|
Name |
Accession |
Description |
Interval |
E-value |
| PccA |
COG4770 |
Acetyl/propionyl-CoA carboxylase, alpha subunit [Lipid transport and metabolism]; |
1-395 |
0e+00 |
|
Acetyl/propionyl-CoA carboxylase, alpha subunit [Lipid transport and metabolism];
Pssm-ID: 443802 [Multi-domain] Cd Length: 466 Bit Score: 713.33 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533372 1 MEKIIQVAKTSAAQAIHPGCGFLSENMEFAELCKQEGIIFIGPPPSAIRDMGIKSTSKSIMAAAGVPVVEGYHGEDQSDQ 80
Cdd:COG4770 63 IDAIIAAAKATGADAIHPGYGFLSENADFAEACEDAGIVFIGPSPEAIRAMGDKIAAKKLMKAAGVPVVPGSDGPVQDAE 142
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533372 81 CLKEHARRIGYPVMIKAVRGGGGKGMRIVRSEQEFQEQLESARREAKKSFNDDAMLIEKFVDTPRHVEVQVFGDHHGNAV 160
Cdd:COG4770 143 EALAIAEEIGYPVLIKASAGGGGKGMRVVRSEEELEEAFESARREAKAAFGDDRVYLEKYIERPRHIEVQVLADKHGNVV 222
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533372 161 YLFERDCSVQRRHQKIIEEAPAPGIKSEVRKKLGEAAVRAAKAVNYVGAGTVEFIMDSKHNFCFMEMNTRLQVEHPVTEM 240
Cdd:COG4770 223 HLGERDCSIQRRHQKVIEEAPSPALTEELRERMGEAAVRAAKAVGYVGAGTVEFLVDADGNFYFLEMNTRLQVEHPVTEM 302
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533372 241 ITGTDLVEWQLRIAAGEKIPLSQEEITLQGHAFEARIYAEDPSNNFMPVAGPLVHLSTPrADPSTRIETGVRQGDEVSVH 320
Cdd:COG4770 303 VTGIDLVEEQIRIAAGEPLPFTQEDIKLRGHAIECRINAEDPARGFLPSPGTITRLRPP-GGPGVRVDSGVYEGYEIPPY 381
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1394533372 321 YDPMIAKLVVWAADRQAALTKLRYSLRQYNIVGLHTNIDFLLNLSGHPEFEAGNVHTDFIPQHHKQLLLSRKAAA 395
Cdd:COG4770 382 YDSMIAKLIVWGPDREEAIARMRRALAEFVIEGVKTNIPFLRALLAHPDFRAGDVDTGFIERELAELLAAAAPEE 456
|
|
| PRK08591 |
PRK08591 |
acetyl-CoA carboxylase biotin carboxylase subunit; Validated |
1-383 |
0e+00 |
|
acetyl-CoA carboxylase biotin carboxylase subunit; Validated
Pssm-ID: 236307 [Multi-domain] Cd Length: 451 Bit Score: 564.81 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533372 1 MEKIIQVAKTSAAQAIHPGCGFLSENMEFAELCKQEGIIFIGPPPSAIRDMGIKSTSKSIMAAAGVPVVEGYHGEDQSDQ 80
Cdd:PRK08591 63 IPAIISAAEITGADAIHPGYGFLSENADFAEICEDSGFTFIGPSAETIRLMGDKVTAKATMKKAGVPVVPGSDGPVDDEE 142
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533372 81 CLKEHARRIGYPVMIKAVRGGGGKGMRIVRSEQEFQEQLESARREAKKSFNDDAMLIEKFVDTPRHVEVQVFGDHHGNAV 160
Cdd:PRK08591 143 EALAIAKEIGYPVIIKATAGGGGRGMRVVRTEAELEKAFSMARAEAKAAFGNPGVYMEKYLENPRHIEIQVLADGHGNAI 222
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533372 161 YLFERDCSVQRRHQKIIEEAPAPGIKSEVRKKLGEAAVRAAKAVNYVGAGTVEFIMDSKHNFCFMEMNTRLQVEHPVTEM 240
Cdd:PRK08591 223 HLGERDCSLQRRHQKVLEEAPSPAITEELRRKIGEAAVKAAKAIGYRGAGTIEFLYEKNGEFYFIEMNTRIQVEHPVTEM 302
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533372 241 ITGTDLVEWQLRIAAGEKIPLSQEEITLQGHAFEARIYAEDPSNNFMPVAGPLVHLSTPrADPSTRIETGVRQGDEVSVH 320
Cdd:PRK08591 303 ITGVDLVKEQIRIAAGEPLSIKQEDIVFRGHAIECRINAEDPAKNFMPSPGKITRYHPP-GGPGVRVDSAVYTGYTIPPY 381
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1394533372 321 YDPMIAKLVVWAADRQAALTKLRYSLRQYNIVGLHTNIDFLLNLSGHPEFEAGNVHTDFIPQH 383
Cdd:PRK08591 382 YDSMIGKLIVHGETREEAIARMKRALSEFVIDGIKTTIPLHLRLLNDPNFQAGDYNIHYLEKK 444
|
|
| PRK06111 |
PRK06111 |
acetyl-CoA carboxylase biotin carboxylase subunit; Validated |
2-386 |
0e+00 |
|
acetyl-CoA carboxylase biotin carboxylase subunit; Validated
Pssm-ID: 180406 [Multi-domain] Cd Length: 450 Bit Score: 535.38 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533372 2 EKIIQVAKTSAAQAIHPGCGFLSENMEFAELCKQEGIIFIGPPPSAIRDMGIKSTSKSIMAAAGVPVVEGYHGEDQSDQC 81
Cdd:PRK06111 64 EKIIEIAKKTGAEAIHPGYGLLSENASFAERCKEEGIVFIGPSADIIAKMGSKIEARRAMQAAGVPVVPGITTNLEDAEE 143
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533372 82 LKEHARRIGYPVMIKAVRGGGGKGMRIVRSEQEFQEQLESARREAKKSFNDDAMLIEKFVDTPRHVEVQVFGDHHGNAVY 161
Cdd:PRK06111 144 AIAIARQIGYPVMLKASAGGGGIGMQLVETEQELTKAFESNKKRAANFFGNGEMYIEKYIEDPRHIEIQLLADTHGNTVY 223
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533372 162 LFERDCSVQRRHQKIIEEAPAPGIKSEVRKKLGEAAVRAAKAVNYVGAGTVEFIMDSKHNFCFMEMNTRLQVEHPVTEMI 241
Cdd:PRK06111 224 LWERECSVQRRHQKVIEEAPSPFLDEETRKAMGERAVQAAKAIGYTNAGTIEFLVDEQKNFYFLEMNTRLQVEHPVTEEI 303
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533372 242 TGTDLVEWQLRIAAGEKIPLSQEEITLQGHAFEARIYAEDPsNNFMPVAGPLVHLSTPRAdPSTRIETGVRQGDEVSVHY 321
Cdd:PRK06111 304 TGIDLVEQQLRIAAGEKLSFTQDDIKRSGHAIEVRIYAEDP-KTFFPSPGKITDLTLPGG-EGVRHDHAVENGVTVTPFY 381
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1394533372 322 DPMIAKLVVWAADRQAALTKLRYSLRQYNIVGLHTNIDFLLNLSGHPEFEAGNVHTDFIPQHHKQ 386
Cdd:PRK06111 382 DPMIAKLIAHGETREEAISRLHDALEELKVEGIKTNIPLLLQVLEDPVFKAGGYTTGFLTKQLVK 446
|
|
| PycA |
COG1038 |
Pyruvate carboxylase [Energy production and conversion]; Pyruvate carboxylase is part of the ... |
1-383 |
2.64e-177 |
|
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: 533.12 E-value: 2.64e-177
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533372 1 MEKIIQVAKTSAAQAIHPGCGFLSENMEFAELCKQEGIIFIGPPPSAIRDMGIKSTSKSIMAAAGVPVVEGYHGEDQSDQ 80
Cdd:COG1038 66 IEEIIRVAKEKGVDAIHPGYGFLSENPEFARACEEAGITFIGPSPEVLEMLGDKVAARAAAIEAGVPVIPGTEGPVDDLE 145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533372 81 CLKEHARRIGYPVMIKAVRGGGGKGMRIVRSEQEFQEQLESARREAKKSFNDDAMLIEKFVDTPRHVEVQVFGDHHGNAV 160
Cdd:COG1038 146 EALAFAEEIGYPVMLKAAAGGGGRGMRVVRSEEELEEAFESARREAKAAFGDDEVFLEKYIERPKHIEVQILGDKHGNIV 225
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533372 161 YLFERDCSVQRRHQKIIEEAPAPGIKSEVRKKLGEAAVRAAKAVNYVGAGTVEFIMDSKHNFCFMEMNTRLQVEHPVTEM 240
Cdd:COG1038 226 HLFERDCSVQRRHQKVVEIAPAPNLDEELREAICEAAVKLAKAVGYVNAGTVEFLVDDDGNFYFIEVNPRIQVEHTVTEE 305
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533372 241 ITGTDLVEWQLRIAAGEK-------IPlSQEEITLQGHAFEARIYAEDPSNNFMPVAGplvhlstpradpstRIET---- 309
Cdd:COG1038 306 VTGIDIVQSQILIAEGYSlddpeigIP-SQEDIRLNGYAIQCRITTEDPANNFMPDTG--------------RITAyrsa 370
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533372 310 ---GVR-------QGDEVSVHYDPMIAKLVVWAADRQAALTKLRYSLRQYNIVGLHTNIDFLLNLSGHPEFEAGNVHTDF 379
Cdd:COG1038 371 ggfGIRldggnayTGAVITPYYDSLLVKVTAWGRTFEEAIRKMRRALREFRIRGVKTNIPFLENVLNHPDFLAGECTTSF 450
|
....
