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Conserved domains on  [gi|505171573|ref|WP_015358675|]
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aminomethyl-transferring glycine dehydrogenase subunit GcvPB [Thermoclostridium stercorarium]

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;
2-483 0e+00

aminomethyl-transferring glycine dehydrogenase subunit GcvPB;


:

Pssm-ID: 235292  Cd Length: 481  Bit Score: 923.36  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505171573   2 LKKEEKLIFELSVPGKGTNLLPECDVEKVeIKNLIPEEYLRNEEIDLPEVNEVDVVRHFTHLSQKNYGVDSGFYPLGSCT 81
Cdd:PRK04366   1 ARWDEPLIFELSRPGRRGYSLPELDVPEV-LESLLPEELLRKEPPELPEVSELEVVRHYTRLSQKNYGVDTGFYPLGSCT 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505171573  82 MKYNPKINEEVSKLPGFMKVHPYQPEETVQGCLQLLYQTERFLSEITGMDRFSLQPAAGAHGEMTGLMIIKAFHQKNGDY 161
Cdd:PRK04366  80 MKYNPKINEKVARLPGFAELHPLQPEETVQGALELMYELQEWLKEITGMDAVTLQPAAGAHGELTGLLMIRAYHEARGDT 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505171573 162 KRTKIIVPDSAHGTNPASAAAVGFDVVEVKSNDRGGIDIDALRELMSDEVAGLMLTNPNTLGLFDENIDLIAEIVHNAGG 241
Cdd:PRK04366 160 KRTEVIVPDSAHGTNPASAAMAGFKVVEIPSNEDGLVDLEALKAAVGEDTAALMLTNPNTLGLFERNILEIAEIVHEAGG 239

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505171573 242 LLYYDGANANAIIGVSRPGDMGFDVVHLNLHKTFgtphggggpgsgpvgVKKELAPFLPKPVVEYSGGKYHLDYDRPLSI 321
Cdd:PRK04366 240 LLYYDGANLNAILGKARPGDMGFDVVHLNLHKTFstphggggpgsgpvgVKEELAPFLPVPVVEKDGDRYRLDYDRPKSI 319

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505171573 322 GKIKSFYGNFLVVVKAYAYIRALGAEGLRKVSEAAVLNANYIKEKLKKYYHLPYDRTCMHEVVFSGQWQKQYGVSTLDIA 401
Cdd:PRK04366 320 GRVRAFYGNFGVLVRAYAYIRSLGAEGLREVSEDAVLNANYLKARLKDIYDLPYDRPCMHEFVLSGKKLKETGVRTLDIA 399

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505171573 402 KRLLDYGYHPPTIYFPLIVREALMIEPTETESKETLDEFINAMIEIANEAKDEPEKLRNAPVNTPVQRLDEATAARKPVL 481
Cdd:PRK04366 400 KRLLDYGFHPPTIYFPLIVPEALMIEPTETESKETLDAFIAAMKQIAEEAKENPELVKEAPHNTPVRRLDEVKAARKPVL 479


                 ..
gi 505171573 482 KY 483
Cdd:PRK04366 480 RW 481
 
Name Accession Description Interval E-value
PRK04366 PRK04366
aminomethyl-transferring glycine dehydrogenase subunit GcvPB;
2-483 0e+00

aminomethyl-transferring glycine dehydrogenase subunit GcvPB;


Pssm-ID: 235292  Cd Length: 481  Bit Score: 923.36  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505171573   2 LKKEEKLIFELSVPGKGTNLLPECDVEKVeIKNLIPEEYLRNEEIDLPEVNEVDVVRHFTHLSQKNYGVDSGFYPLGSCT 81
Cdd:PRK04366   1 ARWDEPLIFELSRPGRRGYSLPELDVPEV-LESLLPEELLRKEPPELPEVSELEVVRHYTRLSQKNYGVDTGFYPLGSCT 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505171573  82 MKYNPKINEEVSKLPGFMKVHPYQPEETVQGCLQLLYQTERFLSEITGMDRFSLQPAAGAHGEMTGLMIIKAFHQKNGDY 161
Cdd:PRK04366  80 MKYNPKINEKVARLPGFAELHPLQPEETVQGALELMYELQEWLKEITGMDAVTLQPAAGAHGELTGLLMIRAYHEARGDT 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505171573 162 KRTKIIVPDSAHGTNPASAAAVGFDVVEVKSNDRGGIDIDALRELMSDEVAGLMLTNPNTLGLFDENIDLIAEIVHNAGG 241
Cdd:PRK04366 160 KRTEVIVPDSAHGTNPASAAMAGFKVVEIPSNEDGLVDLEALKAAVGEDTAALMLTNPNTLGLFERNILEIAEIVHEAGG 239

