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Conserved domains on  [gi|1491220486|gb|RLG97417|]
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aminomethyl-transferring glycine dehydrogenase subunit GcvPB [Candidatus Bathyarchaeota archaeon]

Protein Classification

glycine dehydrogenase subunit 2( domain architecture ID 10012203)

decarboxylating glycine dehydrogenase subunit 2 catalyzes the degradation of glycine as part of the glycine cleavage system

Graphical summary

 Zoom to residue level

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List of domain hits

 Name Accession Description Interval E-value
PRK04366 PRK04366
aminomethyl-transferring glycine dehydrogenase subunit GcvPB;
6-496 0e+00

aminomethyl-transferring glycine dehydrogenase subunit GcvPB;


:

Pssm-ID: 235292  Cd Length: 481  Bit Score: 780.83  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491220486   6 ADWKEPLIFEHSKPGRIGHMVTELEPELVTEIPLeelvPESLLRTEVPDLPEVGEMQVLRHYVRLSQMNYGVNAGkIYPL 85
Cdd:PRK04366    1 ARWDEPLIFELSRPGRRGYSLPELDVPEVLESLL----PEELLRKEPPELPEVSELEVVRHYTRLSQKNYGVDTG-FYPL 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491220486  86 GSCTMKYNPIVNELMAGLPKMAGQHPLQSPETTQGTLKMLYNLKMHFLDITGMDEATLQPAAGAHGEWTGIMLMREYHRE 165
Cdd:PRK04366   76 GSCTMKYNPKINEKVARLPGFAELHPLQPEETVQGALELMYELQEWLKEITGMDAVTLQPAAGAHGELTGLLMIRAYHEA 155

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491220486 166 RGELeQRTEIIVPDSAHGTNPASAHMAGFKTVEIPSNDHGMVDLEALKAAVGPQTAGLMLTNPNTLGIFESEISEISKII 245
Cdd:PRK04366  156 RGDT-KRTEVIVPDSAHGTNPASAAMAGFKVVEIPSNEDGLVDLEALKAAVGEDTAALMLTNPNTLGLFERNILEIAEIV 234

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491220486 246 HEAGGLMYYDGANLNAIMGWCRPGDMGFDIIHSNLHKTFSTPHggggpgagpvavKKFLAKYLPIPDIIEEDGVYKLDYD 325
Cdd:PRK04366  235 HEAGGLLYYDGANLNAILGKARPGDMGFDVVHLNLHKTFSTPHggggpgsgpvgvKEELAPFLPVPVVEKDGDRYRLDYD 314

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491220486 326 KPMSMGKVHGFHGNVGVSLKAYTYMYTMGGSGLKESSELAVLNANYISRQLvsEKGYELTFDpeKPRKHEAVISAGPmLN 405
Cdd:PRK04366  315 RPKSIGRVRAFYGNFGVLVRAYAYIRSLGAEGLREVSEDAVLNANYLKARL--KDIYDLPYD--RPCMHEFVLSGKK-LK 389

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491220486 406 DTGVSALYISKMLLDYGMHAPTTYFPLIVPEALMIEPTESEPVEALDEFIVALKEINDIAYSDPERVLSAPHNTAVTKID 485
Cdd:PRK04366  390 ETGVRTLDIAKRLLDYGFHPPTIYFPLIVPEALMIEPTETESKETLDAFIAAMKQIAEEAKENPELVKEAPHNTPVRRLD 469

                         490
                  ....*....|.
gi 1491220486 486 EARAAHPKTIC 496
Cdd:PRK04366  470 EVKAARKPVLR 480
 
Name Accession Description Interval E-value
PRK04366 PRK04366
aminomethyl-transferring glycine dehydrogenase subunit GcvPB;
6-496 0e+00

aminomethyl-transferring glycine dehydrogenase subunit GcvPB;


Pssm-ID: 235292  Cd Length: 481  Bit Score: 780.83  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491220486   6 ADWKEPLIFEHSKPGRIGHMVTELEPELVTEIPLeelvPESLLRTEVPDLPEVGEMQVLRHYVRLSQMNYGVNAGkIYPL 85
Cdd:PRK04366    1 ARWDEPLIFELSRPGRRGYSLPELDVPEVLESLL----PEELLRKEPPELPEVSELEVVRHYTRLSQKNYGVDTG-FYPL 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491220486  86 GSCTMKYNPIVNELMAGLPKMAGQHPLQSPETTQGTLKMLYNLKMHFLDITGMDEATLQPAAGAHGEWTGIMLMREYHRE 165
Cdd:PRK04366   76 GSCTMKYNPKINEKVARLPGFAELHPLQPEETVQGALELMYELQEWLKEITGMDAVTLQPAAGAHGELTGLLMIRAYHEA 155

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491220486 166 RGELeQRTEIIVPDSAHGTNPASAHMAGFKTVEIPSNDHGMVDLEALKAAVGPQTAGLMLTNPNTLGIFESEISEISKII 245
Cdd:PRK04366  156 RGDT-KRTEVIVPDSAHGTNPASAAMAGFKVVEIPSNEDGLVDLEALKAAVGEDTAALMLTNPNTLGLFERNILEIAEIV 234