gi 1394533372 380 IPQH 383
Cdd:COG1038 451 IDET 454
|
|
| PRK08654 |
PRK08654 |
acetyl-CoA carboxylase biotin carboxylase subunit; |
1-385 |
2.22e-176 |
|
acetyl-CoA carboxylase biotin carboxylase subunit;
Pssm-ID: 236325 [Multi-domain] Cd Length: 499 Bit Score: 509.53 E-value: 2.22e-176
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533372 1 MEKIIQVAKTSAAQAIHPGCGFLSENMEFAELCKQEGIIFIGPPPSAIRDMGIKSTSKSIMAAAGVPVVEGYHGEDQSDQ 80
Cdd:PRK08654 63 IERIIDVAKKAGADAIHPGYGFLAENPEFAKACEKAGIVFIGPSSDVIEAMGSKINAKKLMKKAGVPVLPGTEEGIEDIE 142
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533372 81 CLKEHARRIGYPVMIKAVRGGGGKGMRIVRSEQEFQEQLESARREAKKSFNDDAMLIEKFVDTPRHVEVQVFGDHHGNAV 160
Cdd:PRK08654 143 EAKEIAEEIGYPVIIKASAGGGGIGMRVVYSEEELEDAIESTQSIAQSAFGDSTVFIEKYLEKPRHIEIQILADKHGNVI 222
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533372 161 YLFERDCSVQRRHQKIIEEAPAPGIKSEVRKKLGEAAVRAAKAVNYVGAGTVEFIMdSKHNFCFMEMNTRLQVEHPVTEM 240
Cdd:PRK08654 223 HLGDRECSIQRRHQKLIEEAPSPIMTPELRERMGEAAVKAAKAINYENAGTVEFLY-SNGNFYFLEMNTRLQVEHPITEM 301
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533372 241 ITGTDLVEWQLRIAAGEKIPLSQEEITLQGHAFEARIYAEDPSNNFMPVAGPLVHLSTPrADPSTRIETGVRQGDEVSVH 320
Cdd:PRK08654 302 VTGIDIVKEQIKIAAGEELSFKQEDITIRGHAIECRINAEDPLNDFAPSPGKIKRYRSP-GGPGVRVDSGVHMGYEIPPY 380
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1394533372 321 YDPMIAKLVVWAADRQAALTKLRYSLRQYNIVGLHTNIDFLLNLSGHPEFEAGNVHTDFIPQHHK 385
Cdd:PRK08654 381 YDSMISKLIVWGRTREEAIARMRRALYEYVIVGVKTNIPFHKAVMENENFVRGNLHTHFIEEETT 445
|
|
| PRK12999 |
PRK12999 |
pyruvate carboxylase; Reviewed |
1-394 |
5.62e-171 |
|
pyruvate carboxylase; Reviewed
Pssm-ID: 237263 [Multi-domain] Cd Length: 1146 Bit Score: 517.00 E-value: 5.62e-171
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533372 1 MEKIIQVAKTSAAQAIHPGCGFLSENMEFAELCKQEGIIFIGPPPSAIRDMGIKSTSKSIMAAAGVPVVEGYHGEDQSDQ 80
Cdd:PRK12999 67 IDEIIRVAKQAGVDAIHPGYGFLSENPEFARACAEAGITFIGPTAEVLRLLGDKVAARNAAIKAGVPVIPGSEGPIDDIE 146
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533372 81 CLKEHARRIGYPVMIKAVRGGGGKGMRIVRSEQEFQEQLESARREAKKSFNDDAMLIEKFVDTPRHVEVQVFGDHHGNAV 160
Cdd:PRK12999 147 EALEFAEEIGYPIMLKASAGGGGRGMRIVRSEEELEEAFERAKREAKAAFGNDEVYLEKYVENPRHIEVQILGDKHGNVV 226
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533372 161 YLFERDCSVQRRHQKIIEEAPAPGIKSEVRKKLGEAAVRAAKAVNYVGAGTVEFIMDSKHNFCFMEMNTRLQVEHPVTEM 240
Cdd:PRK12999 227 HLYERDCSVQRRHQKVVEIAPAPGLSEELRERICEAAVKLARAVGYVNAGTVEFLVDADGNFYFIEVNPRIQVEHTVTEE 306
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533372 241 ITGTDLVEWQLRIAAGEKI------PLSQEEITLQGHAFEARIYAEDPSNNFMPVAGplvhlstpradpstRIET----- 309
Cdd:PRK12999 307 VTGIDIVQSQILIAEGATLhdleigIPSQEDIRLRGYAIQCRITTEDPANNFMPDTG--------------RITAyrspg 372
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533372 310 --GVR-------QGDEVSVHYDPMIAKLVVWAADRQAALTKLRYSLRQYNIVGLHTNIDFLLNLSGHPEFEAGNVHTDFI 380
Cdd:PRK12999 373 gfGVRldggnafAGAEITPYYDSLLVKLTAWGRTFEQAVARMRRALREFRIRGVKTNIPFLENVLKHPDFRAGDYTTSFI 452
|
410
....*....|....
gi 1394533372 381 PQhHKQLLLSRKAA 394
Cdd:PRK12999 453 DE-TPELFDFPKRR 465
|
|
| PRK05586 |
PRK05586 |
acetyl-CoA carboxylase biotin carboxylase subunit; |
1-385 |
6.95e-167 |
|
acetyl-CoA carboxylase biotin carboxylase subunit;
Pssm-ID: 180150 [Multi-domain] Cd Length: 447 Bit Score: 483.45 E-value: 6.95e-167
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533372 1 MEKIIQVAKTSAAQAIHPGCGFLSENMEFAELCKQEGIIFIGPPPSAIRDMGIKSTSKSIMAAAGVPVVEGYHGEDQSDQ 80
Cdd:PRK05586 63 IQNIISATVLTGAQAIHPGFGFLSENSKFAKMCKECNIVFIGPDSETIELMGNKSNAREIMIKAGVPVVPGSEGEIENEE 142
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533372 81 CLKEHARRIGYPVMIKAVRGGGGKGMRIVRSEQEFQEQLESARREAKKSFNDDAMLIEKFVDTPRHVEVQVFGDHHGNAV 160
Cdd:PRK05586 143 EALEIAKEIGYPVMVKASAGGGGRGIRIVRSEEELIKAFNTAKSEAKAAFGDDSMYIEKFIENPKHIEFQILGDNYGNVV 222
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533372 161 YLFERDCSVQRRHQKIIEEAPAPGIKSEVRKKLGEAAVRAAKAVNYVGAGTVEFIMDSKHNFCFMEMNTRLQVEHPVTEM 240
Cdd:PRK05586 223 HLGERDCSLQRRNQKVLEEAPSPVMTEELRKKMGEIAVKAAKAVNYKNAGTIEFLLDKDGNFYFMEMNTRIQVEHPITEM 302
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533372 241 ITGTDLVEWQLRIAAGEKIPLSQEEITLQGHAFEARIYAEDPSNNFMPVAGPLVHLSTPrADPSTRIETGVRQGDEVSVH 320
Cdd:PRK05586 303 ITGVDLVKEQIKIAYGEKLSIKQEDIKINGHSIECRINAEDPKNGFMPCPGKIEELYIP-GGLGVRVDSAVYSGYTIPPY 381
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1394533372 321 YDPMIAKLVVWAADRQAALTKLRYSLRQYNIVGLHTNIDFLLNLSGHPEFEAGNVHTDFIPQHHK 385
Cdd:PRK05586 382 YDSMIGKLIVYGKDREEAIQKMKRALGEFIIEGVNTNIDFQFIILEDEEFIKGTYDTSFIEKKLV 446
|
|
| accC |
TIGR00514 |
acetyl-CoA carboxylase, biotin carboxylase subunit; This model represents the biotin ... |
4-383 |
1.39e-164 |
|
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: 477.72 E-value: 1.39e-164
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533372 4 IIQVAKTSAAQAIHPGCGFLSENMEFAELCKQEGIIFIGPPPSAIRDMGIKSTSKSIMAAAGVPVVEGYHGEDQSDQCLK 83
Cdd:TIGR00514 66 IISAAEITGADAIHPGYGFLSENANFAEQCERSGFTFIGPSAESIRLMGDKVSAIETMKKAGVPCVPGSDGLVEDEEENV 145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533372 84 EHARRIGYPVMIKAVRGGGGKGMRIVRSEQEFQEQLESARREAKKSFNDDAMLIEKFVDTPRHVEVQVFGDHHGNAVYLF 163
Cdd:TIGR00514 146 RIAKRIGYPVIIKATAGGGGRGMRVVREPDELVKSISMTRAEAKAAFGNDGVYIEKYIENPRHVEIQVLADKYGNAIYLG 225
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533372 164 ERDCSVQRRHQKIIEEAPAPGIKSEVRKKLGEAAVRAAKAVNYVGAGTVEFIMDSKHNFCFMEMNTRLQVEHPVTEMITG 243
Cdd:TIGR00514 226 ERDCSIQRRHQKLLEEAPSPALTPELRRKMGDAAVKAAVSIGYRGAGTVEFLLDKNGEFYFMEMNTRIQVEHPVTEMITG 305
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533372 244 TDLVEWQLRIAAGEKIPLSQEEITLQGHAFEARIYAEDPSNNFMPVAGPLVHLSTPrADPSTRIETGVRQGDEVSVHYDP 323
Cdd:TIGR00514 306 VDLIKEQIRIAAGEPLSLKQEDVVVRGHAIECRINAEDPIKTFLPSPGRITRYLPP-GGPGVRWDSHVYSGYTVPPYYDS 384
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533372 324 MIAKLVVWAADRQAALTKLRYSLRQYNIVGLHTNIDFLLNLSGHPEFEAGNVHTDFIPQH 383
Cdd:TIGR00514 385 MIGKLITYGKTREVAIARMKRALSEFIIDGIKTTIPFHQRILEDENFQHGGTNIHYLEKK 444
|
|
| urea_carbox |
TIGR02712 |
urea carboxylase; Members of this family are ATP-dependent urea carboxylase, including ... |
1-380 |
5.01e-157 |
|
urea carboxylase; Members of this family are ATP-dependent urea carboxylase, including characterized members from Oleomonas sagaranensis (alpha class Proteobacterium) and yeasts such as Saccharomyces cerevisiae. The allophanate hydrolase domain of the yeast enzyme is not included in this model and is represented by an adjacent gene in Oleomonas sagaranensis. The fusion of urea carboxylase and allophanate hydrolase is designated urea amidolyase. The enzyme from Oleomonas sagaranensis was shown to be highly active on acetamide and formamide as well as urea. [Central intermediary metabolism, Nitrogen metabolism]
Pssm-ID: 274264 [Multi-domain] Cd Length: 1201 Bit Score: 481.84 E-value: 5.01e-157
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533372 1 MEKIIQVAKTSAAQAIHPGCGFLSENMEFAELCKQEGIIFIGPPPSAIRDMGIKSTSKSIMAAAGVPVVEGyHGEDQSDQ 80
Cdd:TIGR02712 62 IDKILAAAKKTGAQAIHPGYGFLSENAAFAEACEAAGIVFVGPTPEQIRKFGLKHTARELAEAAGVPLLPG-TGLLSSLD 140
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533372 81 CLKEHARRIGYPVMIKAVRGGGGKGMRIVRSEQEFQEQLESARREAKKSFNDDAMLIEKFVDTPRHVEVQVFGDHHGNAV 160
Cdd:TIGR02712 141 EALEAAKEIGYPVMLKSTAGGGGIGMQKCDSAAELAEAFETVKRLGESFFGDAGVFLERFVENARHVEVQIFGDGKGKVV 220
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533372 161 YLFERDCSVQRRHQKIIEEAPAPGIKSEVRKKLGEAAVRAAKAVNYVGAGTVEFIMDSKHN-FCFMEMNTRLQVEHPVTE 239
Cdd:TIGR02712 221 ALGERDCSLQRRNQKVVEETPAPNLPPETRQALLAAAERLGEAVNYRSAGTVEFIYDEARDeFYFLEVNTRLQVEHPVTE 300
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533372 240 MITGTDLVEWQLRIAAGEKIPLSQ--EEITLQGHAFEARIYAEDPSNNFMPVAGPLVHLSTPRAdpsTRIETGVRQGDEV 317
Cdd:TIGR02712 301 MVTGLDLVEWMIRIAAGELPDFASlnISLTPRGAAIEARVYAENPAKNFQPSPGLLTDVQFPDD---VRVDTWVETGTEV 377
