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Conserved domains on  [gi|741974136|ref|XP_010817588|]
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pyridoxal-dependent decarboxylase domain-containing protein 1 isoform X1 [Bos taurus]

Protein Classification

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) ...
177-368 2.63e-20

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: 418510  Cd Length: 345  Bit Score: 93.04  E-value: 2.63e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 741974136 177 RVPCNtvfgSQHQMDVAFLEKLIKDDIERGKLPLLLVANAGTAAVGHTDKIGRLKEVCEQYGIWLHVEGvnlatlALGyv 256
Cdd:cd06450  121 LVPVD----EDGRMDPEALEAAIDEDKAEGLNPIMVVATAGTTDTGAIDPLEEIADLAEKYDLWLHVDA------AYG-- 188
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 741974136 257 sSSVLAATK----------CDSMTLTPGPWLGLPAVPAVTLYkhddpaltlvsgltsnkpadklRALPLWLSLQYLGLDG 326
Cdd:cd06450  189 -GFLLPFPEprhldfgierVDSISVDPHKYGLVPLGCSAVLV----------------------RALKLWATLRRFGRDG 245
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 741974136 327 IVERIKHACQLSQRLQESLKKVNHIKILVEDELssPVVVFRF 368
Cdd:cd06450  246 YGEHIDRIVDLAKYLAELIRADPGFELLGEPNL--SLVCFRL 285
 
Name Accession Description Interval E-value
DOPA_deC_like cd06450
DOPA decarboxylase family. This family belongs to pyridoxal phosphate (PLP)-dependent ...
177-368 2.63e-20

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  Cd Length: 345  Bit Score: 93.04  E-value: 2.63e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 741974136 177 RVPCNtvfgSQHQMDVAFLEKLIKDDIERGKLPLLLVANAGTAAVGHTDKIGRLKEVCEQYGIWLHVEGvnlatlALGyv 256
Cdd:cd06450  121 LVPVD----EDGRMDPEALEAAIDEDKAEGLNPIMVVATAGTTDTGAIDPLEEIADLAEKYDLWLHVDA------AYG-- 188
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 741974136 257 sSSVLAATK----------CDSMTLTPGPWLGLPAVPAVTLYkhddpaltlvsgltsnkpadklRALPLWLSLQYLGLDG 326
Cdd:cd06450  189 -GFLLPFPEprhldfgierVDSISVDPHKYGLVPLGCSAVLV----------------------RALKLWATLRRFGRDG 245
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 741974136 327 IVERIKHACQLSQRLQESLKKVNHIKILVEDELssPVVVFRF 368
Cdd:cd06450  246 YGEHIDRIVDLAKYLAELIRADPGFELLGEPNL--SLVCFRL 285
GadA COG0076
Glutamate or tyrosine decarboxylase or a related PLP-dependent protein [Amino acid transport ...
138-368 6.42e-17

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: 83.96  E-value: 6.42e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 741974136 138 DGFNVLYNRKPVLYLSAAARPGLgQYLCNQLGLPFPCLCRVPCNtvfgsqHQMDVAFLEKLIKDDIERGklplLLVANAG 217
Cdd:COG0076  148 LAESGKPGGKPNIVCSETAHFSF-EKAARYLGLGLRRVPTVPTD------YRIDVDALEEAIDENTIGG----VVVGTAG 216
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 741974136 218 TAAVGHTDKIGRLKEVCEQYGIWLHVEGvnlatlALGyvsSSVLAATKC-----------DSMTLTPGPWLGLP------ 280
Cdd:COG0076  217 TTDTGSIDDIEELADIAEEYGIWLHVDA------AFG---GFLLPFLEPdgrwdfglegvDSITVDGHKYGLAPigcgvv 287
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 741974136 281 ------------AVPAVTLYKHDDPALTLVSGLTSNkpadklRALPLWLSLQYLGLDGIVERIKHACQLSQRLQESLKKV 348
Cdd:COG0076  288 lfrdeealrrilIFADYYLPGGGIPNFTILGSRPGR------QALALYANLRRLGREGYRKLLDRTLELARYLAEELEKL 361
                        250       260
                 ....*....|....*....|
gi 741974136 349 NHIKILVEDELssPVVVFRF 368
Cdd:COG0076  362 GDFELVNEPEL--PIVAFRL 379
Pyridoxal_deC pfam00282
Pyridoxal-dependent decarboxylase conserved domain;
145-367 1.77e-12

