunits beta and gamma. The energy released by the decarboxylation reaction of oxaloacetate is coupled to Na+ ion pumping across the membrane. [Transport and binding proteins, Cations and iron carrying compounds, Energy metabolism, Other]
Pssm-ID: 273447 [Multi-domain] Cd Length: 582 Bit Score: 457.72 E-value: 1.56e-148
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 772685243 536 LTDTTFRDAHQSLLATRFRSHDLKKIANP--TAALWpelfSMEMWGGATFDVAYRFLKEDPWKRLEELRKEVPNTLFQML 613
Cdd:TIGR01108 1 ITDVVLRDAHQSLFATRMRTEDMLPIAEKldDVGYW----SLEVWGGATFDACIRFLNEDPWERLRELKKALPNTPLQML 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 772685243 614 LRSSNAVGYTNYPDNVIQEFVKQSAQSGIDVFRIFDSLNWVKGMTLAIDAVRDTGKVAEAAICYTgdildkNRTKYDLAY 693
Cdd:TIGR01108 77 LRGQNLLGYRHYADDVVERFVKKAVENGMDVFRIFDALNDPRNLQAAIQAAKKHGAHAQGTISYT------TSPVHTLET 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 772685243 694 YTSMAKELEAAGAHILGIKDMAGLLKPQAAYELVSALKETIDIPVHLHTHDTSGNGIYMYAKAVEAGVDIIDVAVSSMAG 773
Cdd:TIGR01108 151 YLDLAEELLEMGVDSICIKDMAGILTPKAAYELVSALKKRFGLPVHLHSHATTGMAEMALLKAIEAGADGIDTAISSMSG 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 772685243 774 LTSQPSASGFYHAMEGNARRPEMNVQNVEMLSQYWESVRKYYSEFESGMKSPHTEIYEHEMPGGQYSNLQQQAKGVGLGD 853
Cdd:TIGR01108 231 GTSHPPTETMVAALRGTGYDTGLDIELLLEIAAYFREVRKKYSQFEGQLKGPDSRILVAQVPGGMLSNLESQLKEQNALD 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 772685243 854 RWNEVKEMYRRVNDMFGDIVKVTPSSKVVGDMAlymVQNNLTekdvyekGEQLD-FPDSVVELFKGNIGQPHGGFPEKLQ 932
Cdd:TIGR01108 311 KLDEVLEEIPRVREDLGYPPLVTPTSQIVGTQA---VLNVLT-------GERYKtITKETKGYLKGEYGRTPAPINAELQ 380
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 772685243 933 KLILKGQEPI-TVRPGELLEPvSFEAIKQEFKEQHNLEISDQDAVAYALYPKVFSDYVKTAESygdisvldtPTFFYGMt 1011
Cdd:TIGR01108 381 RKILGDEKPIvDCRPADLLEP-ELDKLRAEVREAGAEKNSIEDVLTYALFPQVGLKFLENRHN---------PAAFEPK- 449
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 772685243 1012 lGEEIEVEIERGKtlivkliSIGEPQPDATRVIYF-ELNGQPREVVIKDESIKSSVQERLKADRTNPSHIA--------- 1081
Cdd:TIGR01108 450 -PEEKVIEQEHAQ-------VVGKYEETHASGSYTvEVEGKAFVVKVSPGGDVSQITASAPANTSGGTVAAkagagtpvt 521
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 772685243 1082 ASMPGTVIKVLTEAGTKVNKGDHLMINEAMKMETTVQAPFSGTIKQVHVKNGEPIQTGDLL 1142
Cdd:TIGR01108 522 APIAGSIVKVKVSEGQTVAEGEVLLILEAMKMETEIKAAAAGTVREILVKVGDAVSVGQVL 582
|
|
| PRK14040 |
PRK14040 |
oxaloacetate decarboxylase subunit alpha; |
532-1145 |
3.37e-133 |
|
oxaloacetate decarboxylase subunit alpha;
Pssm-ID: 237592 [Multi-domain] Cd Length: 593 Bit Score: 417.79 E-value: 3.37e-133
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 772685243 532 KSVLLTDTTFRDAHQSLLATRFRSHDLKKIAnptaalwPEL-----FSMEMWGGATFDVAYRFLKEDPWKRLEELRKEVP 606
Cdd:PRK14040 3 KPLAITDVVLRDAHQSLFATRLRLDDMLPIA-------AKLdkvgyWSLESWGGATFDACIRFLGEDPWERLRELKKAMP 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 772685243 607 NTLFQMLLRSSNAVGYTNYPDNVIQEFVKQSAQSGIDVFRIFDSLNWVKGMTLAIDAVRDTGKVAEAAICYTgdildknr 686
Cdd:PRK14040 76 NTPQQMLLRGQNLLGYRHYADDVVERFVERAVKNGMDVFRVFDAMNDPRNLETALKAVRKVGAHAQGTLSYT-------- 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 772685243 687 TK--YDLAYYTSMAKELEAAGAHILGIKDMAGLLKPQAAYELVSALKETIDIPVHLHTHDTSGNGIYMYAKAVEAGVDII 764
Cdd:PRK14040 148 TSpvHTLQTWVDLAKQLEDMGVDSLCIKDMAGLLKPYAAYELVSRIKKRVDVPLHLHCHATTGLSTATLLKAIEAGIDGV 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 772685243 765 DVAVSSMAGLTSQPSASGFYHAMEGNARRPEMNVQNVEMLSQYWESVRKYYSEFESGMKSPHTEIYEHEMPGGQYSNLQQ 844
Cdd:PRK14040 228 DTAISSMSMTYGHSATETLVATLEGTERDTGLDILKLEEIAAYFREVRKKYAKFEGQLKGVDSRILVAQVPGGMLTNMES 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 772685243 845 QAKGVGLGDRWNEVKEMYRRVNDMFGDIVKVTPSSKVVGDMAlymVQNNLTekdvyekGEQLdfpDSVVE----LFKGNI 920
Cdd:PRK14040 308 QLKEQGAADKLDEVLAEIPRVREDLGFIPLVTPTSQIVGTQA---VLNVLT-------GERY---KTITKetagVLKGEY 374
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 772685243 921 GQPHGGFPEKLQKLILKGQEPITVRPGELLEPvSFEAIKQEFKEQ---HNLEISDQ---DAVAYALYPKVFSDYVKTAes 994
Cdd:PRK14040 375 GATPAPVNAELQARVLEGAEPITCRPADLLAP-ELDKLEAELRRQaqeKGITLAENaidDVLTYALFPQIGLKFLENR-- 451
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 772685243 995 ygdisvlDTPTFFYGMTLGEEIEVEiergktlivklisiGEPQPDATRVIYFELNGQPREVVIKD----ESIKSSVQ--- 1067
Cdd:PRK14040 452 -------HNPAAFEPVPQAEAAQPA--------------AKAEPAGSETYTVEVEGKAYVVKVSEggdiSQITPAAPaaa 510
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 772685243 1068 ----ERLKADRTNPSHIAASMPGTVIKVLTEAGTKVNKGDHLMINEAMKMETTVQAPFSGTIKQVHVKNGEPIQTGDLLL 1143
Cdd:PRK14040 511 paaaAAAAPAAAAGEPVTAPLAGNIFKVIVTEGQTVAEGDVLLILEAMKMETEIRAAQAGTVRGIAVKEGDAVAVGDTLL 590
|
..
gi 772685243 1144 EI 1145
Cdd:PRK14040 591 TL 592
|
|
| PRK12331 |
PRK12331 |
oxaloacetate decarboxylase subunit alpha; |
534-994 |
3.48e-121 |
|
oxaloacetate decarboxylase subunit alpha;
Pssm-ID: 183446 [Multi-domain] Cd Length: 448 Bit Score: 380.97 E-value: 3.48e-121
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 772685243 534 VLLTDTTFRDAHQSLLATRFRSHDLKKIANPTAALwpELFSMEMWGGATFDVAYRFLKEDPWKRLEELRKEVPNTLFQML 613
Cdd:PRK12331 4 IKITETVLRDGQQSLIATRMTTEEMLPILEKLDNA--GYHSLEMWGGATFDACLRFLNEDPWERLRKIRKAVKKTKLQML 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 772685243 614 LRSSNAVGYTNYPDNVIQEFVKQSAQSGIDVFRIFDSLNWVKGMTLAIDAVRDTGKVAEAAICYTGDILdknrtkYDLAY 693
Cdd:PRK12331 82 LRGQNLLGYRNYADDVVESFVQKSVENGIDIIRIFDALNDVRNLETAVKATKKAGGHAQVAISYTTSPV------HTIDY 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 772685243 694 YTSMAKELEAAGAHILGIKDMAGLLKPQAAYELVSALKETIDIPVHLHTHDTSGNGIYMYAKAVEAGVDIIDVAVSSMAG 773
Cdd:PRK12331 156 FVKLAKEMQEMGADSICIKDMAGILTPYVAYELVKRIKEAVTVPLEVHTHATSGIAEMTYLKAIEAGADIIDTAISPFAG 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 772685243 774 LTSQPSASGFYHAMEGNARRPEMNVQNVEMLSQYWESVRKYYSefESGMKSP-----HTEIYEHEMPGGQYSNLQQQAKG 848
Cdd:PRK12331 236 GTSQPATESMVAALQDLGYDTGLDLEELSEIAEYFNPIRDHYR--EEGILNPkvkdvEPKTLIYQVPGGMLSNLLSQLKE 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 772685243 849 VGLGDRWNEVKEMYRRVNDMFGDIVKVTPSSKVVGDMALYmvqNNLTekdvyekGEQLDF-PDSVVELFKGNIGQPHGGF 927
Cdd:PRK12331 314 QGAEDKYEEVLKEVPKVRADLGYPPLVTPLSQMVGTQALM---NVIS-------GERYKMvPNEIKDYVRGLYGRPPAPI 383
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 772685243 928 PEKLQKLILKGQEPITVRPGELLEPvSFEAIKQEFKEQHNleiSDQDAVAYALYPKVFSDYVKTAES 994
Cdd:PRK12331 384 AEEIKKKIIGDEEVITCRPADLIEP-QLEKLREEIAEYAE---SEEDVLSYALFPQQAKDFLGRRED 446
|
|
| PYC_OADA |
pfam02436 |
Conserved carboxylase domain; This domain represents a conserved region in pyruvate ... |
829-1029 |
1.34e-113 |
|
Conserved carboxylase domain; This domain represents a conserved region in pyruvate carboxylase (PYC), oxaloacetate decarboxylase alpha chain (OADA), and transcarboxylase 5s subunit. The domain is found adjacent to the HMGL-like domain (pfam00682) and often close to the biotin_lipoyl domain (pfam00364) of biotin requiring enzymes.
Pssm-ID: 460557 [Multi-domain] Cd Length: 201 Bit Score: 350.99 E-value: 1.34e-113
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 772685243 829 IYEHEMPGGQYSNLQQQAKGVGLGDRWNEVKEMYRRVNDMFGDIVKVTPSSKVVGDMALYMVQNNLTEKDVYEKGEQLDF 908
Cdd:pfam02436 1 VYKHEIPGGQLSNLQQQAKEQGLGDRFDEVLKEYPRVNKDLGDIPKVTPSSQIVGDQAVFNVLNNLTPEDVLGEGRYKDI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 772685243 909 PDSVVELFKGNIGQPHGGFPEKLQKLILKGQEPITVRPGELLEPVSFEAIKQEFKEQHNLEISDQDAVAYALYPKVFSDY 988
Cdd:pfam02436 81 PDSVVDYLKGEYGQPPGGFPEELQKKVLKGEEPITCRPGDLLPPVDLEKLRKELEEKAGRETTEEDVLSYALYPKVAEKF 160
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 772685243 989 VKTAESYGDISVLDTPTFFYGMTLGEEIEVEIERGKTLIVK 1029
Cdd:pfam02436 161 LKFREKYGDVSVLPTPVFFYGLEPGEEYEVEIEGGKYLIVK 201
|
|
| PRK14041 |
PRK14041 |
pyruvate carboxylase subunit B; |
532-990 |
2.06e-111 |
|
pyruvate carboxylase subunit B;
Pssm-ID: 237593 [Multi-domain] Cd Length: 467 Bit Score: 355.63 E-value: 2.06e-111
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 772685243 532 KSVLLTDTTFRDAHQSLLATRFRSHDLKKIANPTAALwpELFSMEMWGGATFDVAYRFLKEDPWKRLEELRKEVPNTLFQ 611
Cdd:PRK14041 1 MKVMFVDTTLRDGHQSLIATRMRTEDMLPALEAFDRM--GFYSMEVWGGATFDVCVRFLNENPWERLKEIRKRLKNTKIQ 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 772685243 612 MLLRSSNAVGYTNYPDNVIQEFVKQSAQSGIDVFRIFDSLNWVKGMTLAIDAVRDTGKVAEAAICYTGDILdknrtkYDL 691
Cdd:PRK14041 79 MLLRGQNLVGYRHYADDVVELFVKKVAEYGLDIIRIFDALNDIRNLEKSIEVAKKHGAHVQGAISYTVSPV------HTL 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 772685243 692 AYYTSMAKELEAAGAHILGIKDMAGLLKPQAAYELVSALKETIDIPVHLHTHDTSGNGIYMYAKAVEAGVDIIDVAVSSM 771
Cdd:PRK14041 153 EYYLEFARELVDMGVDSICIKDMAGLLTPKRAYELVKALKKKFGVPVEVHSHCTTGLASLAYLAAVEAGADMFDTAISPF 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 772685243 772 AGLTSQPSASGFYHAMEGNARRPEMNVQNVEMLSQYWESVRKYYSEFESGMKSPHTEIYEHEMPGGQYSNLQQQAKGVGL 851
Cdd:PRK14041 233 SMGTSQPPFESMYYAFRENGKETDFDRKALKFLVEYFTKVREKYSEYDVGMKSPDSRILVSQIPGGMYSNLVKQLKEQKM 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 772685243 852 GDRWNEVKEMYRRVNDMFGDIVKVTPSSKVVGDMAlymVQNNLTEKDvYEKgeqldFPDSVVELFKGNIGQPHGGFPEKL 931
Cdd:PRK14041 313 LHKLDKVLEEVPRVRKDLGYPPLVTPTSQIVGVQA---VLNVLTGER-YKR-----VTNETKNYVKGLYGRPPAPIDEEL 383
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
gi 772685243 932 QKLILKGQEPITVRPGELLEPvSFEAIKQEFKEqhnLEISDQDAVAYALYPKVFSDYVK 990
Cdd:PRK14041 384 MKKILGDEKPIDCRPADLLEP-ELEKARKELGI---LAETDEDLLIYVILGEVGKKFLK 438
|
|
| PRK14042 |
PRK14042 |
pyruvate carboxylase subunit B; Provisional |
535-1146 |
4.62e-111 |
|
pyruvate carboxylase subunit B; Provisional
Pssm-ID: 172536 [Multi-domain] Cd Length: 596 Bit Score: 359.42 E-value: 4.62e-111
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 772685243 535 LLTDTTFRDAHQSLLATRFRSHDLKKIANPT--AALWpelfSMEMWGGATFDVAYRFLKEDPWKRLEELRKEVPNTLFQM 612
Cdd:PRK14042 5 FITDVTLRDAHQCLIATRMRTEDMLPICNKMddVGFW----AMEVWGGATFDACLRFLKEDPWSRLRQLRQALPNTQLSM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 772685243 613 LLRSSNAVGYTNYPDNVIQEFVKQSAQSGIDVFRIFDSLNWVKGMTLAIDAVRDTGKVAEAAICYTGDILdknrtkYDLA 692
Cdd:PRK14042 81 LLRGQNLLGYRNYADDVVRAFVKLAVNNGVDVFRVFDALNDARNLKVAIDAIKSHKKHAQGAICYTTSPV------HTLD 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 772685243 693 YYTSMAKELEAAGAHILGIKDMAGLLKPQAAYELVSALKETIDIPVHLHTHDTSGNGIYMYAKAVEAGVDIIDVAVSSMA 772
Cdd:PRK14042 155 NFLELGKKLAEMGCDSIAIKDMAGLLTPTVTVELYAGLKQATGLPVHLHSHSTSGLASICHYEAVLAGCNHIDTAISSFS 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 772685243 773 GLTSQPSASGFYHAMEGNARRPEMNVQNVEMLSQYWESVRKYYSEFESGMKSPHTEIYEHEMPGGQYSNLQQQAKGVGLG 852
Cdd:PRK14042 235 GGASHPPTEALVAALTDTPYDTELDLNILLEIDDYFKAVRKKYSQFESEAQNIDPRVQLYQVPGGMISNLYNQLKEQNAL 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 772685243 853 DRWNEVKEMYRRVNDMFGDIVKVTPSSKVVGDMAlymVQNNLTekdvyekGEQLDFPDSVVELF-KGNIGQPHGGFPEKL 931
Cdd:PRK14042 315 DKMDAVHKEIPRVRKDLGYPPLVTPTSQVVGTQA---VINVLT-------GERYKTITNEVKLYcQGKYGTPPGKISSAL 384
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 772685243 932 QKLILKGQEPITVRPGELLePVSFEAIKQEFKEqhnLEISDQDAVAYALYPKVFSDYVktaESYGDISVLDTPTFFYGMT 1011
Cdd:PRK14042 385 RKKAIGRTEVIEVRPGDLL-PNELDQLQNEISD---LALSDEDVLLYAMFPEIGRQFL---EQRKNNQLIPEPLLTQSSA 457
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 772685243 1012 LGEEIEVEIE---RGKTLIVKLISIGEPQpDATRVIYFELNGQPREVVIKDESIKSSVQERLKADRTNPSHIAASMPGTV 1088
Cdd:PRK14042 458 PDNSVMSEFDiilHGESYHVKVAGYGMIE-HGQQSCFLWVDGVPEEVVVQHSELHDKIERSSVNNKIGPGDITVAIPGSI 536
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....*...