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505171573 242 LLYYDGANANAIIGVSRPGDMGFDVVHLNLHKTFgtphggggpgsgpvgVKKELAPFLPKPVVEYSGGKYHLDYDRPLSI 321
Cdd:PRK04366 240 LLYYDGANLNAILGKARPGDMGFDVVHLNLHKTFstphggggpgsgpvgVKEELAPFLPVPVVEKDGDRYRLDYDRPKSI 319

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505171573 322 GKIKSFYGNFLVVVKAYAYIRALGAEGLRKVSEAAVLNANYIKEKLKKYYHLPYDRTCMHEVVFSGQWQKQYGVSTLDIA 401
Cdd:PRK04366 320 GRVRAFYGNFGVLVRAYAYIRSLGAEGLREVSEDAVLNANYLKARLKDIYDLPYDRPCMHEFVLSGKKLKETGVRTLDIA 399

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505171573 402 KRLLDYGYHPPTIYFPLIVREALMIEPTETESKETLDEFINAMIEIANEAKDEPEKLRNAPVNTPVQRLDEATAARKPVL 481
Cdd:PRK04366 400 KRLLDYGFHPPTIYFPLIVPEALMIEPTETESKETLDAFIAAMKQIAEEAKENPELVKEAPHNTPVRRLDEVKAARKPVL 479


                 ..
gi 505171573 482 KY 483
Cdd:PRK04366 480 RW 481
GcvP2 COG1003
Glycine cleavage system protein P (pyridoxal-binding), C-terminal domain [Amino acid transport ...
 26-484 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: 845.47  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505171573  26 DVEKVEIKNLIPEEYLRNEEIDLPEVNEVDVVRHFTHLSQKNYGVDSGFYPLGSCTMKYNPKINEEVSKLPGFMKVHPYQ 105
Cdd:COG1003    4 PEPEADAASLLPEALLRKSPVFLPEVSETEVLRHYTRLSQKNLGLDTGMIPLGSCTMKYNPKINEEPATLPGFANLHPFQ 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505171573 106 PEETVQGCLQLLYQTERFLSEITGMDRFSLQPAAGAHGEMTGLMIIKAFHQKNGDYKRTKIIVPDSAHGTNPASAAAVGF 185
Cdd:COG1003   84 PEETVQGYLELMYELEEWLAEITGMDAVSLQPNAGAQGEYAGLLAIRAYHESRGEGHRNEILIPDSAHGTNPASAAMAGF 163

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505171573 186 DVVEVKSNDRGGIDIDALRELMSDEVAGLMLTNPNTLGLFDENIDLIAEIVHNAGGLLYYDGANANAIIGVSRPGDMGFD 265
Cdd:COG1003  164 KVVVVKSDEDGNVDLEDLKAKVGDRTAALMLTNPSTHGVFEEDIKEICDIVHEAGGLVYYDGANLNAIVGLARPGDMGFD 243

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505171573 266 VVHLNLHKTFgtphggggpgsgpvgVKKELAPFLPKPVVEYSGGKYHLDYDRPLSIGKIKSFYGNFLVVVKAYAYIRALG 345
Cdd:COG1003  244 VCHLNLHKTFstphggggpgsgpvgVKEHLAPFLPGPPVVKDGDKYRLDYDRPKSIGRSAAFYGNAGVLVRAYAYIRMMG 323

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505171573 346 AEGLRKVSEAAVLNANYIKEKLKKYYHLPY--DRTCMHEVVFSGQWQK-QYGVSTLDIAKRLLDYGYHPPTIYFPLIVRE 422
Cdd:COG1003  324 AEGLREATEVAVLNANYLAARLKDHYPVLYtgNGRCAHEFILDLRPLKkETGVTTLDIAKRLLDYGFHAPTMYFPLIVPE 403

                        410       420       430       440       450       460
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 505171573 423 ALMIEPTETESKETLDEFINAMIEIANEAKDEPEKLRNAPVNTPVQRLDEATAARKPVLKYE 484
Cdd:COG1003  404 TLMIEPTESESKEELDRFIDAMIAIREEAREDPEPLKNAPHTTPVRRLDEVYADRNLVLTWR 465
GDC-P cd00613
Glycine cleavage system P-protein, alpha- and beta-subunits. This family consists of Glycine ...
 53-444 2.90e-156

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: 449.37  E-value: 2.90e-156
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505171573  53 EVDVVRHFTHLSQKNYGVDSGFYPLGSCTMKYNPKINEEVSKLPG-FMKVHPYQPEETVQGCLQLLYQTERFLSEITGMD 131
Cdd:cd00613    1 ETEVLRHLKRLASKNKALDQSMSFLGSGTYKHNPPAVIKRNILENeFYTAYTPYQPEISQGRLQALFELQTMLCELTGMD 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505171573 132 --RFSLQPAAGAHGEMTGLMIIKAFHqkngdyKRTKIIVPDSAHGTNPASAA----AVGFDVVEVKSNDRGGIDIDALRE 205
Cdd:cd00613   81 vaNASLQDEATAAAEAAGLAAIRAYH------KRNKVLVPDSAHPTNPAVARtrgePLGIEVVEVPSDEGGTVDLEALKE 154

