|
Name |
Accession |
Description |
Interval |
E-value |
| PRK04366 |
PRK04366 |
aminomethyl-transferring glycine dehydrogenase subunit GcvPB; |
3-483 |
0e+00 |
|
aminomethyl-transferring glycine dehydrogenase subunit GcvPB;
Pssm-ID: 235292 Cd Length: 481 Bit Score: 936.07 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446718383 3 NQDQALIFEVSKEGRIGYSLPKLDVEEVkLEDVFESDYIRVEDAELPEVSELDIMRHYTALSNRNHGVDSGFYPLGSCTM 82
Cdd:PRK04366 2 RWDEPLIFELSRPGRRGYSLPELDVPEV-LESLLPEELLRKEPPELPEVSELEVVRHYTRLSQKNYGVDTGFYPLGSCTM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446718383 83 KYNPKINESVARFAGFANIHPLQDEKTVQGAMELMYDLQEHLIEITGMDTVTLQPAAGAHGEWTGLMLIRAYHEANGDFN 162
Cdd:PRK04366 81 KYNPKINEKVARLPGFAELHPLQPEETVQGALELMYELQEWLKEITGMDAVTLQPAAGAHGELTGLLMIRAYHEARGDTK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446718383 163 RTKVIVPDSAHGTNPASATVAGFETITVKSNEHGLVDLEDLKRVVNEETAALMLTNPNTLGLFEENILEMAEIVHNAGGK 242
Cdd:PRK04366 161 RTEVIVPDSAHGTNPASAAMAGFKVVEIPSNEDGLVDLEALKAAVGEDTAALMLTNPNTLGLFERNILEIAEIVHEAGGL 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446718383 243 LYYDGANLNAVLSQARPGDMGFDVVHLNLHKTFTgphggggpgsgpvgVKADLIPYLPKPILEKTEDGYRFNYDRPEAIG 322
Cdd:PRK04366 241 LYYDGANLNAILGKARPGDMGFDVVHLNLHKTFStphggggpgsgpvgVKEELAPFLPVPVVEKDGDRYRLDYDRPKSIG 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446718383 323 RVKPFYGNFGINVRAYTYIRSMGPDGLRAVTEYAVLNANYMMRRLAPFYDLPFDRHCKHEFVLSGRRQKKLGVRTLDIAK 402
Cdd:PRK04366 321 RVRAFYGNFGVLVRAYAYIRSLGAEGLREVSEDAVLNANYLKARLKDIYDLPYDRPCMHEFVLSGKKLKETGVRTLDIAK 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446718383 403 RLLDFGYHPPTIYFPLNVEECIMIEPTETESKETLDGFIDKMIQIAKEVEENPEVVQEAPHTTVIKRLDETMAARKPVLR 482
Cdd:PRK04366 401 RLLDYGFHPPTIYFPLIVPEALMIEPTETESKETLDAFIAAMKQIAEEAKENPELVKEAPHNTPVRRLDEVKAARKPVLR 480
|
.
gi 446718383 483 Y 483
Cdd:PRK04366 481 W 481
|
|
| GcvP2 |
COG1003 |
Glycine cleavage system protein P (pyridoxal-binding), C-terminal domain [Amino acid transport ... |
25-487 |
0e+00 |
|
Glycine cleavage system protein P (pyridoxal-binding), C-terminal domain [Amino acid transport and metabolism]; Glycine cleavage system protein P (pyridoxal-binding), C-terminal domain is part of the Pathway/BioSystem: Glycine cleavage
Pssm-ID: 440627 Cd Length: 468 Bit Score: 831.98 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446718383 25 LDVEEVKLEDVFESDYIRVEDAELPEVSELDIMRHYTALSNRNHGVDSGFYPLGSCTMKYNPKINESVARFAGFANIHPL 104
Cdd:COG1003 3 LPEPEADAASLLPEALLRKSPVFLPEVSETEVLRHYTRLSQKNLGLDTGMIPLGSCTMKYNPKINEEPATLPGFANLHPF 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446718383 105 QDEKTVQGAMELMYDLQEHLIEITGMDTVTLQPAAGAHGEWTGLMLIRAYHEANGDFNRTKVIVPDSAHGTNPASATVAG 184
Cdd:COG1003 83 QPEETVQGYLELMYELEEWLAEITGMDAVSLQPNAGAQGEYAGLLAIRAYHESRGEGHRNEILIPDSAHGTNPASAAMAG 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446718383 185 FETITVKSNEHGLVDLEDLKRVVNEETAALMLTNPNTLGLFEENILEMAEIVHNAGGKLYYDGANLNAVLSQARPGDMGF 264
