|
Name |
Accession |
Description |
Interval |
E-value |
| PccA |
COG4770 |
Acetyl/propionyl-CoA carboxylase, alpha subunit [Lipid transport and metabolism]; |
1-437 |
0e+00 |
|
Acetyl/propionyl-CoA carboxylase, alpha subunit [Lipid transport and metabolism];
Pssm-ID: 443802 [Multi-domain] Cd Length: 466 Bit Score: 569.65 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759837440 1 MIRRLLVADRGEVARRVFATCRLVGIETVAVYSDADTDAPHVIEADYAVHLPGNTPSATYLQADALIAAAQRAGANAVHP 80
Cdd:COG4770 1 MFKKVLIANRGEIAVRIIRTCRELGIRTVAVYSDADRDALHVRLADEAVCIGPAPAAESYLNIDAIIAAAKATGADAIHP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759837440 81 GIGVLAENSRFAQAVVDAGLIWVGPPPPTLRTLADKIETKKLVAEARVPVLPTFTDPDQVP----------GFPVLIKPA 150
Cdd:COG4770 81 GYGFLSENADFAEACEDAGIVFIGPSPEAIRAMGDKIAAKKLMKAAGVPVVPGSDGPVQDAeealaiaeeiGYPVLIKAS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759837440 151 AGSGGTGMRVVRDAGTLAEAVASTRREVG-----GDVFCEPYVSNVRHIEVPILADAQGAVIPFGERECSVQRRYQKIVE 225
Cdd:COG4770 161 AGGGGKGMRVVRSEEELEEAFESARREAKaafgdDRVYLEKYIERPRHIEVQVLADKHGNVVHLGERDCSIQRRHQKVIE 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759837440 226 ETPSPAVNPALREDLCRAAIIAVRALGYVGAGAVEFLLDSRGDFWFLELTPTLQADHAVTECVSGYDLVRLQLLVAEGGS 305
Cdd:COG4770 241 EAPSPALTEELRERMGEAAVRAAKAVGYVGAGTVEFLVDADGNFYFLEMNTRLQVEHPVTEMVTGIDLVEEQIRIAAGEP 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759837440 306 VPMPG-PPPIRGHAIEVRICAEDPAYAWLPAAGTLHRFAVPDiagefrplpQPGLRLDAGVSDGSVIGMHHDPMLAKLIA 384
Cdd:COG4770 321 LPFTQeDIKLRGHAIECRINAEDPARGFLPSPGTITRLRPPG---------GPGVRVDSGVYEGYEIPPYYDSMIAKLIV 391
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|...
gi 759837440 385 WAPSRQEAARMLASALARTHLHGVVSNRDLLVRVLRHHAFRAGDVDTGFLDRH 437
Cdd:COG4770 392 WGPDREEAIARMRRALAEFVIEGVKTNIPFLRALLAHPDFRAGDVDTGFIERE 444
|
|
| PRK06111 |
PRK06111 |
acetyl-CoA carboxylase biotin carboxylase subunit; Validated |
1-437 |
2.85e-147 |
|
acetyl-CoA carboxylase biotin carboxylase subunit; Validated
Pssm-ID: 180406 [Multi-domain] Cd Length: 450 Bit Score: 435.23 E-value: 2.85e-147
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759837440 1 MIRRLLVADRGEVARRVFATCRLVGIETVAVYSDADTDAPHVIEADYAVHLPGNTPSATYLQADALIAAAQRAGANAVHP 80
Cdd:PRK06111 1 MFQKVLIANRGEIAVRIIRTCQKLGIRTVAIYSEADRDALHVKMADEAYLIGGPRVQESYLNLEKIIEIAKKTGAEAIHP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759837440 81 GIGVLAENSRFAQAVVDAGLIWVGPPPPTLRTLADKIETKKLVAEARVPVLP----TFTDPDQVP------GFPVLIKPA 150
Cdd:PRK06111 81 GYGLLSENASFAERCKEEGIVFIGPSADIIAKMGSKIEARRAMQAAGVPVVPgittNLEDAEEAIaiarqiGYPVMLKAS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759837440 151 AGSGGTGMRVVRDAGTLAEAVASTRREVG-----GDVFCEPYVSNVRHIEVPILADAQGAVIPFGERECSVQRRYQKIVE 225
Cdd:PRK06111 161 AGGGGIGMQLVETEQELTKAFESNKKRAAnffgnGEMYIEKYIEDPRHIEIQLLADTHGNTVYLWERECSVQRRHQKVIE 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759837440 226 ETPSPAVNPALREDLCRAAIIAVRALGYVGAGAVEFLLDSRGDFWFLELTPTLQADHAVTECVSGYDLVRLQLLVAEGGS 305
Cdd:PRK06111 241 EAPSPFLDEETRKAMGERAVQAAKAIGYTNAGTIEFLVDEQKNFYFLEMNTRLQVEHPVTEEITGIDLVEQQLRIAAGEK 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759837440 306 VPMP-GPPPIRGHAIEVRICAEDPAyAWLPAAGTLHRFAVPDiagefrplpQPGLRLDAGVSDGSVIGMHHDPMLAKLIA 384
Cdd:PRK06111 321 LSFTqDDIKRSGHAIEVRIYAEDPK-TFFPSPGKITDLTLPG---------GEGVRHDHAVENGVTVTPFYDPMIAKLIA 390
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|...
gi 759837440 385 WAPSRQEAARMLASALARTHLHGVVSNRDLLVRVLRHHAFRAGDVDTGFLDRH 437
Cdd:PRK06111 391 HGETREEAISRLHDALEELKVEGIKTNIPLLLQVLEDPVFKAGGYTTGFLTKQ 443
|
|
| CPSase_L_D2 |
pfam02786 |
Carbamoyl-phosphate synthase L chain, ATP binding domain; Carbamoyl-phosphate synthase ... |
115-307 |
3.45e-54 |
|
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: 184.43 E-value: 3.45e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759837440 115 DKIETKKLVAEARVPVLPTFTDP-----------DQVpGFPVLIKPAAGSGGTGMRVVRDAGTLAEAVASTRREVG---- 179
Cdd:pfam02786 1 DKVLFKAAMKEAGVPTVPGTAGPveteeealaaaKEI-GYPVIIKAAFGGGGLGMGIARNEEELAELFALALAEAPaafg 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759837440 180 -GDVFCEPYVSNVRHIEVPILADAQGAVIPFGERECSVQRRYQKIVEETPSPAVNPALREDLCRAAIIAVRALGYVGAGA 258
Cdd:pfam02786 80 nPQVLVEKSLKGPKHIEYQVLRDAHGNCITVCNRECSDQRRTQKSIEVAPSQTLTDEERQMLREAAVKIARHLGYVGAGT 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 759837440 259 VEFLLDSR-GDFWFLELTPTLQADHAVTECVSGYDLVRLQLLVAEGGSVP 307
Cdd:pfam02786 160 VEFALDPFsGEYYFIEMNTRLQVEHALAEKATGYDLAKEAAKIALGYPLP 209
|
|
| Biotin_carb_C |
smart00878 |
Biotin carboxylase C-terminal domain; Biotin carboxylase is a component of the acetyl-CoA ... |
320-435 |
3.14e-41 |
|
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: 145.25 E-value: 3.14e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759837440 320 EVRICAEDPAYAWLPAAGTLHRFAVPDiagefrplpQPGLRLDAGVSDGSVIGMHHDPMLAKLIAWAPSRQEAARMLASA 399
Cdd:smart00878 1 ECRINAEDPANGFLPSPGRITRYRFPG---------GPGVRVDSGVYEGYEVPPYYDSMIAKLIVWGEDREEAIARLRRA 71
|
90 100 110
....*....|....*....|....*....|....*.
gi 759837440 400 LARTHLHGVVSNRDLLVRVLRHHAFRAGDVDTGFLD 435
Cdd:smart00878 72 LDEFRIRGVKTNIPFLRALLRHPDFRAGDVDTGFLE 107
|
|
| biotinyl_domain |
cd06850 |
The biotinyl-domain or biotin carboxyl carrier protein (BCCP) domain is present in all ... |
600-665 |
1.41e-21 |
|
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: 88.63 E-value: 1.41e-21
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 759837440 600 LIAPLPGAVRRVLVVPGQRVRAGELLLTLEAMKLEHPVHAPSAGVVSSLPVQPGAEVDTGELLAVL 665
Cdd:cd06850 2 VTAPMPGTVVKVLVKEGDKVEAGQPLAVLEAMKMENEVTAPVAGVVKEILVKEGDQVEAGQLLVVI 67
|
|
| PRK12999 |
PRK12999 |
pyruvate carboxylase; Reviewed |
602-667 |
6.46e-18 |
|
pyruvate carboxylase; Reviewed
Pssm-ID: 237263 [Multi-domain] Cd Length: 1146 Bit Score: 88.27 E-value: 6.46e-18
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 759837440 602 APLPGAVRRVLVVPGQRVRAGELLLTLEAMKLEHPVHAPSAGVVSSLPVQPGAEVDTGELLAVLDP 667
Cdd:PRK12999 1081 APMPGSVVTVLVKEGDEVKAGDPLAVIEAMKMETTITAPVDGTVKRVLVKAGDQVEAGDLLVELEP 1146
|
|
| PycA |
COG1038 |
Pyruvate carboxylase [Energy production and conversion]; Pyruvate carboxylase is part of the ... |
602-665 |
7.02e-18 |
|
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: 88.21 E-value: 7.02e-18
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 759837440 602 APLPGAVRRVLVVPGQRVRAGELLLTLEAMKLEHPVHAPSAGVVSSLPVQPGAEVDTGELLAVL 665
Cdd:COG1038 1081 APMPGTVVKVLVKEGDEVKKGDPLLTIEAMKMETTITAPRDGTVKEVLVKEGDQVEAGDLLIEL 1144
|
|
| PRK14040 |
PRK14040 |
oxaloacetate decarboxylase subunit alpha; |
532-665 |
5.76e-17 |
|
oxaloacetate decarboxylase subunit alpha;
Pssm-ID: 237592 [Multi-domain] Cd Length: 593 Bit Score: 84.60 E-value: 5.76e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759837440 532 APVADEHPPVVVVQAGSGRV-VLNVQGIRLAVHVHRVGDVSYVDSPEGSVALREISrfPLPAPEAAESSLIAPLPGAVRR 610
Cdd:PRK14040 460 VPQAEAAQPAAKAEPAGSETyTVEVEGKAYVVKVSEGGDISQITPAAPAAAPAAAA--AAAPAAAAGEPVTAPLAGNIFK 537
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 759837440 611 VLVVPGQRVRAGELLLTLEAMKLEHPVHAPSAGVVSSLPVQPGAEVDTGELLAVL 665
Cdd:PRK14040 538 VIVTEGQTVAEGDVLLILEAMKMETEIRAAQAGTVRGIAVKEGDAVAVGDTLLTL 592
|
|
| Biotin_lipoyl |
pfam00364 |
Biotin-requiring enzyme; This family covers two Prosite entries, the conserved lysine residue ... |
602-665 |
1.23e-12 |
|
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: 63.39 E-value: 1.23e-12
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 759837440 602 APLPG-----AVRRVLVVPGQRVRAGELLLTLEAMKLEHPVHAPSAGVVSSLPVQPGAEVDTGELLAVL 665
Cdd:pfam00364 5 SPMIGesvreGVVEWLVKVGDKVKAGQPLAEVEAMKMEMEIPAPVAGVVKEILVPEGDTVEVGDPLAKI 73
|
|
| D_ala_D_alaTIGR |
TIGR01205 |
D-alanine--D-alanine ligase; This model describes D-Ala--D-Ala ligase, an enzyme that makes a ... |
115-276 |
3.93e-10 |
|
D-alanine--D-alanine ligase; This model describes D-Ala--D-Ala ligase, an enzyme that makes a required precursor of the bacterial cell wall. It also describes some closely related proteins responsible for resistance to glycopeptide antibiotics such as vancomycin. The mechanism of glyopeptide antibiotic resistance involves the production of D-alanine-D-lactate (VanA and VanB families) or D-alanine-D-serine (VanC). The seed alignment contains only chromosomally encoded D-ala--D-ala ligases, but a number of antibiotic resistance proteins score above the trusted cutoff of this model. [Cell envelope, Biosynthesis and degradation of murein sacculus and peptidoglycan]
Pssm-ID: 273498 [Multi-domain] Cd Length: 315 Bit Score: 61.53 E-value: 3.93e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759837440 115 DKIETKKLVAEARVPVLPT-------FTDPDQVP-------GFPVLIKPAAGSGGTGMRVVRDAGTLAEAVASTrREVGG 180
Cdd:TIGR01205 105 DKLLTKLLWKALGLPTPDYivltqnrASADELECeqvaeplGFPVIVKPAREGSSVGVSKVKSEEELQAALDEA-FEYDE 183
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759837440 181 DVFCEPYVSNvRHIEVPILADAQG----AVIPFGERECSVQRRYQKIVEETPSPA-VNPALREDLCRAAIIAVRALGYVG 255
Cdd:TIGR01205 184 EVLVEQFIKG-RELEVSILGNEEAlpiiEIVPEIEGFYDYEAKYLDGSTEYVIPApLDEELEEKIKELALKAYKALGCRG 262
|
170 180
....*....|....*....|.