Pyridoxal-dependent decarboxylase conserved domain;


Pssm-ID: 395219  Cd Length: 373  Bit Score: 69.75  E-value: 1.77e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 741974136  145 NRKPVLYLSAAArpglgQYLCNQLGLPFPCLCR-VPCNtvfgSQHQMDVAFLEKLIKDDIERGKLPLLLVANAGTAAVGH 223
Cdd:pfam00282 143 LAKLVAYTSDQA-----HSSIEKAALYGGVKLReIPSD----DNGKMRGMDLEKAIEEDKENGLIPFFVVATLGTTGSGA 213
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 741974136  224 TDKIGRLKEVCEQYGIWLHVEGVNLATLALG-YVSSSVLAATKCDSMTLTPGPWLGLPAvPAVTLYKHDDPALTLVSGL- 301
Cdd:pfam00282 214 FDDLQELGDICAKHNLWLHVDAAYGGSAFICpEFRHWLFGIERADSITFNPHKWMLVLL-DCSAVWVKDKEALQQAFQFn 292
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 741974136  302 -----TSNKPAD----------KLRALPLWLSLQYLGLDGIVERIKHACQLSQRLQESLKKVNHIKILVEDELssPVVVF 366
Cdd:pfam00282 293 plylgHTDSAYDtghkqiplsrRFRILKLWFVIRSLGVEGLQNQIRRHVELAQYLEALIRKDGRFEICAEVGL--GLVCF 370

                  .
gi 741974136  367 R 367
Cdd:pfam00282 371 R 371
PRK13520 PRK13520
tyrosine decarboxylase MfnA;
186-367 8.16e-07

tyrosine decarboxylase MfnA;


Pssm-ID: 237409  Cd Length: 371  Bit Score: 51.81  E-value: 8.16e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 741974136 186 SQHQMDVAFLEKLIKDDIergklpLLLVANAGTAAVGHTDKIGRLKEVCEQYGIWLHVE----GVNLATLALGYVSSSVL 261
Cdd:PRK13520 135 DDYRVDVKAVEDLIDDNT------IGIVGIAGTTELGQVDPIPELSKIALENGIFLHVDaafgGFVIPFLDDPPNFDFSL 208
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 741974136 262 AATkcDSMTLTPGPwLGLPAVPA-VTLYKH---------DDPALTLVSG--LTSNKPAdkLRALPLWLSLQYLGLDGIVE 329
Cdd:PRK13520 209 PGV--DSITIDPHK-MGLAPIPAgGILFRDesyldalavDTPYLTSKKQatLTGTRSG--AGVAATYAVMKYLGREGYRK 283
                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 741974136 330 RIKHACQLSQRLQESLKKVNhIKILVEDELssPVVVFR 367
Cdd:PRK13520 284 VVERCMENTRWLAEELKERG-FEPVIEPVL--NIVAFD 318
 
Name Accession Description Interval E-value
DOPA_deC_like cd06450
DOPA decarboxylase family. This family belongs to pyridoxal phosphate (PLP)-dependent ...
177-368 2.63e-20

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  Cd Length: 345  Bit Score: 93.04  E-value: 2.63e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 741974136 177 RVPCNtvfgSQHQMDVAFLEKLIKDDIERGKLPLLLVANAGTAAVGHTDKIGRLKEVCEQYGIWLHVEGvnlatlALGyv 256
Cdd:cd06450  121 LVPVD----EDGRMDPEALEAAIDEDKAEGLNPIMVVATAGTTDTGAIDPLEEIADLAEKYDLWLHVDA------AYG-- 188
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 741974136 257 sSSVLAATK----------CDSMTLTPGPWLGLPAVPAVTLYkhddpaltlvsgltsnkpadklRALPLWLSLQYLGLDG 326
Cdd:cd06450  189 -GFLLPFPEprhldfgierVDSISVDPHKYGLVPLGCSAVLV----------------------RALKLWATLRRFGRDG 245
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 741974136 327 IVERIKHACQLSQRLQESLKKVNHIKILVEDELssPVVVFRF 368
Cdd:cd06450  246 YGEHIDRIVDLAKYLAELIRADPGFELLGEPNL--SLVCFRL 285
GadA COG0076
Glutamate or tyrosine decarboxylase or a related PLP-dependent protein [Amino acid transport ...
138-368 6.42e-17