Cdd:COG1003 163 FKVVVVKSDEDGNVDLEDLKAKVGDRTAALMLTNPSTHGVFEEDIKEICDIVHEAGGLVYYDGANLNAIVGLARPGDMGF 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446718383 265 DVVHLNLHKTFTgphggggpgsgpvgVKADLIPYLPKPILEKTEDGYRFNYDRPEAIGRVKPFYGNFGINVRAYTYIRSM 344
Cdd:COG1003 243 DVCHLNLHKTFStphggggpgsgpvgVKEHLAPFLPGPPVVKDGDKYRLDYDRPKSIGRSAAFYGNAGVLVRAYAYIRMM 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446718383 345 GPDGLRAVTEYAVLNANYMMRRLAPFYDLPF--DRHCKHEFVLSGRRQKK-LGVRTLDIAKRLLDFGYHPPTIYFPLNVE 421
Cdd:COG1003 323 GAEGLREATEVAVLNANYLAARLKDHYPVLYtgNGRCAHEFILDLRPLKKeTGVTTLDIAKRLLDYGFHAPTMYFPLIVP 402
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446718383 422 ECIMIEPTETESKETLDGFIDKMIQIAKEVEENPEVVQEAPHTTVIKRLDETMAARKPVLRYEKPA 487
Cdd:COG1003 403 ETLMIEPTESESKEELDRFIDAMIAIREEAREDPEPLKNAPHTTPVRRLDEVYADRNLVLTWREEE 468
|
|
| GDC-P |
cd00613 |
Glycine cleavage system P-protein, alpha- and beta-subunits. This family consists of Glycine ... |
53-444 |
1.93e-159 |
|
Glycine cleavage system P-protein, alpha- and beta-subunits. This family consists of Glycine cleavage system P-proteins EC:1.4.4.2 from bacterial, mammalian and plant sources. The P protein is part of the glycine decarboxylase multienzyme complex EC:2.1.2.10 (GDC) also annotated as glycine cleavage system or glycine synthase. GDC consists of four proteins P, H, L and T. The reaction catalysed by this protein is: Glycine + lipoylprotein <=> S-aminomethyldihydrolipoylprotein + CO2. Alpha-beta-type dimers associate to form an alpha(2)beta(2) tetramer, where the alpha- and beta-subunits are structurally similar and appear to have arisen by gene duplication and subsequent divergence with a loss of one active site. The members of this CD are widely dispersed among all three forms of cellular life.
Pssm-ID: 99737 [Multi-domain] Cd Length: 398 Bit Score: 457.85 E-value: 1.93e-159
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446718383 53 ELDIMRHYTALSNRNHGVDSGFYPLGSCTMKYNPKINE-SVARFAGFANIHPLQDEKTVQGAMELMYDLQEHLIEITGMD 131
Cdd:cd00613 1 ETEVLRHLKRLASKNKALDQSMSFLGSGTYKHNPPAVIkRNILENEFYTAYTPYQPEISQGRLQALFELQTMLCELTGMD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446718383 132 T--VTLQPAAGAHGEWTGLMLIRAYHeangdfNRTKVIVPDSAHGTNPASATVA----GFETITVKSNEHGLVDLEDLKR 205
Cdd:cd00613 81 VanASLQDEATAAAEAAGLAAIRAYH------KRNKVLVPDSAHPTNPAVARTRgeplGIEVVEVPSDEGGTVDLEALKE 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446718383 206 VVNEETAALMLTNPNTLGLFEENILEMAEIVHNAGGKLYYDGANLNAVLsQARPGDMGFDVVHLNLHKTFTgphggggpg 285
Cdd:cd00613 155 EVSEEVAALMVQYPNTLGVFEDLIKEIADIAHSAGALVYVDGDNLNLTG-LKPPGEYGADIVVGNLQKTGVphggggp-g 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446718383 286 sgpvgVKADLIPYLPKPILEKTED-----GYRFNYDRPEAI-----GRVKPFYGNFGINVRAYTYIRSMGPDGLRAVTEY 355
