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Conserved domains on  [gi|1269208372|ref|NP_001344154|]
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pyridoxal-dependent decarboxylase domain-containing protein 1 isoform 5 [Mus musculus]

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) ...
171-393 9.03e-21

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: 94.58  E-value: 9.03e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1269208372 171 KKPVIYLSAAARPGL---GQYLCNQLglpfpclCRVPCNtmfgSQHQMDVAFLEKLIKDDVERGRLPLLLVANAGTAAVG 247
Cdd:cd06450    94 DKLVIVCSDQAHVSVekaAAYLDVKV-------RLVPVD----EDGRMDPEALEAAIDEDKAEGLNPIMVVATAGTTDTG 162
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1269208372 248 HTDKIGRLKELCEQYGIWLHVEGvnlatlALGyvsSSVLAATK----------CDSMTLTPGLWLGLPAVPAVTLYkhdd 317
Cdd:cd06450   163 AIDPLEEIADLAEKYDLWLHVDA------AYG---GFLLPFPEprhldfgierVDSISVDPHKYGLVPLGCSAVLV---- 229
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1269208372 318 paltlvagltsnkpadklRALPLWLSLQYLGLDGIVERIKHACHLSQRLQESLKKVDHIKILVEDELssPVVVFRF 393
Cdd:cd06450   230 ------------------RALKLWATLRRFGRDGYGEHIDRIVDLAKYLAELIRADPGFELLGEPNL--SLVCFRL 285
 
Name Accession Description Interval E-value
DOPA_deC_like cd06450
DOPA decarboxylase family. This family belongs to pyridoxal phosphate (PLP)-dependent ...
171-393 9.03e-21

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: 94.58  E-value: 9.03e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1269208372 171 KKPVIYLSAAARPGL---GQYLCNQLglpfpclCRVPCNtmfgSQHQMDVAFLEKLIKDDVERGRLPLLLVANAGTAAVG 247
Cdd:cd06450    94 DKLVIVCSDQAHVSVekaAAYLDVKV-------RLVPVD----EDGRMDPEALEAAIDEDKAEGLNPIMVVATAGTTDTG 162
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1269208372 248 HTDKIGRLKELCEQYGIWLHVEGvnlatlALGyvsSSVLAATK----------CDSMTLTPGLWLGLPAVPAVTLYkhdd 317
Cdd:cd06450   163 AIDPLEEIADLAEKYDLWLHVDA------AYG---GFLLPFPEprhldfgierVDSISVDPHKYGLVPLGCSAVLV---- 229
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1269208372 318 paltlvagltsnkpadklRALPLWLSLQYLGLDGIVERIKHACHLSQRLQESLKKVDHIKILVEDELssPVVVFRF 393
Cdd:cd06450   230 ------------------RALKLWATLRRFGRDGYGEHIDRIVDLAKYLAELIRADPGFELLGEPNL--SLVCFRL 285
GadA COG0076
Glutamate or tyrosine decarboxylase or a related PLP-dependent protein [Amino acid transport ...
163-393 7.50e-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: 7.50e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1269208372 163 DGFNVLYNKKPVIYLSAAARPGLgQYLCNQLGLPfpcLCRVPcntMFGSQHQMDVAFLEKLIKDDVERGrlplLLVANAG 242
Cdd:COG0076   148 LAESGKPGGKPNIVCSETAHFSF-EKAARYLGLG---LRRVP---TVPTDYRIDVDALEEAIDENTIGG----VVVGTAG 216
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1269208372 243 TAAVGHTDKIGRLKELCEQYGIWLHVEGvnlatlALGyvsSSVLAATKC-----------DSMTLTPGLWLGLPAVPAVT 311
Cdd:COG0076   217 TTDTGSIDDIEELADIAEEYGIWLHVDA------AFG---GFLLPFLEPdgrwdfglegvDSITVDGHKYGLAPIGCGVV 287
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1269208372 312 LYK----------HDDPALT----LVAGLTSNKPADklRALPLWLSLQYLGLDGIVERIKHACHLSQRLQESLKKVDHIK 377
Cdd:COG0076   288 LFRdeealrriliFADYYLPgggiPNFTILGSRPGR--QALALYANLRRLGREGYRKLLDRTLELARYLAEELEKLGDFE 365
                         250
                  ....*....|....*.
gi 1269208372 378 ILVEDELssPVVVFRF 393
Cdd:COG0076   366 LVNEPEL--PIVAFRL 379
Pyridoxal_deC pfam00282
Pyridoxal-dependent decarboxylase conserved domain;
170-392 1.06e-10