gi 759837440 256 AGAVEFLLDSRGDFWFLELTP 276
Cdd:TIGR01205 263 LARVDFFLDEEGEIYLNEINT 283
|
|
| PDHac_trf_long |
TIGR01348 |
pyruvate dehydrogenase complex dihydrolipoamide acetyltransferase, long form; This model ... |
606-666 |
1.40e-04 |
|
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: 44.87 E-value: 1.40e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 759837440 606 GAVRRVLVVPGQRVRAGELLLTLEAMKLEHPVHAPSAGVVSSLPVQPGAEVDTGELLAVLD 666
Cdd:TIGR01348 14 GEVIEVLVKPGDKVEAGQSLITLESDKASMEVPSSAAGIIKEIKVKVGDTLPVGGVIATLE 74
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| PccA |
COG4770 |
Acetyl/propionyl-CoA carboxylase, alpha subunit [Lipid transport and metabolism]; |
1-437 |
0e+00 |
|
Acetyl/propionyl-CoA carboxylase, alpha subunit [Lipid transport and metabolism];
Pssm-ID: 443802 [Multi-domain] Cd Length: 466 Bit Score: 569.65 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759837440 1 MIRRLLVADRGEVARRVFATCRLVGIETVAVYSDADTDAPHVIEADYAVHLPGNTPSATYLQADALIAAAQRAGANAVHP 80
Cdd:COG4770 1 MFKKVLIANRGEIAVRIIRTCRELGIRTVAVYSDADRDALHVRLADEAVCIGPAPAAESYLNIDAIIAAAKATGADAIHP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759837440 81 GIGVLAENSRFAQAVVDAGLIWVGPPPPTLRTLADKIETKKLVAEARVPVLPTFTDPDQVP----------GFPVLIKPA 150
Cdd:COG4770 81 GYGFLSENADFAEACEDAGIVFIGPSPEAIRAMGDKIAAKKLMKAAGVPVVPGSDGPVQDAeealaiaeeiGYPVLIKAS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759837440 151 AGSGGTGMRVVRDAGTLAEAVASTRREVG-----GDVFCEPYVSNVRHIEVPILADAQGAVIPFGERECSVQRRYQKIVE 225
Cdd:COG4770 161 AGGGGKGMRVVRSEEELEEAFESARREAKaafgdDRVYLEKYIERPRHIEVQVLADKHGNVVHLGERDCSIQRRHQKVIE 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759837440 226 ETPSPAVNPALREDLCRAAIIAVRALGYVGAGAVEFLLDSRGDFWFLELTPTLQADHAVTECVSGYDLVRLQLLVAEGGS 305
Cdd:COG4770 241 EAPSPALTEELRERMGEAAVRAAKAVGYVGAGTVEFLVDADGNFYFLEMNTRLQVEHPVTEMVTGIDLVEEQIRIAAGEP 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759837440 306 VPMPG-PPPIRGHAIEVRICAEDPAYAWLPAAGTLHRFAVPDiagefrplpQPGLRLDAGVSDGSVIGMHHDPMLAKLIA 384
Cdd:COG4770 321 LPFTQeDIKLRGHAIECRINAEDPARGFLPSPGTITRLRPPG---------GPGVRVDSGVYEGYEIPPYYDSMIAKLIV 391
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|...
gi 759837440 385 WAPSRQEAARMLASALARTHLHGVVSNRDLLVRVLRHHAFRAGDVDTGFLDRH 437
Cdd:COG4770 392 WGPDREEAIARMRRALAEFVIEGVKTNIPFLRALLAHPDFRAGDVDTGFIERE 444
|
|
| PRK06111 |
PRK06111 |
acetyl-CoA carboxylase biotin carboxylase subunit; Validated |
1-437 |
2.85e-147 |
|
acetyl-CoA carboxylase biotin carboxylase subunit; Validated
Pssm-ID: 180406 [Multi-domain] Cd Length: 450 Bit Score: 435.23 E-value: 2.85e-147
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759837440 1 MIRRLLVADRGEVARRVFATCRLVGIETVAVYSDADTDAPHVIEADYAVHLPGNTPSATYLQADALIAAAQRAGANAVHP 80
Cdd:PRK06111 1 MFQKVLIANRGEIAVRIIRTCQKLGIRTVAIYSEADRDALHVKMADEAYLIGGPRVQESYLNLEKIIEIAKKTGAEAIHP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759837440 81 GIGVLAENSRFAQAVVDAGLIWVGPPPPTLRTLADKIETKKLVAEARVPVLP----TFTDPDQVP------GFPVLIKPA 150
Cdd:PRK06111 81 GYGLLSENASFAERCKEEGIVFIGPSADIIAKMGSKIEARRAMQAAGVPVVPgittNLEDAEEAIaiarqiGYPVMLKAS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759837440 151 AGSGGTGMRVVRDAGTLAEAVASTRREVG-----GDVFCEPYVSNVRHIEVPILADAQGAVIPFGERECSVQRRYQKIVE 225
Cdd:PRK06111 161 AGGGGIGMQLVETEQELTKAFESNKKRAAnffgnGEMYIEKYIEDPRHIEIQLLADTHGNTVYLWERECSVQRRHQKVIE 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759837440 226 ETPSPAVNPALREDLCRAAIIAVRALGYVGAGAVEFLLDSRGDFWFLELTPTLQADHAVTECVSGYDLVRLQLLVAEGGS 305
Cdd:PRK06111 241 EAPSPFLDEETRKAMGERAVQAAKAIGYTNAGTIEFLVDEQKNFYFLEMNTRLQVEHPVTEEITGIDLVEQQLRIAAGEK 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759837440 306 VPMP-GPPPIRGHAIEVRICAEDPAyAWLPAAGTLHRFAVPDiagefrplpQPGLRLDAGVSDGSVIGMHHDPMLAKLIA 384
Cdd:PRK06111 321 LSFTqDDIKRSGHAIEVRIYAEDPK-TFFPSPGKITDLTLPG---------GEGVRHDHAVENGVTVTPFYDPMIAKLIA 390
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|...
gi 759837440 385 WAPSRQEAARMLASALARTHLHGVVSNRDLLVRVLRHHAFRAGDVDTGFLDRH 437
Cdd:PRK06111 391 HGETREEAISRLHDALEELKVEGIKTNIPLLLQVLEDPVFKAGGYTTGFLTKQ 443
|
|
| PRK08591 |
PRK08591 |
acetyl-CoA carboxylase biotin carboxylase subunit; Validated |
1-437 |
3.19e-142 |
|
acetyl-CoA carboxylase biotin carboxylase subunit; Validated
Pssm-ID: 236307 [Multi-domain] Cd Length: 451 Bit Score: 422.29 E-value: 3.19e-142
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759837440 1 MIRRLLVADRGEVARRVFATCRLVGIETVAVYSDADTDAPHVIEADYAVHLpGNTPSA-TYLQADALIAAAQRAGANAVH 79
Cdd:PRK08591 1 MFDKILIANRGEIALRIIRACKELGIKTVAVHSTADRDALHVQLADEAVCI-GPAPSKkSYLNIPAIISAAEITGADAIH 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759837440 80 PGIGVLAENSRFAQAVVDAGLIWVGPPPPTLRTLADKIETKKLVAEARVPVLP----TFTDPDQVP------GFPVLIKP 149
Cdd:PRK08591 80 PGYGFLSENADFAEICEDSGFTFIGPSAETIRLMGDKVTAKATMKKAGVPVVPgsdgPVDDEEEALaiakeiGYPVIIKA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759837440 150 AAGSGGTGMRVVRDAGTLAEAVASTRREVG-----GDVFCEPYVSNVRHIEVPILADAQGAVIPFGERECSVQRRYQKIV 224
Cdd:PRK08591 160 TAGGGGRGMRVVRTEAELEKAFSMARAEAKaafgnPGVYMEKYLENPRHIEIQVLADGHGNAIHLGERDCSLQRRHQKVL 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759837440 225 EETPSPAVNPALREDLCRAAIIAVRALGYVGAGAVEFLLDSRGDFWFLELTPTLQADHAVTECVSGYDLVRLQLLVAEGG 304
Cdd:PRK08591 240 EEAPSPAITEELRRKIGEAAVKAAKAIGYRGAGTIEFLYEKNGEFYFIEMNTRIQVEHPVTEMITGVDLVKEQIRIAAGE 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759837440 305 SVPMPGPP-PIRGHAIEVRICAEDPAYAWLPAAGTLHRFAVPdiAGefrplpqPGLRLDAGVSDGSVIGMHHDPMLAKLI 383
Cdd:PRK08591 320 PLSIKQEDiVFRGHAIECRINAEDPAKNFMPSPGKITRYHPP--GG-------PGVRVDSAVYTGYTIPPYYDSMIGKLI 390
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....
gi 759837440 384 AWAPSRQEAARMLASALARTHLHGVVSNRDLLVRVLRHHAFRAGDVDTGFLDRH 437
Cdd:PRK08591 391 VHGETREEAIARMKRALSEFVIDGIKTTIPLHLRLLNDPNFQAGDYNIHYLEKK 444
|
|
| PRK08654 |
PRK08654 |
acetyl-CoA carboxylase biotin carboxylase subunit; |
1-440 |
1.20e-137 |
|
acetyl-CoA carboxylase biotin carboxylase subunit;
Pssm-ID: 236325 [Multi-domain] Cd Length: 499 Bit Score: 412.45 E-value: 1.20e-137
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759837440 1 MIRRLLVADRGEVARRVFATCRLVGIETVAVYSDADTDAPHVIEADYAVHLPGNTPSATYLQADALIAAAQRAGANAVHP 80
Cdd:PRK08654 1 MFKKILIANRGEIAIRVMRACRELGIKTVAVYSEADKNALFVKYADEAYPIGPAPPSKSYLNIERIIDVAKKAGADAIHP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759837440 81 GIGVLAENSRFAQAVVDAGLIWVGPPPPTLRTLADKIETKKLVAEARVPVLP----TFTDPDQVP------GFPVLIKPA 150
Cdd:PRK08654 81 GYGFLAENPEFAKACEKAGIVFIGPSSDVIEAMGSKINAKKLMKKAGVPVLPgteeGIEDIEEAKeiaeeiGYPVIIKAS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759837440 151 AGSGGTGMRVVRDAGTLAEAVASTRREVG---GD--VFCEPYVSNVRHIEVPILADAQGAVIPFGERECSVQRRYQKIVE 225
Cdd:PRK08654 161 AGGGGIGMRVVYSEEELEDAIESTQSIAQsafGDstVFIEKYLEKPRHIEIQILADKHGNVIHLGDRECSIQRRHQKLIE 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759837440 226 ETPSPAVNPALREDLCRAAIIAVRALGYVGAGAVEFLLDSrGDFWFLELTPTLQADHAVTECVSGYDLVRLQLLVAEGGS 305
Cdd:PRK08654 241 EAPSPIMTPELRERMGEAAVKAAKAINYENAGTVEFLYSN-GNFYFLEMNTRLQVEHPITEMVTGIDIVKEQIKIAAGEE 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759837440 306 VPMPGPP-PIRGHAIEVRICAEDPAYAWLPAAGTLHRFAVPdiAGefrplpqPGLRLDAGVSDGSVIGMHHDPMLAKLIA 384
Cdd:PRK08654 320 LSFKQEDiTIRGHAIECRINAEDPLNDFAPSPGKIKRYRSP--GG-------PGVRVDSGVHMGYEIPPYYDSMISKLIV 390
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*..