gi 772685243 1089 IKVLTEAGTKVNKGDHLMINEAMKMETTVQAPFSGTIKQVHVKNGEPIQTGDLLLEIE 1146
Cdd:PRK14042 537 IAIHVSAGDEVKAGQAVLVIEAMKMETEIKAPANGVVAEILCQKGDKVTPGQVLIRVE 594
|
|
| PRK12330 |
PRK12330 |
methylmalonyl-CoA carboxytransferase subunit 5S; |
532-991 |
1.12e-101 |
|
methylmalonyl-CoA carboxytransferase subunit 5S;
Pssm-ID: 183445 [Multi-domain] Cd Length: 499 Bit Score: 330.57 E-value: 1.12e-101
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 772685243 532 KSVLLTDTTFRDAHQSLLATRFRSHDL----KKIANptAALWpelfSMEMWGGATFDVAYRFLKEDPWKRLEELRKEVPN 607
Cdd:PRK12330 3 RKIGVTELALRDAHQSLMATRMAMEDMvgacEDIDN--AGYW----SVECWGGATFDACIRFLNEDPWERLRTFRKLMPN 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 772685243 608 TLFQMLLRSSNAVGYTNYPDNVIQEFVKQSAQSGIDVFRIFDSLNWVKGMTLAIDAVRDTGKVAEAAICYTGDILdknrt 687
Cdd:PRK12330 77 SRLQMLLRGQNLLGYRHYEDEVVDRFVEKSAENGMDVFRVFDALNDPRNLEHAMKAVKKVGKHAQGTICYTVSPI----- 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 772685243 688 kYDLAYYTSMAKELEAAGAHILGIKDMAGLLKPQAAYELVSALKETI--DIPVHLHTHDTSGNGIYMYAKAVEAGVDIID 765
Cdd:PRK12330 152 -HTVEGFVEQAKRLLDMGADSICIKDMAALLKPQPAYDIVKGIKEACgeDTRINLHCHSTTGVTLVSLMKAIEAGVDVVD 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 772685243 766 VAVSSMA-GLTSQPSASgFYHAMEGNARRPEMNVQNVEMLSQYWESVRKYYSEFESGMKSPHTEIYEHEMPGGQYSNLQQ 844
Cdd:PRK12330 231 TAISSMSlGPGHNPTES-LVEMLEGTGYTTKLDMDRLLKIRDHFKKVRPKYKEFESKTTGVETEIFKSQIPGGMLSNMES 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 772685243 845 QAKGVGLGDRWNEVKEMYRRVNDMFGDIVKVTPSSKVVGDMAlymVQNNLTEKDVYEKGEqldFPDSVVELFKGNIGQPH 924
Cdd:PRK12330 310 QLKQQGAGDRMDEVLEEVPRVRKDAGYPPLVTPSSQIVGTQA---VFNVLMGRYKVLTGE---FADLMLGYYGETPGERN 383
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 772685243 925 GGFPEKLQKliLKGQEPITVRPGELLEPvSFEAIKQEFKEQHNLEISDQDAVAYALYPKVFSDYVKT 991
Cdd:PRK12330 384 PEVVEQAKK--QAKKEPITCRPADLLEP-EWDKLRAEALALEGCDGSDEDVLTYALFPQVAPKFFAT 447
|
|
| CPSase_L_D2 |
pfam02786 |
Carbamoyl-phosphate synthase L chain, ATP binding domain; Carbamoyl-phosphate synthase ... |
120-325 |
3.14e-91 |
|
Carbamoyl-phosphate synthase L chain, ATP binding domain; Carbamoyl-phosphate synthase catalyzes the ATP-dependent synthesis of carbamyl-phosphate from glutamine or ammonia and bicarbonate. This important enzyme initiates both the urea cycle and the biosynthesis of arginine and/or pyrimidines. The carbamoyl-phosphate synthase (CPS) enzyme in prokaryotes is a heterodimer of a small and large chain. The small chain promotes the hydrolysis of glutamine to ammonia, which is used by the large chain to synthesize carbamoyl phosphate. See pfam00988. The small chain has a GATase domain in the carboxyl terminus. See pfam00117. The ATP binding domain (this one) has an ATP-grasp fold.
Pssm-ID: 397079 [Multi-domain] Cd Length: 209 Bit Score: 291.52 E-value: 3.14e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 772685243 120 DKVKAREQAEKAGIPVIPGSDGPAETLEAVEQFGQTNGYPIIIKASLGGGGRGMRIVRSESEVKEAYERAKSEAKAAFGN 199
Cdd:pfam02786 1 DKVLFKAAMKEAGVPTVPGTAGPVETEEEALAAAKEIGYPVIIKAAFGGGGLGMGIARNEEELAELFALALAEAPAAFGN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 772685243 200 DEVYVEKLIENPKHIEVQVIGDKQGNVVHLFERDCSVQRRHQKVIEVAPSVSLSPELRNQICEAAVALAKNVNYINAGTV 279
Cdd:pfam02786 81 PQVLVEKSLKGPKHIEYQVLRDAHGNCITVCNRECSDQRRTQKSIEVAPSQTLTDEERQMLREAAVKIARHLGYVGAGTV 160
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 772685243 280 EFLV--ANNEFYFIEVNPRVQVEHTITEMITGVDIVQTQILVAQGHTL 325
Cdd:pfam02786 161 EFALdpFSGEYYFIEMNTRLQVEHALAEKATGYDLAKEAAKIALGYPL 208
|
|
| PRK12581 |
PRK12581 |
oxaloacetate decarboxylase; Provisional |
531-998 |
5.98e-84 |
|
oxaloacetate decarboxylase; Provisional
Pssm-ID: 79056 [Multi-domain] Cd Length: 468 Bit Score: 281.24 E-value: 5.98e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 772685243 531 QKSVLLTDTTFRDAHQSLLATRFRSHDLKkianPTAALWPEL--FSMEMWGGATFDVAYRFLKEDPWKRLEELRKEVPNT 608
Cdd:PRK12581 10 QQQVAITETVLRDGHQSLMATRLSIEDML----PVLTILDKIgyYSLECWGGATFDACIRFLNEDPWERLRTLKKGLPNT 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 772685243 609 LFQMLLRSSNAVGYTNYPDNVIQEFVKQSAQSGIDVFRIFDSLNWVKGMTLAIDAVRDTGKVAEAAICYTGDILdknrtk 688
Cdd:PRK12581 86 RLQMLLRGQNLLGYRHYADDIVDKFISLSAQNGIDVFRIFDALNDPRNIQQALRAVKKTGKEAQLCIAYTTSPV------ 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 772685243 689 YDLAYYTSMAKELEAAGAHILGIKDMAGLLKPQAAYELVSALKETIDIPVHLHTHDTSGNGIYMYAKAVEAGVDIIDVAV 768
Cdd:PRK12581 160 HTLNYYLSLVKELVEMGADSICIKDMAGILTPKAAKELVSGIKAMTNLPLIVHTHATSGISQMTYLAAVEAGADRIDTAL 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 772685243 769 SSMAGLTSQPSASGFYHAMEGNARRPEMNVQNVEMLSQYWESVRKYY---SEFESGMKSPHTEIYEHEMPGGQYSNLQQQ 845
Cdd:PRK12581 240 SPFSEGTSQPATESMYLALKEAGYDITLDETLLEQAANHLRQARQKYladGILDPSLLFPDPRTLQYQVPGGMLSNMLSQ 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 772685243 846 AKGVGLGDRWNEVKEMYRRVNDMFGDIVKVTPSSKVVGDMALYMVqnnltekdVYEKGEQLdFPDSVVELFKGNIGQPHG 925
Cdd:PRK12581 320 LKQANAESKLEEVLAEVPRVRKDLGYPPLVTPLSQMVGTQAAMNV--------ILGKPYQM-VSKEIKQYLAGDYGKTPA 390
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 772685243 926 GFPEKLQKLILKGQEPITVRPGELLEPvSFEAIKQEFKEqhnLEISDQDAVAYALYPKVFSDYVKTAESYGDI 998
Cdd:PRK12581 391 PVNEDLKRSQIGSAPVTTNRPADQLSP-EFEVLKAEVAD---LAQTDEDVLTYALFPSVAKPFLTTKYQTDDV 459
|
|
| AccC |
COG0439 |
Biotin carboxylase [Lipid transport and metabolism]; Biotin carboxylase is part of the Pathway ... |
67-322 |
5.53e-68 |
|
Biotin carboxylase [Lipid transport and metabolism]; Biotin carboxylase is part of the Pathway/BioSystem: Fatty acid biosynthesis
Pssm-ID: 440208 [Multi-domain] Cd Length: 263 Bit Score: 229.37 E-value: 5.53e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 772685243 67 DIEGIID----IAKRNKVDAIhpgygfLSEN----IHFAKRCEEEGIvfIGPKSEHLDMFGDKVKAREQAEKAGIPViPG 138
Cdd:COG0439 1 DIDAIIAaaaeLARETGIDAV------LSESefavETAAELAEELGL--PGPSPEAIRAMRDKVLMREALAAAGVPV-PG 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 772685243 139 SDgPAETLEAVEQFGQTNGYPIIIKASLGGGGRGMRIVRSESEVKEAYERAKSEAKAAFGNDEVYVEKLIENPkHIEVQV 218
Cdd:COG0439 72 FA-LVDSPEEALAFAEEIGYPVVVKPADGAGSRGVRVVRDEEELEAALAEARAEAKAGSPNGEVLVEEFLEGR-EYSVEG 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 772685243 219 IGDkQGNVVHlferdCSVQRRHQK---VIE---VAPSVsLSPELRNQICEAAVALAKNVNYIN-AGTVEFLV-ANNEFYF 290
Cdd:COG0439 150 LVR-DGEVVV-----CSITRKHQKppyFVElghEAPSP-LPEELRAEIGELVARALRALGYRRgAFHTEFLLtPDGEPYL 222
|
250 260 270
....*....|....*....|....*....|....
gi 772685243 291 IEVNPRVQVEH--TITEMITGVDIVQTQILVAQG 322
Cdd:COG0439 223 IEINARLGGEHipPLTELATGVDLVREQIRLALG 256
|
|
| DRE_TIM_metallolyase |
cd03174 |
DRE-TIM metallolyase superfamily; The DRE-TIM metallolyase superfamily includes ... |
537-809 |
2.75e-67 |
|
DRE-TIM metallolyase superfamily; The DRE-TIM metallolyase superfamily includes 2-isopropylmalate synthase (IPMS), alpha-isopropylmalate synthase (LeuA), 3-hydroxy-3-methylglutaryl-CoA lyase, homocitrate synthase, citramalate synthase, 4-hydroxy-2-oxovalerate aldolase, re-citrate synthase, transcarboxylase 5S, pyruvate carboxylase, AksA, and FrbC. These members all share a conserved triose-phosphate isomerase (TIM) barrel domain consisting of a core beta(8)-alpha(8) motif with the eight parallel beta strands forming an enclosed barrel surrounded by eight alpha helices. The domain has a catalytic center containing a divalent cation-binding site formed by a cluster of invariant residues that cap the core of the barrel. In addition, the catalytic site includes three invariant residues - an aspartate (D), an arginine (R), and a glutamate (E) - which is the basis for the domain name "DRE-TIM".
Pssm-ID: 163674 [Multi-domain] Cd Length: 265 Bit Score: 227.34 E-value: 2.75e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 772685243 537 TDTTFRDAHQSLLATrFRSHDLKKIANPTAALWpeLFSMEMWGGATFDVAyrFLKEDPWKRLEELRKEVPNTLFQMLLRS 616
Cdd:cd03174 1 TDTTLRDGLQSEGAT-FSTEDKLEIAEALDEAG--VDSIEVGSGASPKAV--PQMEDDWEVLRAIRKLVPNVKLQALVRN 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 772685243 617 SnavgytnypdnviQEFVKQSAQSGIDVFRIFDSLN--------------WVKGMTLAIDAVRDTGKVAEAAICYTGDIl 682
Cdd:cd03174 76 R-------------EKGIERALEAGVDEVRIFDSASethsrknlnksreeDLENAEEAIEAAKEAGLEVEGSLEDAFGC- 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 772685243 683 dknrtKYDLAYYTSMAKELEAAGAHILGIKDMAGLLKPQAAYELVSALKETI-DIPVHLHTHDTSGNGIYMYAKAVEAGV 761
Cdd:cd03174 142 -----KTDPEYVLEVAKALEEAGADEISLKDTVGLATPEEVAELVKALREALpDVPLGLHTHNTLGLAVANSLAALEAGA 216
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 772685243 762 DIIDVAVSSMAGLTSQPSASGFYHAMEGNARRPEMNVQNVEMLSQYWE 809
Cdd:cd03174 217 DRVDGSVNGLGERAGNAATEDLVAALEGLGIDTGIDLEKLLEISRYVE 264
|
|
| Biotin_carb_N |
pfam00289 |
Biotin carboxylase, N-terminal domain; This domain is structurally related to the PreATP-grasp ... |
6-114 |
3.40e-59 |
|
Biotin carboxylase, N-terminal domain; This domain is structurally related to the PreATP-grasp domain. The family contains the N-terminus of biotin carboxylase enzymes, and propionyl-CoA carboxylase A chain.