Pyridoxal-dependent decarboxylase conserved domain;


Pssm-ID: 395219  Cd Length: 373  Bit Score: 63.98  E-value: 1.06e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1269208372 170 NKKPVIYLSAAArpglgQYLCNQLGLPFPCLCR-VPCNtmfgSQHQMDVAFLEKLIKDDVERGRLPLLLVANAGTAAVGH 248
Cdd:pfam00282 143 LAKLVAYTSDQA-----HSSIEKAALYGGVKLReIPSD----DNGKMRGMDLEKAIEEDKENGLIPFFVVATLGTTGSGA 213
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1269208372 249 TDKIGRLKELCEQYGIWLHVEGVNLATLALG-YVSSSVLAATKCDSMTLTPGLWLGLPAvPAVTLYKHDDPALTLVAGL- 326
Cdd:pfam00282 214 FDDLQELGDICAKHNLWLHVDAAYGGSAFICpEFRHWLFGIERADSITFNPHKWMLVLL-DCSAVWVKDKEALQQAFQFn 292
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1269208372 327 -----TSNKPAD----------KLRALPLWLSLQYLGLDGIVERIKHACHLSQRLQESLKKVDHIKILVEDELssPVVVF 391
Cdd:pfam00282 293 plylgHTDSAYDtghkqiplsrRFRILKLWFVIRSLGVEGLQNQIRRHVELAQYLEALIRKDGRFEICAEVGL--GLVCF 370

                  .
gi 1269208372 392 R 392
Cdd:pfam00282 371 R 371
PRK13520 PRK13520
tyrosine decarboxylase MfnA;
211-392 2.49e-06

tyrosine decarboxylase MfnA;


Pssm-ID: 237409  Cd Length: 371  Bit Score: 50.27  E-value: 2.49e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1269208372 211 SQHQMDVAFLEKLIKDDVergrlpLLLVANAGTAAVGHTDKIGRLKELCEQYGIWLHVE----GVNLATLALGYVSSSVL 286
Cdd:PRK13520  135 DDYRVDVKAVEDLIDDNT------IGIVGIAGTTELGQVDPIPELSKIALENGIFLHVDaafgGFVIPFLDDPPNFDFSL 208
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1269208372 287 AATkcDSMTLTPGLwLGLPAVPA-VTLYKH---------DDPALT--LVAGLTSNKPAdkLRALPLWLSLQYLGLDGIVE 354
Cdd:PRK13520  209 PGV--DSITIDPHK-MGLAPIPAgGILFRDesyldalavDTPYLTskKQATLTGTRSG--AGVAATYAVMKYLGREGYRK 283
                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 1269208372 355 RIKHACHLSQRLQESLKKVDhIKILVEDELssPVVVFR 392
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 ...
171-393 9.03e-21