gi 759837440 385 WAPSRQEA-ARMlASALARTHLHGVVSNRDLLVRVLRHHAFRAGDVDTGFLDRHPEV 440
Cdd:PRK08654 391 WGRTREEAiARM-RRALYEYVIVGVKTNIPFHKAVMENENFVRGNLHTHFIEEETTI 446
|
|
| PRK12999 |
PRK12999 |
pyruvate carboxylase; Reviewed |
1-442 |
5.35e-135 |
|
pyruvate carboxylase; Reviewed
Pssm-ID: 237263 [Multi-domain] Cd Length: 1146 Bit Score: 424.55 E-value: 5.35e-135
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759837440 1 MIRRLLVADRGEVARRVFATCRLVGIETVAVYSDADTDAPHVIEADYAVHL-PGNTPSATYLQADALIAAAQRAGANAVH 79
Cdd:PRK12999 4 KIKKVLVANRGEIAIRIFRAATELGIRTVAIYSEEDKLSLHRFKADEAYLIgEGKHPVRAYLDIDEIIRVAKQAGVDAIH 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759837440 80 PGIGVLAENSRFAQAVVDAGLIWVGPPPPTLRTLADKIETKKLVAEARVPVLP----TFTDPDQVP------GFPVLIKP 149
Cdd:PRK12999 84 PGYGFLSENPEFARACAEAGITFIGPTAEVLRLLGDKVAARNAAIKAGVPVIPgsegPIDDIEEALefaeeiGYPIMLKA 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759837440 150 AAGSGGTGMRVVRDAGTLAEAVASTRREVG-----GDVFCEPYVSNVRHIEVPILADAQGAVIPFGERECSVQRRYQKIV 224
Cdd:PRK12999 164 SAGGGGRGMRIVRSEEELEEAFERAKREAKaafgnDEVYLEKYVENPRHIEVQILGDKHGNVVHLYERDCSVQRRHQKVV 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759837440 225 EETPSPAVNPALREDLCRAAIIAVRALGYVGAGAVEFLLDSRGDFWFLELTPTLQADHAVTECVSGYDLVRLQLLVAEGG 304
Cdd:PRK12999 244 EIAPAPGLSEELRERICEAAVKLARAVGYVNAGTVEFLVDADGNFYFIEVNPRIQVEHTVTEEVTGIDIVQSQILIAEGA 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759837440 305 SVPMPGPP-------PIRGHAIEVRICAEDPAYAWLPAAGTLHRFAVPdiAGefrplpqPGLRLDAGVS-DGSVIGMHHD 376
Cdd:PRK12999 324 TLHDLEIGipsqediRLRGYAIQCRITTEDPANNFMPDTGRITAYRSP--GG-------FGVRLDGGNAfAGAEITPYYD 394
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 759837440 377 PMLAKLIAWAPSRQEAARMLASALARTHLHGVVSNRDLLVRVLRHHAFRAGDVDTGFLDRHPEVFA 442
Cdd:PRK12999 395 SLLVKLTAWGRTFEQAVARMRRALREFRIRGVKTNIPFLENVLKHPDFRAGDYTTSFIDETPELFD 460
|
|
| PycA |
COG1038 |
Pyruvate carboxylase [Energy production and conversion]; Pyruvate carboxylase is part of the ... |
1-441 |
8.13e-129 |
|
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: 408.31 E-value: 8.13e-129
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759837440 1 MIRRLLVADRGEVARRVFATCRLVGIETVAVYSDADTDAPHVIEADYAVHL-PGNTPSATYLQADALIAAAQRAGANAVH 79
Cdd:COG1038 3 KIKKVLVANRGEIAIRVFRAATELGIRTVAIYSEEDRYSLHRFKADEAYLIgEGKGPVDAYLDIEEIIRVAKEKGVDAIH 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759837440 80 PGIGVLAENSRFAQAVVDAGLIWVGPPPPTLRTLADKIETKKLVAEARVPVLP----TFTDPDQVP------GFPVLIKP 149
Cdd:COG1038 83 PGYGFLSENPEFARACEEAGITFIGPSPEVLEMLGDKVAARAAAIEAGVPVIPgtegPVDDLEEALafaeeiGYPVMLKA 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759837440 150 AAGSGGTGMRVVRDAGTLAEAVASTRREVG-----GDVFCEPYVSNVRHIEVPILADAQGAVIPFGERECSVQRRYQKIV 224
Cdd:COG1038 163 AAGGGGRGMRVVRSEEELEEAFESARREAKaafgdDEVFLEKYIERPKHIEVQILGDKHGNIVHLFERDCSVQRRHQKVV 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759837440 225 EETPSPAVNPALREDLCRAAI-IAvRALGYVGAGAVEFLLDSRGDFWFLELTPTLQADHAVTECVSGYDLVRLQLLVAEG 303
Cdd:COG1038 243 EIAPAPNLDEELREAICEAAVkLA-KAVGYVNAGTVEFLVDDDGNFYFIEVNPRIQVEHTVTEEVTGIDIVQSQILIAEG 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759837440 304 GSVPMP--GPP-----PIRGHAIEVRICAEDPAYAWLPAAGTL--HRFAvpdiAGefrplpqPGLRLDAG-VSDGSVIGM 373
Cdd:COG1038 322 YSLDDPeiGIPsqediRLNGYAIQCRITTEDPANNFMPDTGRItaYRSA----GG-------FGIRLDGGnAYTGAVITP 390
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 759837440 374 HHDPMLAKLIAWAPSRQEAARMLASALARTHLHGVVSNRDLLVRVLRHHAFRAGDVDTGFLDRHPEVF 441
Cdd:COG1038 391 YYDSLLVKVTAWGRTFEEAIRKMRRALREFRIRGVKTNIPFLENVLNHPDFLAGECTTSFIDETPELF 458
|
|
| PRK05586 |
PRK05586 |
acetyl-CoA carboxylase biotin carboxylase subunit; |
1-436 |
1.13e-112 |
|
acetyl-CoA carboxylase biotin carboxylase subunit;
Pssm-ID: 180150 [Multi-domain] Cd Length: 447 Bit Score: 346.31 E-value: 1.13e-112
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759837440 1 MIRRLLVADRGEVARRVFATCRLVGIETVAVYSDADTDAPHVIEADYAVHLPGNTPSATYLQADALIAAAQRAGANAVHP 80
Cdd:PRK05586 1 MFKKILIANRGEIAVRIIRACREMGIETVAVYSEADKDALHVQLADEAVCIGPASSKDSYLNIQNIISATVLTGAQAIHP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759837440 81 GIGVLAENSRFAQAVVDAGLIWVGPPPPTLRTLADKIETKKLVAEARVPVLP----TFTDPDQV------PGFPVLIKPA 150
Cdd:PRK05586 81 GFGFLSENSKFAKMCKECNIVFIGPDSETIELMGNKSNAREIMIKAGVPVVPgsegEIENEEEAleiakeIGYPVMVKAS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759837440 151 AGSGGTGMRVVRDAGTLAEAVASTRREVG---GD--VFCEPYVSNVRHIEVPILADAQGAVIPFGERECSVQRRYQKIVE 225
Cdd:PRK05586 161 AGGGGRGIRIVRSEEELIKAFNTAKSEAKaafGDdsMYIEKFIENPKHIEFQILGDNYGNVVHLGERDCSLQRRNQKVLE 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759837440 226 ETPSPAVNPALREDLCRAAIIAVRALGYVGAGAVEFLLDSRGDFWFLELTPTLQADHAVTECVSGYDLVRLQLLVAEGGS 305
Cdd:PRK05586 241 EAPSPVMTEELRKKMGEIAVKAAKAVNYKNAGTIEFLLDKDGNFYFMEMNTRIQVEHPITEMITGVDLVKEQIKIAYGEK 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759837440 306 VPMPGPP-PIRGHAIEVRICAEDPAYAWLPAAGTLHRFAVPdiAGefrplpqPGLRLDAGVSDGSVIGMHHDPMLAKLIA 384
Cdd:PRK05586 321 LSIKQEDiKINGHSIECRINAEDPKNGFMPCPGKIEELYIP--GG-------LGVRVDSAVYSGYTIPPYYDSMIGKLIV 391
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|..
gi 759837440 385 WAPSRQEAARMLASALARTHLHGVVSNRDLLVRVLRHHAFRAGDVDTGFLDR 436
Cdd:PRK05586 392 YGKDREEAIQKMKRALGEFIIEGVNTNIDFQFIILEDEEFIKGTYDTSFIEK 443
|
|
| PRK12833 |
PRK12833 |
acetyl-CoA carboxylase biotin carboxylase subunit; Provisional |
2-435 |
1.06e-109 |
|
acetyl-CoA carboxylase biotin carboxylase subunit; Provisional
Pssm-ID: 183781 [Multi-domain] Cd Length: 467 Bit Score: 339.42 E-value: 1.06e-109
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759837440 2 IRRLLVADRGEVARRVFATCRLVGIETVAVYSDADTDAPHVIEADYAVHLPGNTPSATYLQADALIAAAQRAGANAVHPG 81
Cdd:PRK12833 5 IRKVLVANRGEIAVRIIRAARELGMRTVAACSDADRDSLAARMADEAVHIGPSHAAKSYLNPAAILAAARQCGADAIHPG 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759837440 82 IGVLAENSRFAQAVVDAGLIWVGPPPPTLRTLADKIETKKLVAEARVPVLP----TFTDPD------QVPGFPVLIKPAA 151
Cdd:PRK12833 85 YGFLSENAAFAEAVEAAGLIFVGPDAQTIRTMGDKARARRTARRAGVPTVPgsdgVVASLDaalevaARIGYPLMIKAAA 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759837440 152 GSGGTGMRVVRDAGTLAEAVASTRREV-----GGDVFCEPYVSNVRHIEVPILADAQGAVIPFgERECSVQRRYQKIVEE 226
Cdd:PRK12833 165 GGGGRGIRVAHDAAQLAAELPLAQREAqaafgDGGVYLERFIARARHIEVQILGDGERVVHLF-ERECSLQRRRQKILEE 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759837440 227 TPSPAVNPALREDLCRAAIIAVRALGYVGAGAVEFLLD-SRGDFWFLELTPTLQADHAVTECVSGYDLVRLQLLVAEGGS 305
Cdd:PRK12833 244 APSPSLTPAQRDALCASAVRLARQVGYRGAGTLEYLFDdARGEFYFIEMNTRIQVEHPVTEAITGIDLVQEMLRIADGEP 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759837440 306 VPM-PGPPPIRGHAIEVRICAEDPAYAWLPAAGTLHRFAVPDiagefrplpQPGLRLDAGVSDGSVIGMHHDPMLAKLIA 384
Cdd:PRK12833 324 LRFaQGDIALRGAALECRINAEDPLRDFFPNPGRIDALVWPQ---------GPGVRVDSLLYPGYRVPPFYDSLLAKLIV 394
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|.