Pssm-ID: 425585 [Multi-domain] Cd Length: 108 Bit Score: 198.09 E-value: 3.40e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 772685243 6 IQKVLVANRGEIAIRIFRACTELNIRTVAVYSKEDSGSYHRYKADEAYLVGEGKkPIDAYLDIEGIIDIAKRNKVDAIHP 85
Cdd:pfam00289 1 IKKVLIANRGEIAVRIIRACRELGIRTVAVYSEADANSLHVRLADEAVCLGPGP-ASESYLNIDAIIDAAKETGADAIHP 79
|
90 100
....*....|....*....|....*....
gi 772685243 86 GYGFLSENIHFAKRCEEEGIVFIGPKSEH 114
Cdd:pfam00289 80 GYGFLSENAEFARACEEAGIIFIGPSPEA 108
|
|
| Biotin_carb_C |
smart00878 |
Biotin carboxylase C-terminal domain; Biotin carboxylase is a component of the acetyl-CoA ... |
346-453 |
4.84e-50 |
|
Biotin carboxylase C-terminal domain; Biotin carboxylase is a component of the acetyl-CoA carboxylase multi-component enzyme which catalyses the first committed step in fatty acid synthesis in animals, plants and bacteria. Most of the active site residues reported in reference are in this C-terminal domain.
Pssm-ID: 214878 [Multi-domain] Cd Length: 107 Bit Score: 171.83 E-value: 4.84e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 772685243 346 QSRVTTEDPQNDFMPDTGKIMAYRSGGGFGVRLDTGNsFQGAVITPYYDSLLVKLSTWALTFEQAAAKMVRNLQEFRIRG 425
Cdd:smart00878 1 ECRINAEDPANGFLPSPGRITRYRFPGGPGVRVDSGV-YEGYEVPPYYDSMIAKLIVWGEDREEAIARLRRALDEFRIRG 79
|
90 100
....*....|....*....|....*...
gi 772685243 426 IKTNIPFLENVAKHEKFLTGQYDTSFID 453
Cdd:smart00878 80 VKTNIPFLRALLRHPDFRAGDVDTGFLE 107
|
|
| Biotin_carb_C |
pfam02785 |
Biotin carboxylase C-terminal domain; Biotin carboxylase is a component of the acetyl-CoA ... |
346-454 |
7.40e-42 |
|
Biotin carboxylase C-terminal domain; Biotin carboxylase is a component of the acetyl-CoA carboxylase multi-component enzyme which catalyzes the first committed step in fatty acid synthesis in animals, plants and bacteria. Most of the active site residues reported in reference are in this C-terminal domain.
Pssm-ID: 426981 [Multi-domain] Cd Length: 108 Bit Score: 148.80 E-value: 7.40e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 772685243 346 QSRVTTEDPQNDFMPDTGKIMAYRSGGGFGVRLDTGnSFQGAVITPYYDSLLVKLSTWALTFEQAAAKMVRNLQEFRIRG 425
Cdd:pfam02785 1 EARIYAEDPDNNFLPSPGKVTRYRFPGGPGVRVDSG-VYAGYTVSPYYDSMIAKLIVHGPTREEAIARLRRALAEFRIEG 79
|
90 100
....*....|....*....|....*....
gi 772685243 426 IKTNIPFLENVAKHEKFLTGQYDTSFIDT 454
Cdd:pfam02785 80 VKTNIPFLRAILEHPDFRAGEVDTGFLEE 108
|
|
| HMGL-like |
pfam00682 |
HMGL-like; This family contains a diverse set of enzymes. These include various aldolases and ... |
534-807 |
1.48e-27 |
|
HMGL-like; This family contains a diverse set of enzymes. These include various aldolases and a region of pyruvate carboxylase.
Pssm-ID: 459902 [Multi-domain] Cd Length: 264 Bit Score: 113.21 E-value: 1.48e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 772685243 534 VLLTDTTFRDAHQSLlATRFRSHDLKKIAnptAALwpelfsmEMWGGATFDVAYRFLKEDPWKRLEELRKEVPNTLFQML 613
Cdd:pfam00682 2 VAICDTTLRDGEQAL-GVAFSIDEKLAIA---RAL-------DAAGVDEIEVGFPAASEDDFEVVRAIAKVIPHARILVL 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 772685243 614 LRssnavgytnYPDNVIQEFVKQSAQSGIDVFRIFD-------------SLNWVKGMtlAIDAVRDtgkVAEAAICYTGD 680
Cdd:pfam00682 71 CR---------AREHDIKAAVEALKGAGAVRVHVFIatsdlhrkyklgkDREEVAKR--AVAAVKA---ARSRGIDVEFS 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 772685243 681 ILDKNRTkyDLAYYTSMAKELEAAGAHILGIKDMAGLLKPQAAYELVSALKETID--IPVHLHTHDTSGNGIYMYAKAVE 758
Cdd:pfam00682 137 PEDASRT--DPEFLAEVVEAAIEAGATRINIPDTVGVLTPNEAAELISALKARVPnkAIISVHCHNDLGMAVANSLAAVE 214
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 772685243 759 AGVDIIDVAVSSMAGLTSQPSASGFYHAMEGNARRPEMNVQNVEMLSQY 807
Cdd:pfam00682 215 AGADRVDGTVNGIGERAGNAALEEVAAALEGLGVDTGLDLQRLRSIANL 263
|
|
| biotinyl_domain |
cd06850 |
The biotinyl-domain or biotin carboxyl carrier protein (BCCP) domain is present in all ... |
1079-1145 |
6.81e-25 |
|
The biotinyl-domain or biotin carboxyl carrier protein (BCCP) domain is present in all biotin-dependent enzymes, such as acetyl-CoA carboxylase, pyruvate carboxylase, propionyl-CoA carboxylase, methylcrotonyl-CoA carboxylase, geranyl-CoA carboxylase, oxaloacetate decarboxylase, methylmalonyl-CoA decarboxylase, transcarboxylase and urea amidolyase. This domain functions in transferring CO2 from one subsite to another, allowing carboxylation, decarboxylation, or transcarboxylation. During this process, biotin is covalently attached to a specific lysine.
Pssm-ID: 133459 [Multi-domain] Cd Length: 67 Bit Score: 98.64 E-value: 6.81e-25
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 772685243 1079 HIAASMPGTVIKVLTEAGTKVNKGDHLMINEAMKMETTVQAPFSGTIKQVHVKNGEPIQTGDLLLEI 1145
Cdd:cd06850 1 EVTAPMPGTVVKVLVKEGDKVEAGQPLAVLEAMKMENEVTAPVAGVVKEILVKEGDQVEAGQLLVVI 67
|
|
| CarB |
COG0458 |
Carbamoylphosphate synthase large subunit [Amino acid transport and metabolism, Nucleotide ... |
66-297 |
1.82e-24 |
|
Carbamoylphosphate synthase large subunit [Amino acid transport and metabolism, Nucleotide transport and metabolism]; Carbamoylphosphate synthase large subunit is part of the Pathway/BioSystem: Arginine biosynthesis
Pssm-ID: 440226 [Multi-domain] Cd Length: 536 Bit Score: 109.20 E-value: 1.82e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 772685243 66 LDIEGIIDIAKRNKVDAIHPGYG-----FLSENIHfaKRCEEEGIVFIGPKSEHLDMFGDKVKAREQAEKAGIPVIPGsd 140
Cdd:COG0458 57 LTVEDVLDIIEKEKPDGVIVQFGgqtalNLAVELE--EAGILEGVKILGTSPDAIDLAEDRELFKELLDKLGIPQPKS-- 132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 772685243 141 GPAETLEAVEQFGQTNGYPIIIKASLGGGGRGMRIVRSESEVKEAYERAKSeakaAFGNDEVYVEKLIENPKHIEVQVIG 220
Cdd:COG0458 133 GTATSVEEALAIAEEIGYPVIVRPSYVLGGRGMGIVYNEEELEEYLERALK----VSPDHPVLIDESLLGAKEIEVDVVR 208
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 772685243 221 DKQGNVV------HlFER------DcSvqrrhqkvIEVAPSVSLSPELRNQICEAAVALAKNVNYINAGTVEFLVANNEF 288
Cdd:COG0458 209 DGEDNVIivgimeH-IEPagvhsgD-S--------ICVAPPQTLSDKEYQRLRDATLKIARALGVVGLCNIQFAVDDGRV 278
|
....*....
gi 772685243 289 YFIEVNPRV 297
Cdd:COG0458 279 YVIEVNPRA 287
|
|
| carB |
PRK12815 |
carbamoyl phosphate synthase large subunit; Reviewed |
66-325 |
1.27e-21 |
|
carbamoyl phosphate synthase large subunit; Reviewed
Pssm-ID: 237215 [Multi-domain] Cd Length: 1068 Bit Score: 101.97 E-value: 1.27e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 772685243 66 LDIEGIIDIAKRNKVDAIHPGYGFLSEnIHFAKRCEEEGIVFIGPKSEHLDMFGDKVKAREQAEKAGIPVIPGsdGPAET 145
Cdd:PRK12815 617 LTLEDVLNVAEAENIKGVIVQFGGQTA-INLAKGLEEAGLTILGTSPDTIDRLEDRDRFYQLLDELGLPHVPG--LTATD 693
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 772685243 146 LEAVEQFGQTNGYPIIIKASLGGGGRGMRIVRSESEVKEAYERAKSeakaafGNDEVYVEKLIENpKHIEVQVIGDkqGN 225
Cdd:PRK12815 694 EEEAFAFAKRIGYPVLIRPSYVIGGQGMAVVYDEPALEAYLAENAS------QLYPILIDQFIDG-KEYEVDAISD--GE 764
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 772685243 226 VVHL------FERDCSvqrrHQ-KVIEVAPSVSLSPELRNQICEAAVALAKNVNYINAGTVEFLVANNEFYFIEVNPRVQ 298
Cdd:PRK12815 765 DVTIpgiiehIEQAGV----HSgDSIAVLPPQSLSEEQQEKIRDYAIKIAKKLGFRGIMNIQFVLANDEIYVLEVNPRAS 840
|
250 260
....*....|....*....|....*....
gi 772685243 299 veHT--ITEMITGVDIVQTQILVAQGHTL 325
Cdd:PRK12815 841 --RTvpFVSKATGVPLAKLATKVLLGKSL 867
|
|
| AccB |
COG0511 |
Biotin carboxyl carrier protein [Lipid transport and metabolism]; Biotin carboxyl carrier ... |
1072-1146 |
2.91e-20 |
|
Biotin carboxyl carrier protein [Lipid transport and metabolism]; Biotin carboxyl carrier protein is part of the Pathway/BioSystem: Fatty acid biosynthesis
Pssm-ID: 440277 [Multi-domain] Cd Length: 136 Bit Score: 88.03 E-value: 2.91e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 772685243 1072 ADRTNPSHIAASMPGTV-------IKVLTEAGTKVNKGDHLMINEAMKMETTVQAPFSGTIKQVHVKNGEPIQTGDLLLE 1144
Cdd:COG0511 55 AAASGGGAVKSPMVGTFyrapspgAKPFVKVGDKVKAGDTLCIIEAMKMMNEIEAPVSGTVVEILVENGQPVEYGQPLFV 134
|
..
gi 772685243 1145 IE 1146
Cdd:COG0511 135 IE 136
|
|
| CPSaseII_lrg |
TIGR01369 |
carbamoyl-phosphate synthase, large subunit; Carbamoyl-phosphate synthase (CPSase) catalyzes ... |
66-325 |
5.26e-20 |
|
carbamoyl-phosphate synthase, large subunit; Carbamoyl-phosphate synthase (CPSase) catalyzes the first committed step in pyrimidine, arginine, and urea biosynthesis. In general, it is a glutamine-dependent enzyme, EC 6.3.5.5, termed CPSase II in eukaryotes. An exception is the mammalian mitochondrial urea-cycle form, CPSase I, in which the glutamine amidotransferase domain active site Cys on the small subunit has been lost, and the enzyme is ammonia-dependent. In both CPSase I and the closely related, glutamine-dependent CPSase III (allosterically activated by acetyl-glutamate) demonstrated in some other vertebrates, the small and large chain regions are fused in a single polypeptide chain. This model represents the large chain of glutamine-hydrolysing carbamoyl-phosphate synthases, or the corresponding regions of larger, multifunctional proteins, as found in all domains of life, and CPSase I forms are considered exceptions within the family. In several thermophilic species (Methanobacterium thermoautotrophicum, Methanococcus jannaschii, Aquifex aeolicus), the large subunit appears split, at different points, into two separate genes. [Purines, pyrimidines, nucleosides, and nucleotides, Pyrimidine ribonucleotide biosynthesis]
Pssm-ID: 273581 [Multi-domain] Cd Length: 1050 Bit Score: 96.61 E-value: 5.26e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 772685243 66 LDIEGIIDIAKRNKVD--AIHPGyGFLSENIhfAKRCEEEGIVFIGPKSEHLDMFGDKVKAREQAEKAGIPVIPGsdGPA 143
Cdd:TIGR01369 616 LTFEDVMNIIELEKPEgvIVQFG-GQTPLNL--AKALEEAGVPILGTSPESIDRAEDREKFSELLDELGIPQPKW--KTA 690
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 772685243 144 ETLEAVEQFGQTNGYPIIIKASLGGGGRGMRIVRSESEVkeayERAKSEAKAAFGNDEVYVEKLIENPKHIEVQVIGDKQ 223
Cdd:TIGR01369 691 TSVEEAVEFASEIGYPVLVRPSYVLGGRAMEIVYNEEEL----RRYLEEAVAVSPEHPVLIDKYLEDAVEVDVDAVSDGE 766
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 772685243 224 GNVVH-LFErdcsvqrrHqkvIEVA-----------PSVSLSPELRNQICEAAVALAKNVNYINAGTVEFLVANNEFYFI 291
Cdd:TIGR01369 767 EVLIPgIME--------H---IEEAgvhsgdstcvlPPQTLSAEIVDRIKDIVRKIAKELNVKGLMNIQFAVKDGEVYVI 835
|
250 260 270
....*....|....*....|....*....|....