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: 94.58  E-value: 9.03e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1269208372 171 KKPVIYLSAAARPGL---GQYLCNQLglpfpclCRVPCNtmfgSQHQMDVAFLEKLIKDDVERGRLPLLLVANAGTAAVG 247
Cdd:cd06450    94 DKLVIVCSDQAHVSVekaAAYLDVKV-------RLVPVD----EDGRMDPEALEAAIDEDKAEGLNPIMVVATAGTTDTG 162
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1269208372 248 HTDKIGRLKELCEQYGIWLHVEGvnlatlALGyvsSSVLAATK----------CDSMTLTPGLWLGLPAVPAVTLYkhdd 317
Cdd:cd06450   163 AIDPLEEIADLAEKYDLWLHVDA------AYG---GFLLPFPEprhldfgierVDSISVDPHKYGLVPLGCSAVLV---- 229
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1269208372 318 paltlvagltsnkpadklRALPLWLSLQYLGLDGIVERIKHACHLSQRLQESLKKVDHIKILVEDELssPVVVFRF 393
Cdd:cd06450   230 ------------------RALKLWATLRRFGRDGYGEHIDRIVDLAKYLAELIRADPGFELLGEPNL--SLVCFRL 285
GadA COG0076
Glutamate or tyrosine decarboxylase or a related PLP-dependent protein [Amino acid transport ...
163-393 7.50e-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: 7.50e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1269208372 163 DGFNVLYNKKPVIYLSAAARPGLgQYLCNQLGLPfpcLCRVPcntMFGSQHQMDVAFLEKLIKDDVERGrlplLLVANAG 242
Cdd:COG0076   148 LAESGKPGGKPNIVCSETAHFSF-EKAARYLGLG---LRRVP---TVPTDYRIDVDALEEAIDENTIGG----VVVGTAG 216
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1269208372 243 TAAVGHTDKIGRLKELCEQYGIWLHVEGvnlatlALGyvsSSVLAATKC-----------DSMTLTPGLWLGLPAVPAVT 311
Cdd:COG0076   217 TTDTGSIDDIEELADIAEEYGIWLHVDA------AFG---GFLLPFLEPdgrwdfglegvDSITVDGHKYGLAPIGCGVV 287
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1269208372 312 LYK----------HDDPALT----LVAGLTSNKPADklRALPLWLSLQYLGLDGIVERIKHACHLSQRLQESLKKVDHIK 377
Cdd:COG0076   288 LFRdeealrriliFADYYLPgggiPNFTILGSRPGR--QALALYANLRRLGREGYRKLLDRTLELARYLAEELEKLGDFE 365
                         250
                  ....*....|....*.
gi 1269208372 378 ILVEDELssPVVVFRF 393
Cdd:COG0076   366 LVNEPEL--PIVAFRL 379
Pyridoxal_deC pfam00282
Pyridoxal-dependent decarboxylase conserved domain;
170-392 1.06e-10

Pyridoxal-dependent decarboxylase conserved domain;


Pssm-ID: 395219  Cd Length: 373  Bit Score: 63.98  E-value: 1.06e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1269208372 170 NKKPVIYLSAAArpglgQYLCNQLGLPFPCLCR-VPCNtmfgSQHQMDVAFLEKLIKDDVERGRLPLLLVANAGTAAVGH 248
Cdd:pfam00282 143 LAKLVAYTSDQA-----HSSIEKAALYGGVKLReIPSD----DNGKMRGMDLEKAIEEDKENGLIPFFVVATLGTTGSGA 213
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1269208372 249 TDKIGRLKELCEQYGIWLHVEGVNLATLALG-YVSSSVLAATKCDSMTLTPGLWLGLPAvPAVTLYKHDDPALTLVAGL- 326
Cdd:pfam00282 214 FDDLQELGDICAKHNLWLHVDAAYGGSAFICpEFRHWLFGIERADSITFNPHKWMLVLL-DCSAVWVKDKEALQQAFQFn 292
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1269208372 327 -----TSNKPAD----------KLRALPLWLSLQYLGLDGIVERIKHACHLSQRLQESLKKVDHIKILVEDELssPVVVF 391
Cdd:pfam00282 293 plylgHTDSAYDtghkqiplsrRFRILKLWFVIRSLGVEGLQNQIRRHVELAQYLEALIRKDGRFEICAEVGL--GLVCF 370

                  .
gi 1269208372 392 R 392
Cdd:pfam00282 371 R 371
PRK13520 PRK13520
tyrosine decarboxylase MfnA;
211-392 2.49e-06

tyrosine decarboxylase MfnA;