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491220486 246 HEAGGLMYYDGANLNAIMGWCRPGDMGFDIIHSNLHKTFSTPHggggpgagpvavKKFLAKYLPIPDIIEEDGVYKLDYD 325
Cdd:PRK04366  235 HEAGGLLYYDGANLNAILGKARPGDMGFDVVHLNLHKTFSTPHggggpgsgpvgvKEELAPFLPVPVVEKDGDRYRLDYD 314

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491220486 326 KPMSMGKVHGFHGNVGVSLKAYTYMYTMGGSGLKESSELAVLNANYISRQLvsEKGYELTFDpeKPRKHEAVISAGPmLN 405
Cdd:PRK04366  315 RPKSIGRVRAFYGNFGVLVRAYAYIRSLGAEGLREVSEDAVLNANYLKARL--KDIYDLPYD--RPCMHEFVLSGKK-LK 389

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491220486 406 DTGVSALYISKMLLDYGMHAPTTYFPLIVPEALMIEPTESEPVEALDEFIVALKEINDIAYSDPERVLSAPHNTAVTKID 485
Cdd:PRK04366  390 ETGVRTLDIAKRLLDYGFHPPTIYFPLIVPEALMIEPTETESKETLDAFIAAMKQIAEEAKENPELVKEAPHNTPVRRLD 469

                         490
                  ....*....|.
gi 1491220486 486 EARAAHPKTIC 496
Cdd:PRK04366  470 EVKAARKPVLR 480
GcvP2 COG1003
Glycine cleavage system protein P (pyridoxal-binding), C-terminal domain [Amino acid transport ...
 36-501 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: 712.96  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491220486  36 EIPLEELVPESLLRTEVPDLPEVGEMQVLRHYVRLSQMNYGVNAGkIYPLGSCTMKYNPIVNELMAGLPKMAGQHPLQSP 115
Cdd:COG1003     7 EADAASLLPEALLRKSPVFLPEVSETEVLRHYTRLSQKNLGLDTG-MIPLGSCTMKYNPKINEEPATLPGFANLHPFQPE 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491220486 116 ETTQGTLKMLYNLKMHFLDITGMDEATLQPAAGAHGEWTGIMLMREYHRERGElEQRTEIIVPDSAHGTNPASAHMAGFK 195
Cdd:COG1003    86 ETVQGYLELMYELEEWLAEITGMDAVSLQPNAGAQGEYAGLLAIRAYHESRGE-GHRNEILIPDSAHGTNPASAAMAGFK 164

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491220486 196 TVEIPSNDHGMVDLEALKAAVGPQTAGLMLTNPNTLGIFESEISEISKIIHEAGGLMYYDGANLNAIMGWCRPGDMGFDI 275
Cdd:COG1003   165 VVVVKSDEDGNVDLEDLKAKVGDRTAALMLTNPSTHGVFEEDIKEICDIVHEAGGLVYYDGANLNAIVGLARPGDMGFDV 244

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491220486 276 IHSNLHKTFSTPHggggpgagpvavKKFLAKYLPIPDIIEEDGVYKLDYDKPMSMGKVHGFHGNVGVSLKAYTYMYTMGG 355
Cdd:COG1003   245 CHLNLHKTFSTPHggggpgsgpvgvKEHLAPFLPGPPVVKDGDKYRLDYDRPKSIGRSAAFYGNAGVLVRAYAYIRMMGA 324

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491220486 356 SGLKESSELAVLNANYISRQLvsEKGYELTFDPEKPRKHEAVISAGPMLNDTGVSALYISKMLLDYGMHAPTTYFPLIVP 435
Cdd:COG1003   325 EGLREATEVAVLNANYLAARL--KDHYPVLYTGNGRCAHEFILDLRPLKKETGVTTLDIAKRLLDYGFHAPTMYFPLIVP 402

                         410       420       430       440       450       460
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1491220486 436 EALMIEPTESEPVEALDEFIVALKEINDIAYSDPERVLSAPHNTAVTKIDEARAAHPktICLSWRK 501
Cdd:COG1003   403 ETLMIEPTESESKEELDRFIDAMIAIREEAREDPEPLKNAPHTTPVRRLDEVYADRN--LVLTWRE 466
GDC-P cd00613
Glycine cleavage system P-protein, alpha- and beta-subunits. This family consists of Glycine ...
 60-458 3.15e-129

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: 381.58  E-value: 3.15e-129
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491220486  60 EMQVLRHYVRLSQMNYGVNAGkIYPLGSCTMKYNPIVNELMAGLPKM-AGQHPLQSPETTQGTLKMLYNLKMHFLDITGM 138
Cdd:cd00613     1 ETEVLRHLKRLASKNKALDQS-MSFLGSGTYKHNPPAVIKRNILENEfYTAYTPYQPEISQGRLQALFELQTMLCELTGM 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491220486 139 D--EATLQPAAGAHGEWTGIMLMREYHrergeleQRTEIIVPDSAHGTNPASAHMA----GFKTVEIPSNDHGMVDLEAL 212
Cdd:cd00613    80 DvaNASLQDEATAAAEAAGLAAIRAYH-------KRNKVLVPDSAHPTNPAVARTRgeplGIEVVEVPSDEGGTVDLEAL 152