gi 772685243 292 EVNPRVQVEHTITEMITGVDIVQTQILVAQGHTL 325
Cdd:TIGR01369 836 EVNPRASRTVPFVSKATGVPLAKLAVRVMLGKKL 869
|
|
| COG3919 |
COG3919 |
Predicted ATP-dependent carboligase, ATP-grasp superfamily [General function prediction only]; |
23-297 |
1.75e-19 |
|
Predicted ATP-dependent carboligase, ATP-grasp superfamily [General function prediction only];
Pssm-ID: 443124 [Multi-domain] Cd Length: 382 Bit Score: 91.91 E-value: 1.75e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 772685243 23 RACTELNIRTVAVYSKEDS-GSYHRYkADEAYLVGEGKKPIDAYLDieGIIDIAKRNKVDAIHPGY----GFLSENIHFA 97
Cdd:COG3919 22 RSLGEAGVRVIVVDRDPLGpAARSRY-VDEVVVVPDPGDDPEAFVD--ALLELAERHGPDVLIPTGdeyvELLSRHRDEL 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 772685243 98 krceEEGIVFIGPKSEHLDMFGDKVKAREQAEKAGIPV----IPGSDGPAEtlEAVEQFGqtngYPIIIKASLG------ 167
Cdd:COG3919 99 ----EEHYRLPYPDADLLDRLLDKERFYELAEELGVPVpktvVLDSADDLD--ALAEDLG----FPVVVKPADSvgydel 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 772685243 168 --GGGRGMRIVRSESEVKEAYERAKSEAkaafgnDEVYVEKLIENPKHIEVQVIG--DKQGNVVHLFerdcSVQRRHQKV 243
Cdd:COG3919 169 sfPGKKKVFYVDDREELLALLRRIAAAG------YELIVQEYIPGDDGEMRGLTAyvDRDGEVVATF----TGRKLRHYP 238
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 772685243 244 IEVAPSVSLSPELRNQICEAAVALAKNVNYINAGTVEFLV--ANNEFYFIEVNPRV 297
Cdd:COG3919 239 PAGGNSAARESVDDPELEEAARRLLEALGYHGFANVEFKRdpRDGEYKLIEINPRF 294
|
|
| PRK12767 |
PRK12767 |
carbamoyl phosphate synthase-like protein; Provisional |
47-296 |
2.47e-19 |
|
carbamoyl phosphate synthase-like protein; Provisional
Pssm-ID: 237195 [Multi-domain] Cd Length: 326 Bit Score: 90.33 E-value: 2.47e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 772685243 47 YKADEAYLVGEGKKPidAYLDIegIIDIAKRNKVDAIHPGY----GFLSENihfAKRCEEEGIVFIGPKSEHLDMFGDKV 122
Cdd:PRK12767 41 YFADKFYVVPKVTDP--NYIDR--LLDICKKEKIDLLIPLIdpelPLLAQN---RDRFEEIGVKVLVSSKEVIEICNDKW 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 772685243 123 KAREQAEKAGIPViPGSDGPaETLEAVEQFGQTN--GYPIIIKASLGGGGRGMRIVRSESEVKEAYERakseakaafgND 200
Cdd:PRK12767 114 LTYEFLKENGIPT-PKSYLP-ESLEDFKAALAKGelQFPLFVKPRDGSASIGVFKVNDKEELEFLLEY----------VP 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 772685243 201 EVYVEKLIENPKhIEVQVIGDKQGNVVHlferdcSVQRRHQKVI--EVAPSVSlspELRNQICEAAVALAKNVNYINAGT 278
Cdd:PRK12767 182 NLIIQEFIEGQE-YTVDVLCDLNGEVIS------IVPRKRIEVRagETSKGVT---VKDPELFKLAERLAEALGARGPLN 251
|
250
....*....|....*...
gi 772685243 279 VEFLVANNEFYFIEVNPR 296
Cdd:PRK12767 252 IQCFVTDGEPYLFEINPR 269
|
|
| PurK |
COG0026 |
Phosphoribosylaminoimidazole carboxylase (NCAIR synthetase) [Nucleotide transport and ... |
62-297 |
1.05e-18 |
|
Phosphoribosylaminoimidazole carboxylase (NCAIR synthetase) [Nucleotide transport and metabolism]; Phosphoribosylaminoimidazole carboxylase (NCAIR synthetase) is part of the Pathway/BioSystem: Purine biosynthesis
Pssm-ID: 439797 [Multi-domain] Cd Length: 353 Bit Score: 88.98 E-value: 1.05e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 772685243 62 IDAYLDIEGIIDIAKRnkVDAIhpgyGFLSENIHFA--KRCEEEGIVFigPKSEHLDMFGDKVKAREQAEKAGIPVIPGS 139
Cdd:COG0026 37 VADYDDEEALREFAER--CDVV----TFEFENVPAEalEALEAEVPVR--PGPEALEIAQDRLLEKAFLAELGIPVAPFA 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 772685243 140 dgPAETLEAVEQFGQTNGYPIIIKASLGG-GGRGMRIVRSESEVKEAYErakseakaAFGNDEVYVEKLIenPKHIEVQV 218
Cdd:COG0026 109 --AVDSLEDLEAAIAELGLPAVLKTRRGGyDGKGQVVIKSAADLEAAWA--------ALGGGPCILEEFV--PFERELSV 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 772685243 219 IG--DKQGNVVH--LFErdcSVQRRHQKVIEVAPSvSLSPELRNQICEAAVALAKNVNYInaGT--VE-FLVANNEFYFI 291
Cdd:COG0026 177 IVarSPDGEVATypVVE---NVHRNGILDESIAPA-RISEALAAEAEEIAKRIAEALDYV--GVlaVEfFVTKDGELLVN 250
|
....*.
gi 772685243 292 EVNPRV 297
Cdd:COG0026 251 EIAPRP 256
|
|
| CPSaseII_lrg |
TIGR01369 |
carbamoyl-phosphate synthase, large subunit; Carbamoyl-phosphate synthase (CPSase) catalyzes ... |
5-326 |
3.97e-18 |
|
carbamoyl-phosphate synthase, large subunit; Carbamoyl-phosphate synthase (CPSase) catalyzes the first committed step in pyrimidine, arginine, and urea biosynthesis. In general, it is a glutamine-dependent enzyme, EC 6.3.5.5, termed CPSase II in eukaryotes. An exception is the mammalian mitochondrial urea-cycle form, CPSase I, in which the glutamine amidotransferase domain active site Cys on the small subunit has been lost, and the enzyme is ammonia-dependent. In both CPSase I and the closely related, glutamine-dependent CPSase III (allosterically activated by acetyl-glutamate) demonstrated in some other vertebrates, the small and large chain regions are fused in a single polypeptide chain. This model represents the large chain of glutamine-hydrolysing carbamoyl-phosphate synthases, or the corresponding regions of larger, multifunctional proteins, as found in all domains of life, and CPSase I forms are considered exceptions within the family. In several thermophilic species (Methanobacterium thermoautotrophicum, Methanococcus jannaschii, Aquifex aeolicus), the large subunit appears split, at different points, into two separate genes. [Purines, pyrimidines, nucleosides, and nucleotides, Pyrimidine ribonucleotide biosynthesis]
Pssm-ID: 273581 [Multi-domain] Cd Length: 1050 Bit Score: 90.44 E-value: 3.97e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 772685243 5 SIQKVLVANRGEIAI-----------RIFRACTELNIRTVAVYS-----KEDSGSyhrykADEAYLVgegkkPIDAYLdI 68
Cdd:TIGR01369 5 DIKKILVIGSGPIVIgqaaefdysgsQACKALKEEGYRVILVNSnpatiMTDPEM-----ADKVYIE-----PLTPEA-V 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 772685243 69 EGIIdiaKRNKVDAIHPGYG-----FLSENIHFAKRCEEEGIVFIGPKSEHLDMFGDKVKAREQAEKAGIPVIPGsdGPA 143
Cdd:TIGR01369 74 EKII---EKERPDAILPTFGgqtalNLAVELEESGVLEKYGVEVLGTPVEAIKKAEDRELFREAMKEIGEPVPES--EIA 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 772685243 144 ETLEAVEQFGQTNGYPIIIKASLGGGGRGMRIVRSESEVKEAYERAKSEAKAafgnDEVYVEKLIENPKHIEVQVIGDKQ 223
Cdd:TIGR01369 149 HSVEEALAAAKEIGYPVIVRPAFTLGGTGGGIAYNREELKEIAERALSASPI----NQVLVEKSLAGWKEIEYEVMRDSN 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 772685243 224 GNV-------------VHLFERdcsvqrrhqkvIEVAPSVSLSPE----LRNqiceAAVALAKNVNYINAGTVEFLV--A 284
Cdd:TIGR01369 225 DNCitvcnmenfdpmgVHTGDS-----------IVVAPSQTLTDKeyqmLRD----ASIKIIRELGIEGGCNVQFALnpD 289
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 772685243 285 NNEFYFIEVNPRVQVEHTITEMITGVDIVQTQILVAQGHTLH 326
Cdd:TIGR01369 290 SGRYYVIEVNPRVSRSSALASKATGYPIAKVAAKLAVGYTLD 331
|
|
| PRK08225 |
PRK08225 |
acetyl-CoA carboxylase biotin carboxyl carrier protein subunit; Validated |
1078-1146 |
4.38e-16 |
|
acetyl-CoA carboxylase biotin carboxyl carrier protein subunit; Validated
Pssm-ID: 181304 [Multi-domain] Cd Length: 70 Bit Score: 73.67 E-value: 4.38e-16
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 772685243 1078 SHIAASMPGTVIKVLTEAGTKVNKGDHLMINEAMKMETTVQAPFSGTIKQVHVKNGEPIQTGDLLLEIE 1146
Cdd:PRK08225 2 TKVYASMAGNVWKIVVKVGDTVEEGQDVVILESMKMEIPIVAEEAGTVKKINVQEGDFVNEGDVLLEIE 70
|
|
| Biotin_lipoyl |
pfam00364 |
Biotin-requiring enzyme; This family covers two Prosite entries, the conserved lysine residue ... |
1079-1145 |
3.90e-15 |
|
Biotin-requiring enzyme; This family covers two Prosite entries, the conserved lysine residue binds biotin in one group and lipoic acid in the other. Note that the HMM does not currently recognize the Glycine cleavage system H proteins.
Pssm-ID: 395290 [Multi-domain] Cd Length: 73 Bit Score: 71.09 E-value: 3.90e-15
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 772685243 1079 HIAASMPGT-----VIKVLTEAGTKVNKGDHLMINEAMKMETTVQAPFSGTIKQVHVKNGEPIQTGDLLLEI 1145
Cdd:pfam00364 2 EIKSPMIGEsvregVVEWLVKVGDKVKAGQPLAEVEAMKMEMEIPAPVAGVVKEILVPEGDTVEVGDPLAKI 73
|
|
| PRK06549 |
PRK06549 |
acetyl-CoA carboxylase biotin carboxyl carrier protein subunit; Validated |
1023-1145 |
5.21e-15 |
|
acetyl-CoA carboxylase biotin carboxyl carrier protein subunit; Validated
Pssm-ID: 235826 [Multi-domain] Cd Length: 130 Bit Score: 72.92 E-value: 5.21e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 772685243 1023 GKTLIVKLISIGEPQPDATRViyfelngQPREV---VIKDESIKSSVQERLKADRTNPSHIAASMPGTVIKVLTEAGTKV 1099
Cdd:PRK06549 11 GKEYLVEMEEIGAPAQAAAPA-------QPASTpvpVPTEASPQVEAQAPQPAAAAGADAMPSPMPGTILKVLVAVGDQV 83
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 772685243 1100 NKGDHLMINEAMKMETTVQAPFSGTIKQVHVKNGEPIQTGDLLLEI 1145
Cdd:PRK06549 84 TENQPLLILEAMKMENEIVASSAGTVTAIHVTPGQVVNPGDGLITI 129
|
|
| LysX |
COG0189 |
Glutathione synthase, LysX or RimK-type ligase, ATP-grasp superfamily [Amino acid transport ... |
20-314 |
9.01e-15 |
|
Glutathione synthase, LysX or RimK-type ligase, ATP-grasp superfamily [Amino acid transport and metabolism, Coenzyme transport and metabolism, Translation, ribosomal structure and biogenesis, Secondary metabolites biosynthesis, transport and catabolism]; Glutathione synthase, LysX or RimK-type ligase, ATP-grasp superfamily is part of the Pathway/BioSystem: Lysine biosynthesis
Pssm-ID: 439959 [Multi-domain] Cd Length: 289 Bit Score: 76.13 E-value: 9.01e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 772685243 20 RIFRACTELNIRtvavyskedsgsYHRYKADEAYLVGEGKKPIDAYLDIEGiidiakrnkVDAI-----HPGYGFlseni 94
Cdd:COG0189 18 ALIEAAQRRGHE------------VEVIDPDDLTLDLGRAPELYRGEDLSE---------FDAVlpridPPFYGL----- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 772685243 95 HFAKRCEEEGIVFIGPkSEHLDMFGDKVKAREQAEKAGIPVIP--GSDGPAETLEAVEQFGqtngYPIIIKASLGGGGRG 172
Cdd:COG0189 72 ALLRQLEAAGVPVVND-PEAIRRARDKLFTLQLLARAGIPVPPtlVTRDPDDLRAFLEELG----GPVVLKPLDGSGGRG 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 772685243 173 MRIVRSESEVKEAYeraksEAKAAFGNDEVYVEKLIENPKHIE--VQVIGDKqgnVVHLFER-----DCsvqRRHQKVIE 245
Cdd:COG0189 147 VFLVEDEDALESIL-----EALTELGSEPVLVQEFIPEEDGRDirVLVVGGE---PVAAIRRipaegEF---RTNLARGG 215
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 772685243 246 VAPSVSLSPELRnqicEAAVALAKNVNYINAGtVEFLVANNEFYFIEVNPRVQVEHtiTEMITGVDIVQ 314
Cdd:COG0189 216 RAEPVELTDEER----ELALRAAPALGLDFAG-VDLIEDDDGPLVLEVNVTPGFRG--LERATGVDIAE 277
|
|
| carB |
PRK12815 |
carbamoyl phosphate synthase large subunit; Reviewed |
3-326 |
2.47e-14 |
|
carbamoyl phosphate synthase large subunit; Reviewed
Pssm-ID: 237215 [Multi-domain] Cd Length: 1068 Bit Score: 78.09 E-value: 2.47e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 772685243 3 QQSIQKVLVANRGEIAI-----------RIFRACTELNIRTVAVYSKEDSGSYHRYKADEAYLvgegkKPidayLDIEGI 71
Cdd:PRK12815 4 DTDIQKILVIGSGPIVIgqaaefdysgtQACLALKEEGYQVVLVNPNPATIMTDPAPADTVYF-----EP----LTVEFV 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 772685243 72 IDIAKRNKVDAIHPGYGflSEN-IHFAKRCEEEGIV------FIGPKSEHLDMFGDKVKAREQAEKAGIPVipGSDGPAE 144
Cdd:PRK12815 75 KRIIAREKPDALLATLG--GQTaLNLAVKLHEDGILeqygveLLGTNIEAIQKGEDRERFRALMKELGEPV--PESEIVT 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 772685243 145 TLEAVEQFGQTNGYPIIIKASLGGGGRGMRIVRSESEVKEAYERAKSEAKAafgnDEVYVEKLIENPKHIEVQVIGDKQG 224
Cdd:PRK12815 151 SVEEALAFAEKIGFPIIVRPAYTLGGTGGGIAENLEELEQLFKQGLQASPI----HQCLLEESIAGWKEIEYEVMRDRNG 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 772685243 225 NVVHLferdCS------VQRRHQKVIEVAPSVSLS----PELRNqiceAAVALAKNVNYINAGTVEFLVANN--EFYFIE 292
Cdd:PRK12815 227 NCITV----CNmenidpVGIHTGDSIVVAPSQTLTddeyQMLRS----ASLKIISALGVVGGCNIQFALDPKskQYYLIE 298
|
330 340 350
....*....|....*....|....*....|....
