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Conserved domains on  [gi|118097664|ref|XP_414728|]
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pyridoxal-dependent decarboxylase domain-containing protein 1 isoform X2 [Gallus gallus]

Protein Classification

PLP-dependent aminotransferase family protein( domain architecture ID 139552)

PLP-dependent aminotransferase family protein may combine pyridoxal phosphate with an alpha-amino acid to form a Schiff base or aldimine intermediate, which then acts as the substrate in a reaction such as a transamination, racemization, or decarboxylation

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
AAT_I super family cl18945
Aspartate aminotransferase (AAT) superfamily (fold type I) of pyridoxal phosphate (PLP) ...
172-404 5.40e-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).


The actual alignment was detected with superfamily member cd06450:

Pssm-ID: 450240 [Multi-domain]  Cd Length: 345  Bit Score: 89.18  E-value: 5.40e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118097664 172 TKQPVIYISSAARTGLGQAlCNQLGLPLScmcRVPCNtmfgSQHQMDVALLDRLIKDDVECGKLPLLLVANAGTPGAGHT 251
Cdd:cd06450   93 IDKLVIVCSDQAHVSVEKA-AAYLDVKVR---LVPVD----EDGRMDPEALEAAIDEDKAEGLNPIMVVATAGTTDTGAI 164
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118097664 252 DKLGRLKELCEQYNMWLHVEGvnlatlALGyvsSSVLaatkcdsMTLTLGSWL-GLPAVPAVTLykheDPSLSLVAGLTS 330
Cdd:cd06450  165 DPLEEIADLAEKYDLWLHVDA------AYG---GFLL-------PFPEPRHLDfGIERVDSISV----DPHKYGLVPLGC 224
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 118097664 331 SqpVEKLRALPLWLSLQYLGHDGIVERIKHASQLSQRLLENLKNLDFIKTSVEDELssPVVVFKF----FQKYLNRDL 404
Cdd:cd06450  225 S--AVLVRALKLWATLRRFGRDGYGEHIDRIVDLAKYLAELIRADPGFELLGEPNL--SLVCFRLkpsvKLDELNYDL 298
 
Name Accession Description Interval E-value
DOPA_deC_like cd06450
DOPA decarboxylase family. This family belongs to pyridoxal phosphate (PLP)-dependent ...
172-404 5.40e-19

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: 89.18  E-value: 5.40e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118097664 172 TKQPVIYISSAARTGLGQAlCNQLGLPLScmcRVPCNtmfgSQHQMDVALLDRLIKDDVECGKLPLLLVANAGTPGAGHT 251
Cdd:cd06450   93 IDKLVIVCSDQAHVSVEKA-AAYLDVKVR---LVPVD----EDGRMDPEALEAAIDEDKAEGLNPIMVVATAGTTDTGAI 164
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118097664 252 DKLGRLKELCEQYNMWLHVEGvnlatlALGyvsSSVLaatkcdsMTLTLGSWL-GLPAVPAVTLykheDPSLSLVAGLTS 330
Cdd:cd06450  165 DPLEEIADLAEKYDLWLHVDA------AYG---GFLL-------PFPEPRHLDfGIERVDSISV----DPHKYGLVPLGC 224
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 118097664 331 SqpVEKLRALPLWLSLQYLGHDGIVERIKHASQLSQRLLENLKNLDFIKTSVEDELssPVVVFKF----FQKYLNRDL 404
Cdd:cd06450  225 S--AVLVRALKLWATLRRFGRDGYGEHIDRIVDLAKYLAELIRADPGFELLGEPNL--SLVCFRLkpsvKLDELNYDL 298
GadA COG0076
Glutamate or tyrosine decarboxylase or a related PLP-dependent protein [Amino acid transport ...
23-395 1.07e-15

Glutamate or tyrosine decarboxylase or a related PLP-dependent protein [Amino acid transport and metabolism];