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491220486 213 KAAVGPQTAGLMLTNPNTLGIFESEISEISKIIHEAGGLMYYDGANLNAImGWCRPGDMGFDIIHSNLHKTFsTPHGGGG 292
Cdd:cd00613   153 KEEVSEEVAALMVQYPNTLGVFEDLIKEIADIAHSAGALVYVDGDNLNLT-GLKPPGEYGADIVVGNLQKTG-VPHGGGG 230

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491220486 293 PGAGPVAVKKFLAKYLPIPDI-----IEEDGVYKLDYDKPMS-----MGKVHGFHGNVGVSLKAYTYMYTMGGSGLKESS 362
Cdd:cd00613   231 PGAGFFAVKKELVRFLPGRLVgvtkdAEGNRAFRLALQTREQhirreKATSNICTGQALLALMAAMYIVYLGPEGLKEIA 310

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491220486 363 ELAVLNANYISRQLvSEKGYELTFDpeKPRKHEAVISAGPmlnDTGVSALYISKMLLDYGMHAPTTYFPliVPEALMIEP 442
Cdd:cd00613   311 ERAHLNANYLAKRL-KEVGGVLPFN--GPFFHEFVLRLPP---LYGIRAEDLAKALIDGGFHAPTMYLP--VDGTLMIEP 382

                         410
                  ....*....|....*.
gi 1491220486 443 TESEPVEALDEFIVAL 458
Cdd:cd00613   383 TETETKEELDALLEAL 398
Aminotran_5 pfam00266
Aminotransferase class-V; This domain is found in amino transferases, and other enzymes ...
 169-282 2.64e-07

Aminotransferase class-V; This domain is found in amino transferases, and other enzymes including cysteine desulphurase EC:4.4.1.-.


Pssm-ID: 425567 [Multi-domain]  Cd Length: 368  Bit Score: 52.63  E-value: 2.64e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491220486 169 LEQRTEIIVPDSAHGTNPASAHMA----GFKTVEIPSNDHGMVDLEALKAAVGPQTAGLMLT-NPNTLGIFEsEISEISK 243
Cdd:pfam00266  85 LKPGDEIVITEMEHHANLVPWQELakrtGARVRVLPLDEDGLLDLDELEKLITPKTKLVAIThVSNVTGTIQ-PVPEIGK 163

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 1491220486 244 IIHEAGGLMYYDGAnlNAIMGwcRPGDM---GFDIIHSNLHK 282
Cdd:pfam00266 164 LAHQYGALVLVDAA--QAIGH--RPIDVqklGVDFLAFSGHK 201
 
Name Accession Description Interval E-value
PRK04366 PRK04366
aminomethyl-transferring glycine dehydrogenase subunit GcvPB;
6-496 0e+00

aminomethyl-transferring glycine dehydrogenase subunit GcvPB;


Pssm-ID: 235292  Cd Length: 481  Bit Score: 780.83  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491220486   6 ADWKEPLIFEHSKPGRIGHMVTELEPELVTEIPLeelvPESLLRTEVPDLPEVGEMQVLRHYVRLSQMNYGVNAGkIYPL 85
Cdd:PRK04366    1 ARWDEPLIFELSRPGRRGYSLPELDVPEVLESLL----PEELLRKEPPELPEVSELEVVRHYTRLSQKNYGVDTG-FYPL 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491220486  86 GSCTMKYNPIVNELMAGLPKMAGQHPLQSPETTQGTLKMLYNLKMHFLDITGMDEATLQPAAGAHGEWTGIMLMREYHRE 165
Cdd:PRK04366   76 GSCTMKYNPKINEKVARLPGFAELHPLQPEETVQGALELMYELQEWLKEITGMDAVTLQPAAGAHGELTGLLMIRAYHEA 155

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491220486 166 RGELeQRTEIIVPDSAHGTNPASAHMAGFKTVEIPSNDHGMVDLEALKAAVGPQTAGLMLTNPNTLGIFESEISEISKII 245
Cdd:PRK04366  156 RGDT-KRTEVIVPDSAHGTNPASAAMAGFKVVEIPSNEDGLVDLEALKAAVGEDTAALMLTNPNTLGLFERNILEIAEIV 234

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491220486 246 HEAGGLMYYDGANLNAIMGWCRPGDMGFDIIHSNLHKTFSTPHggggpgagpvavKKFLAKYLPIPDIIEEDGVYKLDYD 325
Cdd:PRK04366  235 HEAGGLLYYDGANLNAILGKARPGDMGFDVVHLNLHKTFSTPHggggpgsgpvgvKEELAPFLPVPVVEKDGDRYRLDYD 314