gi 759837440 385 WAPSRQEAARMLASALARTHLHGVVSNRDLLVRVLRHHAFRAGDVDTGFLD 435
Cdd:PRK12833 395 HGEDRAAALARAARALRELRIDGMKTTAPLHRALLADADVRAGRFHTNFLE 445
|
|
| PRK07178 |
PRK07178 |
acetyl-CoA carboxylase biotin carboxylase subunit; |
1-439 |
1.19e-109 |
|
acetyl-CoA carboxylase biotin carboxylase subunit;
Pssm-ID: 180865 [Multi-domain] Cd Length: 472 Bit Score: 339.39 E-value: 1.19e-109
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759837440 1 MIRRLLVADRGEVARRVFATCRLVGIETVAVYSDADTDAPHVIEADYAVHLpGNTPSATYLQADALIAAAQRAGANAVHP 80
Cdd:PRK07178 1 MIKKILIANRGEIAVRIVRACAEMGIRSVAIYSEADRHALHVKRADEAYSI-GADPLAGYLNPRRLVNLAVETGCDALHP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759837440 81 GIGVLAENSRFAQAVVDAGLIWVGPPPPTLRTLADKIETKKLVAEARVPVLP-----------TFTDPDQVpGFPVLIKP 149
Cdd:PRK07178 80 GYGFLSENAELAEICAERGIKFIGPSAEVIRRMGDKTEARRAMIKAGVPVTPgsegnladldeALAEAERI-GYPVMLKA 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759837440 150 AAGSGGTGMRVVRDAGTLAEAVASTRREV-----GGDVFCEPYVSNVRHIEVPILADAQGAVIPFGERECSVQRRYQKIV 224
Cdd:PRK07178 159 TSGGGGRGIRRCNSREELEQNFPRVISEAtkafgSAEVFLEKCIVNPKHIEVQILADSHGNVVHLFERDCSIQRRNQKLI 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759837440 225 EETPSPAVNPALREDLCRAAIIAVRALGYVGAGAVEFLLDSRGDFWFLELTPTLQADHAVTECVSGYDLVRLQLLVAEGG 304
Cdd:PRK07178 239 EIAPSPQLTPEQRAYIGDLAVRAAKAVGYENAGTVEFLLDADGEVYFMEMNTRVQVEHTITEEITGIDIVREQIRIASGL 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759837440 305 SVPMPGPP-PIRGHAIEVRICAEDPAYAWLPAAGTLHRFAVPDiagefrplpQPGLRLDAGVSDGSVIGMHHDPMLAKLI 383
Cdd:PRK07178 319 PLSYKQEDiQHRGFALQFRINAEDPKNDFLPSFGKITRYYAPG---------GPGVRTDTAIYTGYTIPPYYDSMCAKLI 389
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*.
gi 759837440 384 AWAPSRQEAARMLASALARTHLHGVVSNRDLLVRVLRHHAFRAGDVDTGFLDRHPE 439
Cdd:PRK07178 390 VWALTWEEALDRGRRALDDMRVQGVKTTIPYYQEILRNPEFRSGQFNTSFVESHPE 445
|
|
| PRK08462 |
PRK08462 |
acetyl-CoA carboxylase biotin carboxylase subunit; |
2-437 |
3.20e-104 |
|
acetyl-CoA carboxylase biotin carboxylase subunit;
Pssm-ID: 236269 [Multi-domain] Cd Length: 445 Bit Score: 324.39 E-value: 3.20e-104
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759837440 2 IRRLLVADRGEVARRVFATCRLVGIETVAVYSDADTDAPHVIEADYAVHLPGNTPSATYLQADALIAAAQRAGANAVHPG 81
Cdd:PRK08462 4 IKRILIANRGEIALRAIRTIQEMGKEAIAIYSTADKDALYLKYADAKICIGGAKSSESYLNIPAIISAAEIFEADAIFPG 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759837440 82 IGVLAENSRFAQAVVDAGLIWVGPPPPTLRTLADKIETKKLVAEARVPVLP----TFTDPDQVP------GFPVLIKPAA 151
Cdd:PRK08462 84 YGFLSENQNFVEICSHHNIKFIGPSVEVMALMSDKSKAKEVMKRAGVPVIPgsdgALKSYEEAKkiakeiGYPVILKAAA 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759837440 152 GSGGTGMRVVRDAGTLAEAVASTRREV-----GGDVFCEPYVSNVRHIEVPILADAQGAVIPFGERECSVQRRYQKIVEE 226
Cdd:PRK08462 164 GGGGRGMRVVEDESDLENLYLAAESEAlsafgDGTMYMEKFINNPRHIEVQILGDKHGNVIHVGERDCSLQRRHQKLIEE 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759837440 227 TPSPAVNPALREDLCRAAIIAVRALGYVGAGAVEFLLDSRGDFWFLELTPTLQADHAVTECVSGYDLVRLQLLVAEGGSV 306
Cdd:PRK08462 244 SPAVVLDEKTRERLHETAIKAAKAIGYEGAGTFEFLLDSNLDFYFMEMNTRLQVEHTVSEMVSGLDLIEWMIKIAEGEEL 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759837440 307 PMPGPPPIRGHAIEVRICAEDPAyAWLPAAGTLHRFAVPdiAGEfrplpqpGLRLDAGVSDGSVIGMHHDPMLAKLIAWA 386
Cdd:PRK08462 324 PSQESIKLKGHAIECRITAEDPK-KFYPSPGKITKWIAP--GGR-------NVRMDSHAYAGYVVPPYYDSMIGKLIVWG 393
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|.
gi 759837440 387 PSRQEAARMLASALARTHLHGVVSNRDLLVRVLRHHAFRAGDVDTGFLDRH 437
Cdd:PRK08462 394 EDRNRAIAKMKRALKEFKVEGIKTTIPFHLEMMENADFINNKYDTKYLEEH 444
|
|
| PRK08463 |
PRK08463 |
acetyl-CoA carboxylase subunit A; Validated |
1-437 |
1.64e-97 |
|
acetyl-CoA carboxylase subunit A; Validated
Pssm-ID: 169452 [Multi-domain] Cd Length: 478 Bit Score: 307.90 E-value: 1.64e-97
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759837440 1 MIRRLLVADRGEVARRVFATCRLVGIETVAVYSDADTDAPHVIEADYAvHLPGNTPSATYLQADALIAAAQRAGANAVHP 80
Cdd:PRK08463 1 MIHKILIANRGEIAVRVIRACRDLHIKSVAIYTEPDRECLHVKIADEA-YRIGTDPIKGYLDVKRIVEIAKACGADAIHP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759837440 81 GIGVLAENSRFAQAVVDAGLIWVGPPPPTLRTLADKIETKKLVAEARVPVLPTfTDP------DQVP------GFPVLIK 148
Cdd:PRK08463 80 GYGFLSENYEFAKAVEDAGIIFIGPKSEVIRKMGNKNIARYLMKKNGIPIVPG-TEKlnsesmEEIKifarkiGYPVILK 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759837440 149 PAAGSGGTGMRVVRDAGTLAEAVASTRREV-----GGDVFCEPYVSNVRHIEVPILADAQGAVIPFGERECSVQRRYQKI 223
Cdd:PRK08463 159 ASGGGGGRGIRVVHKEEDLENAFESCKREAlayfnNDEVFMEKYVVNPRHIEFQILGDNYGNIIHLCERDCSIQRRHQKV 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759837440 224 VEETPSPAVNPALREDLCRAAIIAVRALGYVGAGAVEFLLDSRGDFWFLELTPTLQADHAVTECVSGYDLVRLQLLVAEG 303
Cdd:PRK08463 239 IEIAPCPSISDNLRKTMGVTAVAAAKAVGYTNAGTIEFLLDDYNRFYFMEMNTRIQVEHGVTEEITGIDLIVRQIRIAAG 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759837440 304 GSVPMPGPP-PIRGHAIEVRICAEDPAYAWLPAAGTLhrfavpdiaGEFRPLPQPGLRLDAGVSDGSVIGMHHDPMLAKL 382
Cdd:PRK08463 319 EILDLEQSDiKPRGFAIEARITAENVWKNFIPSPGKI---------TEYYPALGPSVRVDSHIYKDYTIPPYYDSMLAKL 389
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*
gi 759837440 383 IAWAPSRQEAARMLASALARTHLHGVVSNRDLLVRVLRHHAFRAGDVDTGFLDRH 437
Cdd:PRK08463 390 IVKATSYDLAVNKLERALKEFVIDGIRTTIPFLIAITKTREFRRGYFDTSYIETH 444
|
|
| CPSase_L_D2 |
pfam02786 |
Carbamoyl-phosphate synthase L chain, ATP binding domain; Carbamoyl-phosphate synthase ... |
115-307 |
3.45e-54 |
|
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: 184.43 E-value: 3.45e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759837440 115 DKIETKKLVAEARVPVLPTFTDP-----------DQVpGFPVLIKPAAGSGGTGMRVVRDAGTLAEAVASTRREVG---- 179
Cdd:pfam02786 1 DKVLFKAAMKEAGVPTVPGTAGPveteeealaaaKEI-GYPVIIKAAFGGGGLGMGIARNEEELAELFALALAEAPaafg 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759837440 180 -GDVFCEPYVSNVRHIEVPILADAQGAVIPFGERECSVQRRYQKIVEETPSPAVNPALREDLCRAAIIAVRALGYVGAGA 258
Cdd:pfam02786 80 nPQVLVEKSLKGPKHIEYQVLRDAHGNCITVCNRECSDQRRTQKSIEVAPSQTLTDEERQMLREAAVKIARHLGYVGAGT 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 759837440 259 VEFLLDSR-GDFWFLELTPTLQADHAVTECVSGYDLVRLQLLVAEGGSVP 307
Cdd:pfam02786 160 VEFALDPFsGEYYFIEMNTRLQVEHALAEKATGYDLAKEAAKIALGYPLP 209
|
|
| Biotin_carb_C |
smart00878 |
Biotin carboxylase C-terminal domain; Biotin carboxylase is a component of the acetyl-CoA ... |
320-435 |
3.14e-41 |
|
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: 145.25 E-value: 3.14e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759837440 320 EVRICAEDPAYAWLPAAGTLHRFAVPDiagefrplpQPGLRLDAGVSDGSVIGMHHDPMLAKLIAWAPSRQEAARMLASA 399
Cdd:smart00878 1 ECRINAEDPANGFLPSPGRITRYRFPG---------GPGVRVDSGVYEGYEVPPYYDSMIAKLIVWGEDREEAIARLRRA 71
|
90 100 110
....*....|....*....|....*....|....*.
gi 759837440 400 LARTHLHGVVSNRDLLVRVLRHHAFRAGDVDTGFLD 435
Cdd:smart00878 72 LDEFRIRGVKTNIPFLRALLRHPDFRAGDVDTGFLE 107
|
|
| Biotin_carb_N |
pfam00289 |
Biotin carboxylase, N-terminal domain; This domain is structurally related to the PreATP-grasp ... |
2-107 |
1.03e-39 |
|
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: 141.08 E-value: 1.03e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759837440 2 IRRLLVADRGEVARRVFATCRLVGIETVAVYSDADTDAPHVIEADYAVHLPGNTPSATYLQADALIAAAQRAGANAVHPG 81
Cdd:pfam00289 1 IKKVLIANRGEIAVRIIRACRELGIRTVAVYSEADANSLHVRLADEAVCLGPGPASESYLNIDAIIDAAKETGADAIHPG 80
|
90 100
....*....|....*....|....*.
gi 759837440 82 IGVLAENSRFAQAVVDAGLIWVGPPP 107
Cdd:pfam00289 81 YGFLSENAEFARACEEAGIIFIGPSP 106
|
|
| Biotin_carb_C |
pfam02785 |
Biotin carboxylase C-terminal domain; Biotin carboxylase is a component of the acetyl-CoA ... |
320-436 |
9.16e-37 |
|
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: 133.00 E-value: 9.16e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759837440 320 EVRICAEDPAYAWLPAAGTLHRFAVPDiagefrplpQPGLRLDAGVSDGSVIGMHHDPMLAKLIAWAPSRQEAARMLASA 399
Cdd:pfam02785 1 EARIYAEDPDNNFLPSPGKVTRYRFPG---------GPGVRVDSGVYAGYTVSPYYDSMIAKLIVHGPTREEAIARLRRA 71
|
90 100 110
....*....|....*....|....*....|....*..