Cdd:cd00613 233 agffaVKKELVRFLPGRLVGVTKDaegnrAFRLALQTREQHirrekATSNICTGQALLALMAAMYIVYLGPEGLKEIAER 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446718383 356 AVLNANYMMRRLAPFY-DLPFDRHCKHEFVLSGRrqKKLGVRTLDIAKRLLDFGYHPPTIYFPlnVEECIMIEPTETESK 434
Cdd:cd00613 313 AHLNANYLAKRLKEVGgVLPFNGPFFHEFVLRLP--PLYGIRAEDLAKALIDGGFHAPTMYLP--VDGTLMIEPTETETK 388
|
410
....*....|
gi 446718383 435 ETLDGFIDKM 444
Cdd:cd00613 389 EELDALLEAL 398
|
|
| Beta_elim_lyase |
pfam01212 |
Beta-eliminating lyase; |
118-273 |
3.89e-06 |
|
Beta-eliminating lyase;
Pssm-ID: 426128 [Multi-domain] Cd Length: 288 Bit Score: 48.37 E-value: 3.89e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446718383 118 YDLQEHLIEITGMDTVTLQPAaGAHGEWTGLM-LIRAYHEangdfnrtkVIVPDSAHG---TNPASATVAGFETITVKSN 193
Cdd:pfam01212 35 NRLEDRVAELFGKEAALFVPS-GTAANQLALMaHCQRGDE---------VICGEPAHIhfdETGGHAELGGVQPRPLDGD 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446718383 194 EHGLVDLEDLKRVV-------NEETAALMLTNP-NTLG---LFEENILEMAEIVHNAGGKLYYDGANL--NAVLSQARPG 260
Cdd:pfam01212 105 EAGNMDLEDLEAAIrevgadiFPPTGLISLENThNSAGgqvVSLENLREIAALAREHGIPVHLDGARFanAAVALGVIVK 184
|
170
....*....|....*
gi 446718383 261 DM--GFDVVHLNLHK 273
Cdd:pfam01212 185 EItsYADSVTMCLSK 199
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| PRK04366 |
PRK04366 |
aminomethyl-transferring glycine dehydrogenase subunit GcvPB; |
3-483 |
0e+00 |
|
aminomethyl-transferring glycine dehydrogenase subunit GcvPB;
Pssm-ID: 235292 Cd Length: 481 Bit Score: 936.07 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446718383 3 NQDQALIFEVSKEGRIGYSLPKLDVEEVkLEDVFESDYIRVEDAELPEVSELDIMRHYTALSNRNHGVDSGFYPLGSCTM 82
Cdd:PRK04366 2 RWDEPLIFELSRPGRRGYSLPELDVPEV-LESLLPEELLRKEPPELPEVSELEVVRHYTRLSQKNYGVDTGFYPLGSCTM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446718383 83 KYNPKINESVARFAGFANIHPLQDEKTVQGAMELMYDLQEHLIEITGMDTVTLQPAAGAHGEWTGLMLIRAYHEANGDFN 162
Cdd:PRK04366 81 KYNPKINEKVARLPGFAELHPLQPEETVQGALELMYELQEWLKEITGMDAVTLQPAAGAHGELTGLLMIRAYHEARGDTK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446718383 163 RTKVIVPDSAHGTNPASATVAGFETITVKSNEHGLVDLEDLKRVVNEETAALMLTNPNTLGLFEENILEMAEIVHNAGGK 242
Cdd:PRK04366 161 RTEVIVPDSAHGTNPASAAMAGFKVVEIPSNEDGLVDLEALKAAVGEDTAALMLTNPNTLGLFERNILEIAEIVHEAGGL 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446718383 243 LYYDGANLNAVLSQARPGDMGFDVVHLNLHKTFTgphggggpgsgpvgVKADLIPYLPKPILEKTEDGYRFNYDRPEAIG 322
Cdd:PRK04366 241 LYYDGANLNAILGKARPGDMGFDVVHLNLHKTFStphggggpgsgpvgVKEELAPFLPVPVVEKDGDRYRLDYDRPKSIG 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446718383 323 RVKPFYGNFGINVRAYTYIRSMGPDGLRAVTEYAVLNANYMMRRLAPFYDLPFDRHCKHEFVLSGRRQKKLGVRTLDIAK 402
Cdd:PRK04366 321 RVRAFYGNFGVLVRAYAYIRSLGAEGLREVSEDAVLNANYLKARLKDIYDLPYDRPCMHEFVLSGKKLKETGVRTLDIAK 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446718383 403 RLLDFGYHPPTIYFPLNVEECIMIEPTETESKETLDGFIDKMIQIAKEVEENPEVVQEAPHTTVIKRLDETMAARKPVLR 482
Cdd:PRK04366 401 RLLDYGFHPPTIYFPLIVPEALMIEPTETESKETLDAFIAAMKQIAEEAKENPELVKEAPHNTPVRRLDEVKAARKPVLR 480
|
.