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491220486 326 KPMSMGKVHGFHGNVGVSLKAYTYMYTMGGSGLKESSELAVLNANYISRQLvsEKGYELTFDpeKPRKHEAVISAGPmLN 405
Cdd:PRK04366  315 RPKSIGRVRAFYGNFGVLVRAYAYIRSLGAEGLREVSEDAVLNANYLKARL--KDIYDLPYD--RPCMHEFVLSGKK-LK 389

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491220486 406 DTGVSALYISKMLLDYGMHAPTTYFPLIVPEALMIEPTESEPVEALDEFIVALKEINDIAYSDPERVLSAPHNTAVTKID 485
Cdd:PRK04366  390 ETGVRTLDIAKRLLDYGFHPPTIYFPLIVPEALMIEPTETESKETLDAFIAAMKQIAEEAKENPELVKEAPHNTPVRRLD 469

                         490
                  ....*....|.
gi 1491220486 486 EARAAHPKTIC 496
Cdd:PRK04366  470 EVKAARKPVLR 480
GcvP2 COG1003
Glycine cleavage system protein P (pyridoxal-binding), C-terminal domain [Amino acid transport ...
 36-501 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: 712.96  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491220486  36 EIPLEELVPESLLRTEVPDLPEVGEMQVLRHYVRLSQMNYGVNAGkIYPLGSCTMKYNPIVNELMAGLPKMAGQHPLQSP 115
Cdd:COG1003     7 EADAASLLPEALLRKSPVFLPEVSETEVLRHYTRLSQKNLGLDTG-MIPLGSCTMKYNPKINEEPATLPGFANLHPFQPE 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491220486 116 ETTQGTLKMLYNLKMHFLDITGMDEATLQPAAGAHGEWTGIMLMREYHRERGElEQRTEIIVPDSAHGTNPASAHMAGFK 195
Cdd:COG1003    86 ETVQGYLELMYELEEWLAEITGMDAVSLQPNAGAQGEYAGLLAIRAYHESRGE-GHRNEILIPDSAHGTNPASAAMAGFK 164

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491220486 196 TVEIPSNDHGMVDLEALKAAVGPQTAGLMLTNPNTLGIFESEISEISKIIHEAGGLMYYDGANLNAIMGWCRPGDMGFDI 275
Cdd:COG1003   165 VVVVKSDEDGNVDLEDLKAKVGDRTAALMLTNPSTHGVFEEDIKEICDIVHEAGGLVYYDGANLNAIVGLARPGDMGFDV 244

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491220486 276 IHSNLHKTFSTPHggggpgagpvavKKFLAKYLPIPDIIEEDGVYKLDYDKPMSMGKVHGFHGNVGVSLKAYTYMYTMGG 355
Cdd:COG1003   245 CHLNLHKTFSTPHggggpgsgpvgvKEHLAPFLPGPPVVKDGDKYRLDYDRPKSIGRSAAFYGNAGVLVRAYAYIRMMGA 324

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491220486 356 SGLKESSELAVLNANYISRQLvsEKGYELTFDPEKPRKHEAVISAGPMLNDTGVSALYISKMLLDYGMHAPTTYFPLIVP 435
Cdd:COG1003   325 EGLREATEVAVLNANYLAARL--KDHYPVLYTGNGRCAHEFILDLRPLKKETGVTTLDIAKRLLDYGFHAPTMYFPLIVP 402

                         410       420       430       440       450       460
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1491220486 436 EALMIEPTESEPVEALDEFIVALKEINDIAYSDPERVLSAPHNTAVTKIDEARAAHPktICLSWRK 501
Cdd:COG1003   403 ETLMIEPTESESKEELDRFIDAMIAIREEAREDPEPLKNAPHTTPVRRLDEVYADRN--LVLTWRE 466
GDC-P cd00613
Glycine cleavage system P-protein, alpha- and beta-subunits. This family consists of Glycine ...
 60-458 3.15e-129

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: 381.58  E-value: 3.15e-129
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491220486  60 EMQVLRHYVRLSQMNYGVNAGkIYPLGSCTMKYNPIVNELMAGLPKM-AGQHPLQSPETTQGTLKMLYNLKMHFLDITGM 138
Cdd:cd00613     1 ETEVLRHLKRLASKNKALDQS-MSFLGSGTYKHNPPAVIKRNILENEfYTAYTPYQPEISQGRLQALFELQTMLCELTGM 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491220486 139 D--EATLQPAAGAHGEWTGIMLMREYHrergeleQRTEIIVPDSAHGTNPASAHMA----GFKTVEIPSNDHGMVDLEAL 212
Cdd:cd00613    80 DvaNASLQDEATAAAEAAGLAAIRAYH-------KRNKVLVPDSAHPTNPAVARTRgeplGIEVVEVPSDEGGTVDLEAL 152

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491220486 213 KAAVGPQTAGLMLTNPNTLGIFESEISEISKIIHEAGGLMYYDGANLNAImGWCRPGDMGFDIIHSNLHKTFsTPHGGGG 292
Cdd:cd00613   153 KEEVSEEVAALMVQYPNTLGVFEDLIKEIADIAHSAGALVYVDGDNLNLT-GLKPPGEYGADIVVGNLQKTG-VPHGGGG 230