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: 83.96  E-value: 6.42e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 741974136 138 DGFNVLYNRKPVLYLSAAARPGLgQYLCNQLGLPFPCLCRVPCNtvfgsqHQMDVAFLEKLIKDDIERGklplLLVANAG 217
Cdd:COG0076  148 LAESGKPGGKPNIVCSETAHFSF-EKAARYLGLGLRRVPTVPTD------YRIDVDALEEAIDENTIGG----VVVGTAG 216
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 741974136 218 TAAVGHTDKIGRLKEVCEQYGIWLHVEGvnlatlALGyvsSSVLAATKC-----------DSMTLTPGPWLGLP------ 280
Cdd:COG0076  217 TTDTGSIDDIEELADIAEEYGIWLHVDA------AFG---GFLLPFLEPdgrwdfglegvDSITVDGHKYGLAPigcgvv 287
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 741974136 281 ------------AVPAVTLYKHDDPALTLVSGLTSNkpadklRALPLWLSLQYLGLDGIVERIKHACQLSQRLQESLKKV 348
Cdd:COG0076  288 lfrdeealrrilIFADYYLPGGGIPNFTILGSRPGR------QALALYANLRRLGREGYRKLLDRTLELARYLAEELEKL 361
                        250       260
                 ....*....|....*....|
gi 741974136 349 NHIKILVEDELssPVVVFRF 368
Cdd:COG0076  362 GDFELVNEPEL--PIVAFRL 379
Pyridoxal_deC pfam00282
Pyridoxal-dependent decarboxylase conserved domain;
145-367 1.77e-12

Pyridoxal-dependent decarboxylase conserved domain;


Pssm-ID: 395219  Cd Length: 373  Bit Score: 69.75  E-value: 1.77e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 741974136  145 NRKPVLYLSAAArpglgQYLCNQLGLPFPCLCR-VPCNtvfgSQHQMDVAFLEKLIKDDIERGKLPLLLVANAGTAAVGH 223
Cdd:pfam00282 143 LAKLVAYTSDQA-----HSSIEKAALYGGVKLReIPSD----DNGKMRGMDLEKAIEEDKENGLIPFFVVATLGTTGSGA 213
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 741974136  224 TDKIGRLKEVCEQYGIWLHVEGVNLATLALG-YVSSSVLAATKCDSMTLTPGPWLGLPAvPAVTLYKHDDPALTLVSGL- 301
Cdd:pfam00282 214 FDDLQELGDICAKHNLWLHVDAAYGGSAFICpEFRHWLFGIERADSITFNPHKWMLVLL-DCSAVWVKDKEALQQAFQFn 292
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 741974136  302 -----TSNKPAD----------KLRALPLWLSLQYLGLDGIVERIKHACQLSQRLQESLKKVNHIKILVEDELssPVVVF 366
Cdd:pfam00282 293 plylgHTDSAYDtghkqiplsrRFRILKLWFVIRSLGVEGLQNQIRRHVELAQYLEALIRKDGRFEICAEVGL--GLVCF 370

                  .
gi 741974136  367 R 367
Cdd:pfam00282 371 R 371
PRK13520 PRK13520
tyrosine decarboxylase MfnA;
186-367 8.16e-07

tyrosine decarboxylase MfnA;


Pssm-ID: 237409  Cd Length: 371  Bit Score: 51.81  E-value: 8.16e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 741974136 186 SQHQMDVAFLEKLIKDDIergklpLLLVANAGTAAVGHTDKIGRLKEVCEQYGIWLHVE----GVNLATLALGYVSSSVL 261
Cdd:PRK13520 135 DDYRVDVKAVEDLIDDNT------IGIVGIAGTTELGQVDPIPELSKIALENGIFLHVDaafgGFVIPFLDDPPNFDFSL 208
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 741974136 262 AATkcDSMTLTPGPwLGLPAVPA-VTLYKH---------DDPALTLVSG--LTSNKPAdkLRALPLWLSLQYLGLDGIVE 329
Cdd:PRK13520 209 PGV--DSITIDPHK-MGLAPIPAgGILFRDesyldalavDTPYLTSKKQatLTGTRSG--AGVAATYAVMKYLGREGYRK 283
                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 741974136 330 RIKHACQLSQRLQESLKKVNhIKILVEDELssPVVVFR 367
Cdd:PRK13520 284 VVERCMENTRWLAEELKERG-FEPVIEPVL--NIVAFD 318
PLN02880 PLN02880
tyrosine decarboxylase
146-343 2.67e-05