gi 446718383 483 Y 483
Cdd:PRK04366 481 W 481
|
|
| GcvP2 |
COG1003 |
Glycine cleavage system protein P (pyridoxal-binding), C-terminal domain [Amino acid transport ... |
25-487 |
0e+00 |
|
Glycine cleavage system protein P (pyridoxal-binding), C-terminal domain [Amino acid transport and metabolism]; Glycine cleavage system protein P (pyridoxal-binding), C-terminal domain is part of the Pathway/BioSystem: Glycine cleavage
Pssm-ID: 440627 Cd Length: 468 Bit Score: 831.98 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446718383 25 LDVEEVKLEDVFESDYIRVEDAELPEVSELDIMRHYTALSNRNHGVDSGFYPLGSCTMKYNPKINESVARFAGFANIHPL 104
Cdd:COG1003 3 LPEPEADAASLLPEALLRKSPVFLPEVSETEVLRHYTRLSQKNLGLDTGMIPLGSCTMKYNPKINEEPATLPGFANLHPF 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446718383 105 QDEKTVQGAMELMYDLQEHLIEITGMDTVTLQPAAGAHGEWTGLMLIRAYHEANGDFNRTKVIVPDSAHGTNPASATVAG 184
Cdd:COG1003 83 QPEETVQGYLELMYELEEWLAEITGMDAVSLQPNAGAQGEYAGLLAIRAYHESRGEGHRNEILIPDSAHGTNPASAAMAG 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446718383 185 FETITVKSNEHGLVDLEDLKRVVNEETAALMLTNPNTLGLFEENILEMAEIVHNAGGKLYYDGANLNAVLSQARPGDMGF 264
Cdd:COG1003 163 FKVVVVKSDEDGNVDLEDLKAKVGDRTAALMLTNPSTHGVFEEDIKEICDIVHEAGGLVYYDGANLNAIVGLARPGDMGF 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446718383 265 DVVHLNLHKTFTgphggggpgsgpvgVKADLIPYLPKPILEKTEDGYRFNYDRPEAIGRVKPFYGNFGINVRAYTYIRSM 344
Cdd:COG1003 243 DVCHLNLHKTFStphggggpgsgpvgVKEHLAPFLPGPPVVKDGDKYRLDYDRPKSIGRSAAFYGNAGVLVRAYAYIRMM 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446718383 345 GPDGLRAVTEYAVLNANYMMRRLAPFYDLPF--DRHCKHEFVLSGRRQKK-LGVRTLDIAKRLLDFGYHPPTIYFPLNVE 421
Cdd:COG1003 323 GAEGLREATEVAVLNANYLAARLKDHYPVLYtgNGRCAHEFILDLRPLKKeTGVTTLDIAKRLLDYGFHAPTMYFPLIVP 402
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446718383 422 ECIMIEPTETESKETLDGFIDKMIQIAKEVEENPEVVQEAPHTTVIKRLDETMAARKPVLRYEKPA 487
Cdd:COG1003 403 ETLMIEPTESESKEELDRFIDAMIAIREEAREDPEPLKNAPHTTPVRRLDEVYADRNLVLTWREEE 468
|
|
| GDC-P |
cd00613 |
Glycine cleavage system P-protein, alpha- and beta-subunits. This family consists of Glycine ... |
53-444 |
1.93e-159 |
|
Glycine cleavage system P-protein, alpha- and beta-subunits. This family consists of Glycine cleavage system P-proteins EC:1.4.4.2 from bacterial, mammalian and plant sources. The P protein is part of the glycine decarboxylase multienzyme complex EC:2.1.2.10 (GDC) also annotated as glycine cleavage system or glycine synthase. GDC consists of four proteins P, H, L and T. The reaction catalysed by this protein is: Glycine + lipoylprotein <=> S-aminomethyldihydrolipoylprotein + CO2. Alpha-beta-type dimers associate to form an alpha(2)beta(2) tetramer, where the alpha- and beta-subunits are structurally similar and appear to have arisen by gene duplication and subsequent divergence with a loss of one active site. The members of this CD are widely dispersed among all three forms of cellular life.