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505171573 206 LMSDEVAGLMLTNPNTLGLFDENIDLIAEIVHNAGGLLYYDGANANAiIGVSRPGDMGFDVVHLNLHKTFgtphggggpg 285
Cdd:cd00613  155 EVSEEVAALMVQYPNTLGVFEDLIKEIADIAHSAGALVYVDGDNLNL-TGLKPPGEYGADIVVGNLQKTG---------- 223

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505171573 286 sgpvG-------------VKKELAPFLPKPVVEYSGGK-----YHLDYDRPLSI-----GKIKSFYGNFLVVVKAYAYIR 342
Cdd:cd00613  224 ----VphggggpgagffaVKKELVRFLPGRLVGVTKDAegnraFRLALQTREQHirrekATSNICTGQALLALMAAMYIV 299

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505171573 343 ALGAEGLRKVSEAAVLNANYIKEKLKKYYH-LPYDRTCMHEVVFSGQWqkQYGVSTLDIAKRLLDYGYHPPTIYFPliVR 421
Cdd:cd00613  300 YLGPEGLKEIAERAHLNANYLAKRLKEVGGvLPFNGPFFHEFVLRLPP--LYGIRAEDLAKALIDGGFHAPTMYLP--VD 375

                        410       420
                 ....*....|....*....|...
gi 505171573 422 EALMIEPTETESKETLDEFINAM 444
Cdd:cd00613  376 GTLMIEPTETETKEELDALLEAL 398
GDC-P pfam02347
Glycine cleavage system P-protein; This family consists of Glycine cleavage system P-proteins ...
 32-372 1.18e-07

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: 53.92  E-value: 1.18e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505171573   32 IKNLIPEEYLRNEEIDLPE-VNEVDVVRHFTHLSQKNYGVDSgFYPLGSCTMKYNPKINEEVSKLPGFMKVH-PYQPEET 109
Cdd:pfam02347  27 IGKAVPKNIRFAKPLQLPApKSEYEALAELEAIASKNTVYRS-FIGMGYYDTILPPVILRNILENPEWYTAYtPYQPEIS 105

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505171573  110 vQGCLQLL--YQTerFLSEITGMD--RFSLQPAAGAHGEMtglMIIKAFHQKNgdyKRTKIIVPDSAHgtnPASAAAV-- 183
Cdd:pfam02347 106 -QGRLEALlnFQT--MICDLTGLDiaNASLLDEGTAAAEA---MALAARASKK---KGKKFVVDKDVH---PQTLEVLkt 173

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505171573  184 -----GFDVVEVKSNDRGGIDidalrelmSDEVAGLMLTNPNTLGlFDENIDLIAEIVHNaGGLLYYDGANANAIIGVSR 258
Cdd:pfam02347 174 rakpfGIEIVEVDYTEEGVTD--------LKDVFGVLVQYPNTDG-RIEDYKELIELAHQ-RKSLVVVAADLLALTLLKP 243

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505171573  259 PGDMGFDVVhLNLHKTFGTPHGGGGPGSGPVGVKKELAPFLPKPVV---EYSGGK-----------YHLDYDRPLSigKI 324
Cdd:pfam02347 244 PGEFGADIA-VGSAQRFGVPLGYGGPHAGFFAVKKELVRKMPGRLVgvsKDANGKralrlalqtreQHIRRDKATS--NI 320

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*...
gi 505171573  325 KSfyGNFLVVVKAYAYIRALGAEGLRKVSEAAVLNANYIKEKLKKYYH 372
Cdd:pfam02347 321 CT--AQALLANMASMYAVYHGPNGLKEIARRIHSLTLYLAKALKKLGH 366
 
Name Accession Description Interval E-value
PRK04366 PRK04366
aminomethyl-transferring glycine dehydrogenase subunit GcvPB;
2-483 0e+00

aminomethyl-transferring glycine dehydrogenase subunit GcvPB;


Pssm-ID: 235292  Cd Length: 481  Bit Score: 923.36  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505171573   2 LKKEEKLIFELSVPGKGTNLLPECDVEKVeIKNLIPEEYLRNEEIDLPEVNEVDVVRHFTHLSQKNYGVDSGFYPLGSCT 81
Cdd:PRK04366   1 ARWDEPLIFELSRPGRRGYSLPELDVPEV-LESLLPEELLRKEPPELPEVSELEVVRHYTRLSQKNYGVDTGFYPLGSCT 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505171573  82 MKYNPKINEEVSKLPGFMKVHPYQPEETVQGCLQLLYQTERFLSEITGMDRFSLQPAAGAHGEMTGLMIIKAFHQKNGDY 161
Cdd:PRK04366  80 MKYNPKINEKVARLPGFAELHPLQPEETVQGALELMYELQEWLKEITGMDAVTLQPAAGAHGELTGLLMIRAYHEARGDT 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505171573 162 KRTKIIVPDSAHGTNPASAAAVGFDVVEVKSNDRGGIDIDALRELMSDEVAGLMLTNPNTLGLFDENIDLIAEIVHNAGG 241
Cdd:PRK04366 160 KRTEVIVPDSAHGTNPASAAMAGFKVVEIPSNEDGLVDLEALKAAVGEDTAALMLTNPNTLGLFERNILEIAEIVHEAGG 239