gi 772685243 293 VNPRVQVEHTITEMITGVDIVQTQILVAQGHTLH 326
Cdd:PRK12815 299 VNPRVSRSSALASKATGYPIAKIAAKLAVGYTLN 332
|
|
| PRK05641 |
PRK05641 |
putative acetyl-CoA carboxylase biotin carboxyl carrier protein subunit; Validated |
1080-1145 |
4.10e-14 |
|
putative acetyl-CoA carboxylase biotin carboxyl carrier protein subunit; Validated
Pssm-ID: 235540 [Multi-domain] Cd Length: 153 Bit Score: 71.05 E-value: 4.10e-14
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 772685243 1080 IAASMPGTVIKVLTEAGTKVNKGDHLMINEAMKMETTVQAPFSGTIKQVHVKNGEPIQTGDLLLEI 1145
Cdd:PRK05641 87 VTAPMPGKILRILVREGQQVKVGQGLLILEAMKMENEIPAPKDGVVKKILVKEGDTVDTGQPLIEL 152
|
|
| carB |
PRK05294 |
carbamoyl-phosphate synthase large subunit; |
97-296 |
4.40e-14 |
|
carbamoyl-phosphate synthase large subunit;
Pssm-ID: 235393 [Multi-domain] Cd Length: 1066 Bit Score: 77.44 E-value: 4.40e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 772685243 97 AKRCEEEGIVFIGPKSEHLDMFGDKVKAREQAEKAGIPVIPGsdGPAETLEAVEQFGQTNGYPIIIKASLGGGGRGMRIV 176
Cdd:PRK05294 646 AKALEAAGVPILGTSPDAIDLAEDRERFSKLLEKLGIPQPPN--GTATSVEEALEVAEEIGYPVLVRPSYVLGGRAMEIV 723
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 772685243 177 RSESEVKEaYERaksEAKAAFGNDEVYVEKLIENPKHIEVQVIGDKQgNVV------HlferdcsvqrrhqkvIEVA--- 247
Cdd:PRK05294 724 YDEEELER-YMR---EAVKVSPDHPVLIDKFLEGAIEVDVDAICDGE-DVLiggimeH---------------IEEAgvh 783
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 772685243 248 --------PSVSLSPELRNQICEAAVALAKNVN---YINagtVEFLVANNEFYFIEVNPR 296
Cdd:PRK05294 784 sgdsacslPPQTLSEEIIEEIREYTKKLALELNvvgLMN---VQFAVKDDEVYVIEVNPR 840
|
|
| carB |
PRK05294 |
carbamoyl-phosphate synthase large subunit; |
68-297 |
2.71e-13 |
|
carbamoyl-phosphate synthase large subunit;
Pssm-ID: 235393 [Multi-domain] Cd Length: 1066 Bit Score: 74.75 E-value: 2.71e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 772685243 68 IEGIIdiaKRNKVDAIHPGYG---FLSENIHFAKR--CEEEGIVFIGPKSEHLDMFGDKVKAREQAEKAGIPVIPGsdGP 142
Cdd:PRK05294 74 VEKII---EKERPDAILPTMGgqtALNLAVELAESgvLEKYGVELIGAKLEAIDKAEDRELFKEAMKKIGLPVPRS--GI 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 772685243 143 AETLEAVEQFGQTNGYPIIIKAS--LGGGGRGmrIVRSESEVKEAYERAKseakAAFGNDEVYVEKLIENPKHIEVQVIG 220
Cdd:PRK05294 149 AHSMEEALEVAEEIGYPVIIRPSftLGGTGGG--IAYNEEELEEIVERGL----DLSPVTEVLIEESLLGWKEYEYEVMR 222
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 772685243 221 DKQGNVVHLferdCSvqrrhqkvIE--------------VAPSVSLSPE----LRNqiceAAVALAKNVNYINAGT-VEF 281
Cdd:PRK05294 223 DKNDNCIIV----CS--------IEnidpmgvhtgdsitVAPAQTLTDKeyqmLRD----ASIAIIREIGVETGGCnVQF 286
|
250
....*....|....*...
gi 772685243 282 LV--ANNEFYFIEVNPRV 297
Cdd:PRK05294 287 ALnpKDGRYIVIEMNPRV 304
|
|
| ATP-grasp |
pfam02222 |
ATP-grasp domain; This family does not contain all known ATP-grasp domain members. This family ... |
129-297 |
9.26e-13 |
|
ATP-grasp domain; This family does not contain all known ATP-grasp domain members. This family includes a diverse set of enzymes that possess ATP-dependent carboxylate-amine ligase activity.
Pssm-ID: 396689 [Multi-domain] Cd Length: 169 Bit Score: 67.66 E-value: 9.26e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 772685243 129 EKAGIPVIPGSDgpAETLEAVEQFGQTNGYPIIIKASLGG-GGRGMRIVRSESEVKEAYErakseakaAFGNDEVYVEKL 207
Cdd:pfam02222 1 QKLGLPTPRFMA--AESLEELIEAGQELGYPCVVKARRGGyDGKGQYVVRSEADLPQAWE--------ELGDGPVIVEEF 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 772685243 208 IENPKHIEVQVIGDKQGnVVHLFErdcSVQRRHQK---VIEVAPSvSLSPELRNQICEAAVALAKNVNYINAGTVE-FLV 283
Cdd:pfam02222 71 VPFDRELSVLVVRSVDG-ETAFYP---VVETIQEDgicRLSVAPA-RVPQAIQAEAQDIAKRLVDELGGVGVFGVElFVT 145
|
170
....*....|....
gi 772685243 284 ANNEFYFIEVNPRV 297
Cdd:pfam02222 146 EDGDLLINELAPRP 159
|
|
| PRK06019 |
PRK06019 |
phosphoribosylaminoimidazole carboxylase ATPase subunit; Reviewed |
64-297 |
5.73e-12 |
|
phosphoribosylaminoimidazole carboxylase ATPase subunit; Reviewed
Pssm-ID: 235674 [Multi-domain] Cd Length: 372 Bit Score: 68.64 E-value: 5.73e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 772685243 64 AYLDIEGIIDIAKRnkVDAIhpGYGFlsENI--HFAKRCEEEGIVFIGPKS-EHLdmfGDKVKAREQAEKAGIPVIPGSd 140
Cdd:PRK06019 50 DYDDVAALRELAEQ--CDVI--TYEF--ENVpaEALDALAARVPVPPGPDAlAIA---QDRLTEKQFLDKLGIPVAPFA- 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 772685243 141 gPAETLEAVEQFGQTNGYPIIIKASLGG-GGRGMRIVRSESEVKEAYerakseakAAFGNDEVYVEKLIENPKhiEVQVI 219
Cdd:PRK06019 120 -VVDSAEDLEAALADLGLPAVLKTRRGGyDGKGQWVIRSAEDLEAAW--------ALLGSVPCILEEFVPFER--EVSVI 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 772685243 220 G--DKQGNVVH--LFErdcSVQRRHQKVIEVAPSvSLSPELRNQICEAAVALAKNVNYInaGT--VE-FLVANNEFYFIE 292
Cdd:PRK06019 189 VarGRDGEVVFypLVE---NVHRNGILRTSIAPA-RISAELQAQAEEIASRIAEELDYV--GVlaVEfFVTGDGELLVNE 262
|
....*
gi 772685243 293 VNPRV 297
Cdd:PRK06019 263 IAPRP 267
|
|
| Dala_Dala_lig_C |
pfam07478 |
D-ala D-ala ligase C-terminus; This family represents the C-terminal, catalytic domain of the ... |
131-295 |
9.25e-12 |
|
D-ala D-ala ligase C-terminus; This family represents the C-terminal, catalytic domain of the D-alanine--D-alanine ligase enzyme EC:6.3.2.4. D-Alanine is one of the central molecules of the cross-linking step of peptidoglycan assembly. There are three enzymes involved in the D-alanine branch of peptidoglycan biosynthesis: the pyridoxal phosphate-dependent D-alanine racemase (Alr), the ATP-dependent D-alanine:D-alanine ligase (Ddl), and the ATP-dependent D-alanine:D-alanine-adding enzyme (MurF).
Pssm-ID: 429483 [Multi-domain] Cd Length: 204 Bit Score: 65.42 E-value: 9.25e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 772685243 131 AGIPVIP-----GSDGPAETLEAVEQFGQTNGYPIIIKASLGGGGRGMRIVRSESEVKEAYErakseakAAFGNDE-VYV 204
Cdd:pfam07478 5 AGLPVVPfvtftRADWKLNPKEWCAQVEEALGYPVFVKPARLGSSVGVSKVESREELQAAIE-------EAFQYDEkVLV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 772685243 205 EKLIENPKhIEVQVIGDKQGNVVHLFER--DCSVQRRHQK----VIEVAPSVSLSPELRNQICEAAVALAKNVNYINAGT 278
Cdd:pfam07478 78 EEGIEGRE-IECAVLGNEDPEVSPVGEIvpSGGFYDYEAKyiddSAQIVVPADLEEEQEEQIQELALKAYKALGCRGLAR 156
|
170
....*....|....*...
gi 772685243 279 VEFLV-ANNEFYFIEVNP 295
Cdd:pfam07478 157 VDFFLtEDGEIVLNEVNT 174
|
|
| Biotinyl_lipoyl_domains |
cd06663 |
Biotinyl_lipoyl_domains are present in biotin-dependent carboxylases/decarboxylases, the ... |
1077-1145 |
1.28e-11 |
|
Biotinyl_lipoyl_domains are present in biotin-dependent carboxylases/decarboxylases, the dihydrolipoyl acyltransferase component (E2) of 2-oxo acid dehydrogenases, and the H-protein of the glycine cleavage system (GCS). These domains transport CO2, acyl, or methylamine, respectively, between components of the complex/protein via a biotinyl or lipoyl group, which is covalently attached to a highly conserved lysine residue.
Pssm-ID: 133456 [Multi-domain] Cd Length: 73 Bit Score: 61.30 E-value: 1.28e-11
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 772685243 1077 PSHIAASMPGTVIKVLTEAGTKVNKGDHLMINEAMKMETTVQAPFSGTIKQVHVKNGEPIQTGDLLLEI 1145
Cdd:cd06663 5 PDLAQHLGDGTVVKWLKKVGDKVKKGDVLAEIEAMKATSDVEAPKSGTVKKVLVKEGTKVEGDTPLVKI 73
|
|
| DdlA |
COG1181 |
D-alanine-D-alanine ligase or related ATP-grasp enzyme [Cell wall/membrane/envelope biogenesis, ... |
120-295 |
3.46e-11 |
|
D-alanine-D-alanine ligase or related ATP-grasp enzyme [Cell wall/membrane/envelope biogenesis, General function prediction only]; D-alanine-D-alanine ligase or related ATP-grasp enzyme is part of the Pathway/BioSystem: Mureine biosynthesis
Pssm-ID: 440794 [Multi-domain] Cd Length: 303 Bit Score: 65.51 E-value: 3.46e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 772685243 120 DKVKAREQAEKAGIPVIPGSDGPAETLEAVEQFGQTNGYPIIIKASLGGGGRGMRIVRSESEVKEAYERAkseakAAFGn 199
Cdd:COG1181 95 DKALTKRVLAAAGLPTPPYVVLRRGELADLEAIEEELGLPLFVKPAREGSSVGVSKVKNAEELAAALEEA-----FKYD- 168
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 772685243 200 DEVYVEKLIEnPKHIEVQVIGDKQGNVvhlferdcSVqrrhqkVIEVAPS--------------------VSLSPELRNQ 259
Cdd:COG1181 169 DKVLVEEFID-GREVTVGVLGNGGPRA--------LP------PIEIVPEngfydyeakytdggteyicpARLPEELEER 233
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 772685243 260 ICEAAVALAKNVN---YinaGTVEFLV-ANNEFYFIEVNP 295
Cdd:COG1181 234 IQELALKAFRALGcrgY---ARVDFRLdEDGEPYLLEVNT 270
|
|
| rimK_fam |
TIGR00768 |
alpha-L-glutamate ligase, RimK family; This family, related to bacterial glutathione ... |
76-312 |
2.12e-10 |
|
alpha-L-glutamate ligase, RimK family; This family, related to bacterial glutathione synthetases, contains at least three different alpha-L-glutamate ligases. One is RimK, as in E. coli, which adds additional Glu residues to the native Glu-Glu C-terminus of ribosomal protein S6, but not to Lys-Glu mutants. Most species with a member of this subfamily lack an S6 homolog ending in Glu-Glu, however. Members in Methanococcus jannaschii act instead as a tetrahydromethanopterin:alpha-l-glutamate ligase (MJ0620) and a gamma-F420-2:alpha-l-glutamate ligase (MJ1001).
Pssm-ID: 273261 [Multi-domain] Cd Length: 276 Bit Score: 62.75 E-value: 2.12e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 772685243 76 KRNKVDAIHPGYGFLSENIHFAKRCEEEGIVFIGPkSEHLDMFGDKVKAREQAEKAGIPViPGS---DGPAETLEAVEQF 152
Cdd:TIGR00768 45 ALAELDVVIVRIVSMFRGLAVLRYLESLGVPVINS-SDAILNAGDKFLSHQLLAKAGIPL-PRTglaGSPEEALKLIEEI 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 772685243 153 GqtngYPIIIKASLGGGGRGMRIVRSESEVkeayeRAKSEAKAAFGNDE--VYVEKLIENPKH--IEVQVIGDKqgnVVH 228
Cdd:TIGR00768 123 G----FPVVLKPVFGSWGRGVSLARDRQAA-----ESLLEHFEQLNGPQnlFLVQEYIKKPGGrdIRVFVVGDE---VVA 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 772685243 229 LFERDCSVQRR---HQKviEVAPSVSLSPELRNQICEAAVALAKNVnyinaGTVEFLVANNEFYFIEVNPRVQVEHtiTE 305
Cdd:TIGR00768 191 AIYRITSGHWRsnlARG--GKAEPCSLTEEIEELAIKAAKALGLDV-----AGVDLLESEDGLLVNEVNANPEFKN--SV 261
|
....*..