Pssm-ID: 99737 [Multi-domain] Cd Length: 398 Bit Score: 457.85 E-value: 1.93e-159
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446718383 53 ELDIMRHYTALSNRNHGVDSGFYPLGSCTMKYNPKINE-SVARFAGFANIHPLQDEKTVQGAMELMYDLQEHLIEITGMD 131
Cdd:cd00613 1 ETEVLRHLKRLASKNKALDQSMSFLGSGTYKHNPPAVIkRNILENEFYTAYTPYQPEISQGRLQALFELQTMLCELTGMD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446718383 132 T--VTLQPAAGAHGEWTGLMLIRAYHeangdfNRTKVIVPDSAHGTNPASATVA----GFETITVKSNEHGLVDLEDLKR 205
Cdd:cd00613 81 VanASLQDEATAAAEAAGLAAIRAYH------KRNKVLVPDSAHPTNPAVARTRgeplGIEVVEVPSDEGGTVDLEALKE 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446718383 206 VVNEETAALMLTNPNTLGLFEENILEMAEIVHNAGGKLYYDGANLNAVLsQARPGDMGFDVVHLNLHKTFTgphggggpg 285
Cdd:cd00613 155 EVSEEVAALMVQYPNTLGVFEDLIKEIADIAHSAGALVYVDGDNLNLTG-LKPPGEYGADIVVGNLQKTGVphggggp-g 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446718383 286 sgpvgVKADLIPYLPKPILEKTED-----GYRFNYDRPEAI-----GRVKPFYGNFGINVRAYTYIRSMGPDGLRAVTEY 355
Cdd:cd00613 233 agffaVKKELVRFLPGRLVGVTKDaegnrAFRLALQTREQHirrekATSNICTGQALLALMAAMYIVYLGPEGLKEIAER 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446718383 356 AVLNANYMMRRLAPFY-DLPFDRHCKHEFVLSGRrqKKLGVRTLDIAKRLLDFGYHPPTIYFPlnVEECIMIEPTETESK 434
Cdd:cd00613 313 AHLNANYLAKRLKEVGgVLPFNGPFFHEFVLRLP--PLYGIRAEDLAKALIDGGFHAPTMYLP--VDGTLMIEPTETETK 388
|
410
....*....|
gi 446718383 435 ETLDGFIDKM 444
Cdd:cd00613 389 EELDALLEAL 398
|
|
| PLN02414 |
PLN02414 |
glycine dehydrogenase (decarboxylating) |
52-464 |
1.07e-113 |
|
glycine dehydrogenase (decarboxylating)
Pssm-ID: 178035 [Multi-domain] Cd Length: 993 Bit Score: 358.69 E-value: 1.07e-113
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446718383 52 SELDIMRHYTALSNRNHGVDSGFYPLGSCTMKYNPKINESVARFAGFANIHPLQDEKTVQGAMELMYDLQEHLIEITGMD 131
Cdd:PLN02414 505 SEHELLRYLHRLQNKDLSLVHSMIPLGSCTMKLNATTEMMPVTWPEFANIHPFAPVDQAQGYQEMFEDLGDLLCEITGFD 584
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446718383 132 TVTLQPAAGAHGEWTGLMLIRAYHEANGDFNRTKVIVPDSAHGTNPASATVAGFETITVKSNEHGLVDLEDLKRVVNEET 211
Cdd:PLN02414 585 SFSLQPNAGAAGEYAGLMVIRAYHLSRGDHHRNVCIIPVSAHGTNPASAAMCGMKIVVVGTDAKGNINIEELRKAAEAHK 664
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446718383 212 ---AALMLTNPNTLGLFEENILEMAEIVHNAGGKLYYDGANLNAVLSQARPGDMGFDVVHLNLHKTFTGPHGGGGPGSGP 288
Cdd:PLN02414 665 dnlAALMVTYPSTHGVYEEGIDEICDIIHDNGGQVYMDGANMNAQVGLTSPGFIGADVCHLNLHKTFCIPHGGGGPGMGP 744
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446718383 289 VGVKADLIPYLPKPILEKTEDGYRFNYDRPEAIGRVKPfYGNFGINVRAYTYIRSMGPDGLRAVTEYAVLNANYMMRRLA 368
Cdd:PLN02414 745 IGVKKHLAPFLPSHPVVPTGGIPRPEKTQPLGTISAAP-WGSALILPISYTYIAMMGSEGLTDASKIAILNANYMAKRLE 823
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446718383 369 PFYDLPF---DRHCKHEFVLSGRRQK-KLGVRTLDIAKRLLDFGYHPPTIYFPlnVEECIMIEPTETESKETLDGFIDKM 444
Cdd:PLN02414 824 GHYPVLFrgkNGTCAHEFIIDLRPFKnTAGIEPEDVAKRLMDYGFHAPTMSWP--VPGTLMIEPTESESKAELDRFCDAL 901
|
410 420
....*....|....*....|....*...