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505171573 242 LLYYDGANANAIIGVSRPGDMGFDVVHLNLHKTFgtphggggpgsgpvgVKKELAPFLPKPVVEYSGGKYHLDYDRPLSI 321
Cdd:PRK04366 240 LLYYDGANLNAILGKARPGDMGFDVVHLNLHKTFstphggggpgsgpvgVKEELAPFLPVPVVEKDGDRYRLDYDRPKSI 319

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505171573 322 GKIKSFYGNFLVVVKAYAYIRALGAEGLRKVSEAAVLNANYIKEKLKKYYHLPYDRTCMHEVVFSGQWQKQYGVSTLDIA 401
Cdd:PRK04366 320 GRVRAFYGNFGVLVRAYAYIRSLGAEGLREVSEDAVLNANYLKARLKDIYDLPYDRPCMHEFVLSGKKLKETGVRTLDIA 399

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505171573 402 KRLLDYGYHPPTIYFPLIVREALMIEPTETESKETLDEFINAMIEIANEAKDEPEKLRNAPVNTPVQRLDEATAARKPVL 481
Cdd:PRK04366 400 KRLLDYGFHPPTIYFPLIVPEALMIEPTETESKETLDAFIAAMKQIAEEAKENPELVKEAPHNTPVRRLDEVKAARKPVL 479


                 ..
gi 505171573 482 KY 483
Cdd:PRK04366 480 RW 481
GcvP2 COG1003
Glycine cleavage system protein P (pyridoxal-binding), C-terminal domain [Amino acid transport ...
 26-484 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: 845.47  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505171573  26 DVEKVEIKNLIPEEYLRNEEIDLPEVNEVDVVRHFTHLSQKNYGVDSGFYPLGSCTMKYNPKINEEVSKLPGFMKVHPYQ 105
Cdd:COG1003    4 PEPEADAASLLPEALLRKSPVFLPEVSETEVLRHYTRLSQKNLGLDTGMIPLGSCTMKYNPKINEEPATLPGFANLHPFQ 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505171573 106 PEETVQGCLQLLYQTERFLSEITGMDRFSLQPAAGAHGEMTGLMIIKAFHQKNGDYKRTKIIVPDSAHGTNPASAAAVGF 185
Cdd:COG1003   84 PEETVQGYLELMYELEEWLAEITGMDAVSLQPNAGAQGEYAGLLAIRAYHESRGEGHRNEILIPDSAHGTNPASAAMAGF 163

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505171573 186 DVVEVKSNDRGGIDIDALRELMSDEVAGLMLTNPNTLGLFDENIDLIAEIVHNAGGLLYYDGANANAIIGVSRPGDMGFD 265
Cdd:COG1003  164 KVVVVKSDEDGNVDLEDLKAKVGDRTAALMLTNPSTHGVFEEDIKEICDIVHEAGGLVYYDGANLNAIVGLARPGDMGFD 243

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505171573 266 VVHLNLHKTFgtphggggpgsgpvgVKKELAPFLPKPVVEYSGGKYHLDYDRPLSIGKIKSFYGNFLVVVKAYAYIRALG 345
Cdd:COG1003  244 VCHLNLHKTFstphggggpgsgpvgVKEHLAPFLPGPPVVKDGDKYRLDYDRPKSIGRSAAFYGNAGVLVRAYAYIRMMG 323

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505171573 346 AEGLRKVSEAAVLNANYIKEKLKKYYHLPY--DRTCMHEVVFSGQWQK-QYGVSTLDIAKRLLDYGYHPPTIYFPLIVRE 422
Cdd:COG1003  324 AEGLREATEVAVLNANYLAARLKDHYPVLYtgNGRCAHEFILDLRPLKkETGVTTLDIAKRLLDYGFHAPTMYFPLIVPE 403

                        410       420       430       440       450       460
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 505171573 423 ALMIEPTETESKETLDEFINAMIEIANEAKDEPEKLRNAPVNTPVQRLDEATAARKPVLKYE 484
Cdd:COG1003  404 TLMIEPTESESKEELDRFIDAMIAIREEAREDPEPLKNAPHTTPVRRLDEVYADRNLVLTWR 465
GDC-P cd00613
Glycine cleavage system P-protein, alpha- and beta-subunits. This family consists of Glycine ...
 53-444 2.90e-156

