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Conserved domains on  [gi|201066344|ref|NP_001128433|]
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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) ...
203-394 4.18e-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: 92.27  E-value: 4.18e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 201066344 203 RVPCNtmfgSQHQMDVAFLEKLIKDDVERGRLPLLLVANAGTAAVGHTDKIGRLKELCEQYGIWLHVEGvnlatlALGyv 282
Cdd:cd06450  121 LVPVD----EDGRMDPEALEAAIDEDKAEGLNPIMVVATAGTTDTGAIDPLEEIADLAEKYDLWLHVDA------AYG-- 188
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 201066344 283 sSSVLAATK----------CDSMTLTPGLWLGLPAVPAVTLYkhddpaltliagltsnkpadklRALPLWLSLQYLGLDG 352
Cdd:cd06450  189 -GFLLPFPEprhldfgierVDSISVDPHKYGLVPLGCSAVLV----------------------RALKLWATLRRFGRDG 245
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 201066344 353 IVGRIKHACQLSQRLQESLKKVDHIKILVEDELssPVVVFRF 394
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 ...
203-394 4.18e-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: 92.27  E-value: 4.18e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 201066344 203 RVPCNtmfgSQHQMDVAFLEKLIKDDVERGRLPLLLVANAGTAAVGHTDKIGRLKELCEQYGIWLHVEGvnlatlALGyv 282
Cdd:cd06450  121 LVPVD----EDGRMDPEALEAAIDEDKAEGLNPIMVVATAGTTDTGAIDPLEEIADLAEKYDLWLHVDA------AYG-- 188
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 201066344 283 sSSVLAATK----------CDSMTLTPGLWLGLPAVPAVTLYkhddpaltliagltsnkpadklRALPLWLSLQYLGLDG 352
Cdd:cd06450  189 -GFLLPFPEprhldfgierVDSISVDPHKYGLVPLGCSAVLV----------------------RALKLWATLRRFGRDG 245
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 201066344 353 IVGRIKHACQLSQRLQESLKKVDHIKILVEDELssPVVVFRF 394
Cdd:cd06450  246 YGEHIDRIVDLAKYLAELIRADPGFELLGEPNL--SLVCFRL 285
GadA COG0076
Glutamate or tyrosine decarboxylase or a related PLP-dependent protein [Amino acid transport ...
164-394 8.96e-16

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: 8.96e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 201066344 164 DGFNVLYNKKPIIYLSAAARPglgpylCNQ-----LGLPfpcLCRVPcntMFGSQHQMDVAFLEKLIKDDVERGrlplLL 238
Cdd:COG0076  148 LAESGKPGGKPNIVCSETAHF------SFEkaaryLGLG---LRRVP---TVPTDYRIDVDALEEAIDENTIGG----VV 211
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 201066344 239 VANAGTAAVGHTDKIGRLKELCEQYGIWLHVEGvnlatlALGyvsSSVLAATKC-----------DSMTLTPGLWLGLPA 307
Cdd:COG0076  212 VGTAGTTDTGSIDDIEELADIAEEYGIWLHVDA------AFG---GFLLPFLEPdgrwdfglegvDSITVDGHKYGLAPI 282
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 201066344 308 VPAVTLYK----------HDDPALT----LIAGLTSNKPADklRALPLWLSLQYLGLDGIVGRIKHACQLSQRLQESLKK 373
Cdd:COG0076  283 GCGVVLFRdeealrriliFADYYLPgggiPNFTILGSRPGR--QALALYANLRRLGREGYRKLLDRTLELARYLAEELEK 360
                        250       260
                 ....*....|....*....|.
gi 201066344 374 VDHIKILVEDELssPVVVFRF 394
Cdd:COG0076  361 LGDFELVNEPEL--PIVAFRL 379
Pyridoxal_deC pfam00282
Pyridoxal-dependent decarboxylase conserved domain;
171-393 2.50e-10

Pyridoxal-dependent decarboxylase conserved domain;


Pssm-ID: 395219  Cd Length: 373  Bit Score: 62.82  E-value: 2.50e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 201066344  171 NKKPIIYLSAAARpglgpYLCNQLGLPFPCLCR-VPCNtmfgSQHQMDVAFLEKLIKDDVERGRLPLLLVANAGTAAVGH 249
Cdd:pfam00282 143 LAKLVAYTSDQAH-----SSIEKAALYGGVKLReIPSD----DNGKMRGMDLEKAIEEDKENGLIPFFVVATLGTTGSGA 213
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 201066344  250 TDKIGRLKELCEQYGIWLHVEGVNLATLALG-YVSSSVLAATKCDSMTLTPGLWLGLPA------------------VPA 310
Cdd:pfam00282 214 FDDLQELGDICAKHNLWLHVDAAYGGSAFICpEFRHWLFGIERADSITFNPHKWMLVLLdcsavwvkdkealqqafqFNP 293
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 201066344  311 VTLYKHDDPALTLIAGLTSNKpadKLRALPLWLSLQYLGLDGIVGRIKHACQLSQRLQESLKKVDHIKILVEDELssPVV 390
Cdd:pfam00282 294 LYLGHTDSAYDTGHKQIPLSR---RFRILKLWFVIRSLGVEGLQNQIRRHVELAQYLEALIRKDGRFEICAEVGL--GLV 368