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491220486 293 PGAGPVAVKKFLAKYLPIPDI-----IEEDGVYKLDYDKPMS-----MGKVHGFHGNVGVSLKAYTYMYTMGGSGLKESS 362
Cdd:cd00613   231 PGAGFFAVKKELVRFLPGRLVgvtkdAEGNRAFRLALQTREQhirreKATSNICTGQALLALMAAMYIVYLGPEGLKEIA 310

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491220486 363 ELAVLNANYISRQLvSEKGYELTFDpeKPRKHEAVISAGPmlnDTGVSALYISKMLLDYGMHAPTTYFPliVPEALMIEP 442
Cdd:cd00613   311 ERAHLNANYLAKRL-KEVGGVLPFN--GPFFHEFVLRLPP---LYGIRAEDLAKALIDGGFHAPTMYLP--VDGTLMIEP 382

                         410
                  ....*....|....*.
gi 1491220486 443 TESEPVEALDEFIVAL 458
Cdd:cd00613   383 TETETKEELDALLEAL 398
PLN02414 PLN02414
glycine dehydrogenase (decarboxylating)
 60-486 4.49e-98

glycine dehydrogenase (decarboxylating)


Pssm-ID: 178035 [Multi-domain]  Cd Length: 993  Bit Score: 317.86  E-value: 4.49e-98
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491220486  60 EMQVLRHYVRLSQMNYGVNAGKIyPLGSCTMKYNPIVNELMAGLPKMAGQHPLQSPETTQGTLKMLYNLKMHFLDITGMD 139
Cdd:PLN02414  506 EHELLRYLHRLQNKDLSLVHSMI-PLGSCTMKLNATTEMMPVTWPEFANIHPFAPVDQAQGYQEMFEDLGDLLCEITGFD 584

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491220486 140 EATLQPAAGAHGEWTGIMLMREYHRERGElEQRTEIIVPDSAHGTNPASAHMAGFKTVEIPSNDHGMVDLEALKAAVGPQ 219
Cdd:PLN02414  585 SFSLQPNAGAAGEYAGLMVIRAYHLSRGD-HHRNVCIIPVSAHGTNPASAAMCGMKIVVVGTDAKGNINIEELRKAAEAH 663

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491220486 220 T---AGLMLTNPNTLGIFESEISEISKIIHEAGGLMYYDGANLNAIMGWCRPGDMGFDIIHSNLHKTFSTPHGGGGPGAG 296
Cdd:PLN02414  664 KdnlAALMVTYPSTHGVYEEGIDEICDIIHDNGGQVYMDGANMNAQVGLTSPGFIGADVCHLNLHKTFCIPHGGGGPGMG 743

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491220486 297 PVAVKKFLAKYLPIPDIIEEDGVykLDYDKPMSMGKVHGF-HGNVGVSLKAYTYMYTMGGSGLKESSELAVLNANYISRQ 375
Cdd:PLN02414  744 PIGVKKHLAPFLPSHPVVPTGGI--PRPEKTQPLGTISAApWGSALILPISYTYIAMMGSEGLTDASKIAILNANYMAKR 821

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491220486 376 LvsEKGYELTFD-PEKPRKHEAVISAGPMLNDTGVSALYISKMLLDYGMHAPTTYFPliVPEALMIEPTESEPVEALDEF 454
Cdd:PLN02414  822 L--EGHYPVLFRgKNGTCAHEFIIDLRPFKNTAGIEPEDVAKRLMDYGFHAPTMSWP--VPGTLMIEPTESESKAELDRF 897

                         410       420       430       440
                  ....*....|....*....|....*....|....*....|
gi 1491220486 455 IVAL----KEINDI--AYSDPE-RVL-SAPHNTAVTKIDE 486
Cdd:PLN02414  898 CDALisirEEIADIenGKADREnNVLkGAPHPPSLLMADK 937
AAT_I cd01494
Aspartate aminotransferase (AAT) superfamily (fold type I) of pyridoxal phosphate (PLP) ...
 125-284 6.40e-19

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: 83.97  E-value: 6.40e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491220486 125 LYNLKMHFLDIT--GMDEATLQPAaGAHGEWTGIMLMREYHRErgeleqrteIIVPDSAHGTNPAS-AHMAGFKTVEIPS 201
Cdd:cd01494     2 LEELEEKLARLLqpGNDKAVFVPS-GTGANEAALLALLGPGDE---------VIVDANGHGSRYWVaAELAGAKPVPVPV 71

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491220486 202 NDHGMVDLEAL---KAAVGPQTAGLMLTNPNTLGIFESEISEISKIIHEAGGLMYYDGANLNAIMGW--CRPGDMGFDII 276
Cdd:cd01494    72 DDAGYGGLDVAileELKAKPNVALIVITPNTTSGGVLVPLKEIRKIAKEYGILLLVDAASAGGASPApgVLIPEGGADVV 151