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: 449.37  E-value: 2.90e-156
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505171573  53 EVDVVRHFTHLSQKNYGVDSGFYPLGSCTMKYNPKINEEVSKLPG-FMKVHPYQPEETVQGCLQLLYQTERFLSEITGMD 131
Cdd:cd00613    1 ETEVLRHLKRLASKNKALDQSMSFLGSGTYKHNPPAVIKRNILENeFYTAYTPYQPEISQGRLQALFELQTMLCELTGMD 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505171573 132 --RFSLQPAAGAHGEMTGLMIIKAFHqkngdyKRTKIIVPDSAHGTNPASAA----AVGFDVVEVKSNDRGGIDIDALRE 205
Cdd:cd00613   81 vaNASLQDEATAAAEAAGLAAIRAYH------KRNKVLVPDSAHPTNPAVARtrgePLGIEVVEVPSDEGGTVDLEALKE 154

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505171573 206 LMSDEVAGLMLTNPNTLGLFDENIDLIAEIVHNAGGLLYYDGANANAiIGVSRPGDMGFDVVHLNLHKTFgtphggggpg 285
Cdd:cd00613  155 EVSEEVAALMVQYPNTLGVFEDLIKEIADIAHSAGALVYVDGDNLNL-TGLKPPGEYGADIVVGNLQKTG---------- 223

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505171573 286 sgpvG-------------VKKELAPFLPKPVVEYSGGK-----YHLDYDRPLSI-----GKIKSFYGNFLVVVKAYAYIR 342
Cdd:cd00613  224 ----VphggggpgagffaVKKELVRFLPGRLVGVTKDAegnraFRLALQTREQHirrekATSNICTGQALLALMAAMYIV 299

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505171573 343 ALGAEGLRKVSEAAVLNANYIKEKLKKYYH-LPYDRTCMHEVVFSGQWqkQYGVSTLDIAKRLLDYGYHPPTIYFPliVR 421
Cdd:cd00613  300 YLGPEGLKEIAERAHLNANYLAKRLKEVGGvLPFNGPFFHEFVLRLPP--LYGIRAEDLAKALIDGGFHAPTMYLP--VD 375

                        410       420
                 ....*....|....*....|...
gi 505171573 422 EALMIEPTETESKETLDEFINAM 444
Cdd:cd00613  376 GTLMIEPTETETKEELDALLEAL 398
PLN02414 PLN02414
glycine dehydrogenase (decarboxylating)
 52-462 1.80e-115

glycine dehydrogenase (decarboxylating)


Pssm-ID: 178035 [Multi-domain]  Cd Length: 993  Bit Score: 362.93  E-value: 1.80e-115
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505171573  52 NEVDVVRHFTHLSQKNYGVDSGFYPLGSCTMKYNPKINEEVSKLPGFMKVHPYQPEETVQGCLQLLYQTERFLSEITGMD 131
Cdd:PLN02414 505 SEHELLRYLHRLQNKDLSLVHSMIPLGSCTMKLNATTEMMPVTWPEFANIHPFAPVDQAQGYQEMFEDLGDLLCEITGFD 584

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505171573 132 RFSLQPAAGAHGEMTGLMIIKAFHQKNGDYKRTKIIVPDSAHGTNPASAAAVGFDVVEVKSNDRGGIDIDALR---ELMS 208
Cdd:PLN02414 585 SFSLQPNAGAAGEYAGLMVIRAYHLSRGDHHRNVCIIPVSAHGTNPASAAMCGMKIVVVGTDAKGNINIEELRkaaEAHK 664

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505171573 209 DEVAGLMLTNPNTLGLFDENIDLIAEIVHNAGGLLYYDGANANAIIGVSRPGDMGFDVVHLNLHKTFGTPHGGGGPGSGP 288
Cdd:PLN02414 665 DNLAALMVTYPSTHGVYEEGIDEICDIIHDNGGQVYMDGANMNAQVGLTSPGFIGADVCHLNLHKTFCIPHGGGGPGMGP 744

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505171573 289 VGVKKELAPFLPK-PVVEYSGGkyhLDYDRPLSIGKIKSF-YGNFLVVVKAYAYIRALGAEGLRKVSEAAVLNANYIKEK 366
Cdd:PLN02414 745 IGVKKHLAPFLPShPVVPTGGI---PRPEKTQPLGTISAApWGSALILPISYTYIAMMGSEGLTDASKIAILNANYMAKR 821

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505171573 367 LKKYYHLPY---DRTCMHEVVFSGQWQKQY-GVSTLDIAKRLLDYGYHPPTIYFPliVREALMIEPTETESKETLDEFIN 442
Cdd:PLN02414 822 LEGHYPVLFrgkNGTCAHEFIIDLRPFKNTaGIEPEDVAKRLMDYGFHAPTMSWP--VPGTLMIEPTESESKAELDRFCD 899