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1394533372 318 SVHYDPMIAKLVVWAADRQAALTKLRYSLRQYNIVGLHTNIDFLLNLSGHPEFEAGNVHTDFI 380
Cdd:TIGR02712 378 SPEYDPMLAKIIVHGSDREDAILKLHQALAETRVYGIETNLDYLRSILSSETFRSAQVSTRTL 440
|
|
| PRK07178 |
PRK07178 |
acetyl-CoA carboxylase biotin carboxylase subunit; |
3-392 |
1.12e-149 |
|
acetyl-CoA carboxylase biotin carboxylase subunit;
Pssm-ID: 180865 [Multi-domain] Cd Length: 472 Bit Score: 440.31 E-value: 1.12e-149
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533372 3 KIIQVAKTSAAQAIHPGCGFLSENMEFAELCKQEGIIFIGPPPSAIRDMGIKSTSKSIMAAAGVPVVEGYHGEDQS-DQC 81
Cdd:PRK07178 64 RLVNLAVETGCDALHPGYGFLSENAELAEICAERGIKFIGPSAEVIRRMGDKTEARRAMIKAGVPVTPGSEGNLADlDEA 143
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533372 82 LKEhARRIGYPVMIKAVRGGGGKGMRIVRSEQEFQEQLESARREAKKSFNDDAMLIEKFVDTPRHVEVQVFGDHHGNAVY 161
Cdd:PRK07178 144 LAE-AERIGYPVMLKATSGGGGRGIRRCNSREELEQNFPRVISEATKAFGSAEVFLEKCIVNPKHIEVQILADSHGNVVH 222
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533372 162 LFERDCSVQRRHQKIIEEAPAPGIKSEVRKKLGEAAVRAAKAVNYVGAGTVEFIMDSKHNFCFMEMNTRLQVEHPVTEMI 241
Cdd:PRK07178 223 LFERDCSIQRRNQKLIEIAPSPQLTPEQRAYIGDLAVRAAKAVGYENAGTVEFLLDADGEVYFMEMNTRVQVEHTITEEI 302
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533372 242 TGTDLVEWQLRIAAGEKIPLSQEEITLQGHAFEARIYAEDPSNNFMPVAGPLVHLSTPrADPSTRIETGVRQGDEVSVHY 321
Cdd:PRK07178 303 TGIDIVREQIRIASGLPLSYKQEDIQHRGFALQFRINAEDPKNDFLPSFGKITRYYAP-GGPGVRTDTAIYTGYTIPPYY 381
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1394533372 322 DPMIAKLVVWAADRQAALTKLRYSLRQYNIVGLHTNIDFLLNLSGHPEFEAGNVHTDFIPQHHKQLLLSRK 392
Cdd:PRK07178 382 DSMCAKLIVWALTWEEALDRGRRALDDMRVQGVKTTIPYYQEILRNPEFRSGQFNTSFVESHPELTNYSIK 452
|
|
| PRK08462 |
PRK08462 |
acetyl-CoA carboxylase biotin carboxylase subunit; |
4-383 |
2.45e-147 |
|
acetyl-CoA carboxylase biotin carboxylase subunit;
Pssm-ID: 236269 [Multi-domain] Cd Length: 445 Bit Score: 433.40 E-value: 2.45e-147
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533372 4 IIQVAKTSAAQAIHPGCGFLSENMEFAELCKQEGIIFIGPPPSAIRDMGIKSTSKSIMAAAGVPVVEGYHGEDQSDQCLK 83
Cdd:PRK08462 68 IISAAEIFEADAIFPGYGFLSENQNFVEICSHHNIKFIGPSVEVMALMSDKSKAKEVMKRAGVPVIPGSDGALKSYEEAK 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533372 84 EHARRIGYPVMIKAVRGGGGKGMRIVRSEQEFQEQLESARREAKKSFNDDAMLIEKFVDTPRHVEVQVFGDHHGNAVYLF 163
Cdd:PRK08462 148 KIAKEIGYPVILKAAAGGGGRGMRVVEDESDLENLYLAAESEALSAFGDGTMYMEKFINNPRHIEVQILGDKHGNVIHVG 227
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533372 164 ERDCSVQRRHQKIIEEAPAPGIKSEVRKKLGEAAVRAAKAVNYVGAGTVEFIMDSKHNFCFMEMNTRLQVEHPVTEMITG 243
Cdd:PRK08462 228 ERDCSLQRRHQKLIEESPAVVLDEKTRERLHETAIKAAKAIGYEGAGTFEFLLDSNLDFYFMEMNTRLQVEHTVSEMVSG 307
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533372 244 TDLVEWQLRIAAGEKIPlSQEEITLQGHAFEARIYAEDPsNNFMPVAGPLVHLSTPrADPSTRIETGVRQGDEVSVHYDP 323
Cdd:PRK08462 308 LDLIEWMIKIAEGEELP-SQESIKLKGHAIECRITAEDP-KKFYPSPGKITKWIAP-GGRNVRMDSHAYAGYVVPPYYDS 384
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533372 324 MIAKLVVWAADRQAALTKLRYSLRQYNIVGLHTNIDFLLNLSGHPEFEAGNVHTDFIPQH 383
Cdd:PRK08462 385 MIGKLIVWGEDRNRAIAKMKRALKEFKVEGIKTTIPFHLEMMENADFINNKYDTKYLEEH 444
|
|
| PRK12833 |
PRK12833 |
acetyl-CoA carboxylase biotin carboxylase subunit; Provisional |
2-380 |
4.09e-143 |
|
acetyl-CoA carboxylase biotin carboxylase subunit; Provisional
Pssm-ID: 183781 [Multi-domain] Cd Length: 467 Bit Score: 423.40 E-value: 4.09e-143
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533372 2 EKIIQVAKTSAAQAIHPGCGFLSENMEFAELCKQEGIIFIGPPPSAIRDMGIKSTSKSIMAAAGVPVVEGYHGEDQSDQC 81
Cdd:PRK12833 67 AAILAAARQCGADAIHPGYGFLSENAAFAEAVEAAGLIFVGPDAQTIRTMGDKARARRTARRAGVPTVPGSDGVVASLDA 146
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533372 82 LKEHARRIGYPVMIKAVRGGGGKGMRIVRSEQEFQEQLESARREAKKSFNDDAMLIEKFVDTPRHVEVQVFGDHHgNAVY 161
Cdd:PRK12833 147 ALEVAARIGYPLMIKAAAGGGGRGIRVAHDAAQLAAELPLAQREAQAAFGDGGVYLERFIARARHIEVQILGDGE-RVVH 225
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533372 162 LFERDCSVQRRHQKIIEEAPAPGIKSEVRKKLGEAAVRAAKAVNYVGAGTVEFIMD-SKHNFCFMEMNTRLQVEHPVTEM 240
Cdd:PRK12833 226 LFERECSLQRRRQKILEEAPSPSLTPAQRDALCASAVRLARQVGYRGAGTLEYLFDdARGEFYFIEMNTRIQVEHPVTEA 305
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533372 241 ITGTDLVEWQLRIAAGEKIPLSQEEITLQGHAFEARIYAEDPSNNFMPVAGPLVHLSTPRAdPSTRIETGVRQGDEVSVH 320
Cdd:PRK12833 306 ITGIDLVQEMLRIADGEPLRFAQGDIALRGAALECRINAEDPLRDFFPNPGRIDALVWPQG-PGVRVDSLLYPGYRVPPF 384
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533372 321 YDPMIAKLVVWAADRQAALTKLRYSLRQYNIVGLHTNIDFLLNLSGHPEFEAGNVHTDFI 380
Cdd:PRK12833 385 YDSLLAKLIVHGEDRAAALARAARALRELRIDGMKTTAPLHRALLADADVRAGRFHTNFL 444
|
|
| PRK08463 |
PRK08463 |
acetyl-CoA carboxylase subunit A; Validated |
2-388 |
6.54e-141 |
|
acetyl-CoA carboxylase subunit A; Validated
Pssm-ID: 169452 [Multi-domain] Cd Length: 478 Bit Score: 418.06 E-value: 6.54e-141
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533372 2 EKIIQVAKTSAAQAIHPGCGFLSENMEFAELCKQEGIIFIGPPPSAIRDMGIKSTSKSIMAAAGVPVVEGYHG-EDQSDQ 80
Cdd:PRK08463 63 KRIVEIAKACGADAIHPGYGFLSENYEFAKAVEDAGIIFIGPKSEVIRKMGNKNIARYLMKKNGIPIVPGTEKlNSESME 142
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533372 81 CLKEHARRIGYPVMIKAVRGGGGKGMRIVRSEQEFQEQLESARREAKKSFNDDAMLIEKFVDTPRHVEVQVFGDHHGNAV 160
Cdd:PRK08463 143 EIKIFARKIGYPVILKASGGGGGRGIRVVHKEEDLENAFESCKREALAYFNNDEVFMEKYVVNPRHIEFQILGDNYGNII 222
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533372 161 YLFERDCSVQRRHQKIIEEAPAPGIKSEVRKKLGEAAVRAAKAVNYVGAGTVEFIMDSKHNFCFMEMNTRLQVEHPVTEM 240
Cdd:PRK08463 223 HLCERDCSIQRRHQKVIEIAPCPSISDNLRKTMGVTAVAAAKAVGYTNAGTIEFLLDDYNRFYFMEMNTRIQVEHGVTEE 302
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533372 241 ITGTDLVEWQLRIAAGEKIPLSQEEITLQGHAFEARIYAEDPSNNFMPVAGPLVHLsTPRADPSTRIETGVRQGDEVSVH 320
Cdd:PRK08463 303 ITGIDLIVRQIRIAAGEILDLEQSDIKPRGFAIEARITAENVWKNFIPSPGKITEY-YPALGPSVRVDSHIYKDYTIPPY 381
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1394533372 321 YDPMIAKLVVWAADRQAALTKLRYSLRQYNIVGLHTNIDFLLNLSGHPEFEAGNVHTDFIPQHHKQLL 388
Cdd:PRK08463 382 YDSMLAKLIVKATSYDLAVNKLERALKEFVIDGIRTTIPFLIAITKTREFRRGYFDTSYIETHMQELL 449
|
|
| pyruv_carbox |
TIGR01235 |
pyruvate carboxylase; This enzyme plays a role in gluconeogensis but not glycolysis. [Energy ... |
1-383 |
1.48e-137 |
|
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: 429.63 E-value: 1.48e-137
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533372 1 MEKIIQVAKTSAAQAIHPGCGFLSENMEFAELCKQEGIIFIGPPPSAIRDMGIKSTSKSIMAAAGVPVVEGYHGEDQSDQ 80
Cdd:TIGR01235 63 IDEIIRVAKLNGVDAIHPGYGFLSENSEFADACNKAGIIFIGPKAEVMDQLGDKVAARNLAIKAGVPVVPGTDGPPETME 142
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533372 81 CLKEHARRIGYPVMIKAVRGGGGKGMRIVRSEQEFQEQLESARREAKKSFNDDAMLIEKFVDTPRHVEVQVFGDHHGNAV 160
Cdd:TIGR01235 143 EVLDFAAAIGYPVIIKASWGGGGRGMRVVRSEADVADAFQRAKSEAKAAFGNDEVYVEKLIERPRHIEVQLLGDKHGNVV 222
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533372 161 YLFERDCSVQRRHQKIIEEAPAPGIKSEVRKKLGEAAVRAAKAVNYVGAGTVEFIMDSKHNFCFMEMNTRLQVEHPVTEM 240
Cdd:TIGR01235 223 HLFERDCSVQRRHQKVVEVAPAPYLSREVRDEIAEYAVKLAKAVNYINAGTVEFLVDNDGKFYFIEVNPRIQVEHTVTEE 302
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533372 241 ITGTDLVEWQLRIAAGEKIPL------SQEEITLQGHAFEARIYAEDPSNNFMPVAGPLVHLSTPRADpSTRIETGVR-Q 313
Cdd:TIGR01235 303 ITGIDIVQAQIHIADGASLPTpqlgvpNQEDIRTNGYAIQCRVTTEDPANNFQPDTGRIEAYRSAGGF-GIRLDGGNSyA 381
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533372 314 GDEVSVHYDPMIAKLVVWAADRQAALTKLRYSLRQYNIVGLHTNIDFLLNLSGHPEFEAGNVHTDFIPQH 383
Cdd:TIGR01235 382 GAIITPYYDSLLVKVSAWASTPEEAAAKMDRALREFRIRGVKTNIPFLENVLGHPKFLDGSYDTRFIDTT 451
|
|
| CPSase_L_D2 |
pfam02786 |
Carbamoyl-phosphate synthase L chain, ATP binding domain; Carbamoyl-phosphate synthase ... |
54-260 |
3.91e-90 |
|
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: 277.65 E-value: 3.91e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533372 54 KSTSKSIMAAAGVPVVEGYHGEDQSDQCLKEHARRIGYPVMIKAVRGGGGKGMRIVRSEQEFQEQLESARREAKKSFNDD 133