                  ....*...
gi 1491220486 277 HSNLHKTF 284
Cdd:cd01494   152 TFSLHKNL 159
PRK00451 PRK00451
aminomethyl-transferring glycine dehydrogenase subunit GcvPA;
39-461 1.69e-18

aminomethyl-transferring glycine dehydrogenase subunit GcvPA;


Pssm-ID: 234769 [Multi-domain]  Cd Length: 447  Bit Score: 87.89  E-value: 1.69e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491220486  39 LEEL---VPESLLRTEVPDLPE-VGEMQVLRHYVRLSQMNYGVN-------AGkIYPlgsctmKYNP-IVNELmaglpkm 106
Cdd:PRK00451   24 IDELfadIPEELRLKRPLDLPPgLSEMELLRHLRELAAKNKTAEeypsflgAG-AYD------HYIPaVVDHI------- 89

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491220486 107 AGQH-------PLQsPETTQGTLKMLY-------NLkmhfldiTGMD--EATLQPAAGAHGEwtgIMLMReyHRERGele 170
Cdd:PRK00451   90 ISRSefytaytPYQ-PEISQGTLQAIFeyqtmicEL-------TGMDvaNASMYDGATALAE---AALMA--VRITK--- 153

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491220486 171 qRTEIIVPDSAHgtnPAS-------AHMAGFKTVEIPSNDhGMVDLEALKAAVGPQTAGLMLTNPNTLGIFEsEISEISK 243
Cdd:PRK00451  154 -RKKVLVSGAVH---PEYrevlktyLKGQGIEVVEVPYED-GVTDLEALEAAVDDDTAAVVVQYPNFFGVIE-DLEEIAE 227

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491220486 244 IIHEAGGLMyydganlnaIMGwC---------RPGDMGFDI---------IHSNlhktFSTPHGGggpgagpvavkkFLA 305
Cdd:PRK00451  228 IAHAGGALF---------IVG-VdpvslgllkPPGEYGADIvvgegqplgIPLS----FGGPYLG------------FFA 281

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491220486 306 ---KYL-PIPDII-----EEDGVYkldydkpmsmgkvhGF---------HG-------NVG-----VSLKAYTYMYTMGG 355
Cdd:PRK00451  282 trkKLVrQMPGRLvgetvDADGKR--------------GFvltlqareqHIrrekatsNICtnqalNALAAAIYMSLLGP 347

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491220486 356 SGLKESSELAVLNANYISRQLVSEKGYELtFDpeKPRKHEAVIsagpmlnDTGVSALYISKMLLDYGMHAPttyFPL--I 433
Cdd:PRK00451  348 EGLRELAEQNHQKAHYLAERLAEIGGVEL-FD--GPFFNEFVV-------RLPKPAEEVNEALLEKGILGG---YDLgrY 414

                         490       500       510
                  ....*....|....*....|....*....|.
gi 1491220486 434 VPE---ALMIEPTESEPVEALDEFIVALKEI 461
Cdd:PRK00451  415 YPElgnHLLVCVTEKRTKEDIDALVAALGEV 445
GcvP1 COG0403
Glycine cleavage system protein P (pyridoxal-binding), N-terminal domain [Amino acid transport ...
 39-275 3.08e-17

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: 83.93  E-value: 3.08e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491220486  39 LEEL---VPESLLRTEVPDLPE-VGEMQVLRHYVRLSQMNygvnagKIYP--LGsctmkynpivnelmaglpkmAG--QH 110
Cdd:COG0403    27 LDELfddIPAEIRLKRPLDLPEaLSEAELLRHLRALAAKN------KVLTsfIG--------------------AGyyDH 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491220486 111 --------------------PLQsPETTQGTLKMLYNlkmhF----LDITGM--------DEATlqpAAGahgewTGIML 158
Cdd:COG0403    81 yvpavvrnilerpefytaytPYQ-PEISQGRLQALFE----FqtmvAELTGMdvanaslyDGAT---AAA-----EAMLM 147

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491220486 159 MREYHRergeleQRTEIIVPDSAHgtnPAS-------AHMAGFKTVEIPSNDhGMVDLEALKAAVGPQTAGLMLTNPNTL 231
Cdd:COG0403   148 ARRVTK------RSNKVLVSEDVH---PQTravlktyAEPLGIEVVEVPDED-GVTDLEALKALLDDDVAGVLVQYPNFF 217

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....
gi 1491220486 232 GIFEsEISEISKIIHEAGGLMYYdGANLNAIMGWCRPGDMGFDI 275
Cdd:COG0403   218 GVIE-DLRAIAEAAHAAGALVIV-AADPLSLGLLKPPGELGADI 259
Aminotran_5 pfam00266
Aminotransferase class-V; This domain is found in amino transferases, and other enzymes ...
 169-282 2.64e-07

Aminotransferase class-V; This domain is found in amino transferases, and other enzymes including cysteine desulphurase EC:4.4.1.-.