gi 759837440 400 LARTHLHGVVSNRDLLVRVLRHHAFRAGDVDTGFLDR 436
Cdd:pfam02785 72 LAEFRIEGVKTNIPFLRAILEHPDFRAGEVDTGFLEE 108
|
|
| AccC |
COG0439 |
Biotin carboxylase [Lipid transport and metabolism]; Biotin carboxylase is part of the Pathway ... |
79-309 |
2.00e-34 |
|
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: 131.92 E-value: 2.00e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759837440 79 HPGIGVLAEN----SRFAQAVVDAGLIwvGPPPPTLRTLADKIETKKLVAEARVPVLPT--FTDPDQVP------GFPVL 146
Cdd:COG0439 16 TGIDAVLSESefavETAAELAEELGLP--GPSPEAIRAMRDKVLMREALAAAGVPVPGFalVDSPEEALafaeeiGYPVV 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759837440 147 IKPAAGSGGTGMRVVRDAGTLAEAVASTRREV-----GGDVFCEPYVSNvRHIEVPILADaQGAVIPfgereCSVQRRYQ 221
Cdd:COG0439 94 VKPADGAGSRGVRVVRDEEELEAALAEARAEAkagspNGEVLVEEFLEG-REYSVEGLVR-DGEVVV-----CSITRKHQ 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759837440 222 K---IVE---ETPSPaVNPALREDLCRAAIIAVRALGYV-GAGAVEFLLDSRGDFWFLELTPTLQADHA--VTECVSGYD 292
Cdd:COG0439 167 KppyFVElghEAPSP-LPEELRAEIGELVARALRALGYRrGAFHTEFLLTPDGEPYLIEINARLGGEHIppLTELATGVD 245
|
250
....*....|....*..
gi 759837440 293 LVRLQLLVAEGGSVPMP 309
Cdd:COG0439 246 LVREQIRLALGEPRILD 262
|
|
| biotinyl_domain |
cd06850 |
The biotinyl-domain or biotin carboxyl carrier protein (BCCP) domain is present in all ... |
600-665 |
1.41e-21 |
|
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: 88.63 E-value: 1.41e-21
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 759837440 600 LIAPLPGAVRRVLVVPGQRVRAGELLLTLEAMKLEHPVHAPSAGVVSSLPVQPGAEVDTGELLAVL 665
Cdd:cd06850 2 VTAPMPGTVVKVLVKEGDKVEAGQPLAVLEAMKMENEVTAPVAGVVKEILVKEGDQVEAGQLLVVI 67
|
|
| PRK12999 |
PRK12999 |
pyruvate carboxylase; Reviewed |
602-667 |
6.46e-18 |
|
pyruvate carboxylase; Reviewed
Pssm-ID: 237263 [Multi-domain] Cd Length: 1146 Bit Score: 88.27 E-value: 6.46e-18
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 759837440 602 APLPGAVRRVLVVPGQRVRAGELLLTLEAMKLEHPVHAPSAGVVSSLPVQPGAEVDTGELLAVLDP 667
Cdd:PRK12999 1081 APMPGSVVTVLVKEGDEVKAGDPLAVIEAMKMETTITAPVDGTVKRVLVKAGDQVEAGDLLVELEP 1146
|
|
| PycA |
COG1038 |
Pyruvate carboxylase [Energy production and conversion]; Pyruvate carboxylase is part of the ... |
602-665 |
7.02e-18 |
|
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: 88.21 E-value: 7.02e-18
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 759837440 602 APLPGAVRRVLVVPGQRVRAGELLLTLEAMKLEHPVHAPSAGVVSSLPVQPGAEVDTGELLAVL 665
Cdd:COG1038 1081 APMPGTVVKVLVKEGDEVKKGDPLLTIEAMKMETTITAPRDGTVKEVLVKEGDQVEAGDLLIEL 1144
|
|
| PRK14040 |
PRK14040 |
oxaloacetate decarboxylase subunit alpha; |
532-665 |
5.76e-17 |
|
oxaloacetate decarboxylase subunit alpha;
Pssm-ID: 237592 [Multi-domain] Cd Length: 593 Bit Score: 84.60 E-value: 5.76e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759837440 532 APVADEHPPVVVVQAGSGRV-VLNVQGIRLAVHVHRVGDVSYVDSPEGSVALREISrfPLPAPEAAESSLIAPLPGAVRR 610
Cdd:PRK14040 460 VPQAEAAQPAAKAEPAGSETyTVEVEGKAYVVKVSEGGDISQITPAAPAAAPAAAA--AAAPAAAAGEPVTAPLAGNIFK 537
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 759837440 611 VLVVPGQRVRAGELLLTLEAMKLEHPVHAPSAGVVSSLPVQPGAEVDTGELLAVL 665
Cdd:PRK14040 538 VIVTEGQTVAEGDVLLILEAMKMETEIRAAQAGTVRGIAVKEGDAVAVGDTLLTL 592
|
|
| PylC |
COG2232 |
Pyrrolysine biosynthesis ligase PylC and related enzymes, ATP-grasp superfamily [Amino acid ... |
3-402 |
1.54e-16 |
|
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: 81.89 E-value: 1.54e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759837440 3 RRLLVAdrGEVARRVFATCRLVGIETVAV--YSDADTDAPhvieADYAVHLPGNTPSATYLQ-ADALIAAAQRAGANAVH 79
Cdd:COG2232 5 PDLLIA--GFSARALAQSARRAGYRVYAVdlFADLDTRAL----AERWVRLDAESCGFDLEDlPAALLELAAADDPDGLV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759837440 80 PGIGvlAENSRFAQAVVDAGLIWVGPPPPTLRTLADKIETKKLVAEARVPVLPTFTDPDQVPgFPVLIKPAAGSGGTGMR 159
Cdd:COG2232 79 YGSG--FENFPELLERLARRLPLLGNPPEVVRRVKDPLRFFALLDELGIPHPETRFEPPPDP-GPWLVKPIGGAGGWHIR 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759837440 160 VVRDAGTLAEavastrrevgGDVFCEpYVSNvRHIEVPILADAQGA-VIPFGErecsvqrryQKIVEETPSP-------- 230
Cdd:COG2232 156 PADSEAPPAP----------GRYFQR-YVEG-TPASVLFLADGSDArVLGFNR---------QLIGPAGERPfryggnig 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759837440 231 --AVNPALREDLCRAAIIAVRALGYVGAGAVEFLLDSrGDFWFLELTPTLQADHAVTECVSGYDLVRLQLLvAEGGSVPM 308
Cdd:COG2232 215 plALPPALAEEMRAIAEALVAALGLVGLNGVDFILDG-DGPYVLEVNPRPQASLDLYEDATGGNLFDAHLR-ACRGELPE 292
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759837440 309 PGPPPIRGHAIEvRICaedpaYAwlPAAGTL-HRFAVPDIAgefRPLPQPGLRLDAGvsdgsvigmhhDPmLAKLIAWAP 387
Cdd:COG2232 293 VPRPKPRRVAAK-AIL-----YA--PRDLTIpDDLSWPPWV---ADIPAPGTRIEKG-----------EP-VCTVLAEGP 349
|
410
....*....|....*
gi 759837440 388 SRQEAARMLASALAR 402
Cdd:COG2232 350 TAEAARALLERRAEE 364
|
|
| PRK09282 |
PRK09282 |
pyruvate carboxylase subunit B; Validated |
581-667 |
9.08e-16 |
|
pyruvate carboxylase subunit B; Validated
Pssm-ID: 236449 [Multi-domain] Cd Length: 592 Bit Score: 80.66 E-value: 9.08e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759837440 581 ALREISRFPLPAPEAaESSLIAPLPGAVRRVLVVPGQRVRAGELLLTLEAMKLEHPVHAPSAGVVSSLPVQPGAEVDTGE 660
Cdd:PRK09282 507 PLKEIVVGGRPRASA-PGAVTSPMPGTVVKVKVKEGDKVKAGDTVLVLEAMKMENEIQAPVDGTVKEILVKEGDRVNPGD 585
|
....*..
gi 759837440 661 LLAVLDP 667
Cdd:PRK09282 586 VLMEIEP 592
|
|
| PRK05641 |
PRK05641 |
putative acetyl-CoA carboxylase biotin carboxyl carrier protein subunit; Validated |
589-662 |
5.12e-15 |
|
putative acetyl-CoA carboxylase biotin carboxyl carrier protein subunit; Validated
Pssm-ID: 235540 [Multi-domain] Cd Length: 153 Bit Score: 72.97 E-value: 5.12e-15
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 759837440 589 PLPAPEAA-ESSLIAPLPGAVRRVLVVPGQRVRAGELLLTLEAMKLEHPVHAPSAGVVSSLPVQPGAEVDTGELL 662
Cdd:PRK05641 75 PAPAPASAgENVVTAPMPGKILRILVREGQQVKVGQGLLILEAMKMENEIPAPKDGVVKKILVKEGDTVDTGQPL 149
|
|
| DdlA |
COG1181 |
D-alanine-D-alanine ligase or related ATP-grasp enzyme [Cell wall/membrane/envelope biogenesis, ... |
103-277 |
1.91e-14 |
|
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: 74.37 E-value: 1.91e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759837440 103 VGPPPPTLRTLADKIETKKLVAEARVPVLP--TFTDPDQVP--------GFPVLIKPAAGSGGTGMRVVRDAGTLAEAVA 172
Cdd:COG1181 83 TGSGVLASALAMDKALTKRVLAAAGLPTPPyvVLRRGELADleaieeelGLPLFVKPAREGSSVGVSKVKNAEELAAALE 162
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759837440 173 sTRREVGGDVFCEPYVSNvRHIEVPILADAQGAVIPFGERE-----CSVQRRYQ--KIVEETPSPaVNPALREDLCRAAI 245
Cdd:COG1181 163 -EAFKYDDKVLVEEFIDG-REVTVGVLGNGGPRALPPIEIVpengfYDYEAKYTdgGTEYICPAR-LPEELEERIQELAL 239
|
170 180 190
....*....|....*....|....*....|....*...