Cdd:pfam02786 2 KVLFKAAMKEAGVPTVPGTAGPVETEEEALAAAKEIGYPVIIKAAFGGGGLGMGIARNEEELAELFALALAEAPAAFGNP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533372 134 AMLIEKFVDTPRHVEVQVFGDHHGNAVYLFERDCSVQRRHQKIIEEAPAPGIKSEVRKKLGEAAVRAAKAVNYVGAGTVE 213
Cdd:pfam02786 82 QVLVEKSLKGPKHIEYQVLRDAHGNCITVCNRECSDQRRTQKSIEVAPSQTLTDEERQMLREAAVKIARHLGYVGAGTVE 161
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1394533372 214 FIMDSKH-NFCFMEMNTRLQVEHPVTEMITGTDLVEWQLRIAAGEKIP 260
Cdd:pfam02786 162 FALDPFSgEYYFIEMNTRLQVEHALAEKATGYDLAKEAAKIALGYPLP 209
|
|
| AccC |
COG0439 |
Biotin carboxylase [Lipid transport and metabolism]; Biotin carboxylase is part of the Pathway ... |
1-263 |
1.80e-67 |
|
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: 220.51 E-value: 1.80e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533372 1 MEKIIQVAKTSAAQaiHPGCGFLSEN----MEFAELCKQEGIIfiGPPPSAIRDMGIKSTSKSIMAAAGVPVVEGYHGED 76
Cdd:COG0439 2 IDAIIAAAAELARE--TGIDAVLSESefavETAAELAEELGLP--GPSPEAIRAMRDKVLMREALAAAGVPVPGFALVDS 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533372 77 QSDqcLKEHARRIGYPVMIKAVRGGGGKGMRIVRSEQEFQEQLESARREAKKSFNDDAMLIEKFVDTpRHVEVQVFGdHH 156
Cdd:COG0439 78 PEE--ALAFAEEIGYPVVVKPADGAGSRGVRVVRDEEELEAALAEARAEAKAGSPNGEVLVEEFLEG-REYSVEGLV-RD 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533372 157 GNAVYlferdCSVQRRHQK---IIE---EAPAPgIKSEVRKKLGEAAVRAAKAVNYV-GAGTVEFIMDSKHNFCFMEMNT 229
Cdd:COG0439 154 GEVVV-----CSITRKHQKppyFVElghEAPSP-LPEELRAEIGELVARALRALGYRrGAFHTEFLLTPDGEPYLIEINA 227
|
250 260 270
....*....|....*....|....*....|....*.
gi 1394533372 230 RLQVEH--PVTEMITGTDLVEWQLRIAAGEKIPLSQ 263
Cdd:COG0439 228 RLGGEHipPLTELATGVDLVREQIRLALGEPRILDP 263
|
|
| Biotin_carb_C |
smart00878 |
Biotin carboxylase C-terminal domain; Biotin carboxylase is a component of the acetyl-CoA ... |
274-380 |
1.14e-49 |
|
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: 167.59 E-value: 1.14e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533372 274 EARIYAEDPSNNFMPVAGPLVHLSTPrADPSTRIETGVRQGDEVSVHYDPMIAKLVVWAADRQAALTKLRYSLRQYNIVG 353
Cdd:smart00878 1 ECRINAEDPANGFLPSPGRITRYRFP-GGPGVRVDSGVYEGYEVPPYYDSMIAKLIVWGEDREEAIARLRRALDEFRIRG 79
|
90 100
....*....|....*....|....*..
gi 1394533372 354 LHTNIDFLLNLSGHPEFEAGNVHTDFI 380
Cdd:smart00878 80 VKTNIPFLRALLRHPDFRAGDVDTGFL 106
|
|
| Biotin_carb_C |
pfam02785 |
Biotin carboxylase C-terminal domain; Biotin carboxylase is a component of the acetyl-CoA ... |
274-382 |
1.25e-49 |
|
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: 167.67 E-value: 1.25e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533372 274 EARIYAEDPSNNFMPVAGPLVHLSTPrADPSTRIETGVRQGDEVSVHYDPMIAKLVVWAADRQAALTKLRYSLRQYNIVG 353
Cdd:pfam02785 1 EARIYAEDPDNNFLPSPGKVTRYRFP-GGPGVRVDSGVYAGYTVSPYYDSMIAKLIVHGPTREEAIARLRRALAEFRIEG 79
|
90 100
....*....|....*....|....*....
gi 1394533372 354 LHTNIDFLLNLSGHPEFEAGNVHTDFIPQ 382
Cdd:pfam02785 80 VKTNIPFLRAILEHPDFRAGEVDTGFLEE 108
|
|
| biotinyl_domain |
cd06850 |
The biotinyl-domain or biotin carboxyl carrier protein (BCCP) domain is present in all ... |
542-605 |
1.91e-24 |
|
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: 96.72 E-value: 1.91e-24
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1394533372 542 APMTGTIEKVFVKAGDKVKAGDSLMVMIAMKMEHTIKSPKDGTVKKVFYREGAQANRHTPLVEF 605
Cdd:cd06850 4 APMPGTVVKVLVKEGDKVEAGQPLAVLEAMKMENEVTAPVAGVVKEILVKEGDQVEAGQLLVVI 67
|
|
| Biotinyl_lipoyl_domains |
cd06663 |
Biotinyl_lipoyl_domains are present in biotin-dependent carboxylases/decarboxylases, the ... |
539-605 |
3.77e-23 |
|
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: 93.28 E-value: 3.77e-23
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1394533372 539 GPLAPM------TGTIEKVFVKAGDKVKAGDSLMVMIAMKMEHTIKSPKDGTVKKVFYREGAQANRHTPLVEF 605
Cdd:cd06663 1 TILIPDlaqhlgDGTVVKWLKKVGDKVKKGDVLAEIEAMKATSDVEAPKSGTVKKVLVKEGTKVEGDTPLVKI 73
|
|
| DdlA |
COG1181 |
D-alanine-D-alanine ligase or related ATP-grasp enzyme [Cell wall/membrane/envelope biogenesis, ... |
54-229 |
3.37e-22 |
|
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: 97.48 E-value: 3.37e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533372 54 KSTSKSIMAAAGVPVVEGYHGEDQSDQCLKEHARRIGYPVMIKAVRGGGGKGMRIVRSEQEFQEQLESARREakksfnDD 133
Cdd:COG1181 96 KALTKRVLAAAGLPTPPYVVLRRGELADLEAIEEELGLPLFVKPAREGSSVGVSKVKNAEELAAALEEAFKY------DD 169
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533372 134 AMLIEKFVDtPRHVEVQVFGDHH-----------GNAVYLFErdcsVQRRHQKIIEEAPAPgIKSEVRKKLGEAAVRAAK 202
Cdd:COG1181 170 KVLVEEFID-GREVTVGVLGNGGpralppieivpENGFYDYE----AKYTDGGTEYICPAR-LPEELEERIQELALKAFR 243
|
170 180
....*....|....*....|....*..
gi 1394533372 203 AVNYVGAGTVEFIMDSKHNFCFMEMNT 229
Cdd:COG1181 244 ALGCRGYARVDFRLDEDGEPYLLEVNT 270
|
|
| Biotin_carb_N |
pfam00289 |
Biotin carboxylase, N-terminal domain; This domain is structurally related to the PreATP-grasp ... |
1-47 |
6.45e-21 |
|
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: 87.93 E-value: 6.45e-21
10 20 30 40
....*....|....*....|....*....|....*....|....*..
gi 1394533372 1 MEKIIQVAKTSAAQAIHPGCGFLSENMEFAELCKQEGIIFIGPPPSA 47
Cdd:pfam00289 62 IDAIIDAAKETGADAIHPGYGFLSENAEFARACEEAGIIFIGPSPEA 108
|
|
| PRK05641 |
PRK05641 |
putative acetyl-CoA carboxylase biotin carboxyl carrier protein subunit; Validated |
523-604 |
4.29e-19 |
|
putative acetyl-CoA carboxylase biotin carboxyl carrier protein subunit; Validated
Pssm-ID: 235540 [Multi-domain] Cd Length: 153 Bit Score: 84.53 E-value: 4.29e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533372 523 PVPKYLSSVSSQETQGGP---LAPMTGTIEKVFVKAGDKVKAGDSLMVMIAMKMEHTIKSPKDGTVKKVFYREGAQANRH 599
Cdd:PRK05641 67 PTPVAPAAPAPAPASAGEnvvTAPMPGKILRILVREGQQVKVGQGLLILEAMKMENEIPAPKDGVVKKILVKEGDTVDTG 146
|
....*
gi 1394533372 600 TPLVE 604
Cdd:PRK05641 147 QPLIE 151
|
|
| PycA |
COG1038 |
Pyruvate carboxylase [Energy production and conversion]; Pyruvate carboxylase is part of the ... |
542-595 |
1.11e-17 |
|
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: 87.44 E-value: 1.11e-17
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 1394533372 542 APMTGTIEKVFVKAGDKVKAGDSLMVMIAMKMEHTIKSPKDGTVKKVFYREGAQ 595
Cdd:COG1038 1081 APMPGTVVKVLVKEGDEVKKGDPLLTIEAMKMETTITAPRDGTVKEVLVKEGDQ 1134
|
|
| PRK09282 |
PRK09282 |
pyruvate carboxylase subunit B; Validated |
523-606 |
1.31e-17 |
|
pyruvate carboxylase subunit B; Validated
Pssm-ID: 236449 [Multi-domain] Cd Length: 592 Bit Score: 86.43 E-value: 1.31e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533372 523 PVPKYLSSVSSQETQGGPL-APMTGTIEKVFVKAGDKVKAGDSLMVMIAMKMEHTIKSPKDGTVKKVFYREGAQANRHTP 601
Cdd:PRK09282 507 PLKEIVVGGRPRASAPGAVtSPMPGTVVKVKVKEGDKVKAGDTVLVLEAMKMENEIQAPVDGTVKEILVKEGDRVNPGDV 586
|
....*
gi 1394533372 602 LVEFE 606
Cdd:PRK09282 587 LMEIE 591
|
|
| PRK12999 |
PRK12999 |
pyruvate carboxylase; Reviewed |
542-595 |
2.62e-17 |
|
pyruvate carboxylase; Reviewed
Pssm-ID: 237263 [Multi-domain] Cd Length: 1146 Bit Score: 86.35 E-value: 2.62e-17
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 1394533372 542 APMTGTIEKVFVKAGDKVKAGDSLMVMIAMKMEHTIKSPKDGTVKKVFYREGAQ 595
Cdd:PRK12999 1081 APMPGSVVTVLVKEGDEVKAGDPLAVIEAMKMETTITAPVDGTVKRVLVKAGDQ 1134
|
|
| Dala_Dala_lig_C |
pfam07478 |
D-ala D-ala ligase C-terminus; This family represents the C-terminal, catalytic domain of the ... |
60-229 |
2.78e-16 |
|
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: 77.74 E-value: 2.78e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533372 60 IMAAAGVPVV-------EGYHgEDQSDQCLKEHARrIGYPVMIKAVRGGGGKGMRIVRSEQEFQEQLESARREakksfnD 132
Cdd:pfam07478 1 LLKAAGLPVVpfvtftrADWK-LNPKEWCAQVEEA-LGYPVFVKPARLGSSVGVSKVESREELQAAIEEAFQY------D 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533372 133 DAMLIEKFVDTpRHVEVQVFGDHHGNAVYLFER--DCSVQRRHQKIIEEA-----PApGIKSEVRKKLGEAAVRAAKAVN 205
Cdd:pfam07478 73 EKVLVEEGIEG-REIECAVLGNEDPEVSPVGEIvpSGGFYDYEAKYIDDSaqivvPA-DLEEEQEEQIQELALKAYKALG 150
|
170 180
....*....|....*....|....