Pssm-ID: 223154 [Multi-domain]  Cd Length: 460  Bit Score: 80.49  E-value: 1.07e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118097664  23 AMKMLEDSQRKVEEENEKKYARKDIPGPLQGSGQDMVSILQLVQNL--MHGEEEEESSQAYRLqnvgeqGHMALLGHSLA 100
Cdd:COG0076    5 IDKDMLNSKRYSGDSLSPLFGALSDSRMAPEKGEPLEEVLDELAELliKDELYLDGHPRANLA------GFCPTRVPPVA 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118097664 101 AYI-------SVLDKERLRkLTTRILSDTTLWLCRLFRYEN---------GSayyheddrEGLLKICRLVIHTCYEDytV 164
Cdd:COG0076   79 AELlvsalnkNLGDPDESP-AAAELEERVVNMLSDLLGAPEeasgtftsgGT--------EANLLALLAARERWRKR--A 147
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118097664 165 EGFNVLCTKQPVIYISSAARTGLGQAlCNQLGLPLScmcRVPcntMFGSQHQMDVALLDRLIKDDVECGklplLLVANAG 244
Cdd:COG0076  148 LAESGKPGGKPNIVCSETAHFSFEKA-ARYLGLGLR---RVP---TVPTDYRIDVDALEEAIDENTIGG----VVVGTAG 216
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118097664 245 TPGAGHTDKLGRLKELCEQYNMWLHVEGvnlatlALGyvsSSVLAATKC-----------DSMTLTLGSWLGLPAVPAVT 313
Cdd:COG0076  217 TTDTGSIDDIEELADIAEEYGIWLHVDA------AFG---GFLLPFLEPdgrwdfglegvDSITVDGHKYGLAPIGCGVV 287
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118097664 314 LYK----------HEDPSLS----LVAGLTSSQPVEklRALPLWLSLQYLGHDGIVERIKHASQLSQRLLENLKNLDFIK 379
Cdd:COG0076  288 LFRdeealrriliFADYYLPgggiPNFTILGSRPGR--QALALYANLRRLGREGYRKLLDRTLELARYLAEELEKLGDFE 365
                        410
                 ....*....|....*.
gi 118097664 380 TSVEDELssPVVVFKF 395
Cdd:COG0076  366 LVNEPEL--PIVAFRL 379
Pyridoxal_deC pfam00282
Pyridoxal-dependent decarboxylase conserved domain;
175-271 6.56e-07

Pyridoxal-dependent decarboxylase conserved domain;


Pssm-ID: 395219  Cd Length: 373  Bit Score: 52.42  E-value: 6.56e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118097664  175 PVIYISSAARTGLGQAlcnqlGLPLSCMCR-VPCNtmfgSQHQMDVALLDRLIKDDVECGKLPLLLVANAGTPGAGHTDK 253
Cdd:pfam00282 146 LVAYTSDQAHSSIEKA-----ALYGGVKLReIPSD----DNGKMRGMDLEKAIEEDKENGLIPFFVVATLGTTGSGAFDD 216
                          90
                  ....*....|....*...
gi 118097664  254 LGRLKELCEQYNMWLHVE 271
Cdd:pfam00282 217 LQELGDICAKHNLWLHVD 234
PLN02880 PLN02880
tyrosine decarboxylase
176-271 1.51e-03

tyrosine decarboxylase


Pssm-ID: 215475 [Multi-domain]  Cd Length: 490  Bit Score: 41.82  E-value: 1.51e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118097664 176 VIYISSAARTGLGQAlCNQLGL-PLSC-MCRVPCNTMFGsqhqMDVALLDRLIKDDVECGKLPLLLVANAGTPGAGHTDK 253
Cdd:PLN02880 183 VVYASDQTHSALQKA-CQIAGIhPENCrLLKTDSSTNYA----LAPELLSEAISTDLSSGLIPFFLCATVGTTSSTAVDP 257
                         90
                 ....*....|....*...
gi 118097664 254 LGRLKELCEQYNMWLHVE 271
Cdd:PLN02880 258 LLELGKIAKSNGMWFHVD 275
 
Name Accession Description Interval E-value
DOPA_deC_like cd06450
DOPA decarboxylase family. This family belongs to pyridoxal phosphate (PLP)-dependent ...
172-404 5.40e-19

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: 89.18  E-value: 5.40e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118097664 172 TKQPVIYISSAARTGLGQAlCNQLGLPLScmcRVPCNtmfgSQHQMDVALLDRLIKDDVECGKLPLLLVANAGTPGAGHT 251
Cdd:cd06450   93 IDKLVIVCSDQAHVSVEKA-AAYLDVKVR---LVPVD----EDGRMDPEALEAAIDEDKAEGLNPIMVVATAGTTDTGAI 164
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118097664 252 DKLGRLKELCEQYNMWLHVEGvnlatlALGyvsSSVLaatkcdsMTLTLGSWL-GLPAVPAVTLykheDPSLSLVAGLTS 330
Cdd:cd06450  165 DPLEEIADLAEKYDLWLHVDA------AYG---GFLL-------PFPEPRHLDfGIERVDSISV----DPHKYGLVPLGC 224
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 118097664 331 SqpVEKLRALPLWLSLQYLGHDGIVERIKHASQLSQRLLENLKNLDFIKTSVEDELssPVVVFKF----FQKYLNRDL 404
Cdd:cd06450  225 S--AVLVRALKLWATLRRFGRDGYGEHIDRIVDLAKYLAELIRADPGFELLGEPNL--SLVCFRLkpsvKLDELNYDL 298
GadA COG0076
Glutamate or tyrosine decarboxylase or a related PLP-dependent protein [Amino acid transport ...
23-395 1.07e-15