gi 772685243 306 MITGVDI 312
Cdd:TIGR00768 262 KTTGVNI 268
|
|
| PRK05889 |
PRK05889 |
biotin/lipoyl-binding carrier protein; |
1080-1145 |
2.25e-08 |
|
biotin/lipoyl-binding carrier protein;
Pssm-ID: 180306 [Multi-domain] Cd Length: 71 Bit Score: 52.12 E-value: 2.25e-08
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 772685243 1080 IAASMPGTVIKVLTEAGTKVNKGDHLMINEAMKMETTVQAPFSGTIKQVHVKNGEPIQTGDLLLEI 1145
Cdd:PRK05889 5 VRAEIVASVLEVVVNEGDQIGKGDTLVLLESMKMEIPVLAEVAGTVSKVSVSVGDVIQAGDLIAVI 70
|
|
| aksA |
PRK11858 |
trans-homoaconitate synthase; Reviewed |
683-768 |
4.37e-08 |
|
trans-homoaconitate synthase; Reviewed
Pssm-ID: 183341 [Multi-domain] Cd Length: 378 Bit Score: 56.72 E-value: 4.37e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 772685243 683 DKNRTkyDLAYYTSMAKELEAAGAHILGIKDMAGLLKPQAAYELVSALKETIDIPVHLHTHDTSG----NGIYmyakAVE 758
Cdd:PRK11858 138 DASRT--DLDFLIEFAKAAEEAGADRVRFCDTVGILDPFTMYELVKELVEAVDIPIEVHCHNDFGmataNALA----GIE 211
|
90
....*....|
gi 772685243 759 AGVDIIDVAV 768
Cdd:PRK11858 212 AGAKQVHTTV 221
|
|
| PLN02735 |
PLN02735 |
carbamoyl-phosphate synthase |
74-325 |
4.40e-08 |
|
carbamoyl-phosphate synthase
Pssm-ID: 215391 [Multi-domain] Cd Length: 1102 Bit Score: 57.87 E-value: 4.40e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 772685243 74 IAKRNKVDAIHPGYGFLSEnIHFAKRCEEEGIV------FIGPKSEHLDMFGDKVKAREQAEKAGIPVIPgsDGPAETLE 147
Cdd:PLN02735 93 VIAKERPDALLPTMGGQTA-LNLAVALAESGILekygveLIGAKLDAIKKAEDRELFKQAMEKIGLKTPP--SGIATTLD 169
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 772685243 148 AVEQFGQTNG-YPIIIKA--SLGGGGRGMrivrsesevkeAYERAKSEA-----KAAFGNDEVYVEKLIENPKHIEVQVI 219
Cdd:PLN02735 170 ECFEIAEDIGeFPLIIRPafTLGGTGGGI-----------AYNKEEFETickagLAASITSQVLVEKSLLGWKEYELEVM 238
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 772685243 220 GDKQGNVVHLferdCSVQR------RHQKVIEVAPSVSLSPELRNQICEAAVALAKNVNYINAGT-VEFLV--ANNEFYF 290
Cdd:PLN02735 239 RDLADNVVII----CSIENidpmgvHTGDSITVAPAQTLTDKEYQRLRDYSVAIIREIGVECGGSnVQFAVnpVDGEVMI 314
|
250 260 270
....*....|....*....|....*....|....*
gi 772685243 291 IEVNPRVQVEHTITEMITGVDIVQTQILVAQGHTL 325
Cdd:PLN02735 315 IEMNPRVSRSSALASKATGFPIAKMAAKLSVGYTL 349
|
|
| ddl |
PRK01372 |
D-alanine--D-alanine ligase; Reviewed |
120-294 |
5.54e-08 |
|
D-alanine--D-alanine ligase; Reviewed
Pssm-ID: 234948 [Multi-domain] Cd Length: 304 Bit Score: 55.89 E-value: 5.54e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 772685243 120 DKVKAREQAEKAGIPVIPGS--DGPAETLEAVEQFGqtngYPIIIKASLGGGGRGMRIVRSESEVKEAYERAkseakAAF 197
Cdd:PRK01372 98 DKLRTKLVWQAAGLPTPPWIvlTREEDLLAAIDKLG----LPLVVKPAREGSSVGVSKVKEEDELQAALELA-----FKY 168
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 772685243 198 GnDEVYVEKLIENPKhIEVQVIGDKQGNVVHL-------------FERDCsvqrRHqkvIEVAPsvsLSPELRNQICEAA 264
Cdd:PRK01372 169 D-DEVLVEKYIKGRE-LTVAVLGGKALPVIEIvpagefydyeakyLAGGT----QY---ICPAG---LPAEIEAELQELA 236
|
170 180 190
....*....|....*....|....*....|.
gi 772685243 265 VALAKNVNYINAGTVEFLV-ANNEFYFIEVN 294
Cdd:PRK01372 237 LKAYRALGCRGWGRVDFMLdEDGKPYLLEVN 267
|
|
| PLN02948 |
PLN02948 |
phosphoribosylaminoimidazole carboxylase |
96-296 |
2.02e-07 |
|
phosphoribosylaminoimidazole carboxylase
Pssm-ID: 178534 [Multi-domain] Cd Length: 577 Bit Score: 55.07 E-value: 2.02e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 772685243 96 FAKRC------------------EEEGiVFIGPKSEHLDMFGDKVKAREQAEKAGIPVIPGSDGPaeTLEAVEQFGQTNG 157
Cdd:PLN02948 80 FAKRCdvltveiehvdvdtlealEKQG-VDVQPKSSTIRIIQDKYAQKVHFSKHGIPLPEFMEID--DLESAEKAGDLFG 156
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 772685243 158 YPIIIKAS-LGGGGRGMRIVRSESEVkeayerakSEAKAAFGNDE--VYVEKLIENPKHIEVQVIGDKQGNVV--HLFEr 232
Cdd:PLN02948 157 YPLMLKSRrLAYDGRGNAVAKTEEDL--------SSAVAALGGFErgLYAEKWAPFVKELAVMVARSRDGSTRcyPVVE- 227
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 772685243 233 dcSVQRR---HqkVIEVAPSVSLS-PELRNQICEAAVALAKnvnyiNAGT--VE-FLVANNEFYFIEVNPR 296
Cdd:PLN02948 228 --TIHKDnicH--VVEAPANVPWKvAKLATDVAEKAVGSLE-----GAGVfgVElFLLKDGQILLNEVAPR 289
|
|
| DRE_TIM_HMGL |
cd07938 |
3-hydroxy-3-methylglutaryl-CoA lyase, catalytic TIM barrel domain; ... |
696-774 |
2.08e-07 |
|
3-hydroxy-3-methylglutaryl-CoA lyase, catalytic TIM barrel domain; 3-hydroxy-3-methylglutaryl-CoA lyase (HMGL) catalyzes the cleavage of HMG-CoA to acetyl-CoA and acetoacetate, one of the terminal steps in ketone body generation and leucine degradation, and is a key enzyme in the pathway that supplies metabolic fuel to extrahepatic tissues. Mutations in HMGL cause a human autosomal recessive disorder called primary metabolic aciduria that affects ketogenesis and leucine catabolism and can be fatal due to an inability to tolerate hypoglycemia. HMGL has a TIM barrel domain with a catalytic center containing a divalent cation-binding site formed by a cluster of invariant residues that cap the core of the barrel. The cleavage of HMG-CoA requires the presence of a divalent cation like Mg2+ or Mn2+, and the reaction is thought to involve general acid/base catalysis. This family belongs to the DRE-TIM metallolyase superfamily. DRE-TIM metallolyases include 2-isopropylmalate synthase (IPMS), alpha-isopropylmalate synthase (LeuA), 3-hydroxy-3-methylglutaryl-CoA lyase, homocitrate synthase, citramalate synthase, 4-hydroxy-2-oxovalerate aldolase, re-citrate synthase, transcarboxylase 5S, pyruvate carboxylase, AksA, and FrbC. These members all share a conserved triose-phosphate isomerase (TIM) barrel domain consisting of a core beta(8)-alpha(8) motif with the eight parallel beta strands forming an enclosed barrel surrounded by eight alpha helices. The domain has a catalytic center containing a divalent cation-binding site formed by a cluster of invariant residues that cap the core of the barrel. In addition, the catalytic site includes three invariant residues - an aspartate (D), an arginine (R), and a glutamate (E) - which is the basis for the domain name "DRE-TIM".
Pssm-ID: 163676 Cd Length: 274 Bit Score: 53.55 E-value: 2.08e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 772685243 696 SMAKELEAAGAHILGIKDMAGLLKPQAAYELVSALKETI-DIPVHLHTHDTSGNGIYMYAKAVEAGVDIIDvavSSMAGL 774
Cdd:cd07938 153 EVAERLLDLGCDEISLGDTIGVATPAQVRRLLEAVLERFpDEKLALHFHDTRGQALANILAALEAGVRRFD---SSVGGL 229
|
|
| ATP-grasp_3 |
pfam02655 |
ATP-grasp domain; No functional information or experimental verification of function is known ... |
119-298 |
3.52e-07 |
|
ATP-grasp domain; No functional information or experimental verification of function is known in this family. This family appears to be an ATP-grasp domain (Pers. obs. A Bateman).
Pssm-ID: 396979 [Multi-domain] Cd Length: 160 Bit Score: 51.23 E-value: 3.52e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 772685243 119 GDKVKAREQAEKAGIPViPGSDGPAETLEAveqfgqtnGYPIIIKASLGGGGRGMRIVRSESEvkeayerakseakAAFG 198
Cdd:pfam02655 2 SDKLKTYKALKNAGVPT-PETLQAEELLRE--------EKKYVVKPRDGCGGEGVRKVENGRE-------------DEAF 59
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 772685243 199 NDEVYVEKLIENpKHIEVQVIGDKQGNVVHLFERdcsvQRRHQKVIEVAPSVSLSP---ELRNQICEAAVALAKNVNYIN 275
Cdd:pfam02655 60 IENVLVQEFIEG-EPLSVSLLSDGEKALPLSVNR----QYIDNGGSGFVYAGNVTPsrtELKEEIIELAEEVVECLPGLR 134
|
170 180
....*....|....*....|....*
gi 772685243 276 --AGtVEFLVANNEFYFIEVNPRVQ 298
Cdd:pfam02655 135 gyVG-VDLVLKDNEPYVIEVNPRIT 158
|
|
| DRE_TIM_HOA |
cd07943 |
4-hydroxy-2-oxovalerate aldolase, N-terminal catalytic TIM barrel domain; 4-hydroxy ... |
698-774 |
3.53e-07 |
|
4-hydroxy-2-oxovalerate aldolase, N-terminal catalytic TIM barrel domain; 4-hydroxy 2-ketovalerate aldolase (Also known as 4-hydroxy-2-ketovalerate aldolase and 4-hydroxy-2-oxopentanoate aldolase (HOA)) converts 4-hydroxy-2-oxopentanoate to acetaldehyde and pyruvate, the penultimate step in the meta-cleavage pathway for the degradation of phenols, cresols and catechol. This family includes the Escherichia coli MhpE aldolase, the Pseudomonas DmpG aldolase, and the Burkholderia xenovorans BphI pyruvate aldolase. In Pseudomonas, the DmpG aldolase tightly associates with a dehydrogenase (DmpF ) and is inactive without it. HOA has a canonical TIM-barrel fold with a C-terminal extension that forms a funnel leading to the active site. This family belongs to the DRE-TIM metallolyase superfamily. DRE-TIM metallolyases include 2-isopropylmalate synthase (IPMS), alpha-isopropylmalate synthase (LeuA), 3-hydroxy-3-methylglutaryl-CoA lyase, homocitrate synthase, citramalate synthase, 4-hydroxy-2-oxovalerate aldolase, re-citrate synthase, transcarboxylase 5S, pyruvate carboxylase, AksA, and FrbC. These members all share a conserved triose-phosphate isomerase (TIM) barrel domain consisting of a core beta(8)-alpha(8) motif with the eight parallel beta strands forming an enclosed barrel surrounded by eight alpha helices. The domain has a catalytic center containing a divalent cation-binding site formed by a cluster of invariant residues that cap the core of the barrel. In addition, the catalytic site includes three invariant residues - an aspartate (D), an arginine (R), and a glutamate (E) - which is the basis for the domain name "DRE-TIM".
Pssm-ID: 163681 Cd Length: 263 Bit Score: 52.89 E-value: 3.53e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 772685243 698 AKELEAAGAHILGIKDMAGLLKPQAAYELVSALKETIDI-PVHLHTHDTSG----NGIYmyakAVEAGVDIIDVavsSMA 772
Cdd:cd07943 147 AKLMESYGADCVYVTDSAGAMLPDDVRERVRALREALDPtPVGFHGHNNLGlavaNSLA----AVEAGATRIDG---SLA 219
|
..
gi 772685243 773 GL 774
Cdd:cd07943 220 GL 221
|
|
| PDHac_trf_long |
TIGR01348 |
pyruvate dehydrogenase complex dihydrolipoamide acetyltransferase, long form; This model ... |
1086-1148 |
7.43e-07 |
|
pyruvate dehydrogenase complex dihydrolipoamide acetyltransferase, long form; This model describes a subset of pyruvate dehydrogenase complex dihydrolipoamide acetyltransferase specifically close by both phylogenetic and per cent identity (UPGMA) trees. Members of this set include two or three copies of the lipoyl-binding domain. E. coli AceF is a member of this model, while mitochondrial and some other bacterial forms belong to a separate model. [Energy metabolism, Pyruvate dehydrogenase]
Pssm-ID: 273566 [Multi-domain] Cd Length: 546 Bit Score: 53.34 E-value: 7.43e-07
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 772685243 1086 GTVIKVLTEAGTKVNKGDHLMINEAMKMETTVQAPFSGTIKQVHVKNGEPIQTGDLLLEIEKA 1148
Cdd:TIGR01348 130 VTVIEVLVKVGDTVSADQSLITLESDKASMEVPAPASGVVKSVKVKVGDSVPTGDLILTLSVA 192
|
|
| PylC |
COG2232 |
Pyrrolysine biosynthesis ligase PylC and related enzymes, ATP-grasp superfamily [Amino acid ... |
49-353 |
1.03e-06 |
|
Pyrrolysine biosynthesis ligase PylC and related enzymes, ATP-grasp superfamily [Amino acid transport and metabolism];
Pssm-ID: 441833 [Multi-domain] Cd Length: 370 Bit Score: 52.23 E-value: 1.03e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 772685243 49 ADEAYLVGEGKKPIDAYLDIEGIIDIAKRNKVDAIHPGYGFlsENIHFAKRCEEEGIVFIGPKSEHLDMFGDKVKAREQA 128
Cdd:COG2232 43 AERWVRLDAESCGFDLEDLPAALLELAAADDPDGLVYGSGF--ENFPELLERLARRLPLLGNPPEVVRRVKDPLRFFALL 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 772685243 129 EKAGIPVipgsdgPaETLEAVEQfgqtNGYPIIIKASLGGGGRGMRIVRSEsevkeayerakseakaAFGNDEVYVEKLI 208
Cdd:COG2232 121 DELGIPH------P-ETRFEPPP----DPGPWLVKPIGGAGGWHIRPADSE----------------APPAPGRYFQRYV 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 772685243 209 E----------NPKHIEV-----QVIGDK-------QGNVVHLferdcsvqrrhqkvievapsvSLSPELRNQICEAAVA 266
Cdd:COG2232 174 EgtpasvlflaDGSDARVlgfnrQLIGPAgerpfryGGNIGPL---------------------ALPPALAEEMRAIAEA 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 772685243 267 LAKNVNYINAGTVEFLVANNEFYFIEVNPRVQVEHTITEMITGVDIVQTQILVAQGHtLHSKKVNIPEQKDISTIGYAIQ 346
Cdd:COG2232 233 LVAALGLVGLNGVDFILDGDGPYVLEVNPRPQASLDLYEDATGGNLFDAHLRACRGE-LPEVPRPKPRRVAAKAILYAPR 311
|
....*..
gi 772685243 347 SRVTTED 353
Cdd:COG2232 312 DLTIPDD 318
|
|
| PRK09389 |
PRK09389 |
(R)-citramalate synthase; Provisional |
687-768 |
1.18e-06 |
|
(R)-citramalate synthase; Provisional
Pssm-ID: 236493 [Multi-domain] Cd Length: 488 Bit Score: 52.63 E-value: 1.18e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 772685243 687 TKYDLAYYTSMAKELEAAGAHILGIKDMAGLLKPQAAYELVSALKETIDIPVHLHTHDTSGNGIYMYAKAVEAGVDIIDV 766
Cdd:PRK09389 138 SRADLDFLKELYKAGIEAGADRICFCDTVGILTPEKTYELFKRLSELVKGPVSIHCHNDFGLAVANTLAALAAGADQVHV 217
|
..
gi 772685243 767 AV 768
Cdd:PRK09389 218 TI 219
|
|
| AceF |
COG0508 |
Pyruvate/2-oxoglutarate dehydrogenase complex, dihydrolipoamide acyltransferase (E2) component ... |
1086-1145 |
1.80e-06 |
|
Pyruvate/2-oxoglutarate dehydrogenase complex, dihydrolipoamide acyltransferase (E2) component [Energy production and conversion]; Pyruvate/2-oxoglutarate dehydrogenase complex, dihydrolipoamide acyltransferase (E2) component is part of the Pathway/BioSystem: Pyruvate oxidation
Pssm-ID: 440274 [Multi-domain] Cd Length: 77 Bit Score: 46.60 E-value: 1.80e-06
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 772685243 1086 GTVIKVLTEAGTKVNKGDHLMINEAMKMETTVQAPFSGTIKQVHVKNGEPIQTGDLLLEI 1145
Cdd:COG0508 17 GTIVEWLVKEGDTVKEGDPLAEVETDKATMEVPAPAAGVLLEILVKEGDTVPVGAVIAVI 76
|
|
| DRE_TIM_NifV |
cd07939 |
Streptomyces rubellomurinus FrbC and related proteins, catalytic TIM barrel domain; FrbC (NifV) ... |
683-768 |
3.07e-06 |
|
Streptomyces rubellomurinus FrbC and related proteins, catalytic TIM barrel domain; FrbC (NifV) of Streptomyces rubellomurinus catalyzes the condensation of acetyl-CoA and alpha-ketoglutarate to form homocitrate and CoA, a reaction similar to one catalyzed by homocitrate synthase. The gene encoding FrbC is one of several genes required for the biosynthesis of FR900098, a potent antimalarial antibiotic. This protein is also required for assembly of the nitrogenase MoFe complex but its exact role is unknown. This family also includes the NifV proteins of Heliobacterium chlorum and Gluconacetobacter diazotrophicus, which appear to be orthologous to FrbC. This family belongs to the DRE-TIM metallolyase superfamily. DRE-TIM metallolyases include 2-isopropylmalate synthase (IPMS), alpha-isopropylmalate synthase (LeuA), 3-hydroxy-3-methylglutaryl-CoA lyase, homocitrate synthase, citramalate synthase, 4-hydroxy-2-oxovalerate aldolase, re-citrate synthase, transcarboxylase 5S, pyruvate carboxylase, AksA, and FrbC. These members all share a conserved triose-phosphate isomerase (TIM) barrel domain consisting of a core beta(8)-alpha(8) motif with the eight parallel beta strands forming an enclosed barrel surrounded by eight alpha helices. The domain has a catalytic center containing a divalent cation-binding site formed by a cluster of invariant residues that cap the core of the barrel. In addition, the catalytic site includes three invariant residues - an aspartate (D), an arginine (R), and a glutamate (E) - which is the basis for the domain name "DRE-TIM".