gi 1394533372 206 YVGAGTVEFIMDSKHNFCFMEMNT 229
Cdd:pfam07478 151 CRGLARVDFFLTEDGEIVLNEVNT 174
|
|
| COG3919 |
COG3919 |
Predicted ATP-dependent carboligase, ATP-grasp superfamily [General function prediction only]; |
22-260 |
4.54e-16 |
|
Predicted ATP-dependent carboligase, ATP-grasp superfamily [General function prediction only];
Pssm-ID: 443124 [Multi-domain] Cd Length: 382 Bit Score: 80.36 E-value: 4.54e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533372 22 FLSENMEfaELckQEGIIFIGPPPSAIRDMGIKSTSKSIMAAAGVPVVEGYHGEDQSDqcLKEHARRIGYPVMIKAVRG- 100
Cdd:COG3919 90 LLSRHRD--EL--EEHYRLPYPDADLLDRLLDKERFYELAEELGVPVPKTVVLDSADD--LDALAEDLGFPVVVKPADSv 163
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533372 101 -------GGGKGMRIVRSEQEFQEQLESARREakksfnDDAMLIEKFVDTPRHVEVQVFG--DHHGNAVYLFerdcsVQR 171
Cdd:COG3919 164 gydelsfPGKKKVFYVDDREELLALLRRIAAA------GYELIVQEYIPGDDGEMRGLTAyvDRDGEVVATF-----TGR 232
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533372 172 RHQkiieEAPAPG-----IKSEVRKKLGEAAVRAAKAVNYVGAGTVEFIMDSKHN-FCFMEMNTRL--QVEHPVtemITG 243
Cdd:COG3919 233 KLR----HYPPAGgnsaaRESVDDPELEEAARRLLEALGYHGFANVEFKRDPRDGeYKLIEINPRFwrSLYLAT---AAG 305
|
250
....*....|....*..
gi 1394533372 244 TDLVEWQLRIAAGEKIP 260
Cdd:COG3919 306 VNFPYLLYDDAVGRPLE 322
|
|
| ddl |
PRK01372 |
D-alanine--D-alanine ligase; Reviewed |
57-229 |
1.20e-15 |
|
D-alanine--D-alanine ligase; Reviewed
Pssm-ID: 234948 [Multi-domain] Cd Length: 304 Bit Score: 77.84 E-value: 1.20e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533372 57 SKSIMAAAGVPVVEGYHGEDQSDQCLKEHarRIGYPVMIKAVRGGGGKGMRIVRSEQEFQEQLESARReakksfNDDAML 136
Cdd:PRK01372 102 TKLVWQAAGLPTPPWIVLTREEDLLAAID--KLGLPLVVKPAREGSSVGVSKVKEEDELQAALELAFK------YDDEVL 173
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533372 137 IEKFVDTPrhvEVQ--VFGDH--------HGNAVYLFE----RDCSvqrrhQKIIeeaPApGIKSEVRKKLGEAAVRAAK 202
Cdd:PRK01372 174 VEKYIKGR---ELTvaVLGGKalpvieivPAGEFYDYEakylAGGT-----QYIC---PA-GLPAEIEAELQELALKAYR 241
|
170 180
....*....|....*....|....*..
gi 1394533372 203 AVNYVGAGTVEFIMDSKHNFCFMEMNT 229
Cdd:PRK01372 242 ALGCRGWGRVDFMLDEDGKPYLLEVNT 268
|
|
| AccB |
COG0511 |
Biotin carboxyl carrier protein [Lipid transport and metabolism]; Biotin carboxyl carrier ... |
542-606 |
1.13e-14 |
|
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: 71.08 E-value: 1.13e-14
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1394533372 542 APMTGTI-------EKVFVKAGDKVKAGDSLMVMIAMKMEHTIKSPKDGTVKKVFYREGAQANRHTPLVEFE 606
Cdd:COG0511 65 SPMVGTFyrapspgAKPFVKVGDKVKAGDTLCIIEAMKMMNEIEAPVSGTVVEILVENGQPVEYGQPLFVIE 136
|
|
| Biotin_lipoyl |
pfam00364 |
Biotin-requiring enzyme; This family covers two Prosite entries, the conserved lysine residue ... |
542-605 |
1.63e-14 |
|
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: 68.78 E-value: 1.63e-14
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1394533372 542 APMTGT-----IEKVFVKAGDKVKAGDSLMVMIAMKMEHTIKSPKDGTVKKVFYREGAQANRHTPLVEF 605
Cdd:pfam00364 5 SPMIGEsvregVVEWLVKVGDKVKAGQPLAEVEAMKMEMEIPAPVAGVVKEILVPEGDTVEVGDPLAKI 73
|
|
| PRK14040 |
PRK14040 |
oxaloacetate decarboxylase subunit alpha; |
521-593 |
1.77e-14 |
|
oxaloacetate decarboxylase subunit alpha;
Pssm-ID: 237592 [Multi-domain] Cd Length: 593 Bit Score: 76.51 E-value: 1.77e-14
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1394533372 521 DIPVPKYLSSVSSQETQGGPL-APMTGTIEKVFVKAGDKVKAGDSLMVMIAMKMEHTIKSPKDGTVKKVFYREG 593
Cdd:PRK14040 507 PAAAPAAAAAAAPAAAAGEPVtAPLAGNIFKVIVTEGQTVAEGDVLLILEAMKMETEIRAAQAGTVRGIAVKEG 580
|
|
| ddl |
PRK01966 |
D-alanine--D-alanine ligase; |
54-229 |
4.46e-14 |
|
D-alanine--D-alanine ligase;
Pssm-ID: 234993 [Multi-domain] Cd Length: 333 Bit Score: 73.62 E-value: 4.46e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533372 54 KSTSKSIMAAAGVPVVEGY--HGEDQSDQCLKEHARRIGYPVMIKAVRGGGGKGMRIVRSEQEFQEQLESARREakksfn 131
Cdd:PRK01966 124 KILTKRLLAAAGIPVAPYVvlTRGDWEEASLAEIEAKLGLPVFVKPANLGSSVGISKVKNEEELAAALDLAFEY------ 197
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533372 132 DDAMLIEKFVDtPRHVEVqvfgdhhgnAVYLFERDCSV------------------QRRHQKIIeeaPAPgIKSEVRKKL 193
Cdd:PRK01966 198 DRKVLVEQGIK-GREIEC---------AVLGNDPKASVpgeivkpddfydyeakylDGSAELII---PAD-LSEELTEKI 263
|
170 180 190
....*....|....*....|....*....|....*.