Glutamate or tyrosine decarboxylase or a related PLP-dependent protein [Amino acid transport and metabolism];


Pssm-ID: 223154 [Multi-domain]  Cd Length: 460  Bit Score: 80.49  E-value: 1.07e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118097664  23 AMKMLEDSQRKVEEENEKKYARKDIPGPLQGSGQDMVSILQLVQNL--MHGEEEEESSQAYRLqnvgeqGHMALLGHSLA 100
Cdd:COG0076    5 IDKDMLNSKRYSGDSLSPLFGALSDSRMAPEKGEPLEEVLDELAELliKDELYLDGHPRANLA------GFCPTRVPPVA 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118097664 101 AYI-------SVLDKERLRkLTTRILSDTTLWLCRLFRYEN---------GSayyheddrEGLLKICRLVIHTCYEDytV 164
Cdd:COG0076   79 AELlvsalnkNLGDPDESP-AAAELEERVVNMLSDLLGAPEeasgtftsgGT--------EANLLALLAARERWRKR--A 147
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118097664 165 EGFNVLCTKQPVIYISSAARTGLGQAlCNQLGLPLScmcRVPcntMFGSQHQMDVALLDRLIKDDVECGklplLLVANAG 244
Cdd:COG0076  148 LAESGKPGGKPNIVCSETAHFSFEKA-ARYLGLGLR---RVP---TVPTDYRIDVDALEEAIDENTIGG----VVVGTAG 216
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118097664 245 TPGAGHTDKLGRLKELCEQYNMWLHVEGvnlatlALGyvsSSVLAATKC-----------DSMTLTLGSWLGLPAVPAVT 313
Cdd:COG0076  217 TTDTGSIDDIEELADIAEEYGIWLHVDA------AFG---GFLLPFLEPdgrwdfglegvDSITVDGHKYGLAPIGCGVV 287
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118097664 314 LYK----------HEDPSLS----LVAGLTSSQPVEklRALPLWLSLQYLGHDGIVERIKHASQLSQRLLENLKNLDFIK 379
Cdd:COG0076  288 LFRdeealrriliFADYYLPgggiPNFTILGSRPGR--QALALYANLRRLGREGYRKLLDRTLELARYLAEELEKLGDFE 365
                        410
                 ....*....|....*.
gi 118097664 380 TSVEDELssPVVVFKF 395
Cdd:COG0076  366 LVNEPEL--PIVAFRL 379
Pyridoxal_deC pfam00282
Pyridoxal-dependent decarboxylase conserved domain;
175-271 6.56e-07

Pyridoxal-dependent decarboxylase conserved domain;


Pssm-ID: 395219  Cd Length: 373  Bit Score: 52.42  E-value: 6.56e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118097664  175 PVIYISSAARTGLGQAlcnqlGLPLSCMCR-VPCNtmfgSQHQMDVALLDRLIKDDVECGKLPLLLVANAGTPGAGHTDK 253
Cdd:pfam00282 146 LVAYTSDQAHSSIEKA-----ALYGGVKLReIPSD----DNGKMRGMDLEKAIEEDKENGLIPFFVVATLGTTGSGAFDD 216
                          90
                  ....*....|....*...
gi 118097664  254 LGRLKELCEQYNMWLHVE 271
Cdd:pfam00282 217 LQELGDICAKHNLWLHVD 234
PLN02880 PLN02880
tyrosine decarboxylase
176-271 1.51e-03

tyrosine decarboxylase


Pssm-ID: 215475 [Multi-domain]  Cd Length: 490  Bit Score: 41.82  E-value: 1.51e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118097664 176 VIYISSAARTGLGQAlCNQLGL-PLSC-MCRVPCNTMFGsqhqMDVALLDRLIKDDVECGKLPLLLVANAGTPGAGHTDK 253
Cdd:PLN02880 183 VVYASDQTHSALQKA-CQIAGIhPENCrLLKTDSSTNYA----LAPELLSEAISTDLSSGLIPFFLCATVGTTSSTAVDP 257
                         90
                 ....*....|....*...
gi 118097664 254 LGRLKELCEQYNMWLHVE 271
Cdd:PLN02880 258 LLELGKIAKSNGMWFHVD 275
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.20
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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