Pssm-ID: 425567 [Multi-domain]  Cd Length: 368  Bit Score: 52.63  E-value: 2.64e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491220486 169 LEQRTEIIVPDSAHGTNPASAHMA----GFKTVEIPSNDHGMVDLEALKAAVGPQTAGLMLT-NPNTLGIFEsEISEISK 243
Cdd:pfam00266  85 LKPGDEIVITEMEHHANLVPWQELakrtGARVRVLPLDEDGLLDLDELEKLITPKTKLVAIThVSNVTGTIQ-PVPEIGK 163

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 1491220486 244 IIHEAGGLMYYDGAnlNAIMGwcRPGDM---GFDIIHSNLHK 282
Cdd:pfam00266 164 LAHQYGALVLVDAA--QAIGH--RPIDVqklGVDFLAFSGHK 201
DOPA_deC_like cd06450
DOPA decarboxylase family. This family belongs to pyridoxal phosphate (PLP)-dependent ...
 154-257 5.94e-07

DOPA decarboxylase family. This family belongs to pyridoxal phosphate (PLP)-dependent aspartate aminotransferase superfamily (fold I). The major groups in this CD correspond to DOPA/tyrosine decarboxylase (DDC), histidine decarboxylase (HDC), and glutamate decarboxylase (GDC). DDC is active as a dimer and catalyzes the decarboxylation of tyrosine. GDC catalyzes the decarboxylation of glutamate and HDC catalyzes the decarboxylation of histidine.


Pssm-ID: 99743 [Multi-domain]  Cd Length: 345  Bit Score: 51.44  E-value: 5.94e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491220486 154 TGIMLMREYHRER-----GELEQRTEIIVPDSAHGTNPASAHMAGFKTVEIPSNDHGMVDLEALKAAV------GPQTAG 222
Cdd:cd06450    72 LALLAARDRARKRlkaggGRGIDKLVIVCSDQAHVSVEKAAAYLDVKVRLVPVDEDGRMDPEALEAAIdedkaeGLNPIM 151

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 1491220486 223 LMLTNPNT-LGIFEsEISEISKIIHEAGGLMYYDGA 257
Cdd:cd06450   152 VVATAGTTdTGAID-PLEEIADLAEKYDLWLHVDAA 186
CsdA COG0520
Selenocysteine lyase/Cysteine desulfurase [Amino acid transport and metabolism];
167-257 1.05e-06

Selenocysteine lyase/Cysteine desulfurase [Amino acid transport and metabolism];


Pssm-ID: 440286 [Multi-domain]  Cd Length: 396  Bit Score: 50.91  E-value: 1.05e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491220486 167 GELEQRTEIIVPDSAHGTNPASAHMA----GFKTVEIPSNDHGMVDLEALKAAVGPQTAGLMLTN-PNTLGIfESEISEI 241
Cdd:COG0520    98 GRLKPGDEILITEMEHHSNIVPWQELaertGAEVRVIPLDEDGELDLEALEALLTPRTKLVAVTHvSNVTGT-VNPVKEI 176

                          90
                  ....*....|....*.
gi 1491220486 242 SKIIHEAGGLMYYDGA 257
Cdd:COG0520   177 AALAHAHGALVLVDGA 192
AspB COG0436
Aspartate/methionine/tyrosine aminotransferase [Amino acid transport and metabolism]; ...
 174-229 2.03e-06

Aspartate/methionine/tyrosine aminotransferase [Amino acid transport and metabolism]; Aspartate/methionine/tyrosine aminotransferase is part of the Pathway/BioSystem: Isoleucine, leucine, valine biosynthesis


Pssm-ID: 440205 [Multi-domain]  Cd Length: 387  Bit Score: 50.13  E-value: 2.03e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1491220486 174 EIIVPDSAHGTNPASAHMAGFKTVEIPSN--DHGMVDLEALKAAVGPQTAGLMLTNPN 229
Cdd:COG0436   116 EVLVPDPGYPSYRAAVRLAGGKPVPVPLDeeNGFLPDPEALEAAITPRTKAIVLNSPN 173
HisC COG0079
Histidinol-phosphate/aromatic aminotransferase or cobyric acid decarboxylase [Amino acid ...
 169-229 1.26e-05

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: 47.43  E-value: 1.26e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1491220486 169 LEQRTEIIVPD---SAHgtnPASAHMAGFKTVEIPSNDHGMVDLEALKAAVGPQTAGLMLTNPN 229
Cdd:COG0079    86 LGPGDEVLVPEptfSEY---PIAARAAGAEVVEVPLDEDFSLDLDALLAAITERTDLVFLCNPN 146
AAT_like cd00609
Aspartate aminotransferase family. This family belongs to pyridoxal phosphate (PLP)-dependent ...
 174-287 1.76e-05

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: 46.95  E-value: 1.76e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491220486 174 EIIVPDSAHGTNPASAHMAGFKTVEIPSNDHGM--VDLEALKAAVGPQTAGLMLTNP-NTLGIF--ESEISEISKIIHEA 248
Cdd:cd00609    85 EVLVPDPTYPGYEAAARLAGAEVVPVPLDEEGGflLDLELLEAAKTPKTKLLYLNNPnNPTGAVlsEEELEELAELAKKH 164