gi 1394533372 194 GEAAVRAAKAVNYVGAGTVEFIMDSKHNFCFMEMNT 229
Cdd:PRK01966 264 RELAIKAFKALGCSGLARVDFFLTEDGEIYLNEINT 299
|
|
| PurK |
COG0026 |
Phosphoribosylaminoimidazole carboxylase (NCAIR synthetase) [Nucleotide transport and ... |
43-214 |
3.32e-13 |
|
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: 71.26 E-value: 3.32e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533372 43 PPPSAIR---DmgiKSTSKSIMAAAGVPVVEGYHGEDQSDqcLKEHARRIGYPVMIKAVRGG-GGKGMRIVRSEQEFQeq 118
Cdd:COG0026 79 PGPEALEiaqD---RLLEKAFLAELGIPVAPFAAVDSLED--LEAAIAELGLPAVLKTRRGGyDGKGQVVIKSAADLE-- 151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533372 119 lesarrEAKKSFNDDAMLIEKFVDTPRHVEVQVFGDHHGNAVY--LFErdcSVQRRHqkIIEE--APApGIKSEVRKKLG 194
Cdd:COG0026 152 ------AAWAALGGGPCILEEFVPFERELSVIVARSPDGEVATypVVE---NVHRNG--ILDEsiAPA-RISEALAAEAE 219
|
170 180
....*....|....*....|
gi 1394533372 195 EAAVRAAKAVNYVGAGTVEF 214
Cdd:COG0026 220 EIAKRIAEALDYVGVLAVEF 239
|
|
| LysX |
COG0189 |
Glutathione synthase, LysX or RimK-type ligase, ATP-grasp superfamily [Amino acid transport ... |
27-228 |
5.08e-12 |
|
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: 66.89 E-value: 5.08e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533372 27 MEFAELCKQEGIIFIgPPPSAIRDMGIKSTSKSIMAAAGVPVVEGYHGEDQSDqcLKEHARRIGYPVMIKAVRGGGGKGM 106
Cdd:COG0189 71 LALLRQLEAAGVPVV-NDPEAIRRARDKLFTLQLLARAGIPVPPTLVTRDPDD--LRAFLEELGGPVVLKPLDGSGGRGV 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533372 107 RIVRSEQEFQEQLesarrEAKKSFNDDAMLIEKFVDTPRHVEVQVF--GdhhGNAVYLFERDcsVQRRHQKIIEEAPAPG 184
Cdd:COG0189 148 FLVEDEDALESIL-----EALTELGSEPVLVQEFIPEEDGRDIRVLvvG---GEPVAAIRRI--PAEGEFRTNLARGGRA 217
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1394533372 185 IKSEVRKKLGEAAVRAAKAV--NYVGagtVEFIMDsKHNFCFMEMN 228
Cdd:COG0189 218 EPVELTDEERELALRAAPALglDFAG---VDLIED-DDGPLVLEVN 259
|
|
| PRK02186 |
PRK02186 |
argininosuccinate lyase; Provisional |
7-346 |
1.67e-11 |
|
argininosuccinate lyase; Provisional
Pssm-ID: 235010 [Multi-domain] Cd Length: 887 Bit Score: 67.56 E-value: 1.67e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533372 7 VAKTSAAQAIH------PGCGFLSENMEF-----AELCKQEGIIfiGPPPSAIRDMGIKSTSKSIMAAAGVPVVEGYHGE 75
Cdd:PRK02186 52 SADTSDPDRIHrfvsslDGVAGIMSSSEYfievaSEVARRLGLP--AANTEAIRTCRDKKRLARTLRDHGIDVPRTHALA 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533372 76 DQSDqcLKEHARRIGYPVMIKAVRGGGGKGMRIVRSEQEFQEQLESARREAKKSFnddamLIEKFVDTPRHvEVQVFGDH 155
Cdd:PRK02186 130 LRAV--ALDALDGLTYPVVVKPRMGSGSVGVRLCASVAEAAAHCAALRRAGTRAA-----LVQAYVEGDEY-SVETLTVA 201
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533372 156 HGNAVYlferdcSVQRRHQ-------KIIEEAPAPgIKSEVRKKLGEAAVRAAKAVNY-VGAGTVEFIMdSKHNFCFMEM 227
Cdd:PRK02186 202 RGHQVL------GITRKHLgppphfvEIGHDFPAP-LSAPQRERIVRTVLRALDAVGYaFGPAHTELRV-RGDTVVIIEI 273
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533372 228 NTRLQVEH-PVT-EMITGTDLVEWQLRIAAGE--------------KIPLSQEEITLQGHAFEARIYAEDPSNNFMPVAG 291
Cdd:PRK02186 274 NPRLAGGMiPVLlEEAFGVDLLDHVIDLHLGVaafadptakrygaiRFVLPARSGVLRGLLFLPDDIAARPELRFHPLKQ 353
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1394533372 292 PlVHLSTPRADPSTRIETGVRQGDE---VSVHYDPMIAKLVV-------WAADRQAALTKLRYSL 346
Cdd:PRK02186 354 P-GDALRLEGDFRDRIAAVVCAGDHrdsVAAAAERAVAGLSIdigdaarAAALNDAGAGAARPGL 417
|
|
| carB |
PRK12815 |
carbamoyl phosphate synthase large subunit; Reviewed |
60-259 |
2.84e-11 |
|
carbamoyl phosphate synthase large subunit; Reviewed
Pssm-ID: 237215 [Multi-domain] Cd Length: 1068 Bit Score: 66.92 E-value: 2.84e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533372 60 IMAAAGVPVVEGYHGEDQSDqcLKEHARRIGYPVMIKAVRGGGGKGMRIVRSEQEFQEQLESArreakkSFNDDAMLIEK 139
Cdd:PRK12815 677 LLDELGLPHVPGLTATDEEE--AFAFAKRIGYPVLIRPSYVIGGQGMAVVYDEPALEAYLAEN------ASQLYPILIDQ 748
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533372 140 FVDTpRHVEVQVFGDhhGNAVYL---FErdcsvqrrHqkiIEEA-----------PAPGIKSEVRKKLGEAAVRAAKAVN 205
Cdd:PRK12815 749 FIDG-KEYEVDAISD--GEDVTIpgiIE--------H---IEQAgvhsgdsiavlPPQSLSEEQQEKIRDYAIKIAKKLG 814
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1394533372 206 YVGAGTVEFIMDSKhNFCFMEMNTRLQVEHPVTEMITGTDLVEWQLRIAAGEKI 259
Cdd:PRK12815 815 FRGIMNIQFVLAND-EIYVLEVNPRASRTVPFVSKATGVPLAKLATKVLLGKSL 867
|
|
| CarB |
COG0458 |
Carbamoylphosphate synthase large subunit [Amino acid transport and metabolism, Nucleotide ... |
27-218 |
8.18e-11 |
|
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: 64.90 E-value: 8.18e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533372 27 MEFAELCKQEGIIFIGPPPSAI-----RDMgikstSKSIMAAAGVPVVEGYHGEDQSDqcLKEHARRIGYPVMIKA--VR 99
Cdd:COG0458 88 VELEEAGILEGVKILGTSPDAIdlaedREL-----FKELLDKLGIPQPKSGTATSVEE--ALAIAEEIGYPVIVRPsyVL 160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533372 100 GGggKGMRIVRSEQEFQEQLEsarrEAKKSFNDDAMLIEKFVDTPRHVEVQVFGDHHGNAVYLferdCSVQrrHqkiIEE 179
Cdd:COG0458 161 GG--RGMGIVYNEEELEEYLE----RALKVSPDHPVLIDESLLGAKEIEVDVVRDGEDNVIIV----GIME--H---IEP 225
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1394533372 180 A-----------PAPGIKSEVRKKLGEAAVRAAKAVNYVGAGTVEFIMDS 218
Cdd:COG0458 226 AgvhsgdsicvaPPQTLSDKEYQRLRDATLKIARALGVVGLCNIQFAVDD 275
|
|
| ATP-grasp |
pfam02222 |
ATP-grasp domain; This family does not contain all known ATP-grasp domain members. This family ... |
62-214 |
1.19e-10 |
|
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: 60.35 E-value: 1.19e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533372 62 AAAGVPVVEGYHGEDQSDqcLKEHARRIGYPVMIKAVRGG-GGKGMRIVRSEqefqEQLESARREAKksfnDDAMLIEKF 140
Cdd:pfam02222 1 QKLGLPTPRFMAAESLEE--LIEAGQELGYPCVVKARRGGyDGKGQYVVRSE----ADLPQAWEELG----DGPVIVEEF 70
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1394533372 141 VDTPRHVEVQVFGDHHGnAVYLFErdcSVQRRHQK---IIEEAPAPgIKSEVRKKLGEAAVRAAKAVNYVGAGTVEF 214
Cdd:pfam02222 71 VPFDRELSVLVVRSVDG-ETAFYP---VVETIQEDgicRLSVAPAR-VPQAIQAEAQDIAKRLVDELGGVGVFGVEL 142
|
|
| PRK06019 |
PRK06019 |
phosphoribosylaminoimidazole carboxylase ATPase subunit; Reviewed |
43-214 |
2.43e-10 |
|
phosphoribosylaminoimidazole carboxylase ATPase subunit; Reviewed
Pssm-ID: 235674 [Multi-domain] Cd Length: 372 Bit Score: 62.48 E-value: 2.43e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533372 43 PPPSAIR---DmgiKSTSKSIMAAAGVPVVEgYHG-EDQSDqcLKEHARRIGYPVMIKAVRGG-GGKGMRIVRSEQEFQe 117
Cdd:PRK06019 90 PGPDALAiaqD---RLTEKQFLDKLGIPVAP-FAVvDSAED--LEAALADLGLPAVLKTRRGGyDGKGQWVIRSAEDLE- 162
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533372 118 qlesarrEAKKSFNDDAMLIEKFVDTPRHVEVQVFGDHHGNAVY--LFErdcSVQRRHQKIIEEAPAPgIKSEVRKKLGE 195
Cdd:PRK06019 163 -------AAWALLGSVPCILEEFVPFEREVSVIVARGRDGEVVFypLVE---NVHRNGILRTSIAPAR-ISAELQAQAEE 231
|
170
....*....|....*....
gi 1394533372 196 AAVRAAKAVNYVGAGTVEF 214
Cdd:PRK06019 232 IASRIAEELDYVGVLAVEF 250
|
|
| PRK06549 |
PRK06549 |
acetyl-CoA carboxylase biotin carboxyl carrier protein subunit; Validated |
542-603 |
2.77e-10 |
|
acetyl-CoA carboxylase biotin carboxyl carrier protein subunit; Validated
Pssm-ID: 235826 [Multi-domain] Cd Length: 130 Bit Score: 58.28 E-value: 2.77e-10
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1394533372 542 APMTGTIEKVFVKAGDKVKAGDSLMVMIAMKMEHTIKSPKDGTVKKVFYREGAQANRHTPLV 603
Cdd:PRK06549 66 SPMPGTILKVLVAVGDQVTENQPLLILEAMKMENEIVASSAGTVTAIHVTPGQVVNPGDGLI 127
|
|
| PRK08225 |
PRK08225 |
acetyl-CoA carboxylase biotin carboxyl carrier protein subunit; Validated |
542-606 |
2.80e-10 |
|
acetyl-CoA carboxylase biotin carboxyl carrier protein subunit; Validated
Pssm-ID: 181304 [Multi-domain] Cd Length: 70 Bit Score: 56.33 E-value: 2.80e-10
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1394533372 542 APMTGTIEKVFVKAGDKVKAGDSLMVMIAMKMEHTIKSPKDGTVKKVFYREGAQANRHTPLVEFE 606
Cdd:PRK08225 6 ASMAGNVWKIVVKVGDTVEEGQDVVILESMKMEIPIVAEEAGTVKKINVQEGDFVNEGDVLLEIE 70
|
|
| CPSaseII_lrg |
TIGR01369 |
carbamoyl-phosphate synthase, large subunit; Carbamoyl-phosphate synthase (CPSase) catalyzes ... |
83-259 |
3.42e-10 |
|
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: 63.09 E-value: 3.42e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533372 83 KEHARRIGYPVMIKAVRGGGGKGMRIVRSEQEFQEQLEsarrEAKKSFNDDAMLIEKFVDTPRHVEVQVFGDHHGNAVY- 161
Cdd:TIGR01369 697 VEFASEIGYPVLVRPSYVLGGRAMEIVYNEEELRRYLE----EAVAVSPEHPVLIDKYLEDAVEVDVDAVSDGEEVLIPg 772
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533372 162 LFErdcsvqrrHqkiIEEA-----------PAPGIKSEVRKKLGEAAVRAAKAVNYVGAGTVEFIMDSkHNFCFMEMNTR 230
Cdd:TIGR01369 773 IME--------H---IEEAgvhsgdstcvlPPQTLSAEIVDRIKDIVRKIAKELNVKGLMNIQFAVKD-GEVYVIEVNPR 840
|
170 180
....*....|....*....|....*....
gi 1394533372 231 LQVEHPVTEMITGTDLVEWQLRIAAGEKI 259
Cdd:TIGR01369 841 ASRTVPFVSKATGVPLAKLAVRVMLGKKL 869
|
|
| rimK_fam |
TIGR00768 |
alpha-L-glutamate ligase, RimK family; This family, related to bacterial glutathione ... |
44-248 |
2.37e-09 |
|
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: 58.51 E-value: 2.37e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533372 44 PPSAIRDMGIKSTSKSIMAAAGVPVVEG--YHGEDQSDQCLKEharrIGYPVMIKAVRGGGGKGMRIVRSEQEFQEQLES 121
Cdd:TIGR00768 79 SSDAILNAGDKFLSHQLLAKAGIPLPRTglAGSPEEALKLIEE----IGFPVVLKPVFGSWGRGVSLARDRQAAESLLEH 154
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533372 122 ARREAKKSfndDAMLIEKFVDTPRHVEVQVF--GDHHGNAVYL-----FERDCSVQRRHQKIieeapapgiksEVRKKLG 194
Cdd:TIGR00768 155 FEQLNGPQ---NLFLVQEYIKKPGGRDIRVFvvGDEVVAAIYRitsghWRSNLARGGKAEPC-----------SLTEEIE 220
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1394533372 195 EAAVRAAKAVNyVGAGTVEFIMdSKHNFCFMEMNTRLQVEHpvTEMITGTDLVE 248
Cdd:TIGR00768 221 ELAIKAAKALG-LDVAGVDLLE-SEDGLLVNEVNANPEFKN--SVKTTGVNIAG 270
|
|
| lipoyl_domain |
cd06849 |
Lipoyl domain of the dihydrolipoyl acyltransferase component (E2) of 2-oxo acid dehydrogenases. ... |
520-605 |
3.03e-09 |
|
Lipoyl domain of the dihydrolipoyl acyltransferase component (E2) of 2-oxo acid dehydrogenases. 2-oxo acid dehydrogenase multienzyme complexes, like pyruvate dehydrogenase (PDH), 2-oxoglutarate dehydrogenase (OGDH) and branched-chain 2-oxo acid dehydrogenase (BCDH), contain at least three different enzymes, 2-oxo acid dehydrogenase (E1), dihydrolipoyl acyltransferase (E2) and dihydrolipoamide dehydrogenase (E3) and play a key role in redox regulation. E2, the central component of the complex, catalyzes the transfer of the acyl group of CoA from E1 to E3 via reductive acetylation of a lipoyl group covalently attached to a lysine residue.