                        410       420
                 ....*....|....*....|....*...
gi 505171573 443 AMIEIANEAKD--------EPEKLRNAP 462
Cdd:PLN02414 900 ALISIREEIADiengkadrENNVLKGAP 927
PRK00451 PRK00451
aminomethyl-transferring glycine dehydrogenase subunit GcvPA;
36-449 1.81e-27

aminomethyl-transferring glycine dehydrogenase subunit GcvPA;


Pssm-ID: 234769 [Multi-domain]  Cd Length: 447  Bit Score: 114.47  E-value: 1.81e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505171573  36 IPEEYLRNEEIDLPE-VNEVDVVRHFTHLSQKNYGVDS-------GFYPlgsctmKYNPKINEEVSKLPGFMKVH-PYQP 106
Cdd:PRK00451  31 IPEELRLKRPLDLPPgLSEMELLRHLRELAAKNKTAEEypsflgaGAYD------HYIPAVVDHIISRSEFYTAYtPYQP 104

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505171573 107 EETvQGCLQLL--YQTerFLSEITGMD--RFSLQPAAGAHGEMTgLMiikAFHQKngdyKRTKIIVPDSAHgtnPASAAA 182
Cdd:PRK00451 105 EIS-QGTLQAIfeYQT--MICELTGMDvaNASMYDGATALAEAA-LM---AVRIT----KRKKVLVSGAVH---PEYREV 170

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505171573 183 V-------GFDVVEVKSNDrGGIDIDALRELMSDEVAGLMLTNPNTLGLFdENIDLIAEIVHNAGGLLyydgananaIIG 255
Cdd:PRK00451 171 LktylkgqGIEVVEVPYED-GVTDLEALEAAVDDDTAAVVVQYPNFFGVI-EDLEEIAEIAHAGGALF---------IVG 239

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505171573 256 V--------SRPGDMGFDVV---------HLNL---HKTFgtphggggpgsgpVGVKKELAPFLPKPVV---EYSGGKY- 311
Cdd:PRK00451 240 VdpvslgllKPPGEYGADIVvgegqplgiPLSFggpYLGF-------------FATRKKLVRQMPGRLVgetVDADGKRg 306

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505171573 312 ----------HldydrplsI--GKIKSfygNF-----LVVVKAYAYIRALGAEGLRKVSEAAVLNANYIKEKLKKY-YHL 373
Cdd:PRK00451 307 fvltlqareqH--------IrrEKATS---NIctnqaLNALAAAIYMSLLGPEGLRELAEQNHQKAHYLAERLAEIgGVE 375

                        410       420       430       440       450       460       470
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 505171573 374 PYDRTCMHEVVFsgqwqkQYGVSTLDIAKRLLDYGYH---PPTIYFPLiVREALMIEPTETESKETLDEFINAMIEIAN 449
Cdd:PRK00451 376 LFDGPFFNEFVV------RLPKPAEEVNEALLEKGILggyDLGRYYPE-LGNHLLVCVTEKRTKEDIDALVAALGEVLA 447
GcvP1 COG0403
Glycine cleavage system protein P (pyridoxal-binding), N-terminal domain [Amino acid transport ...
 36-444 3.42e-22

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: 98.95  E-value: 3.42e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505171573  36 IPEEYLRNEEIDLPE-VNEVDVVRHFTHLSQKNYGVDS----GFYPlgsctmKYNPKINEEVSKLPGFMKVH-PYQPEET 109
Cdd:COG0403   34 IPAEIRLKRPLDLPEaLSEAELLRHLRALAAKNKVLTSfigaGYYD------HYVPAVVRNILERPEFYTAYtPYQPEIS 107

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505171573 110 vQGCLQLL--YQTerFLSEITGMD--RFSLQPAAGAHGE-MtgLMiikAFHQKNgdyKRTKIIVPDSAHgtnPAS----- 179
Cdd:COG0403  108 -QGRLQALfeFQT--MVAELTGMDvaNASLYDGATAAAEaM--LM---ARRVTK---RSNKVLVSEDVH---PQTravlk 173

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505171573 180 --AAAVGFDVVEVKSNDrGGIDIDALRELMSDEVAGLMLTNPNTLGLFdENIDLIAEIVHNAGGLLYydgANANAI-IGV 256
Cdd:COG0403  174 tyAEPLGIEVVEVPDED-GVTDLEALKALLDDDVAGVLVQYPNFFGVI-EDLRAIAEAAHAAGALVI---VAADPLsLGL 248

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505171573 257 -SRPGDMGFDVV---------HLNlhktfgtphggggpgsgpvgvkkelapflpkpvveYSGGkyHL-------DYDRPL 319
Cdd:COG0403  249 lKPPGELGADIVvgegqrlgvPLG-----------------------------------FGGP--HAgffatreKLVRQM 291