gi 446718383 445 IQIAKEVEE--------NPEVVQEAPHT 464
Cdd:PLN02414 902 ISIREEIADiengkadrENNVLKGAPHP 929
|
|
| PRK00451 |
PRK00451 |
aminomethyl-transferring glycine dehydrogenase subunit GcvPA; |
47-444 |
4.18e-17 |
|
aminomethyl-transferring glycine dehydrogenase subunit GcvPA;
Pssm-ID: 234769 [Multi-domain] Cd Length: 447 Bit Score: 83.26 E-value: 4.18e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446718383 47 ELPE-VSELDIMRHYTALSNRNHGVDS-------GFYPlgsctmKYNPKINESVARFAGFANIH-PLQDEKTvQGAMELM 117
Cdd:PRK00451 42 DLPPgLSEMELLRHLRELAAKNKTAEEypsflgaGAYD------HYIPAVVDHIISRSEFYTAYtPYQPEIS-QGTLQAI 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446718383 118 YDLQEHLIEITGMDTVT--LQPAAGAHGEwTGLMLIRAyheaNGdfnRTKVIVPDSAHgtnPASATV-------AGFETI 188
Cdd:PRK00451 115 FEYQTMICELTGMDVANasMYDGATALAE-AALMAVRI----TK---RKKVLVSGAVH---PEYREVlktylkgQGIEVV 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446718383 189 TVKSNEhGLVDLEDLKRVVNEETAALMLTNPNTLGLFEEnILEMAEIVHnAGGKLYYDGAN---LnAVLsqARPGDMGFD 265
Cdd:PRK00451 184 EVPYED-GVTDLEALEAAVDDDTAAVVVQYPNFFGVIED-LEEIAEIAH-AGGALFIVGVDpvsL-GLL--KPPGEYGAD 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446718383 266 VV----------------HLNLhktFTgphggggpgsgpvgVKADLIPYLPKPILEKTED--GYR-FN---YDRPEAIGR 323
Cdd:PRK00451 258 IVvgegqplgiplsfggpYLGF---FA--------------TRKKLVRQMPGRLVGETVDadGKRgFVltlQAREQHIRR 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446718383 324 VKpfyG--NFGIN-----VRAYTYIRSMGPDGLRAVTEYAVLNANYMMRRLA--PFYdLPFDRHCKHEFVLsgrrqkKLG 394
Cdd:PRK00451 321 EK---AtsNICTNqalnaLAAAIYMSLLGPEGLRELAEQNHQKAHYLAERLAeiGGV-ELFDGPFFNEFVV------RLP 390
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|...
gi 446718383 395 VRTLDIAKRLLDFGYH---PPTIYFPlNVEECIMIEPTETESKETLDGFIDKM 444
Cdd:PRK00451 391 KPAEEVNEALLEKGILggyDLGRYYP-ELGNHLLVCVTEKRTKEDIDALVAAL 442
|
|
| AAT_I |
cd01494 |
Aspartate aminotransferase (AAT) superfamily (fold type I) of pyridoxal phosphate (PLP) ... |
116-276 |
1.50e-14 |
|
Aspartate aminotransferase (AAT) superfamily (fold type I) of pyridoxal phosphate (PLP)-dependent enzymes. PLP combines with an alpha-amino acid to form a compound called a Schiff base or aldimine intermediate, which depending on the reaction, is the substrate in four kinds of reactions (1) transamination (movement of amino groups), (2) racemization (redistribution of enantiomers), (3) decarboxylation (removing COOH groups), and (4) various side-chain reactions depending on the enzyme involved. Pyridoxal phosphate (PLP) dependent enzymes were previously classified into alpha, beta and gamma classes, based on the chemical characteristics (carbon atom involved) of the reaction they catalyzed. The availability of several structures allowed a comprehensive analysis of the evolutionary classification of PLP dependent enzymes, and it was found that the functional classification did not always agree with the evolutionary history of these enzymes. Structure and sequence analysis has revealed that the PLP dependent enzymes can be classified into four major groups of different evolutionary origin: aspartate aminotransferase superfamily (fold type I), tryptophan synthase beta superfamily (fold type II), alanine racemase superfamily (fold type III), and D-amino acid superfamily (fold type IV) and Glycogen phophorylase family (fold type V).
Pssm-ID: 99742 [Multi-domain] Cd Length: 170 Bit Score: 71.64 E-value: 1.50e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446718383 116 LMYDLQEHLIEIT--GMDTVTLQPAaGAHGEWTGLMLIRAYHeangdfnrTKVIVPDSAHGTNPAS-ATVAGFETITVKS 192
Cdd:cd01494 1 KLEELEEKLARLLqpGNDKAVFVPS-GTGANEAALLALLGPG--------DEVIVDANGHGSRYWVaAELAGAKPVPVPV 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446718383 193 NEHG-----LVDLEDLKRVvnEETAALMLTNPNTLGLFEENILEMAEIVHNAGGKLYYDGANL--NAVLSQARPGDMGFD 265
Cdd:cd01494 72 DDAGyggldVAILEELKAK--PNVALIVITPNTTSGGVLVPLKEIRKIAKEYGILLLVDAASAggASPAPGVLIPEGGAD 149
|
170
....*....|.