Pssm-ID: 133458 [Multi-domain] Cd Length: 74 Bit Score: 53.56 E-value: 3.03e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533372 520 IDIPVPKYLSSVSSqetqggplapmtGTIEKVFVKAGDKVKAGDSLMVMIAMKMEHTIKSPKDGTVKKVFYREGAQANRH 599
Cdd:cd06849 1 TEIKMPDLGESMTE------------GTIVEWLVKEGDSVEEGDVLAEVETDKATVEVEAPAAGVLAKILVEEGDTVPVG 68
|
....*.
gi 1394533372 600 TPLVEF 605
Cdd:cd06849 69 QVIAVI 74
|
|
| PRK12767 |
PRK12767 |
carbamoyl phosphate synthase-like protein; Provisional |
21-260 |
3.21e-08 |
|
carbamoyl phosphate synthase-like protein; Provisional
Pssm-ID: 237195 [Multi-domain] Cd Length: 326 Bit Score: 55.66 E-value: 3.21e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533372 21 GFLSENM-EFAElckqEGIIFIGPPPSAIRDMGIKSTSKSIMAAAGVPVVEGYHGEDQSDQCLKEHARRIGYPVMIKAVR 99
Cdd:PRK12767 82 PLLAQNRdRFEE----IGVKVLVSSKEVIEICNDKWLTYEFLKENGIPTPKSYLPESLEDFKAALAKGELQFPLFVKPRD 157
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533372 100 GGGGKGMRIVRSEqefqEQLESARREAKKsfnddaMLIEKFVDTPRhVEVQVFGDHHGNAVYLFERdcsvqRRHQKIIEE 179
Cdd:PRK12767 158 GSASIGVFKVNDK----EELEFLLEYVPN------LIIQEFIEGQE-YTVDVLCDLNGEVISIVPR-----KRIEVRAGE 221
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533372 180 ApapgIKSEVRK--KLGEAAVRAAKAVNYVGAGTVEFIMDSKhNFCFMEMNTRLQVEHPVTEMiTGTDLVEWQLRIAAGE 257
Cdd:PRK12767 222 T----SKGVTVKdpELFKLAERLAEALGARGPLNIQCFVTDG-EPYLFEINPRFGGGYPLSYM-AGANEPDWIIRNLLGG 295
|
...
gi 1394533372 258 KIP 260
Cdd:PRK12767 296 ENE 298
|
|
| PRK11856 |
PRK11856 |
branched-chain alpha-keto acid dehydrogenase subunit E2; Reviewed |
544-616 |
9.79e-08 |
|
branched-chain alpha-keto acid dehydrogenase subunit E2; Reviewed
Pssm-ID: 237001 [Multi-domain] Cd Length: 411 Bit Score: 54.41 E-value: 9.79e-08
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1394533372 544 MT-GTIEKVFVKAGDKVKAGDSLMVM----IAMKMEhtikSPKDGTVKKVFYREGAQANRHTPLVEFEEEESDKRESE 616
Cdd:PRK11856 14 MTeGEIVEWLVKVGDTVKEGQPLAEVetdkATVEIP----SPVAGTVAKLLVEEGDVVPVGSVIAVIEEEGEAEAAAA 87
|
|
| PRK14016 |
PRK14016 |
cyanophycin synthetase; Provisional |
58-141 |
1.67e-07 |
|
cyanophycin synthetase; Provisional
Pssm-ID: 237586 [Multi-domain] Cd Length: 727 Bit Score: 54.39 E-value: 1.67e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533372 58 KSIMAAAGVPVVEGY--HGEDQsdqcLKEHARRIGYPVMIKAVRGGGGKGMRI-VRSEqefqEQLESARREAKKSFNDda 134
Cdd:PRK14016 219 KRLLAAAGVPVPEGRvvTSAED----AWEAAEEIGYPVVVKPLDGNHGRGVTVnITTR----EEIEAAYAVASKESSD-- 288
|
....*..
gi 1394533372 135 MLIEKFV 141
Cdd:PRK14016 289 VIVERYI 295
|
|
| AceF |
COG0508 |
Pyruvate/2-oxoglutarate dehydrogenase complex, dihydrolipoamide acyltransferase (E2) component ... |
546-605 |
2.29e-07 |
|
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: 48.52 E-value: 2.29e-07
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1394533372 546 GTIEKVFVKAGDKVKAGDSLMVMIAMK--MEhtIKSPKDGTVKKVFYREGAQANRHTPLVEF 605
Cdd:COG0508 17 GTIVEWLVKEGDTVKEGDPLAEVETDKatME--VPAPAAGVLLEILVKEGDTVPVGAVIAVI 76
|
|
| PRK11855 |
PRK11855 |
dihydrolipoamide acetyltransferase; Reviewed |
546-610 |
3.67e-07 |
|
dihydrolipoamide acetyltransferase; Reviewed
Pssm-ID: 237000 [Multi-domain] Cd Length: 547 Bit Score: 52.90 E-value: 3.67e-07
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1394533372 546 GTIEKVFVKAGDKVKAGDSLM-VMI--AMkMEhtIKSPKDGTVKKVFYREGAQANRHTPLVEFEEEES 610
Cdd:PRK11855 133 VEVIEWLVKVGDTVEEDQSLItVETdkAT-ME--IPSPVAGVVKEIKVKVGDKVSVGSLLVVIEVAAA 197
|
|
| PRK11855 |
PRK11855 |
dihydrolipoamide acetyltransferase; Reviewed |
546-609 |
8.80e-07 |
|
dihydrolipoamide acetyltransferase; Reviewed
Pssm-ID: 237000 [Multi-domain] Cd Length: 547 Bit Score: 51.75 E-value: 8.80e-07
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1394533372 546 GTIEKVFVKAGDKVKAGDSLM-VMI--AMkMEhtIKSPKDGTVKKVFYREGAQANRHTPLVEFEEEE 609
Cdd:PRK11855 16 VEVIEWLVKEGDTVEEDQPLVtVETdkAT-ME--IPSPAAGVVKEIKVKVGDTVSVGGLLAVIEAAG 79
|
|
| PLN02983 |
PLN02983 |
biotin carboxyl carrier protein of acetyl-CoA carboxylase |
523-602 |
1.04e-06 |
|
biotin carboxyl carrier protein of acetyl-CoA carboxylase
Pssm-ID: 215533 [Multi-domain] Cd Length: 274 Bit Score: 50.61 E-value: 1.04e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533372 523 PVPKYLSSVSSQETqggPL-APMTGTI-------EKVFVKAGDKVKAGDSLMVMIAMKMEHTIKSPKDGTVKKVFYREGA 594
Cdd:PLN02983 185 ASPPPAKAPKSSHP---PLkSPMAGTFyrspapgEPPFVKVGDKVQKGQVVCIIEAMKLMNEIEADQSGTIVEILAEDGK 261
|
....*...
gi 1394533372 595 QANRHTPL 602
Cdd:PLN02983 262 PVSVDTPL 269
|
|
| PRK14042 |
PRK14042 |
pyruvate carboxylase subunit B; Provisional |
529-606 |
1.32e-06 |
|
pyruvate carboxylase subunit B; Provisional
Pssm-ID: 172536 [Multi-domain] Cd Length: 596 Bit Score: 51.26 E-value: 1.32e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1394533372 529 SSVSSQETQGGPLAPMTGTIEKVFVKAGDKVKAGDSLMVMIAMKMEHTIKSPKDGTVKKVFYREGAQANRHTPLVEFE 606
Cdd:PRK14042 517 SSVNNKIGPGDITVAIPGSIIAIHVSAGDEVKAGQAVLVIEAMKMETEIKAPANGVVAEILCQKGDKVTPGQVLIRVE 594
|
|
| carB |
PRK05294 |
carbamoyl-phosphate synthase large subunit; |
86-208 |
4.03e-06 |
|
carbamoyl-phosphate synthase large subunit;
Pssm-ID: 235393 [Multi-domain] Cd Length: 1066 Bit Score: 50.10 E-value: 4.03e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533372 86 ARRIGYPVMikaVRGG---GGKGMRIVRSEQEfqeqLESARREAKKSFNDDAMLIEKFVDTPRHVEVQVFGDhhGNAVYL 162
Cdd:PRK05294 700 AEEIGYPVL---VRPSyvlGGRAMEIVYDEEE----LERYMREAVKVSPDHPVLIDKFLEGAIEVDVDAICD--GEDVLI 770
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1394533372 163 ---FErdcsvqrrHqkiIEEApapGIKS--------------EVRKKLGEAAVRAAKAVNYVG 208
Cdd:PRK05294 771 ggiME--------H---IEEA---GVHSgdsacslppqtlseEIIEEIREYTKKLALELNVVG 819
|
|
| CPSaseII_lrg |
TIGR01369 |
carbamoyl-phosphate synthase, large subunit; Carbamoyl-phosphate synthase (CPSase) catalyzes ... |
37-231 |
1.87e-05 |
|
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: 48.07 E-value: 1.87e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533372 37 GIIFIGPPPSAIRDMGIKSTSKSIMAAAGVPVVEGYHGEDQsDQCLkEHARRIGYPVMIKAVRGGGGKGMRIVRSEQEFQ 116
Cdd:TIGR01369 111 GVEVLGTPVEAIKKAEDRELFREAMKEIGEPVPESEIAHSV-EEAL-AAAKEIGYPVIVRPAFTLGGTGGGIAYNREELK 188
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533372 117 EQLESARREAKKsfndDAMLIEKFVDTPRHVEVQVFGDHHGNAVYLferdCSVQR-----RHQ-KIIEEAPAPGIKSEVR 190
Cdd:TIGR01369 189 EIAERALSASPI----NQVLVEKSLAGWKEIEYEVMRDSNDNCITV----CNMENfdpmgVHTgDSIVVAPSQTLTDKEY 260
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1394533372 191 KKLGEAAVRAAKAVNYVGAGTVEFIMDSK-HNFCFMEMNTRL 231
Cdd:TIGR01369 261 QMLRDASIKIIRELGIEGGCNVQFALNPDsGRYYVIEVNPRV 302
|
|
| PLN02948 |
PLN02948 |
phosphoribosylaminoimidazole carboxylase |
19-210 |
3.17e-05 |
|
phosphoribosylaminoimidazole carboxylase
Pssm-ID: 178534 [Multi-domain] Cd Length: 577 Bit Score: 46.98 E-value: 3.17e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533372 19 GCGFLSENME------FAELCKQEgiIFIGPPPSAIRDMGIKSTSKSIMAAAGVPVVEgyHGEDQSDQCLKEHARRIGYP 92
Cdd:PLN02948 83 RCDVLTVEIEhvdvdtLEALEKQG--VDVQPKSSTIRIIQDKYAQKVHFSKHGIPLPE--FMEIDDLESAEKAGDLFGYP 158
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533372 93 VMIKAVRGG-GGKGMRIVRSEQEfqeqLESArrEAKKSFNDDAMLIEKFVDTPRHVEVQVFGDHHGNAV-Y-LFErdcSV 169
Cdd:PLN02948 159 LMLKSRRLAyDGRGNAVAKTEED----LSSA--VAALGGFERGLYAEKWAPFVKELAVMVARSRDGSTRcYpVVE---TI 229
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1394533372 170 QRRHQKIIEEAPAPgIKSEVRKKLGEAAVRAAKAVNyvGAG 210
Cdd:PLN02948 230 HKDNICHVVEAPAN-VPWKVAKLATDVAEKAVGSLE--GAG 267
|
|
| RimK |
pfam08443 |
RimK-like ATP-grasp domain; This ATP-grasp domain is found in the ribosomal S6 modification ... |
54-246 |
1.96e-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: 42.87 E-value: 1.96e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533372 54 KSTSKSIMAAAG--VPVVEGYHGEDQSDQCLKEHARRigYPVMIKAVRGGGGKGMRIVRSEQEFqEQLESARREakksfn 131
Cdd:pfam08443 4 KAKSHQLLAKHGigPPNTRLAWYPEDAEQFIEQIKRQ--FPVIVKSIYGSQGIGVFLAEDEQKL-RQTLSATNE------ 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533372 132 ddAMLIEKFVDTP--RHVEVQVFGDHHGNAVYLFERDCSVQRRHQKiieeaPAPGIKSEVRKKLGEAAVRAAKAVNYVGA 209
Cdd:pfam08443 75 --QILVQEFIAEAnnEDIRCLVVGDQVVGALHRQSNEGDFRSNLHR-----GGVGEKYQLSQEETELAIKAAQAMQLDVA 147
|
170 180 190
....*....|....*....|....*....|....*..