gi 759837440 246 IAVRALGYVGAGAVEFLLDSRGDFWFLE------LTPT 277
Cdd:COG1181 240 KAFRALGCRGYARVDFRLDEDGEPYLLEvntlpgMTPT 277
|
|
| AccB |
COG0511 |
Biotin carboxyl carrier protein [Lipid transport and metabolism]; Biotin carboxyl carrier ... |
562-666 |
4.49e-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: 69.54 E-value: 4.49e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759837440 562 VHVHRVGDVSY--VDSPEGSVALREISRFPLPAPEAAESSLI-APLPGAVRR-------VLVVPGQRVRAGELLLTLEAM 631
Cdd:COG0511 22 VRIKRGGAAAAapVAAPAAAAPAAAAPAAAAAAAAASGGGAVkSPMVGTFYRapspgakPFVKVGDKVKAGDTLCIIEAM 101
|
90 100 110
....*....|....*....|....*....|....*
gi 759837440 632 KLEHPVHAPSAGVVSSLPVQPGAEVDTGELLAVLD 666
Cdd:COG0511 102 KMMNEIEAPVSGTVVEILVENGQPVEYGQPLFVIE 136
|
|
| Biotin_lipoyl |
pfam00364 |
Biotin-requiring enzyme; This family covers two Prosite entries, the conserved lysine residue ... |
602-665 |
1.23e-12 |
|
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: 63.39 E-value: 1.23e-12
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 759837440 602 APLPG-----AVRRVLVVPGQRVRAGELLLTLEAMKLEHPVHAPSAGVVSSLPVQPGAEVDTGELLAVL 665
Cdd:pfam00364 5 SPMIGesvreGVVEWLVKVGDKVKAGQPLAEVEAMKMEMEIPAPVAGVVKEILVPEGDTVEVGDPLAKI 73
|
|
| PRK06549 |
PRK06549 |
acetyl-CoA carboxylase biotin carboxyl carrier protein subunit; Validated |
589-662 |
4.34e-11 |
|
acetyl-CoA carboxylase biotin carboxyl carrier protein subunit; Validated
Pssm-ID: 235826 [Multi-domain] Cd Length: 130 Bit Score: 60.98 E-value: 4.34e-11
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 759837440 589 PLPAPEAAESSLIAPLPGAVRRVLVVPGQRVRAGELLLTLEAMKLEHPVHAPSAGVVSSLPVQPGAEVDTGELL 662
Cdd:PRK06549 53 PQPAAAAGADAMPSPMPGTILKVLVAVGDQVTENQPLLILEAMKMENEIVASSAGTVTAIHVTPGQVVNPGDGL 126
|
|
| COG3919 |
COG3919 |
Predicted ATP-dependent carboligase, ATP-grasp superfamily [General function prediction only]; |
105-307 |
2.24e-10 |
|
Predicted ATP-dependent carboligase, ATP-grasp superfamily [General function prediction only];
Pssm-ID: 443124 [Multi-domain] Cd Length: 382 Bit Score: 63.02 E-value: 2.24e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759837440 105 PPPPTLRTLADKIETKKLVAEARVPV-----LPTFTDPDQVP---GFPVLIKPAAGS--------GGTGMRVVRDAGTLA 168
Cdd:COG3919 107 PDADLLDRLLDKERFYELAEELGVPVpktvvLDSADDLDALAedlGFPVVVKPADSVgydelsfpGKKKVFYVDDREELL 186
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759837440 169 EAVAsTRREVGGDVFCEPYVSNVRHIEVPI--LADAQGAVIPFgerecSVQRRyqkiVEETPSPAVNPALRE-----DLC 241
Cdd:COG3919 187 ALLR-RIAAAGYELIVQEYIPGDDGEMRGLtaYVDRDGEVVAT-----FTGRK----LRHYPPAGGNSAAREsvddpELE 256
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 759837440 242 RAAIIAVRALGYVGAGAVEFLLDSR-GDFWFLELTPTLQADHAVTeCVSGYDLVRLQLLVAEGGSVP 307
Cdd:COG3919 257 EAARRLLEALGYHGFANVEFKRDPRdGEYKLIEINPRFWRSLYLA-TAAGVNFPYLLYDDAVGRPLE 322
|
|
| PRK08225 |
PRK08225 |
acetyl-CoA carboxylase biotin carboxyl carrier protein subunit; Validated |
598-666 |
3.63e-10 |
|
acetyl-CoA carboxylase biotin carboxyl carrier protein subunit; Validated
Pssm-ID: 181304 [Multi-domain] Cd Length: 70 Bit Score: 56.33 E-value: 3.63e-10
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 759837440 598 SSLIAPLPGAVRRVLVVPGQRVRAGELLLTLEAMKLEHPVHAPSAGVVSSLPVQPGAEVDTGELLAVLD 666
Cdd:PRK08225 2 TKVYASMAGNVWKIVVKVGDTVEEGQDVVILESMKMEIPIVAEEAGTVKKINVQEGDFVNEGDVLLEIE 70
|
|
| D_ala_D_alaTIGR |
TIGR01205 |
D-alanine--D-alanine ligase; This model describes D-Ala--D-Ala ligase, an enzyme that makes a ... |
115-276 |
3.93e-10 |
|
D-alanine--D-alanine ligase; This model describes D-Ala--D-Ala ligase, an enzyme that makes a required precursor of the bacterial cell wall. It also describes some closely related proteins responsible for resistance to glycopeptide antibiotics such as vancomycin. The mechanism of glyopeptide antibiotic resistance involves the production of D-alanine-D-lactate (VanA and VanB families) or D-alanine-D-serine (VanC). The seed alignment contains only chromosomally encoded D-ala--D-ala ligases, but a number of antibiotic resistance proteins score above the trusted cutoff of this model. [Cell envelope, Biosynthesis and degradation of murein sacculus and peptidoglycan]
Pssm-ID: 273498 [Multi-domain] Cd Length: 315 Bit Score: 61.53 E-value: 3.93e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759837440 115 DKIETKKLVAEARVPVLPT-------FTDPDQVP-------GFPVLIKPAAGSGGTGMRVVRDAGTLAEAVASTrREVGG 180
Cdd:TIGR01205 105 DKLLTKLLWKALGLPTPDYivltqnrASADELECeqvaeplGFPVIVKPAREGSSVGVSKVKSEEELQAALDEA-FEYDE 183
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759837440 181 DVFCEPYVSNvRHIEVPILADAQG----AVIPFGERECSVQRRYQKIVEETPSPA-VNPALREDLCRAAIIAVRALGYVG 255
Cdd:TIGR01205 184 EVLVEQFIKG-RELEVSILGNEEAlpiiEIVPEIEGFYDYEAKYLDGSTEYVIPApLDEELEEKIKELALKAYKALGCRG 262
|
170 180
....*....|....*....|.
gi 759837440 256 AGAVEFLLDSRGDFWFLELTP 276
Cdd:TIGR01205 263 LARVDFFLDEEGEIYLNEINT 283
|
|
| Dala_Dala_lig_C |
pfam07478 |
D-ala D-ala ligase C-terminus; This family represents the C-terminal, catalytic domain of the ... |
142-276 |
5.92e-08 |
|
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: 53.47 E-value: 5.92e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759837440 142 GFPVLIKPAAGSGGTGMRVVRDAGTLAEAVASTRREvGGDVFCEPYVSNvRHIEVPILADAQGAVIPFGERECSV----- 216
Cdd:pfam07478 36 GYPVFVKPARLGSSVGVSKVESREELQAAIEEAFQY-DEKVLVEEGIEG-REIECAVLGNEDPEVSPVGEIVPSGgfydy 113
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 759837440 217 QRRYQKIVEETPSPA-VNPALREDLCRAAIIAVRALGYVGAGAVEFLLDSRGDFWFLELTP 276
Cdd:pfam07478 114 EAKYIDDSAQIVVPAdLEEEQEEQIQELALKAYKALGCRGLARVDFFLTEDGEIVLNEVNT 174
|
|
| ddl |
PRK01372 |
D-alanine--D-alanine ligase; Reviewed |
115-273 |
1.20e-07 |
|
D-alanine--D-alanine ligase; Reviewed
Pssm-ID: 234948 [Multi-domain] Cd Length: 304 Bit Score: 53.96 E-value: 1.20e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759837440 115 DKIETKKLVAEARVPV-----LPTFTDPDQVP---GFPVLIKPAAGSGGTGMRVVRDAGTLAEAVASTRReVGGDVFCEP 186
Cdd:PRK01372 98 DKLRTKLVWQAAGLPTppwivLTREEDLLAAIdklGLPLVVKPAREGSSVGVSKVKEEDELQAALELAFK-YDDEVLVEK 176
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759837440 187 YVSNvRHIEVPILADAQGAVIpfgeRECSVQRRY-----------QKIVeetPSPaVNPALREDLCRAAIIAVRALGYVG 255
Cdd:PRK01372 177 YIKG-RELTVAVLGGKALPVI----EIVPAGEFYdyeakylaggtQYIC---PAG-LPAEIEAELQELALKAYRALGCRG 247
|
170
....*....|....*...
gi 759837440 256 AGAVEFLLDSRGDFWFLE 273
Cdd:PRK01372 248 WGRVDFMLDEDGKPYLLE 265
|
|
| PRK07051 |
PRK07051 |
biotin carboxyl carrier domain-containing protein; |
596-666 |
6.09e-07 |
|
biotin carboxyl carrier domain-containing protein;
Pssm-ID: 180811 [Multi-domain] Cd Length: 80 Bit Score: 47.31 E-value: 6.09e-07
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 759837440 596 AESSLIAPLPGAVRR-------VLVVPGQRVRAGELLLTLEAMKLEHPVHAPSAGVVSSLPVQPGAEVDTGELLAVLD 666
Cdd:PRK07051 2 AQHEIVSPLPGTFYRrpspdapPYVEVGDAVAAGDVVGLIEVMKQFTEVEAEAAGRVVEFLVEDGEPVEAGQVLARIE 79
|
|
| PurK |
COG0026 |
Phosphoribosylaminoimidazole carboxylase (NCAIR synthetase) [Nucleotide transport and ... |
105-276 |
6.82e-07 |
|
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: 52.00 E-value: 6.82e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759837440 105 PPPPTLRTLADKIETKKLVAEARVPVLP--TFTDPDQVP------GFPVLIKPAA-GSGGTGMRVVRDAGTLAEAVAstr 175
Cdd:COG0026 79 PGPEALEIAQDRLLEKAFLAELGIPVAPfaAVDSLEDLEaaiaelGLPAVLKTRRgGYDGKGQVVIKSAADLEAAWA--- 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759837440 176 rEVGGDvfcePYVsnvrhIEvpiladaqgAVIPFgERECSVQ--RR-------------YQK--IVEETPSPA-VNPALR 237
Cdd:COG0026 156 -ALGGG----PCI-----LE---------EFVPF-ERELSVIvaRSpdgevatypvvenVHRngILDESIAPArISEALA 215
|
170 180 190
....*....|....*....|....*....|....*....