tyrosine decarboxylase


Pssm-ID: 215475  Cd Length: 490  Bit Score: 47.21  E-value: 2.67e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 741974136 146 RKPVLYLSAAARPGLgQYLCnQLGLPFPCLCRV---PCNTVFGSQHQMdvafLEKLIKDDIERGKLPLLLVANAGTAAVG 222
Cdd:PLN02880 180 EKLVVYASDQTHSAL-QKAC-QIAGIHPENCRLlktDSSTNYALAPEL----LSEAISTDLSSGLIPFFLCATVGTTSST 253
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 741974136 223 HTDKIGRLKEVCEQYGIWLHVEGvnlatlalGYVSSSVL---------AATKCDSMTLTPGPWLgLPAVPAVTLYKHDDP 293
Cdd:PLN02880 254 AVDPLLELGKIAKSNGMWFHVDA--------AYAGSACIcpeyrhyidGVEEADSFNMNAHKWF-LTNFDCSLLWVKDRN 324
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 741974136 294 ALTLVSG----LTSNKPAD----------------KLRALPLWLSLQYLGLDGIVERIKHACQLSQRLQE 343
Cdd:PLN02880 325 ALIQSLStnpeFLKNKASQansvvdykdwqiplgrRFRSLKLWMVLRLYGVENLQSYIRNHIKLAKEFEQ 394
PLN02590 PLN02590
probable tyrosine decarboxylase
195-368 8.51e-05

probable tyrosine decarboxylase


Pssm-ID: 178200  Cd Length: 539  Bit Score: 45.86  E-value: 8.51e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 741974136 195 LEKLIKDDIERGKLPLLLVANAGTAAVGHTDKIGRLKEVCEQYGIWLHVEGVNLATLALGYVSSSVLAATK-CDSMTLTP 273
Cdd:PLN02590 274 LEEAISHDLAKGFIPFFICATVGTTSSAAVDPLVPLGNIAKKYGIWLHVDAAYAGNACICPEYRKFIDGIEnADSFNMNA 353
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 741974136 274 GPWLgLPAVPAVTLYKHDdpALTLVSGLTSNKP----------------------ADKLRALPLWLSLQYLGLDGIVERI 331
Cdd:PLN02590 354 HKWL-FANQTCSPLWVKD--RYSLIDALKTNPEylefkvskkdtvvnykdwqislSRRFRSLKLWMVLRLYGSENLRNFI 430
                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 741974136 332 KHACQLSQRLQESLKKVNHIKILVEDELSspVVVFRF 368
Cdd:PLN02590 431 RDHVNLAKHFEDYVAQDPSFEVVTTRYFS--LVCFRL 465
PLN03032 PLN03032
serine decarboxylase; Provisional
192-367 5.13e-03

serine decarboxylase; Provisional


Pssm-ID: 166673 [Multi-domain]  Cd Length: 374  Bit Score: 39.81  E-value: 5.13e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 741974136 192 VAFLEKLIKDdieRGKlPLLLVANAGTAAVGHTDKIGRLKEVCEQYGI-----WLHVEGVnLATLALGYVSSSVLAATK- 265
Cdd:PLN03032 149 DDLERALAKN---RDK-PAILNVNIGTTVKGAVDDLDRILRILKELGYtedrfYIHCDGA-LFGLMMPFVSRAPEVTFRk 223
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 741974136 266 -CDSMTLTPGPWLGLPaVP---AVTLYKHDDPALTLVSGLTSNKPA-----DKLRALPLWLSLQYLGLDGIVERIKHACQ 336
Cdd:PLN03032 224 pIGSVSVSGHKFLGCP-MPcgvALTRKKHVKALSQNVEYLNSRDATimgsrNGHAPLYLWYTLRRKGYRGIKRDVQHCMR 302
                        170       180       190
                 ....*....|....*....|....*....|.
gi 741974136 337 LSQRLQESLKKVNHIKILveDELSSPVVVFR 367
Cdd:PLN03032 303 NAHYLKDRLTEAGLTCRL--NELSSTVVFER 331
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.19
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
  • Marchler-Bauer A et al. (2015), "CDD: NCBI's conserved domain database.", Nucleic Acids Res.43(D)222-6.
  • Marchler-Bauer A et al. (2011), "CDD: a Conserved Domain Database for the functional annotation of proteins.", Nucleic Acids Res.39(D)225-9.
  • Marchler-Bauer A, Bryant SH (2004), "CD-Search: protein domain annotations on the fly.", Nucleic Acids Res.32(W)327-331.
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