Pssm-ID: 163677 [Multi-domain] Cd Length: 259 Bit Score: 50.20 E-value: 3.07e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 772685243 683 DKNRTkyDLAYYTSMAKELEAAGAHILGIKDMAGLLKPQAAYELVSALKETIDIPVHLHTHDTSG----NGIymyaKAVE 758
Cdd:cd07939 132 DASRA--DPDFLIEFAEVAQEAGADRLRFADTVGILDPFTTYELIRRLRAATDLPLEFHAHNDLGlataNTL----AAVR 205
|
90
....*....|
gi 772685243 759 AGVDIIDVAV 768
Cdd:cd07939 206 AGATHVSVTV 215
|
|
| PDHac_trf_long |
TIGR01348 |
pyruvate dehydrogenase complex dihydrolipoamide acetyltransferase, long form; This model ... |
1080-1146 |
3.08e-06 |
|
pyruvate dehydrogenase complex dihydrolipoamide acetyltransferase, long form; This model describes a subset of pyruvate dehydrogenase complex dihydrolipoamide acetyltransferase specifically close by both phylogenetic and per cent identity (UPGMA) trees. Members of this set include two or three copies of the lipoyl-binding domain. E. coli AceF is a member of this model, while mitochondrial and some other bacterial forms belong to a separate model. [Energy metabolism, Pyruvate dehydrogenase]
Pssm-ID: 273566 [Multi-domain] Cd Length: 546 Bit Score: 51.41 E-value: 3.08e-06
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 772685243 1080 IAASMPGTVIKVLTEAGTKVNKGDHLMINEAMKMETTVQAPFSGTIKQVHVKNGEPIQTGDLLLEIE 1146
Cdd:TIGR01348 8 IGDNEEGEVIEVLVKPGDKVEAGQSLITLESDKASMEVPSSAAGIIKEIKVKVGDTLPVGGVIATLE 74
|
|
| PRK07051 |
PRK07051 |
biotin carboxyl carrier domain-containing protein; |
1080-1146 |
3.73e-06 |
|
biotin carboxyl carrier domain-containing protein;
Pssm-ID: 180811 [Multi-domain] Cd Length: 80 Bit Score: 45.77 E-value: 3.73e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 772685243 1080 IAASMPGTVIK-------VLTEAGTKVNKGDHLMINEAMKMETTVQAPFSGTIKQVHVKNGEPIQTGDLLLEIE 1146
Cdd:PRK07051 6 IVSPLPGTFYRrpspdapPYVEVGDAVAAGDVVGLIEVMKQFTEVEAEAAGRVVEFLVEDGEPVEAGQVLARIE 79
|
|
| PLN02735 |
PLN02735 |
carbamoyl-phosphate synthase |
157-296 |
5.84e-06 |
|
carbamoyl-phosphate synthase
Pssm-ID: 215391 [Multi-domain] Cd Length: 1102 Bit Score: 50.55 E-value: 5.84e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 772685243 157 GYPIIIKASLGGGGRGMRIVRSESEVKEAYERAKSEAKaafgNDEVYVEKLIENPKHIEVQVIGDKQGNVV--------- 227
Cdd:PLN02735 737 GYPVVVRPSYVLGGRAMEIVYSDDKLKTYLETAVEVDP----ERPVLVDKYLSDATEIDVDALADSEGNVViggimehie 812
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 772685243 228 ----HLFERDCSVqrrhqkvievaPSVSLSPELRNQICEAAVALAKNVNYINAGTVEFLV-ANNEFYFIEVNPR 296
Cdd:PLN02735 813 qagvHSGDSACSL-----------PTQTIPSSCLATIRDWTTKLAKRLNVCGLMNCQYAItPSGEVYIIEANPR 875
|
|
| PRK14016 |
PRK14016 |
cyanophycin synthetase; Provisional |
131-231 |
7.92e-06 |
|
cyanophycin synthetase; Provisional
Pssm-ID: 237586 [Multi-domain] Cd Length: 727 Bit Score: 50.15 E-value: 7.92e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 772685243 131 AGIPVIPGS--DGPAETLEAVEQFGqtngYPIIIKASLGGGGRGMRI-VRSESEVKEAYERAKSEakaafgNDEVYVEKL 207
Cdd:PRK14016 225 AGVPVPEGRvvTSAEDAWEAAEEIG----YPVVVKPLDGNHGRGVTVnITTREEIEAAYAVASKE------SSDVIVERY 294
|
90 100 110
....*....|....*....|....*....|....*....
gi 772685243 208 IENPKH---------------IEVQVIGDKQGNVVHLFE 231
Cdd:PRK14016 295 IPGKDHrllvvggklvaaarrEPPHVIGDGKHTIRELIE 333
|
|
| ddl |
PRK01966 |
D-alanine--D-alanine ligase; |
120-295 |
1.42e-05 |
|
D-alanine--D-alanine ligase;
Pssm-ID: 234993 [Multi-domain] Cd Length: 333 Bit Score: 48.58 E-value: 1.42e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 772685243 120 DKVKAREQAEKAGIPVIP------GSDGPAETLEAVEQFGqtngYPIIIKASLGGGGRGMRIVRSESEVKEAyerakseA 193
Cdd:PRK01966 123 DKILTKRLLAAAGIPVAPyvvltrGDWEEASLAEIEAKLG----LPVFVKPANLGSSVGISKVKNEEELAAA-------L 191
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 772685243 194 KAAFGND-EVYVEKLIeNPKHIEVQVIGdkqgnvvhlFERDCSVqrrhqkVIEVAPS--------------------VSL 252
Cdd:PRK01966 192 DLAFEYDrKVLVEQGI-KGREIECAVLG---------NDPKASV------PGEIVKPddfydyeakyldgsaeliipADL 255
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 772685243 253 SPELRNQICEAAVALAKNVNyiNAGT--VEFLV-ANNEFYFIEVNP 295
Cdd:PRK01966 256 SEELTEKIRELAIKAFKALG--CSGLarVDFFLtEDGEIYLNEINT 299
|
|
| PRK08195 |
PRK08195 |
4-hyroxy-2-oxovalerate/4-hydroxy-2-oxopentanoic acid aldolase,; Validated |
698-774 |
1.61e-05 |
|
4-hyroxy-2-oxovalerate/4-hydroxy-2-oxopentanoic acid aldolase,; Validated
Pssm-ID: 181282 [Multi-domain] Cd Length: 337 Bit Score: 48.29 E-value: 1.61e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 772685243 698 AKELEAAGAHILGIKDMAGLLKPQAAYELVSALKETI--DIPVHLHTHDTSGNGIYMYAKAVEAGVDIIDvavSSMAGL 774
Cdd:PRK08195 150 AKLMESYGAQCVYVVDSAGALLPEDVRDRVRALRAALkpDTQVGFHGHNNLGLGVANSLAAVEAGATRID---GSLAGL 225
|
|
| PurD |
COG0151 |
Phosphoribosylamine-glycine ligase [Nucleotide transport and metabolism]; ... |
61-205 |
2.46e-05 |
|
Phosphoribosylamine-glycine ligase [Nucleotide transport and metabolism]; Phosphoribosylamine-glycine ligase is part of the Pathway/BioSystem: Purine biosynthesis
Pssm-ID: 439921 [Multi-domain] Cd Length: 422 Bit Score: 48.09 E-value: 2.46e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 772685243 61 PIDAyLDIEGIIDIAKRNKVD-------AihPgygfLSENIhfAKRCEEEGIVFIGPKSE--HLDmfGDKVKAREQAEKA 131
Cdd:COG0151 45 DIDV-TDIEALVAFAKEENIDlvvvgpeA--P----LVAGI--VDAFRAAGIPVFGPSKAaaQLE--GSKAFAKEFMARY 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 772685243 132 GIPVIPGS--DGPAETLEAVEQFGqtngYPIIIKASlgG--GGRGMRIVRSESEVKEAYERAKSEAKaaFGN--DEVYVE 205
Cdd:COG0151 114 GIPTAAYRvfTDLEEALAYLEEQG----APIVVKAD--GlaAGKGVVVAETLEEALAAVDDMLADGK--FGDagARVVIE 185
|
|
| Biotin_lipoyl_2 |
pfam13533 |
Biotin-lipoyl like; |
1116-1147 |
2.88e-05 |
|
Biotin-lipoyl like;
Pssm-ID: 433286 Cd Length: 50 Bit Score: 42.43 E-value: 2.88e-05
10 20 30
....*....|....*....|....*....|..
gi 772685243 1116 TVQAPFSGTIKQVHVKNGEPIQTGDLLLEIEK 1147
Cdd:pfam13533 4 KIASPVSGKVVAVNVKEGQQVKKGDVLATLDS 35
|
|
| DRE_TIM_HCS |
cd07948 |
Saccharomyces cerevisiae homocitrate synthase and related proteins, catalytic TIM barrel ... |
701-768 |
4.63e-05 |
|
Saccharomyces cerevisiae homocitrate synthase and related proteins, catalytic TIM barrel domain; Homocitrate synthase (HCS) catalyzes the condensation of acetyl-CoA and alpha-ketoglutarate to form homocitrate, the first step in the lysine biosynthesis pathway. This family includes the Yarrowia lipolytica LYS1 protein as well as the Saccharomyces cerevisiae LYS20 and LYS21 proteins. This family belongs to the DRE-TIM metallolyase superfamily. DRE-TIM metallolyases include 2-isopropylmalate synthase (IPMS), alpha-isopropylmalate synthase (LeuA), 3-hydroxy-3-methylglutaryl-CoA lyase, homocitrate synthase, citramalate synthase, 4-hydroxy-2-oxovalerate aldolase, re-citrate synthase, transcarboxylase 5S, pyruvate carboxylase, AksA, and FrbC. These members all share a conserved triose-phosphate isomerase (TIM) barrel domain consisting of a core beta(8)-alpha(8) motif with the eight parallel beta strands forming an enclosed barrel surrounded by eight alpha helices. The domain has a catalytic center containing a divalent cation-binding site formed by a cluster of invariant residues that cap the core of the barrel. In addition, the catalytic site includes three invariant residues - an aspartate (D), an arginine (R), and a glutamate (E) - which is the basis for the domain name "DRE-TIM".
Pssm-ID: 163685 Cd Length: 262 Bit Score: 46.56 E-value: 4.63e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 772685243 701 LEAAGAHILGIKDMAGLLKPQAAYELVSALKETIDIPVHLHTHDTSGNGIYMYAKAVEAGVDIIDVAV 768
Cdd:cd07948 150 VDKLGVNRVGIADTVGIATPRQVYELVRTLRGVVSCDIEFHGHNDTGCAIANAYAALEAGATHIDTTV 217
|
|
| DRE_TIM_IPMS |
cd07940 |
2-isopropylmalate synthase (IPMS), N-terminal catalytic TIM barrel domain; 2-isopropylmalate ... |
683-768 |
5.97e-05 |
|
2-isopropylmalate synthase (IPMS), N-terminal catalytic TIM barrel domain; 2-isopropylmalate synthase (IPMS) catalyzes an aldol-type condensation of acetyl-CoA and 2-oxoisovalerate yielding 2-isopropylmalate and CoA, the first committed step in leucine biosynthesis. This family includes the Arabidopsis thaliana IPMS1 and IPMS2 proteins, the Glycine max GmN56 protein, and the Brassica insularis BatIMS protein. This family also includes a group of archeal IPMS-like proteins represented by the Methanocaldococcus jannaschii AksA protein. AksA catalyzes the condensation of alpha-ketoglutarate and acetyl-CoA to form trans-homoaconitate, one of 13 steps in the conversion of alpha-ketoglutarate and acetylCoA to alpha-ketosuberate, a precursor to coenzyme B and biotin. AksA also catalyzes the condensation of alpha-ketoadipate or alpha-ketopimelate with acetylCoA to form, respectively, the (R)-homocitrate homologs (R)-2-hydroxy-1,2,5-pentanetricarboxylic acid and (R)-2-hydroxy-1,2,6- hexanetricarboxylic acid. This family belongs to the DRE-TIM metallolyase superfamily. DRE-TIM metallolyases include 2-isopropylmalate synthase (IPMS), alpha-isopropylmalate synthase (LeuA), 3-hydroxy-3-methylglutaryl-CoA lyase, homocitrate synthase, citramalate synthase, 4-hydroxy-2-oxovalerate aldolase, re-citrate synthase, transcarboxylase 5S, pyruvate carboxylase, AksA, and FrbC. These members all share a conserved triose-phosphate isomerase (TIM) barrel domain consisting of a core beta(8)-alpha(8) motif with the eight parallel beta strands forming an enclosed barrel surrounded by eight alpha helices. The domain has a catalytic center containing a divalent cation-binding site formed by a cluster of invariant residues that cap the core of the barrel. In addition, the catalytic site includes three invariant residues - an aspartate (D), an arginine (R), and a glutamate (E) - which is the basis for the domain name "DRE-TIM".