gi 759837440 238 EDLCRAAIIAVRALGYVGAGAVEFLLDSRGDFWFLELTP 276
Cdd:COG0026 216 AEAEEIAKRIAEALDYVGVLAVEFFVTKDGELLVNEIAP 254
|
|
| PRK02186 |
PRK02186 |
argininosuccinate lyase; Provisional |
104-402 |
2.09e-06 |
|
argininosuccinate lyase; Provisional
Pssm-ID: 235010 [Multi-domain] Cd Length: 887 Bit Score: 51.00 E-value: 2.09e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759837440 104 GPPPPTLRTLADKIETKKLVAEARVPVLPTF---TDPDQVP-----GFPVLIKPAAGSGGTGMRVVRDAGTLAEAVASTR 175
Cdd:PRK02186 96 AANTEAIRTCRDKKRLARTLRDHGIDVPRTHalaLRAVALDaldglTYPVVVKPRMGSGSVGVRLCASVAEAAAHCAALR 175
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759837440 176 REVGGDVFCEPYVSNvRHIEVPILADAQG-AVIPFGERECSVQRRYQKIVEETPSPAVNPAlREDLCRAAIIAVRALGY- 253
Cdd:PRK02186 176 RAGTRAALVQAYVEG-DEYSVETLTVARGhQVLGITRKHLGPPPHFVEIGHDFPAPLSAPQ-RERIVRTVLRALDAVGYa 253
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759837440 254 VGAGAVEFLLdsRGD-FWFLELTPTLQADH--AVTECVSGYDL----VRLQLlvaegGSVPMPGPPPIRGHAIEVRICAE 326
Cdd:PRK02186 254 FGPAHTELRV--RGDtVVIIEINPRLAGGMipVLLEEAFGVDLldhvIDLHL-----GVAAFADPTAKRYGAIRFVLPAR 326
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 759837440 327 DPAYAWLPAAGTlHRFAVPDIagEFRPLPQPG--LRLDAGVSDgsvigmhhdpMLAKLIAWAPSRQEAARMLASALAR 402
Cdd:PRK02186 327 SGVLRGLLFLPD-DIAARPEL--RFHPLKQPGdaLRLEGDFRD----------RIAAVVCAGDHRDSVAAAAERAVAG 391
|
|
| PRK14042 |
PRK14042 |
pyruvate carboxylase subunit B; Provisional |
604-662 |
4.37e-06 |
|
pyruvate carboxylase subunit B; Provisional
Pssm-ID: 172536 [Multi-domain] Cd Length: 596 Bit Score: 49.72 E-value: 4.37e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 759837440 604 LPGAVRRVLVVPGQRVRAGELLLTLEAMKLEHPVHAPSAGVVSSLPVQPGAEVDTGELL 662
Cdd:PRK14042 532 IPGSIIAIHVSAGDEVKAGQAVLVIEAMKMETEIKAPANGVVAEILCQKGDKVTPGQVL 590
|
|
| AceF |
COG0508 |
Pyruvate/2-oxoglutarate dehydrogenase complex, dihydrolipoamide acyltransferase (E2) component ... |
606-665 |
4.74e-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: 44.67 E-value: 4.74e-06
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 759837440 606 GAVRRVLVVPGQRVRAGELLLTLEAMKLEHPVHAPSAGVVSSLPVQPGAEVDTGELLAVL 665
Cdd:COG0508 17 GTIVEWLVKEGDTVKEGDPLAEVETDKATMEVPAPAAGVLLEILVKEGDTVPVGAVIAVI 76
|
|
| ATP-grasp |
pfam02222 |
ATP-grasp domain; This family does not contain all known ATP-grasp domain members. This family ... |
142-276 |
5.19e-06 |
|
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: 47.25 E-value: 5.19e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759837440 142 GFPVLIK-PAAGSGGTGMRVVRDAGTLAEAVASTRrevGGDVFCEPYVSNVRHIEVPILADAQGAVipfgeRECSVQRRY 220
Cdd:pfam02222 27 GYPCVVKaRRGGYDGKGQYVVRSEADLPQAWEELG---DGPVIVEEFVPFDRELSVLVVRSVDGET-----AFYPVVETI 98
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 759837440 221 QK--IVEETPSPAvnPALREDLCRAAIIAVRA---LGYVGAGAVEFLLDSRGDFWFLELTP 276
Cdd:pfam02222 99 QEdgICRLSVAPA--RVPQAIQAEAQDIAKRLvdeLGGVGVFGVELFVTEDGDLLINELAP 157
|
|
| Biotinyl_lipoyl_domains |
cd06663 |
Biotinyl_lipoyl_domains are present in biotin-dependent carboxylases/decarboxylases, the ... |
606-665 |
7.55e-06 |
|
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: 44.35 E-value: 7.55e-06
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 759837440 606 GAVRRVLVVPGQRVRAGELLLTLEAMKLEHPVHAPSAGVVSSLPVQPGAEVDTGELLAVL 665
Cdd:cd06663 14 GTVVKWLKKVGDKVKKGDVLAEIEAMKATSDVEAPKSGTVKKVLVKEGTKVEGDTPLVKI 73
|
|
| PRK05889 |
PRK05889 |
biotin/lipoyl-binding carrier protein; |
602-666 |
8.06e-06 |
|
biotin/lipoyl-binding carrier protein;
Pssm-ID: 180306 [Multi-domain] Cd Length: 71 Bit Score: 44.03 E-value: 8.06e-06
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 759837440 602 APLPGAVRRVLVVPGQRVRAGELLLTLEAMKLEHPVHAPSAGVVSSLPVQPGAEVDTGELLAVLD 666
Cdd:PRK05889 7 AEIVASVLEVVVNEGDQIGKGDTLVLLESMKMEIPVLAEVAGTVSKVSVSVGDVIQAGDLIAVIS 71
|
|
| PRK14573 |
PRK14573 |
bifunctional UDP-N-acetylmuramate--L-alanine ligase/D-alanine--D-alanine ligase; |
102-276 |
1.04e-05 |
|
bifunctional UDP-N-acetylmuramate--L-alanine ligase/D-alanine--D-alanine ligase;
Pssm-ID: 184752 [Multi-domain] Cd Length: 809 Bit Score: 48.66 E-value: 1.04e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759837440 102 WVGPPPPTLRTLADKIETKKLVAEARVPVLP----TFTDPDQVP-----------GFPVLIKPAAGSGGTGMRVVRDAGT 166
Cdd:PRK14573 555 YTGPSLAFSAIAMDKVLTKRFASDVGVPVVPyqplTLAGWKREPelclahiveafSFPMFVKTAHLGSSIGVFEVHNVEE 634
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759837440 167 LAEAVaSTRREVGGDVFCEPYVSNVRHIEVPILADAQGAVIPFGERE-------CSVQRRY-------QKIVEETpspAV 232
Cdd:PRK14573 635 LRDKI-SEAFLYDTDVFVEESRLGSREIEVSCLGDGSSAYVIAGPHErrgsggfIDYQEKYglsgkssAQIVFDL---DL 710
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 759837440 233 NPALREDLCRAAIIAVRALGYVGAGAVEFLLDSRGDFWFLELTP 276
Cdd:PRK14573 711 SKESQEQVLELAERIYRLLQGKGSCRIDFFLDEEGNFWLSEMNP 754
|
|
| LysX |
COG0189 |
Glutathione synthase, LysX or RimK-type ligase, ATP-grasp superfamily [Amino acid transport ... |
90-188 |
2.04e-05 |
|
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: 46.86 E-value: 2.04e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759837440 90 RFAQAVVDAGLIWVgPPPPTLRTLADKIETKKLVAEARVPVLPTF--TDPDQVP------GFPVLIKPAAGSGGTGMRVV 161
Cdd:COG0189 72 ALLRQLEAAGVPVV-NDPEAIRRARDKLFTLQLLARAGIPVPPTLvtRDPDDLRafleelGGPVVLKPLDGSGGRGVFLV 150
|
90 100
....*....|....*....|....*..
gi 759837440 162 RDAGTLAEAVASTRREVGGDVFCEPYV 188
Cdd:COG0189 151 EDEDALESILEALTELGSEPVLVQEFI 177
|
|
| carB |
PRK12815 |
carbamoyl phosphate synthase large subunit; Reviewed |
92-318 |
3.23e-05 |
|
carbamoyl phosphate synthase large subunit; Reviewed
Pssm-ID: 237215 [Multi-domain] Cd Length: 1068 Bit Score: 47.27 E-value: 3.23e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759837440 92 AQAVVDAGLIWVGPPPPTLRTLADKIETKKLVAEARVPVLP--TFTDPDQVP------GFPVLIKPAAGSGGTGMRVVRD 163
Cdd:PRK12815 647 AKGLEEAGLTILGTSPDTIDRLEDRDRFYQLLDELGLPHVPglTATDEEEAFafakriGYPVLIRPSYVIGGQGMAVVYD 726
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759837440 164 AGTLAEavastrrevggdvFCEPYVSNVRHI-----------EVPILADAQGAVIPfgerecsvqrryqKIVEE------ 226
Cdd:PRK12815 727 EPALEA-------------YLAENASQLYPIlidqfidgkeyEVDAISDGEDVTIP-------------GIIEHieqagv 780
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759837440 227 --------TPSPAVNPALREDLCRAAIIAVRALGYVGAGAVEFLLDSrGDFWFLELTPtlQADH--AVTECVSGYDLVRL 296
Cdd:PRK12815 781 hsgdsiavLPPQSLSEEQQEKIRDYAIKIAKKLGFRGIMNIQFVLAN-DEIYVLEVNP--RASRtvPFVSKATGVPLAKL 857
|
250 260
....*....|....*....|..
gi 759837440 297 QLLVAEGGSVPMPGPPPIRGHA 318
Cdd:PRK12815 858 ATKVLLGKSLAELGYPNGLWPG 879
|
|
| PRK06019 |
PRK06019 |
phosphoribosylaminoimidazole carboxylase ATPase subunit; Reviewed |
105-276 |
5.68e-05 |
|
phosphoribosylaminoimidazole carboxylase ATPase subunit; Reviewed
Pssm-ID: 235674 [Multi-domain] Cd Length: 372 Bit Score: 45.91 E-value: 5.68e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759837440 105 PPPPTLRTLADKIETKKLVAEARVPVlPTF---TDPDQVP------GFPVLIKPAAGsG--GTGMRVVRDAGTLAEAVAS 173
Cdd:PRK06019 90 PGPDALAIAQDRLTEKQFLDKLGIPV-APFavvDSAEDLEaaladlGLPAVLKTRRG-GydGKGQWVIRSAEDLEAAWAL 167
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759837440 174 TrrevgGDVFC--EPYVSNVRhiEVPILA--DAQGAVIPFgerecSVQRRYQK--IVEETPSPA-VNPALREDLCRAAII 246
Cdd:PRK06019 168 L-----GSVPCilEEFVPFER--EVSVIVarGRDGEVVFY-----PLVENVHRngILRTSIAPArISAELQAQAEEIASR 235
|
170 180 190
....*....|....*....|....*....|
gi 759837440 247 AVRALGYVGAGAVEFLLDSRGDFWFLELTP 276
Cdd:PRK06019 236 IAEELDYVGVLAVEFFVTGDGELLVNEIAP 265
|
|
| PDHac_trf_long |
TIGR01348 |
pyruvate dehydrogenase complex dihydrolipoamide acetyltransferase, long form; This model ... |
606-666 |
1.40e-04 |
|
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: 44.87 E-value: 1.40e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 759837440 606 GAVRRVLVVPGQRVRAGELLLTLEAMKLEHPVHAPSAGVVSSLPVQPGAEVDTGELLAVLD 666
Cdd:TIGR01348 14 GEVIEVLVKPGDKVEAGQSLITLESDKASMEVPSSAAGIIKEIKVKVGDTLPVGGVIATLE 74
|
|
| sucB |
TIGR01347 |
2-oxoglutarate dehydrogenase complex dihydrolipoamide succinyltransferase (E2 component); This ... |
592-665 |
1.46e-04 |
|
2-oxoglutarate dehydrogenase complex dihydrolipoamide succinyltransferase (E2 component); This model describes the TCA cycle 2-oxoglutarate system E2 component, dihydrolipoamide succinyltransferase. It is closely related to the pyruvate dehydrogenase E2 component, dihydrolipoamide acetyltransferase. The seed for this model includes mitochondrial and Gram-negative bacterial forms. Mycobacterial candidates are highly derived, differ in having and extra copy of the lipoyl-binding domain at the N-terminus. They score below the trusted cutoff, but above the noise cutoff and above all examples of dihydrolipoamide acetyltransferase. [Energy metabolism, TCA cycle]
Pssm-ID: 273565 [Multi-domain] Cd Length: 403 Bit Score: 44.72 E-value: 1.46e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 759837440 592 APEAAESslIAPlpGAVRRVLVVPGQRVRAGELLLTLEAMKLEHPVHAPSAGVVSSLPVQPGAEVDTGELLAVL 665
Cdd:TIGR01347 5 VPELAES--ITE--GTVAEWHKKVGDTVKRDENIVEIETDKVVLEVPSPADGVLQEILFKEGDTVESGQVLAIL 74
|
|
| ATP-grasp_3 |
pfam02655 |
ATP-grasp domain; No functional information or experimental verification of function is known ... |
114-280 |
1.74e-04 |
|
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: 42.37 E-value: 1.74e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759837440 114 ADKIETKKLVAEARVPVLPTFTDPDQVPGF-PVLIKPAAGSGGTGMRVVRDAGTLAEAvastrrevGGDVFCEPYVSNvR 192
Cdd:pfam02655 2 SDKLKTYKALKNAGVPTPETLQAEELLREEkKYVVKPRDGCGGEGVRKVENGREDEAF--------IENVLVQEFIEG-E 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759837440 193 HIEVPILADAQGAVIPFGERE----CSVQRRYQKivEETPSPAVnpaLREDLCRAAIIAVRAL----GYVGagaVEFLLD 264
Cdd:pfam02655 73 PLSVSLLSDGEKALPLSVNRQyidnGGSGFVYAG--NVTPSRTE---LKEEIIELAEEVVECLpglrGYVG---VDLVLK 144
|
170
....*....|....*.