gi 446718383 266 VVHLNLHKTFT 276
Cdd:cd01494 150 VVTFSLHKNLG 160
|
|
| GcvP1 |
COG0403 |
Glycine cleavage system protein P (pyridoxal-binding), N-terminal domain [Amino acid transport ... |
111-444 |
3.30e-13 |
|
Glycine cleavage system protein P (pyridoxal-binding), N-terminal domain [Amino acid transport and metabolism]; Glycine cleavage system protein P (pyridoxal-binding), N-terminal domain is part of the Pathway/BioSystem: Glycine cleavage
Pssm-ID: 440172 [Multi-domain] Cd Length: 442 Bit Score: 71.21 E-value: 3.30e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446718383 111 QGAMELMYDLQEHLIEITGMDTVT--LQPAAGAHGEwTGLMLIRAYHEANgdfnrtKVIVPDSAHgtnPASATV------ 182
Cdd:COG0403 108 QGRLQALFEFQTMVAELTGMDVANasLYDGATAAAE-AMLMARRVTKRSN------KVLVSEDVH---PQTRAVlktyae 177
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446718383 183 -AGFETITVkSNEHGLVDLEDLKRVVNEETAALMLTNPNTLGLFEEnILEMAEIVHNAGGKLYYdGANLNA--VLsqARP 259
Cdd:COG0403 178 pLGIEVVEV-PDEDGVTDLEALKALLDDDVAGVLVQYPNFFGVIED-LRAIAEAAHAAGALVIV-AADPLSlgLL--KPP 252
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446718383 260 GDMGFDVV----------------HLNLhktFTgphggggpgsgpvgVKADLIPYLPkpilektedgyrfnydrpeaiGR 323
Cdd:COG0403 253 GELGADIVvgegqrlgvplgfggpHAGF---FA--------------TREKLVRQMP---------------------GR 294
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446718383 324 VkpfygnFGINV-----RAYT--------YIR------------------------SMGPDGLRAVTEYAVLNANYMMRR 366
Cdd:COG0403 295 L------VGVTVdadgkRAFRltlqtreqHIRrekatsnictnqallalaasmyavYHGPEGLKEIAERIHQKAHYLAER 368
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446718383 367 LAPF-YDLPFDRHCKHEFVLsgrrqkKLGVRTLDIAKRLLDFGYHPPtiyFPLNV--EECIMIEPTETESKETLDGFIDK 443
Cdd:COG0403 369 LAALgVEVPFNGPFFDEFVV------RLPKPAAEINAALLEKGILGG---LNLRRvdDDTLLVAVTETTTKEDIDALVEA 439
|
.
gi 446718383 444 M 444
Cdd:COG0403 440 L 440
|
|
| Beta_elim_lyase |
pfam01212 |
Beta-eliminating lyase; |
118-273 |
3.89e-06 |
|
Beta-eliminating lyase;
Pssm-ID: 426128 [Multi-domain] Cd Length: 288 Bit Score: 48.37 E-value: 3.89e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446718383 118 YDLQEHLIEITGMDTVTLQPAaGAHGEWTGLM-LIRAYHEangdfnrtkVIVPDSAHG---TNPASATVAGFETITVKSN 193
Cdd:pfam01212 35 NRLEDRVAELFGKEAALFVPS-GTAANQLALMaHCQRGDE---------VICGEPAHIhfdETGGHAELGGVQPRPLDGD 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446718383 194 EHGLVDLEDLKRVV-------NEETAALMLTNP-NTLG---LFEENILEMAEIVHNAGGKLYYDGANL--NAVLSQARPG 260
Cdd:pfam01212 105 EAGNMDLEDLEAAIrevgadiFPPTGLISLENThNSAGgqvVSLENLREIAALAREHGIPVHLDGARFanAAVALGVIVK 184
|
170
....*....|....*
gi 446718383 261 DM--GFDVVHLNLHK 273
Cdd:pfam01212 185 EItsYADSVTMCLSK 199
|
|
| GDC-P |
pfam02347 |
Glycine cleavage system P-protein; This family consists of Glycine cleavage system P-proteins ... |
32-267 |
1.88e-04 |
|
Glycine cleavage system P-protein; This family consists of Glycine cleavage system P-proteins EC:1.4.4.2 from bacterial, mammalian and plant sources. The P protein is part of the glycine decarboxylase multienzyme complex EC:2.1.2.10 (GDC) also annotated as glycine cleavage system or glycine synthase. GDC consists of four proteins P, H, L and T. The reaction catalyzed by this protein is:- Glycine + lipoylprotein <=> S-aminomethyldihydrolipoylprotein + CO2
Pssm-ID: 396772 [Multi-domain] Cd Length: 428 Bit Score: 43.90 E-value: 1.88e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446718383 32 LEDVFESDY---IRV-EDAELPE-VSELDIMRHYTALSNRNHGVDSgFYPLGSCTMKYNPKINESVARFAGFANIH-PLQ 105
Cdd:pfam02347 23 LDDLIGKAVpknIRFaKPLQLPApKSEYEALAELEAIASKNTVYRS-FIGMGYYDTILPPVILRNILENPEWYTAYtPYQ 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446718383 106 DEKTvQGAMELMYDLQEHLIEITGMDTV--TLQPAAGAHGEWTGLMlirayheANGDFNRTKVIVPDSAhgTNPASATVA 183
Cdd:pfam02347 102 PEIS-QGRLEALLNFQTMICDLTGLDIAnaSLLDEGTAAAEAMALA-------ARASKKKGKKFVVDKD--VHPQTLEVL 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446718383 184 -------GFETITVKSNEHGLVDLEDlkrvvneeTAALMLTNPNTLGlFEENILEMAEIVHNaGGKLYYDGANLNAVLSQ 256
Cdd:pfam02347 172 ktrakpfGIEIVEVDYTEEGVTDLKD--------VFGVLVQYPNTDG-RIEDYKELIELAHQ-RKSLVVVAADLLALTLL 241
|
250
....*....|.