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505171573 320 S---IGKIKSFYGN--F-------------------------LVVVKAYAYIRALGAEGLRKVSEAAVLNANYIKEKLKK 369
Cdd:COG0403  292 PgrlVGVTVDADGKraFrltlqtreqhirrekatsnictnqaLLALAASMYAVYHGPEGLKEIAERIHQKAHYLAERLAA 371

                        410       420       430       440       450       460       470
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 505171573 370 Y-YHLPYDRTCMHEVVFsgqwqkQYGVSTLDIAKRLLDYGYHPPtiyFPL--IVREALMIEPTETESKETLDEFINAM 444
Cdd:COG0403  372 LgVEVPFNGPFFDEFVV------RLPKPAAEINAALLEKGILGG---LNLrrVDDDTLLVAVTETTTKEDIDALVEAL 440
AAT_I cd01494
Aspartate aminotransferase (AAT) superfamily (fold type I) of pyridoxal phosphate (PLP) ...
 128-275 6.98e-17

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: 78.19  E-value: 6.98e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505171573 128 TGMDRFSLQPAaGAHGEMTGLMIIKafhqKNGDYkrtkIIVPDSAHGTNPASAAAV-GFDVVEVKSND--RGGIDIDALR 204
Cdd:cd01494   15 PGNDKAVFVPS-GTGANEAALLALL----GPGDE----VIVDANGHGSRYWVAAELaGAKPVPVPVDDagYGGLDVAILE 85

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 505171573 205 ELM-SDEVAGLMLTNPNTLGLFDENIDLIAEIVHNAGGLLYYDGANANAIIGVS--RPGDMGFDVVHLNLHKTF 275
Cdd:cd01494   86 ELKaKPNVALIVITPNTTSGGVLVPLKEIRKIAKEYGILLLVDAASAGGASPAPgvLIPEGGADVVTFSLHKNL 159
GDC-P pfam02347
Glycine cleavage system P-protein; This family consists of Glycine cleavage system P-proteins ...
 32-372 1.18e-07

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: 53.92  E-value: 1.18e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505171573   32 IKNLIPEEYLRNEEIDLPE-VNEVDVVRHFTHLSQKNYGVDSgFYPLGSCTMKYNPKINEEVSKLPGFMKVH-PYQPEET 109
Cdd:pfam02347  27 IGKAVPKNIRFAKPLQLPApKSEYEALAELEAIASKNTVYRS-FIGMGYYDTILPPVILRNILENPEWYTAYtPYQPEIS 105

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505171573  110 vQGCLQLL--YQTerFLSEITGMD--RFSLQPAAGAHGEMtglMIIKAFHQKNgdyKRTKIIVPDSAHgtnPASAAAV-- 183
Cdd:pfam02347 106 -QGRLEALlnFQT--MICDLTGLDiaNASLLDEGTAAAEA---MALAARASKK---KGKKFVVDKDVH---PQTLEVLkt 173

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505171573  184 -----GFDVVEVKSNDRGGIDidalrelmSDEVAGLMLTNPNTLGlFDENIDLIAEIVHNaGGLLYYDGANANAIIGVSR 258
Cdd:pfam02347 174 rakpfGIEIVEVDYTEEGVTD--------LKDVFGVLVQYPNTDG-RIEDYKELIELAHQ-RKSLVVVAADLLALTLLKP 243

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505171573  259 PGDMGFDVVhLNLHKTFGTPHGGGGPGSGPVGVKKELAPFLPKPVV---EYSGGK-----------YHLDYDRPLSigKI 324
Cdd:pfam02347 244 PGEFGADIA-VGSAQRFGVPLGYGGPHAGFFAVKKELVRKMPGRLVgvsKDANGKralrlalqtreQHIRRDKATS--NI 320

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*...
gi 505171573  325 KSfyGNFLVVVKAYAYIRALGAEGLRKVSEAAVLNANYIKEKLKKYYH 372
Cdd:pfam02347 321 CT--AQALLANMASMYAVYHGPNGLKEIARRIHSLTLYLAKALKKLGH 366
GadA COG0076
Glutamate or tyrosine decarboxylase or a related PLP-dependent protein [Amino acid transport ...
 145-450 7.35e-06

Glutamate or tyrosine decarboxylase or a related PLP-dependent protein [Amino acid transport and metabolism]; Glutamate or tyrosine decarboxylase or a related PLP-dependent protein is part of the Pathway/BioSystem: Pantothenate/CoA biosynthesis


Pssm-ID: 439846 [Multi-domain]  Cd Length: 460  Bit Score: 48.29  E-value: 7.35e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505171573 145 MTGLMI-----IKAFHQKNG--DYKRTKIIVPDSAHGTNPASAAAVGFD---VVEVKSNDRGGIDIDALRELMSD----- 209
Cdd:COG0076  139 LLALLAardraLARRVRAEGlpGAPRPRIVVSEEAHSSVDKAARLLGLGrdaLRKVPVDEDGRMDPDALEAAIDEdraag 218