gi 1394533372 210 GtVEfIMDSKHNFCFMEMNTRLQVEhpVTEMITGTDL 246
Cdd:pfam08443 148 G-VD-LLRQKRGLLVCEVNSSPGLE--GIEKTLGINI 180
|
|
| PurD |
COG0151 |
Phosphoribosylamine-glycine ligase [Nucleotide transport and metabolism]; ... |
30-142 |
2.17e-04 |
|
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: 43.85 E-value: 2.17e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533372 30 AELCKQEGI--IFIGP--PPSA-----IRDMGI---------------KSTSKSIMAAAGVPVVEGYHGEDQSDqcLKEH 85
Cdd:COG0151 55 VAFAKEENIdlVVVGPeaPLVAgivdaFRAAGIpvfgpskaaaqlegsKAFAKEFMARYGIPTAAYRVFTDLEE--ALAY 132
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1394533372 86 ARRIGYPVMIKAVRGGGGKGMRIVRSEQEfqeqlesARREAKKSFNDDAM-------LIEKFVD 142
Cdd:COG0151 133 LEEQGAPIVVKADGLAAGKGVVVAETLEE-------ALAAVDDMLADGKFgdagarvVIEEFLE 189
|
|
| aceF |
PRK11854 |
pyruvate dehydrogenase dihydrolipoyltransacetylase; Validated |
546-610 |
7.96e-04 |
|
pyruvate dehydrogenase dihydrolipoyltransacetylase; Validated
Pssm-ID: 236999 [Multi-domain] Cd Length: 633 Bit Score: 42.30 E-value: 7.96e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1394533372 546 GTIEKVFVKAGDKVKAGDSLMVMIAMKMEHTIKSPKDGTVKKVFYREGAQANRHTPLVEFEEEES 610
Cdd:PRK11854 15 VEVTEILVKVGDKVEAEQSLITVEGDKASMEVPSPQAGVVKEIKVKVGDKVETGALIMIFESADG 79
|
|
| PLN02735 |
PLN02735 |
carbamoyl-phosphate synthase |
86-230 |
1.06e-03 |
|
carbamoyl-phosphate synthase
Pssm-ID: 215391 [Multi-domain] Cd Length: 1102 Bit Score: 42.07 E-value: 1.06e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533372 86 ARRIGYPVMIKAVRGGGGKGMRIVRSEQEFQEQLESARREAKksfnDDAMLIEKFVDTPRHVEVQVFGDHHGNAVYlfer 165
Cdd:PLN02735 733 AKRIGYPVVVRPSYVLGGRAMEIVYSDDKLKTYLETAVEVDP----ERPVLVDKYLSDATEIDVDALADSEGNVVI---- 804
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1394533372 166 dCSVQRRhqkiIEEA-----------PAPGIKSEVRKKLGEAAVRAAKAVNYVGAGTVEFIMDSKHNFCFMEMNTR 230
Cdd:PLN02735 805 -GGIMEH----IEQAgvhsgdsacslPTQTIPSSCLATIRDWTTKLAKRLNVCGLMNCQYAITPSGEVYIIEANPR 875
|
|
| PRK05889 |
PRK05889 |
biotin/lipoyl-binding carrier protein; |
542-593 |
1.22e-03 |
|
biotin/lipoyl-binding carrier protein;
Pssm-ID: 180306 [Multi-domain] Cd Length: 71 Bit Score: 37.87 E-value: 1.22e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 1394533372 542 APMTGTIEKVFVKAGDKVKAGDSLMVMIAMKMEHTIKSPKDGTVKKVFYREG 593
Cdd:PRK05889 7 AEIVASVLEVVVNEGDQIGKGDTLVLLESMKMEIPVLAEVAGTVSKVSVSVG 58
|
|
| PurT |
COG0027 |
Formate-dependent phosphoribosylglycinamide formyltransferase (GAR transformylase) [Nucleotide ... |
82-142 |
1.48e-03 |
|
Formate-dependent phosphoribosylglycinamide formyltransferase (GAR transformylase) [Nucleotide transport and metabolism]; Formate-dependent phosphoribosylglycinamide formyltransferase (GAR transformylase) is part of the Pathway/BioSystem: Purine biosynthesis
Pssm-ID: 439798 [Multi-domain] Cd Length: 393 Bit Score: 41.26 E-value: 1.48e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1394533372 82 LKEHARRIGYPVMIKAVRGGGGKGMRIVRSEqefqEQLESARREAKKS--FNDDAMLIEKFVD 142
Cdd:COG0027 141 LRAAVEEIGYPCVVKPVMSSSGKGQSVVRSP----ADIEAAWEYAQEGgrGGAGRVIVEGFVD 199
|
|
| ATP-grasp_4 |
pfam13535 |
ATP-grasp domain; This family includes a diverse set of enzymes that possess ATP-dependent ... |
89-162 |
1.63e-03 |
|
ATP-grasp domain; This family includes a diverse set of enzymes that possess ATP-dependent carboxylate-amine ligase activity.
Pssm-ID: 316093 [Multi-domain] Cd Length: 160 Bit Score: 39.57 E-value: 1.63e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533372 89 IGYPVMIKAVRGGGGKGMRIVRSEQEFQEQLESARRE--------AKKSFNDDAMLIEKFVDTPrHVEVQVFGDHHGNAV 160
Cdd:pfam13535 1 IPYPCVIKPSVGFFSVGVYKINNREEWKAAFAAIREEieqwkemyPEAVVDGGSFLVEEYIEGE-EFAVDAYFDENGEPV 79
|
..
gi 1394533372 161 YL 162
Cdd:pfam13535 80 IL 81
|
|
| PycA |
COG1038 |
Pyruvate carboxylase [Energy production and conversion]; Pyruvate carboxylase is part of the ... |
542-568 |
1.81e-03 |
|
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: 41.60 E-value: 1.81e-03
10 20
....*....|....*....|....*..
gi 1394533372 542 APMTGTIEKVFVKAGDKVKAGDSLMVM 568
Cdd:COG1038 1118 APRDGTVKEVLVKEGDQVEAGDLLIEL 1144
|
|
| PRK12999 |
PRK12999 |
pyruvate carboxylase; Reviewed |
541-568 |
2.44e-03 |
|
pyruvate carboxylase; Reviewed
Pssm-ID: 237263 [Multi-domain] Cd Length: 1146 Bit Score: 40.89 E-value: 2.44e-03
10 20
....*....|....*....|....*...
gi 1394533372 541 LAPMTGTIEKVFVKAGDKVKAGDSLMVM 568
Cdd:PRK12999 1117 TAPVDGTVKRVLVKAGDQVEAGDLLVEL 1144
|
|
| GARS_A |
pfam01071 |
Phosphoribosylglycinamide synthetase, ATP-grasp (A) domain; Phosphoribosylglycinamide ... |
54-154 |
2.84e-03 |
|
Phosphoribosylglycinamide synthetase, ATP-grasp (A) domain; Phosphoribosylglycinamide synthetase catalyzes the second step in the de novo biosynthesis of purine. The reaction catalyzed by Phosphoribosylglycinamide synthetase is the ATP- dependent addition of 5-phosphoribosylamine to glycine to form 5'phosphoribosylglycinamide. This domain is related to the ATP-grasp domain of biotin carboxylase/carbamoyl phosphate synthetase (see pfam02786).
Pssm-ID: 395851 [Multi-domain] Cd Length: 194 Bit Score: 39.19 E-value: 2.84e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533372 54 KSTSKSIMAAAGVPVVEGYHGEDQSDqcLKEHARRIGYPVM-IKAVRGGGGKGMRIVRSEQEFQEQLESARREAKKSFND 132
Cdd:pfam01071 3 KSFAKDFMKRYGIPTAEYETFTDPEE--AKSYIQEAGFPAIvVKADGLAAGKGVIVASSNEEAIKAVDEILEQKKFGEAG 80
|
90 100
....*....|....*....|..
gi 1394533372 133 DAMLIEKFVDTPRhVEVQVFGD 154
Cdd:pfam01071 81 ETVVIEEFLEGEE-VSVLAFVD 101
|
|
| purT |
PRK09288 |
formate-dependent phosphoribosylglycinamide formyltransferase; |
82-128 |
4.81e-03 |
|
formate-dependent phosphoribosylglycinamide formyltransferase;
Pssm-ID: 236454 [Multi-domain] Cd Length: 395 Bit Score: 39.74 E-value: 4.81e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*..
gi 1394533372 82 LKEHARRIGYPVMIKAVRGGGGKGMRIVRSEqefqEQLESARREAKK 128
Cdd:PRK09288 141 LRAAVEEIGYPCVVKPVMSSSGKGQSVVRSP----EDIEKAWEYAQE 183
|
|
| AcrA |
COG0845 |
Multidrug efflux pump subunit AcrA (membrane-fusion protein) [Cell wall/membrane/envelope ... |
542-568 |
7.89e-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: 38.77 E-value: 7.89e-03
10 20
....*....|....*....|....*..
gi 1394533372 542 APMTGTIEKVFVKAGDKVKAGDSLMVM 568
Cdd:COG0845 28 ARVSGRVEEVLVDEGDRVKKGQVLARL 54
|
|
| |