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 1491220486 249 GGL---------MYYDGANLNAIMGWcrpgDMGFDIIHSN-LHKTFSTP 287
Cdd:cd00609   165 GILiisdeayaeLVYDGEPPPALALL----DAYERVIVLRsFSKTFGLP 209
GDC-P pfam02347
Glycine cleavage system P-protein; This family consists of Glycine cleavage system P-proteins ...
 111-275 2.36e-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: 43.52  E-value: 2.36e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491220486 111 PLQsPETTQGTLKMLYNLKMHFLDITGMD--EATLQPAAGAHGEwtgIMLMREYHRERgeleqRTEIIVPDSAHGTNPAS 188
Cdd:pfam02347  99 PYQ-PEISQGRLEALLNFQTMICDLTGLDiaNASLLDEGTAAAE---AMALAARASKK-----KGKKFVVDKDVHPQTLE 169

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491220486 189 -----AHMAGFKTVEipsndhgmVDLEALKAAVGPQTAGLMLTNPNTLGIFEsEISEISKIIHEaGGLMYYDGANLNAIM 263
Cdd:pfam02347 170 vlktrAKPFGIEIVE--------VDYTEEGVTDLKDVFGVLVQYPNTDGRIE-DYKELIELAHQ-RKSLVVVAADLLALT 239

                         170
                  ....*....|..
gi 1491220486 264 GWCRPGDMGFDI 275
Cdd:pfam02347 240 LLKPPGEFGADI 251
argD PRK01278
acetylornithine transaminase protein; Provisional
 155-225 3.21e-04

acetylornithine transaminase protein; Provisional


Pssm-ID: 179270 [Multi-domain]  Cd Length: 389  Bit Score: 42.90  E-value: 3.21e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491220486 155 GIMLMREYHRERGElEQRTEIIVPDSA-HG--------TNPASAH------MAGFKTVEIPsndhgmvDLEALKAAVGPQ 219
Cdd:PRK01278  104 AIKTARRYHYGKGH-PERYRIITFEGAfHGrtlatiaaGGQEKYLegfgplVPGFDQVPFG-------DIEALKAAITPN 175


                  ....*.
gi 1491220486 220 TAGLML 225
Cdd:PRK01278  176 TAAILI 181
PLN02509 PLN02509
cystathionine beta-lyase
 208-278 4.63e-04

cystathionine beta-lyase


Pssm-ID: 178125 [Multi-domain]  Cd Length: 464  Bit Score: 42.71  E-value: 4.63e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1491220486 208 DLEALKAAVGPQTAGLMLTNPNTLGIFESEISEISKIIHEAGGLMYYDganlNAIMG--WCRPGDMGFDII-HS 278
Cdd:PLN02509  206 NLDEVAAAIGPQTKLVWLESPTNPRQQISDIRKIAEMAHAQGALVLVD----NSIMSpvLSRPLELGADIVmHS 275
TA_like cd06502
Low-specificity threonine aldolase (TA). This family belongs to pyridoxal phosphate (PLP) ...
 127-287 5.60e-04

Low-specificity threonine aldolase (TA). This family belongs to pyridoxal phosphate (PLP)-dependent aspartate aminotransferase superfamily (fold I). TA catalyzes the conversion of L-threonine or L-allo-threonine to glycine and acetaldehyde in a secondary glycine biosynthetic pathway.


Pssm-ID: 99748 [Multi-domain]  Cd Length: 338  Bit Score: 42.32  E-value: 5.60e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491220486 127 NLKMHFLDITGMDEATLQPAaGAHGEWTGIMLmreyHRERGEleqrtEIIVPDSAHGTNP---ASAHMAGFKTVEIPSND 203
Cdd:cd06502    36 KLEARAAELFGKEAALFVPS-GTAANQLALAA----HTQPGG-----SVICHETAHIYTDeagAPEFLSGVKLLPVPGEN 105

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491220486 204 hGMVDLEALKAAV-------GPQTAGLMLTNPNTLGIFES--EISEISKIIHEAGGLMYYDGANL-NA-------IMGWC 266
Cdd:cd06502   106 -GKLTPEDLEAAIrprddihFPPPSLVSLENTTEGGTVYPldELKAISALAKENGLPLHLDGARLaNAaaalgvaLKTYK 184

                         170       180
                  ....*....|....*....|.
gi 1491220486 267 RpgdmGFDIIHSNLHKTFSTP 287
Cdd:cd06502   185 S----GVDSVSFCLSKGGGAP 201
PLN02651 PLN02651
cysteine desulfurase
 193-257 2.16e-03

cysteine desulfurase


Pssm-ID: 178257 [Multi-domain]  Cd Length: 364  Bit Score: 40.41  E-value: 2.16e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1491220486 193 GFKTVEIPSNDHGMVDLEALKAAVGPQTA--GLMLTNpNTLGIFESeISEISKIIHEAGGLMYYDGA 257
Cdd:PLN02651  112 GFEVTYLPVKSDGLVDLDELAAAIRPDTAlvSVMAVN-NEIGVIQP-VEEIGELCREKKVLFHTDAA 176
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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