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505171573 210 -EVAGLMLTNPNT-LGLFDeNIDLIAEIVHNAGGLLYYDGANANAIIgVSRPGDMGFDVVH------LNLHKTFgtphgg 281
Cdd:COG0076  219 lNPIAVVATAGTTnTGAID-PLAEIADIAREHGLWLHVDAAYGGFAL-PSPELRHLLDGIEradsitVDPHKWL------ 290

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505171573 282 ggpgsgpvgvkkelapFLPKPV------------------VEYSGGKYHLDYDrplsigkiksfYGNFLV-------VVK 336
Cdd:COG0076  291 ----------------YVPYGCgavlvrdpellreafsfhASYLGPADDGVPN-----------LGDYTLelsrrfrALK 343

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505171573 337 AYAYIRALGAEGLRKVSEAAVLNANYIKEKLKKYYHLpydrTCMHEVVFS-------GQWQKQYGVSTLDIAKRLLDYG- 408
Cdd:COG0076  344 LWATLRALGREGYRELIERCIDLARYLAEGIAALPGF----ELLAPPELNivcfrykPAGLDEEDALNYALRDRLRARGr 419

                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....
gi 505171573 409 -YHPPTIYFPLIV-REALMiEPTETEskETLDEFINAMIEIANE 450
Cdd:COG0076  420 aFLSPTKLDGRVVlRLVVL-NPRTTE--DDVDALLDDLREAAAE 460
Aminotran_5 pfam00266
Aminotransferase class-V; This domain is found in amino transferases, and other enzymes ...
 155-273 1.08e-05

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: 47.63  E-value: 1.08e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505171573  155 HQKNGDykrtKIIVPDSAHGTN--PASAAA--VGFDVVEVKSNDRGGIDIDALRELMSDEVAGLMLT-NPNTLGLFDEnI 229
Cdd:pfam00266  84 SLKPGD----EIVITEMEHHANlvPWQELAkrTGARVRVLPLDEDGLLDLDELEKLITPKTKLVAIThVSNVTGTIQP-V 158

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 505171573  230 DLIAEIVHNAGGLLYYDGANAnaiIGvSRPGDM---GFDVVHLNLHK 273
Cdd:pfam00266 159 PEIGKLAHQYGALVLVDAAQA---IG-HRPIDVqklGVDFLAFSGHK 201
CsdA COG0520
Selenocysteine lyase/Cysteine desulfurase [Amino acid transport and metabolism];
180-248 2.64e-04

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


Pssm-ID: 440286 [Multi-domain]  Cd Length: 396  Bit Score: 43.20  E-value: 2.64e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 505171573 180 AAAVGFDVVEVKSNDRGGIDIDALRELMSDEVAGLMLTN-PNTLGLfdEN-IDLIAEIVHNAGGLLYYDGA 248
Cdd:COG0520  124 AERTGAEVRVIPLDEDGELDLEALEALLTPRTKLVAVTHvSNVTGT--VNpVKEIAALAHAHGALVLVDGA 192
DOPA_deC_like cd06450
DOPA decarboxylase family. This family belongs to pyridoxal phosphate (PLP)-dependent ...
 162-409 1.41e-03

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: 40.65  E-value: 1.41e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505171573 162 KRTKIIVPDSAHGTNPASAAAVGFDVVEVKSNDRGGIDIDALRELMSDEVAG----LML--TNPNT-LGLFDeNIDLIAE 234
Cdd:cd06450   94 DKLVIVCSDQAHVSVEKAAAYLDVKVRLVPVDEDGRMDPEALEAAIDEDKAEglnpIMVvaTAGTTdTGAID-PLEEIAD 172

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505171573 235 IVHNAGGLLYYDGANANAIIGVSRPGDMGF-----DVVHLNLHKTFgtphggggpgsgpvgvkkeLAPFlpkpvveysgg 309
Cdd:cd06450  173 LAEKYDLWLHVDAAYGGFLLPFPEPRHLDFgiervDSISVDPHKYG-------------------LVPL----------- 222

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505171573 310 kyhldydrplSIGKiksfygnFLV-VVKAYAYIRALGAEGLRKVSEAAVLNANYIKEKLKKyyhLPYDRTCMHE----VV 384
Cdd:cd06450  223 ----------GCSA-------VLVrALKLWATLRRFGRDGYGEHIDRIVDLAKYLAELIRA---DPGFELLGEPnlslVC 282

                        250       260
                 ....*....|....*....|....*
gi 505171573 385 FSGQWQKQYGVSTLDIAKRLLDYGY 409
Cdd:cd06450  283 FRLKPSVKLDELNYDLSDRLNERGG 307
 
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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