gi 446718383 257 ARPGDMGFDVV 267
Cdd:pfam02347 242 KPPGEFGADIA 252
|
|
| AAT_like |
cd00609 |
Aspartate aminotransferase family. This family belongs to pyridoxal phosphate (PLP)-dependent ... |
149-275 |
3.09e-04 |
|
Aspartate aminotransferase family. This family belongs to pyridoxal phosphate (PLP)-dependent aspartate aminotransferase superfamily (fold I). Pyridoxal phosphate combines with an alpha-amino acid to form a compound called a Schiff base or aldimine intermediate, which depending on the reaction, is the substrate in four kinds of reactions (1) transamination (movement of amino groups), (2) racemization (redistribution of enantiomers), (3) decarboxylation (removing COOH groups), and (4) various side-chain reactions depending on the enzyme involved. Pyridoxal phosphate (PLP) dependent enzymes were previously classified into alpha, beta and gamma classes, based on the chemical characteristics (carbon atom involved) of the reaction they catalyzed. The availability of several structures allowed a comprehensive analysis of the evolutionary classification of PLP dependent enzymes, and it was found that the functional classification did not always agree with the evolutionary history of these enzymes. The major groups in this CD corresponds to Aspartate aminotransferase a, b and c, Tyrosine, Alanine, Aromatic-amino-acid, Glutamine phenylpyruvate, 1-Aminocyclopropane-1-carboxylate synthase, Histidinol-phosphate, gene products of malY and cobC, Valine-pyruvate aminotransferase and Rhizopine catabolism regulatory protein.
Pssm-ID: 99734 [Multi-domain] Cd Length: 350 Bit Score: 43.10 E-value: 3.09e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446718383 149 MLIRAYHEAnGDfnrtKVIVPDSAHGTNPASATVAGFETITVKSNEHG--LVDLEDLKRVVNEETAALMLTNPN-----T 221
Cdd:cd00609 74 LLLRALLNP-GD----EVLVPDPTYPGYEAAARLAGAEVVPVPLDEEGgfLLDLELLEAAKTPKTKLLYLNNPNnptgaV 148
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446718383 222 LGlfEENILEMAEIVHNAG---------GKLYYDGANLNAVLSqarpGDMGFDVVHLN-LHKTF 275
Cdd:cd00609 149 LS--EEELEELAELAKKHGiliisdeayAELVYDGEPPPALAL----LDAYERVIVLRsFSKTF 206
|
|
| HisC |
COG0079 |
Histidinol-phosphate/aromatic aminotransferase or cobyric acid decarboxylase [Amino acid ... |
149-220 |
5.89e-04 |
|
Histidinol-phosphate/aromatic aminotransferase or cobyric acid decarboxylase [Amino acid transport and metabolism]; Histidinol-phosphate/aromatic aminotransferase or cobyric acid decarboxylase is part of the Pathway/BioSystem: Cobalamine/B12 biosynthesis
Pssm-ID: 439849 [Multi-domain] Cd Length: 341 Bit Score: 42.04 E-value: 5.89e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446718383 149 MLIRAYHEAnGDfnrtKVIVPD---SAHgtnPASATVAGFETITVKSNEHGLVDLEDLKRVVNEETAALMLTNPN 220
Cdd:COG0079 80 LLARAFLGP-GD----EVLVPEptfSEY---PIAARAAGAEVVEVPLDEDFSLDLDALLAAITERTDLVFLCNPN 146
|
|
| CsdA |
COG0520 |
Selenocysteine lyase/Cysteine desulfurase [Amino acid transport and metabolism]; |
184-248 |
1.57e-03 |
|
Selenocysteine lyase/Cysteine desulfurase [Amino acid transport and metabolism];
Pssm-ID: 440286 [Multi-domain] Cd Length: 396 Bit Score: 40.89 E-value: 1.57e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446718383 184 GFETITVKSNEHGLVDLEDLKRVVNEETAALMLTN-PNTLGLfeenIL---EMAEIVHNAGGKLYYDGA 248
Cdd:COG0520 128 GAEVRVIPLDEDGELDLEALEALLTPRTKLVAVTHvSNVTGT----VNpvkEIAALAHAHGALVLVDGA 192
|
|
| |