Pssm-ID: 237409  Cd Length: 371  Bit Score: 50.27  E-value: 2.49e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1269208372 211 SQHQMDVAFLEKLIKDDVergrlpLLLVANAGTAAVGHTDKIGRLKELCEQYGIWLHVE----GVNLATLALGYVSSSVL 286
Cdd:PRK13520  135 DDYRVDVKAVEDLIDDNT------IGIVGIAGTTELGQVDPIPELSKIALENGIFLHVDaafgGFVIPFLDDPPNFDFSL 208
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1269208372 287 AATkcDSMTLTPGLwLGLPAVPA-VTLYKH---------DDPALT--LVAGLTSNKPAdkLRALPLWLSLQYLGLDGIVE 354
Cdd:PRK13520  209 PGV--DSITIDPHK-MGLAPIPAgGILFRDesyldalavDTPYLTskKQATLTGTRSG--AGVAATYAVMKYLGREGYRK 283
                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 1269208372 355 RIKHACHLSQRLQESLKKVDhIKILVEDELssPVVVFR 392
Cdd:PRK13520  284 VVERCMENTRWLAEELKERG-FEPVIEPVL--NIVAFD 318
PLN02880 PLN02880
tyrosine decarboxylase
171-428 2.84e-05

tyrosine decarboxylase


Pssm-ID: 215475  Cd Length: 490  Bit Score: 47.21  E-value: 2.84e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1269208372 171 KKPVIYLSAAARPGLgQYLCnQLGLPFPCLCRV---PCNTMFGSQHQMdvafLEKLIKDDVERGRLPLLLVANAGTAAVG 247
Cdd:PLN02880  180 EKLVVYASDQTHSAL-QKAC-QIAGIHPENCRLlktDSSTNYALAPEL----LSEAISTDLSSGLIPFFLCATVGTTSST 253
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1269208372 248 HTDKIGRLKELCEQYGIWLHVEGvnlatlalGYVSSSVL---------AATKCDSMTLTPGLWLgLPAVPAVTLYKHDDP 318
Cdd:PLN02880  254 AVDPLLELGKIAKSNGMWFHVDA--------AYAGSACIcpeyrhyidGVEEADSFNMNAHKWF-LTNFDCSLLWVKDRN 324
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1269208372 319 ALTLVAG----LTSNKPAD----------------KLRALPLWLSLQYLGLDGIVERIKHACHLSQRLQEslkkvdhiki 378
Cdd:PLN02880  325 ALIQSLStnpeFLKNKASQansvvdykdwqiplgrRFRSLKLWMVLRLYGVENLQSYIRNHIKLAKEFEQ---------- 394
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|
gi 1269208372 379 LVEDELSSPVVVFRFFqelpaSDSAFKAVPVSNIAPAAVGRERHSCDALN 428
Cdd:PLN02880  395 LVAQDSRFEVVTPRIF-----SLVCFRLVPPKNNEDNGNKLNHDLLDAVN 439
PLN02590 PLN02590
probable tyrosine decarboxylase
220-428 1.12e-04

probable tyrosine decarboxylase


Pssm-ID: 178200  Cd Length: 539  Bit Score: 45.47  E-value: 1.12e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1269208372 220 LEKLIKDDVERGRLPLLLVANAGTAAVGHTDKIGRLKELCEQYGIWLHVEGVNLATLALGYVSSSVLAATK-CDSMTLTP 298
Cdd:PLN02590  274 LEEAISHDLAKGFIPFFICATVGTTSSAAVDPLVPLGNIAKKYGIWLHVDAAYAGNACICPEYRKFIDGIEnADSFNMNA 353
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1269208372 299 GLWLgLPAVPAVTLYKHDdpALTLVAGLTSNKP----------------------ADKLRALPLWLSLQYLGLDGIVERI 356
Cdd:PLN02590  354 HKWL-FANQTCSPLWVKD--RYSLIDALKTNPEylefkvskkdtvvnykdwqislSRRFRSLKLWMVLRLYGSENLRNFI 430
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1269208372 357 KHACHLSQRLQESLKKVDHIKilvedelsspVVVFRFFqelpaSDSAFKAVPVSNIAPAAVGRERHSCDALN 428
Cdd:PLN02590  431 RDHVNLAKHFEDYVAQDPSFE----------VVTTRYF-----SLVCFRLAPVDGDEDQCNERNRELLAAVN 487
 
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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