Pssm-ID: 163678 Cd Length: 268 Bit Score: 46.29 E-value: 5.97e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 772685243 683 DKNRTkyDLAYYTSMAKELEAAGAHILGIKDMAGLLKPQAAYELVSALKE---TIDIPVHLHTHDTSG----NGIYmyak 755
Cdd:cd07940 136 DATRT--DLDFLIEVVEAAIEAGATTINIPDTVGYLTPEEFGELIKKLKEnvpNIKVPISVHCHNDLGlavaNSLA---- 209
|
90
....*....|...
gi 772685243 756 AVEAGVDIIDVAV 768
Cdd:cd07940 210 AVEAGARQVECTI 222
|
|
| PRK11855 |
PRK11855 |
dihydrolipoamide acetyltransferase; Reviewed |
1086-1146 |
6.54e-05 |
|
dihydrolipoamide acetyltransferase; Reviewed
Pssm-ID: 237000 [Multi-domain] Cd Length: 547 Bit Score: 47.12 E-value: 6.54e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 772685243 1086 GTVIKVLTEAGTKVNKGDHLMINEAMKMETTVQAPFSGTIKQVHVKNGEPIQTGDLLLEIE 1146
Cdd:PRK11855 16 VEVIEWLVKEGDTVEEDQPLVTVETDKATMEIPSPAAGVVKEIKVKVGDTVSVGGLLAVIE 76
|
|
| aceF |
PRK11854 |
pyruvate dehydrogenase dihydrolipoyltransacetylase; Validated |
1086-1148 |
7.58e-05 |
|
pyruvate dehydrogenase dihydrolipoyltransacetylase; Validated
Pssm-ID: 236999 [Multi-domain] Cd Length: 633 Bit Score: 46.92 E-value: 7.58e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 772685243 1086 GTVIKVLTEAGTKVNKGDHLMINEAMKMETTVQAPFSGTIKQVHVKNGEPIQTGDLLLEIEKA 1148
Cdd:PRK11854 118 VEVTEILVKVGDTVEAEQSLITVEGDKASMEVPAPFAGTVKEIKVNVGDKVSTGSLIMVFEVA 180
|
|
| aceF |
PRK11854 |
pyruvate dehydrogenase dihydrolipoyltransacetylase; Validated |
1086-1148 |
7.91e-05 |
|
pyruvate dehydrogenase dihydrolipoyltransacetylase; Validated
Pssm-ID: 236999 [Multi-domain] Cd Length: 633 Bit Score: 46.92 E-value: 7.91e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 772685243 1086 GTVIKVLTEAGTKVNKGDHLMINEAMKMETTVQAPFSGTIKQVHVKNGEPIQTGDLLLEIEKA 1148
Cdd:PRK11854 219 VEVTEVMVKVGDKVEAEQSLITVEGDKASMEVPAPFAGTVKEIKVNVGDKVKTGSLIMRFEVE 281
|
|
| purT |
PRK09288 |
formate-dependent phosphoribosylglycinamide formyltransferase; |
143-296 |
1.77e-04 |
|
formate-dependent phosphoribosylglycinamide formyltransferase;
Pssm-ID: 236454 [Multi-domain] Cd Length: 395 Bit Score: 45.13 E-value: 1.77e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 772685243 143 AETLEAVEQFGQTNGYPIIIKASLGGGGRGMRIVRSESEVKEAYERAKSEAKAafGNDEVYVEKLIE------------- 209
Cdd:PRK09288 135 ADSLEELRAAVEEIGYPCVVKPVMSSSGKGQSVVRSPEDIEKAWEYAQEGGRG--GAGRVIVEEFIDfdyeitlltvrav 212
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 772685243 210 NPK--------HIevQVIGDKQgnvvhlferdCSVQrrhqkvievaPSvSLSPELRNQICEAAVALAKNVNyiNAGT--V 279
Cdd:PRK09288 213 DGGthfcapigHR--QEDGDYR----------ESWQ----------PQ-PMSPAALEEAQEIAKKVTDALG--GRGLfgV 267
|
170
....*....|....*..
gi 772685243 280 EFLVANNEFYFIEVNPR 296
Cdd:PRK09288 268 ELFVKGDEVYFSEVSPR 284
|
|
| RimK |
pfam08443 |
RimK-like ATP-grasp domain; This ATP-grasp domain is found in the ribosomal S6 modification ... |
120-312 |
1.81e-04 |
|
RimK-like ATP-grasp domain; This ATP-grasp domain is found in the ribosomal S6 modification enzyme RimK.
Pssm-ID: 369879 [Multi-domain] Cd Length: 188 Bit Score: 43.64 E-value: 1.81e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 772685243 120 DKVKAREQAEKAGI--PVIPGSDGPAETLEAVEQFGQtnGYPIIIKASLGGGGRGMRIVRSESEVKEAYERAkseakaaf 197
Cdd:pfam08443 3 DKAKSHQLLAKHGIgpPNTRLAWYPEDAEQFIEQIKR--QFPVIVKSIYGSQGIGVFLAEDEQKLRQTLSAT-------- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 772685243 198 gNDEVYVEKLIE--NPKHIEVQVIGDKQGNVVHLFERDCSVqRRHQKVIEVAPSVSLSPELRnqicEAAVALAKNVNYIN 275
Cdd:pfam08443 73 -NEQILVQEFIAeaNNEDIRCLVVGDQVVGALHRQSNEGDF-RSNLHRGGVGEKYQLSQEET----ELAIKAAQAMQLDV 146
|
170 180 190
....*....|....*....|....*....|....*..
gi 772685243 276 AGtVEFLVANNEFYFIEVNPRVQVEhtITEMITGVDI 312
Cdd:pfam08443 147 AG-VDLLRQKRGLLVCEVNSSPGLE--GIEKTLGINI 180
|
|
| LeuA |
COG0119 |
Isopropylmalate/homocitrate/citramalate synthases [Amino acid transport and metabolism]; ... |
687-768 |
2.17e-04 |
|
Isopropylmalate/homocitrate/citramalate synthases [Amino acid transport and metabolism]; Isopropylmalate/homocitrate/citramalate synthases is part of the Pathway/BioSystem: Isoleucine, leucine, valine biosynthesis
Pssm-ID: 439889 [Multi-domain] Cd Length: 452 Bit Score: 45.16 E-value: 2.17e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 772685243 687 TKYDLAYYTSMAKELEAAGAHILGIKDMAGLLKPQAAYELVSALKETI-DIPVHLHTHDTSG----NGIYmyakAVEAGV 761
Cdd:COG0119 143 TRTDPDFLLEVLEAAIEAGADRINLPDTVGGATPNEVADLIEELRERVpDVILSVHCHNDLGlavaNSLA----AVEAGA 218
|
....*..
gi 772685243 762 DIIDVAV 768
Cdd:COG0119 219 DQVEGTI 225
|
|
| PRK02186 |
PRK02186 |
argininosuccinate lyase; Provisional |
120-312 |
6.06e-04 |
|
argininosuccinate lyase; Provisional
Pssm-ID: 235010 [Multi-domain] Cd Length: 887 Bit Score: 44.07 E-value: 6.06e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 772685243 120 DKVKAREQAEKAGIPViPGSDGPAETLEaVEQFGQTNGYPIIIKASLGGGGRGMRIVRSESEVKEAYERAKSEAKAAFgn 199
Cdd:PRK02186 107 DKKRLARTLRDHGIDV-PRTHALALRAV-ALDALDGLTYPVVVKPRMGSGSVGVRLCASVAEAAAHCAALRRAGTRAA-- 182
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 772685243 200 devYVEKLIENPKHiEVQVIGDKQGNVV------HLFERDCSVQRRHqkvieVAPSVSLSPELRNQICEAAVALAKnVNY 273
Cdd:PRK02186 183 ---LVQAYVEGDEY-SVETLTVARGHQVlgitrkHLGPPPHFVEIGH-----DFPAPLSAPQRERIVRTVLRALDA-VGY 252
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 772685243 274 -INAGTVEFLVANNEFYFIEVNPR-------VQVEHtitemITGVDI 312
Cdd:PRK02186 253 aFGPAHTELRVRGDTVVIIEINPRlaggmipVLLEE-----AFGVDL 294
|
|
| HlyD_3 |
pfam13437 |
HlyD family secretion protein; This is a family of largely bacterial haemolysin translocator ... |
1116-1145 |
6.84e-04 |
|
HlyD family secretion protein; This is a family of largely bacterial haemolysin translocator HlyD proteins.
Pssm-ID: 433206 [Multi-domain] Cd Length: 104 Bit Score: 40.04 E-value: 6.84e-04
10 20 30
....*....|....*....|....*....|
gi 772685243 1116 TVQAPFSGTIKQVHVKNGEPIQTGDLLLEI 1145
Cdd:pfam13437 1 TIRAPVDGVVAELNVEEGQVVQAGDPLATI 30
|
|
| GCV_H |
pfam01597 |
Glycine cleavage H-protein; This is a family of glycine cleavage H-proteins, part of the ... |
1078-1131 |
8.82e-04 |
|
Glycine cleavage H-protein; This is a family of glycine cleavage H-proteins, part of the glycine cleavage multienzyme complex (GCV) found in bacteria and the mitochondria of eukaryotes. GCV catalyzes the catabolism of glycine in eukaryotes. A lipoyl group is attached to a completely conserved lysine residue. The H protein shuttles the methylamine group of glycine from the P protein to the T protein.
Pssm-ID: 396258 Cd Length: 122 Bit Score: 40.39 E-value: 8.82e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 772685243 1078 SHIAASMPGTVIKV-LTEAGTKVNKGDHLMINEAMKMETTVQAPFSGTIKQVHVK 1131
Cdd:pfam01597 23 TDFAQAQLGDIVFVeLPEVGTKVKKGESLAAIESVKAASPIYAPVSGEVVEVNEK 77
|
|
| DRE_TIM_HOA_like |
cd07944 |
4-hydroxy-2-oxovalerate aldolase-like, N-terminal catalytic TIM barrel domain; This family of ... |
626-771 |
9.63e-04 |
|
4-hydroxy-2-oxovalerate aldolase-like, N-terminal catalytic TIM barrel domain; This family of bacterial enzymes is sequence-similar to 4-hydroxy-2-oxovalerate aldolase (HOA) but its exact function is unknown. This family includes the Bacteroides vulgatus Bvu_2661 protein and belongs to the DRE-TIM metallolyase superfamily. DRE-TIM metallolyases include 2-isopropylmalate synthase (IPMS), alpha-isopropylmalate synthase (LeuA), 3-hydroxy-3-methylglutaryl-CoA lyase, homocitrate synthase, citramalate synthase, 4-hydroxy-2-oxovalerate aldolase, re-citrate synthase, transcarboxylase 5S, pyruvate carboxylase, AksA, and FrbC. These members all share a conserved triose-phosphate isomerase (TIM) barrel domain consisting of a core beta(8)-alpha(8) motif with the eight parallel beta strands forming an enclosed barrel surrounded by eight alpha helices. The domain has a catalytic center containing a divalent cation-binding site formed by a cluster of invariant residues that cap the core of the barrel. In addition, the catalytic site includes three invariant residues - an aspartate (D), an arginine (R), and a glutamate (E) - which is the basis for the domain name "DRE-TIM".
Pssm-ID: 163682 Cd Length: 266 Bit Score: 42.55 E-value: 9.63e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 772685243 626 PDNVIQEFVKQSAQSGIDVFRI-FDSLNWVKGMTLaIDAVRDTG-KVAEAAIcytgdildkNRTKYDLAYYTSMAKELEA 703
Cdd:cd07944 80 YGNDDIDLLEPASGSVVDMIRVaFHKHEFDEALPL-IKAIKEKGyEVFFNLM---------AISGYSDEELLELLELVNE 149
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 772685243 704 AGAHILGIKDMAGLLKPQAAYELVSALKE--TIDIPVHLHTHDTSGNGIYMYAKAVEAGVDIIDVAVSSM 771
Cdd:cd07944 150 IKPDVFYIVDSFGSMYPEDIKRIISLLRSnlDKDIKLGFHAHNNLQLALANTLEAIELGVEIIDATVYGM 219
|
|
| PRK11855 |
PRK11855 |
dihydrolipoamide acetyltransferase; Reviewed |
1086-1146 |
1.05e-03 |
|
dihydrolipoamide acetyltransferase; Reviewed
Pssm-ID: 237000 [Multi-domain] Cd Length: 547 Bit Score: 42.89 E-value: 1.05e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 772685243 1086 GTVIKVLTEAGTKVNKGDHLMINEAMKMETTVQAPFSGTIKQVHVKNGEPIQTGDLLLEIE 1146
Cdd:PRK11855 133 VEVIEWLVKVGDTVEEDQSLITVETDKATMEIPSPVAGVVKEIKVKVGDKVSVGSLLVVIE 193
|
|
| EmrA |
COG1566 |
Multidrug resistance efflux pump EmrA [Defense mechanisms]; |
1114-1146 |
1.44e-03 |
|
Multidrug resistance efflux pump EmrA [Defense mechanisms];
Pssm-ID: 441174 [Multi-domain] Cd Length: 331 Bit Score: 42.34 E-value: 1.44e-03
10 20 30
....*....|....*....|....*....|...
gi 772685243 1114 ETTVQAPFSGTIKQVHVKNGEPIQTGDLLLEIE 1146
Cdd:COG1566 45 VVTVAAKVSGRVTEVLVKEGDRVKKGQVLARLD 77
|
|
| sucC |
PRK00696 |
ADP-forming succinate--CoA ligase subunit beta; |
124-200 |
4.69e-03 |
|
ADP-forming succinate--CoA ligase subunit beta;
Pssm-ID: 234813 [Multi-domain] Cd Length: 388 Bit Score: 40.84 E-value: 4.69e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 772685243 124 AREQAEKAGIPVIPGsdGPAETL-EAVEQFGQTNGYPIIIKASLGGGGR----GMRIVRSESEVKEAyerakseAKAAFG 198
Cdd:PRK00696 8 AKELFAKYGVPVPRG--IVATTPeEAVEAAEELGGGVWVVKAQVHAGGRgkagGVKLAKSPEEAREF-------AKQILG 78
|
..
gi 772685243 199 ND 200
Cdd:PRK00696 79 MT 80
|
|
| AcrA |
COG0845 |
Multidrug efflux pump subunit AcrA (membrane-fusion protein) [Cell wall/membrane/envelope ... |
1114-1146 |
7.02e-03 |
|
Multidrug efflux pump subunit AcrA (membrane-fusion protein) [Cell wall/membrane/envelope biogenesis, Defense mechanisms];
Pssm-ID: 440606 [Multi-domain] Cd Length: 324 Bit Score: 39.93 E-value: 7.02e-03
10 20 30
....*....|....*....|....*....|...
gi 772685243 1114 ETTVQAPFSGTIKQVHVKNGEPIQTGDLLLEIE 1146
Cdd:COG0845 23 EVEVRARVSGRVEEVLVDEGDRVKKGQVLARLD 55
|
|
| biotinyl_domain |
cd06850 |
The biotinyl-domain or biotin carboxyl carrier protein (BCCP) domain is present in all ... |
1116-1146 |
8.82e-03 |
|
The biotinyl-domain or biotin carboxyl carrier protein (BCCP) domain is present in all biotin-dependent enzymes, such as acetyl-CoA carboxylase, pyruvate carboxylase, propionyl-CoA carboxylase, methylcrotonyl-CoA carboxylase, geranyl-CoA carboxylase, oxaloacetate decarboxylase, methylmalonyl-CoA decarboxylase, transcarboxylase and urea amidolyase. This domain functions in transferring CO2 from one subsite to another, allowing carboxylation, decarboxylation, or transcarboxylation. During this process, biotin is covalently attached to a specific lysine.
Pssm-ID: 133459 [Multi-domain] Cd Length: 67 Bit Score: 35.85 E-value: 8.82e-03
10 20 30
....*....|....*....|....*....|.
gi 772685243 1116 TVQAPFSGTIKQVHVKNGEPIQTGDLLLEIE 1146
Cdd:cd06850 1 EVTAPMPGTVVKVLVKEGDKVEAGQPLAVLE 31
|
|
| |