gi 759837440 265 SRGDFwFLELTPTLQA 280
Cdd:pfam02655 145 DNEPY-VIEVNPRITT 159
|
|
| aceF |
PRK11854 |
pyruvate dehydrogenase dihydrolipoyltransacetylase; Validated |
606-668 |
1.75e-04 |
|
pyruvate dehydrogenase dihydrolipoyltransacetylase; Validated
Pssm-ID: 236999 [Multi-domain] Cd Length: 633 Bit Score: 44.61 E-value: 1.75e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 759837440 606 GAVRRVLVVPGQRVRAGELLLTLEAMKLEHPVHAPSAGVVSSLPVQPGAEVDTGELLAVLDPE 668
Cdd:PRK11854 15 VEVTEILVKVGDKVEAEQSLITVEGDKASMEVPSPQAGVVKEIKVKVGDKVETGALIMIFESA 77
|
|
| aceF |
PRK11854 |
pyruvate dehydrogenase dihydrolipoyltransacetylase; Validated |
589-665 |
1.80e-04 |
|
pyruvate dehydrogenase dihydrolipoyltransacetylase; Validated
Pssm-ID: 236999 [Multi-domain] Cd Length: 633 Bit Score: 44.61 E-value: 1.80e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759837440 589 PLPAPEAAESSLIAPLP------GAVRRVLVVPGQRVRAGELLLTLEAMKLEHPVHAPSAGVVSSLPVQPGAEVDTGELL 662
Cdd:PRK11854 196 PAAAPAAAAGVKDVNVPdiggdeVEVTEVMVKVGDKVEAEQSLITVEGDKASMEVPAPFAGTVKEIKVNVGDKVKTGSLI 275
|
...
gi 759837440 663 AVL 665
Cdd:PRK11854 276 MRF 278
|
|
| PDHac_trf_long |
TIGR01348 |
pyruvate dehydrogenase complex dihydrolipoamide acetyltransferase, long form; This model ... |
592-668 |
2.68e-04 |
|
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: 44.10 E-value: 2.68e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759837440 592 APEAAESSLI--APLP-------GAVRRVLVVPGQRVRAGELLLTLEAMKLEHPVHAPSAGVVSSLPVQPGAEVDTGELL 662
Cdd:TIGR01348 107 APAAGQSSGVqeVTVPdigdiekVTVIEVLVKVGDTVSADQSLITLESDKASMEVPAPASGVVKSVKVKVGDSVPTGDLI 186
|
....*.
gi 759837440 663 AVLDPE 668
Cdd:TIGR01348 187 LTLSVA 192
|
|
| aceF |
PRK11854 |
pyruvate dehydrogenase dihydrolipoyltransacetylase; Validated |
589-665 |
3.19e-04 |
|
pyruvate dehydrogenase dihydrolipoyltransacetylase; Validated
Pssm-ID: 236999 [Multi-domain] Cd Length: 633 Bit Score: 43.84 E-value: 3.19e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759837440 589 PLPAPEAAESSLIAPLPGA----------------VRRVLVVPGQRVRAGELLLTLEAMKLEHPVHAPSAGVVSSLPVQP 652
Cdd:PRK11854 85 PAQAEEKKEAAPAAAPAAAaakdvhvpdigsdeveVTEILVKVGDTVEAEQSLITVEGDKASMEVPAPFAGTVKEIKVNV 164
|
90
....*....|...
gi 759837440 653 GAEVDTGELLAVL 665
Cdd:PRK11854 165 GDKVSTGSLIMVF 177
|
|
| ddl |
PRK01966 |
D-alanine--D-alanine ligase; |
115-273 |
5.66e-04 |
|
D-alanine--D-alanine ligase;
Pssm-ID: 234993 [Multi-domain] Cd Length: 333 Bit Score: 42.42 E-value: 5.66e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759837440 115 DKIETKKLVAEARVPVLP--TFTDPDQVP----------GFPVLIKPA-AGSgGTGMRVVRDAGTLAEAVASTRREvggD 181
Cdd:PRK01966 123 DKILTKRLLAAAGIPVAPyvVLTRGDWEEaslaeieaklGLPVFVKPAnLGS-SVGISKVKNEEELAAALDLAFEY---D 198
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759837440 182 --VFCEPYVsNVRHIEVPILADAQGAVIPfGEREC-----SVQRRY--QKIVEETPSPaVNPALREDLCRAAIIAVRALG 252
Cdd:PRK01966 199 rkVLVEQGI-KGREIECAVLGNDPKASVP-GEIVKpddfyDYEAKYldGSAELIIPAD-LSEELTEKIRELAIKAFKALG 275
|
170 180
....*....|....*....|.
gi 759837440 253 YVGAGAVEFLLDSRGDFWFLE 273
Cdd:PRK01966 276 CSGLARVDFFLTEDGEIYLNE 296
|
|
| PRK14569 |
PRK14569 |
D-alanyl-alanine synthetase A; Provisional |
86-277 |
1.27e-03 |
|
D-alanyl-alanine synthetase A; Provisional
Pssm-ID: 173033 [Multi-domain] Cd Length: 296 Bit Score: 41.20 E-value: 1.27e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759837440 86 AENSRFAQAVVDAGLIWVGPPPPTLRTLADKIETKKLVAEARVP------VLPTFTDPDQVpGFPVLIKPAAGSGGTGMR 159
Cdd:PRK14569 69 GENGRVSALLEMLEIKHTSSSMKSSVITMDKMISKEILMHHRMPtpmakfLTDKLVAEDEI-SFPVAVKPSSGGSSIATF 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759837440 160 VVRDAGTLAEAVASTRREvgGDVFCEPYVSNvRHIEVPILADAQGAVI---PFGERECSVQRRYQKIVEETPSpavnpal 236
Cdd:PRK14569 148 KVKSIQELKHAYEEASKY--GEVMIEQWVTG-KEITVAIVNDEVYSSVwiePQNEFYDYESKYSGKSIYHSPS------- 217
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 759837440 237 reDLCRAAIIAVRAL--------GYVGAGAVEFLLDSRGDFWFLELTPT 277
Cdd:PRK14569 218 --GLCEQKELEVRQLakkaydllGCSGHARVDFIYDDRGNFYIMEINSS 264
|
|
| PLN02948 |
PLN02948 |
phosphoribosylaminoimidazole carboxylase |
103-276 |
1.60e-03 |
|
phosphoribosylaminoimidazole carboxylase
Pssm-ID: 178534 [Multi-domain] Cd Length: 577 Bit Score: 41.58 E-value: 1.60e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759837440 103 VGPPPPTLRTLADKIETKKLVAEARVPvLPTFTDPDQVP---------GFPVLIKPAAGS-GGTGMRVVRDAGTLAEAVA 172
Cdd:PLN02948 109 VQPKSSTIRIIQDKYAQKVHFSKHGIP-LPEFMEIDDLEsaekagdlfGYPLMLKSRRLAyDGRGNAVAKTEEDLSSAVA 187
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759837440 173 StrreVGG---DVFCEPYVSNVRHIEVPILADAQGAVIPFGEREcSVQRRyqKIVEETPSPA-VNPALREDLCRAAIIAV 248
Cdd:PLN02948 188 A----LGGferGLYAEKWAPFVKELAVMVARSRDGSTRCYPVVE-TIHKD--NICHVVEAPAnVPWKVAKLATDVAEKAV 260
|
170 180
....*....|....*....|....*...
gi 759837440 249 RALGYVGAGAVEFLLDSRGDFWFLELTP 276
Cdd:PLN02948 261 GSLEGAGVFGVELFLLKDGQILLNEVAP 288
|
|
| PRK05704 |
PRK05704 |
2-oxoglutarate dehydrogenase complex dihydrolipoyllysine-residue succinyltransferase; |
592-668 |
1.87e-03 |
|
2-oxoglutarate dehydrogenase complex dihydrolipoyllysine-residue succinyltransferase;
Pssm-ID: 235571 [Multi-domain] Cd Length: 407 Bit Score: 40.97 E-value: 1.87e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 759837440 592 APEAAESslIAPlpGAVRRVLVVPGQRVRAGELLLTLEAMKLEHPVHAPSAGVVSSLPVQPGAEVDTGELLAVLDPE 668
Cdd:PRK05704 7 VPTLPES--VTE--ATIATWHKKPGDAVKRDEVLVEIETDKVVLEVPAPAAGVLSEILAEEGDTVTVGQVLGRIDEG 79
|
|
| PRK12767 |
PRK12767 |
carbamoyl phosphate synthase-like protein; Provisional |
34-276 |
2.65e-03 |
|
carbamoyl phosphate synthase-like protein; Provisional
Pssm-ID: 237195 [Multi-domain] Cd Length: 326 Bit Score: 40.25 E-value: 2.65e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759837440 34 DADTDAPHVIEADYAVHLPGNTpSATYLqaDALIAAAQRAGANAVHPGI----GVLAEN-SRFAqavvDAGLIWVGPPPP 108
Cdd:PRK12767 32 DISELAPALYFADKFYVVPKVT-DPNYI--DRLLDICKKEKIDLLIPLIdpelPLLAQNrDRFE----EIGVKVLVSSKE 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759837440 109 TLRTLADKIETKKLVAEARVPVLPTFTDPD----------QVPGFPVLIKPAAGSGGTGMRVVRDAGTLAEAVASTR--- 175
Cdd:PRK12767 105 VIEICNDKWLTYEFLKENGIPTPKSYLPESledfkaalakGELQFPLFVKPRDGSASIGVFKVNDKEELEFLLEYVPnli 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759837440 176 -------REVGGDVFCepyvsnvrhievpilaDAQGAVIpfgereCSVQRR---------YQKIVEEtpspavnpalRED 239
Cdd:PRK12767 185 iqefiegQEYTVDVLC----------------DLNGEVI------SIVPRKrievragetSKGVTVK----------DPE 232
|
250 260 270
....*....|....*....|....*....|....*..
gi 759837440 240 LCRAAIIAVRALGYVGAGAVEFLLDSrGDFWFLELTP 276
Cdd:PRK12767 233 LFKLAERLAEALGARGPLNIQCFVTD-GEPYLFEINP 268
|
|
| PRK12999 |
PRK12999 |
pyruvate carboxylase; Reviewed |
597-629 |
3.25e-03 |
|
pyruvate carboxylase; Reviewed
Pssm-ID: 237263 [Multi-domain] Cd Length: 1146 Bit Score: 40.89 E-value: 3.25e-03
10 20 30
....*....|....*....|....*....|...
gi 759837440 597 ESSLIAPLPGAVRRVLVVPGQRVRAGELLLTLE 629
Cdd:PRK12999 1113 ETTITAPVDGTVKRVLVKAGDQVEAGDLLVELE 1145
|
|
| PRK11855 |
PRK11855 |
dihydrolipoamide acetyltransferase; Reviewed |
606-668 |
4.48e-03 |
|
dihydrolipoamide acetyltransferase; Reviewed
Pssm-ID: 237000 [Multi-domain] Cd Length: 547 Bit Score: 40.19 E-value: 4.48e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 759837440 606 GAVRRVLVVPGQRVRAGELLLTLEAMKLEHPVHAPSAGVVSSLPVQPGAEVDTGELLAVLDPE 668
Cdd:PRK11855 16 VEVIEWLVKEGDTVEEDQPLVTVETDKATMEIPSPAAGVVKEIKVKVGDTVSVGGLLAVIEAA 78
|
|
| PycA |
COG1038 |
Pyruvate carboxylase [Energy production and conversion]; Pyruvate carboxylase is part of the ... |
597-628 |
6.30e-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: 40.06 E-value: 6.30e-03
10 20 30
....*....|....*....|....*....|..
gi 759837440 597 ESSLIAPLPGAVRRVLVVPGQRVRAGELLLTL 628
Cdd:COG1038 1113 ETTITAPRDGTVKEVLVKEGDQVEAGDLLIEL 1144
|
|
| PRK14875 |
PRK14875 |
acetoin dehydrogenase E2 subunit dihydrolipoyllysine-residue acetyltransferase; Provisional |
606-668 |
7.44e-03 |
|
acetoin dehydrogenase E2 subunit dihydrolipoyllysine-residue acetyltransferase; Provisional
Pssm-ID: 184875 [Multi-domain] Cd Length: 371 Bit Score: 39.16 E-value: 7.44e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 759837440 606 GAVRRVLVVPGQRVRAGELLLTLEAMKLEHPVHAPSAGVVSSLPVQPGAEVDTGELLAVLDPE 668
Cdd:PRK14875 17 GKVAGWLVQEGDEVEKGDELLDVETDKITNEVEAPAAGTLRRQVAQEGETLPVGALLAVVADA 79
|
|
| |