                  ...
gi 201066344  391 VFR 393
Cdd:pfam00282 369 CFR 371
PRK13520 PRK13520
tyrosine decarboxylase MfnA;
212-393 4.58e-06

tyrosine decarboxylase MfnA;


Pssm-ID: 237409  Cd Length: 371  Bit Score: 49.50  E-value: 4.58e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 201066344 212 SQHQMDVAFLEKLIKDDVergrlpLLLVANAGTAAVGHTDKIGRLKELCEQYGIWLHVE----GVNLATLALGYVSSSVL 287
Cdd:PRK13520 135 DDYRVDVKAVEDLIDDNT------IGIVGIAGTTELGQVDPIPELSKIALENGIFLHVDaafgGFVIPFLDDPPNFDFSL 208
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 201066344 288 AATkcDSMTLTPGLwLGLPAVPA-VTLYKH---------DDPALTLI--AGLTSNKPAdkLRALPLWLSLQYLGLDGIVG 355
Cdd:PRK13520 209 PGV--DSITIDPHK-MGLAPIPAgGILFRDesyldalavDTPYLTSKkqATLTGTRSG--AGVAATYAVMKYLGREGYRK 283
                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 201066344 356 RIKHACQLSQRLQESLKKVDhIKILVEDELssPVVVFR 393
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 ...
203-394 4.18e-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: 92.27  E-value: 4.18e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 201066344 203 RVPCNtmfgSQHQMDVAFLEKLIKDDVERGRLPLLLVANAGTAAVGHTDKIGRLKELCEQYGIWLHVEGvnlatlALGyv 282
Cdd:cd06450  121 LVPVD----EDGRMDPEALEAAIDEDKAEGLNPIMVVATAGTTDTGAIDPLEEIADLAEKYDLWLHVDA------AYG-- 188
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 201066344 283 sSSVLAATK----------CDSMTLTPGLWLGLPAVPAVTLYkhddpaltliagltsnkpadklRALPLWLSLQYLGLDG 352
Cdd:cd06450  189 -GFLLPFPEprhldfgierVDSISVDPHKYGLVPLGCSAVLV----------------------RALKLWATLRRFGRDG 245
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 201066344 353 IVGRIKHACQLSQRLQESLKKVDHIKILVEDELssPVVVFRF 394
Cdd:cd06450  246 YGEHIDRIVDLAKYLAELIRADPGFELLGEPNL--SLVCFRL 285
GadA COG0076
Glutamate or tyrosine decarboxylase or a related PLP-dependent protein [Amino acid transport ...
164-394 8.96e-16

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: 8.96e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 201066344 164 DGFNVLYNKKPIIYLSAAARPglgpylCNQ-----LGLPfpcLCRVPcntMFGSQHQMDVAFLEKLIKDDVERGrlplLL 238
Cdd:COG0076  148 LAESGKPGGKPNIVCSETAHF------SFEkaaryLGLG---LRRVP---TVPTDYRIDVDALEEAIDENTIGG----VV 211
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 201066344 239 VANAGTAAVGHTDKIGRLKELCEQYGIWLHVEGvnlatlALGyvsSSVLAATKC-----------DSMTLTPGLWLGLPA 307
Cdd:COG0076  212 VGTAGTTDTGSIDDIEELADIAEEYGIWLHVDA------AFG---GFLLPFLEPdgrwdfglegvDSITVDGHKYGLAPI 282
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 201066344 308 VPAVTLYK----------HDDPALT----LIAGLTSNKPADklRALPLWLSLQYLGLDGIVGRIKHACQLSQRLQESLKK 373
Cdd:COG0076  283 GCGVVLFRdeealrriliFADYYLPgggiPNFTILGSRPGR--QALALYANLRRLGREGYRKLLDRTLELARYLAEELEK 360
                        250       260
                 ....*....|....*....|.
gi 201066344 374 VDHIKILVEDELssPVVVFRF 394
Cdd:COG0076  361 LGDFELVNEPEL--PIVAFRL 379
Pyridoxal_deC pfam00282
Pyridoxal-dependent decarboxylase conserved domain;
171-393 2.50e-10

Pyridoxal-dependent decarboxylase conserved domain;


Pssm-ID: 395219  Cd Length: 373  Bit Score: 62.82  E-value: 2.50e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 201066344  171 NKKPIIYLSAAARpglgpYLCNQLGLPFPCLCR-VPCNtmfgSQHQMDVAFLEKLIKDDVERGRLPLLLVANAGTAAVGH 249
Cdd:pfam00282 143 LAKLVAYTSDQAH-----SSIEKAALYGGVKLReIPSD----DNGKMRGMDLEKAIEEDKENGLIPFFVVATLGTTGSGA 213
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 201066344  250 TDKIGRLKELCEQYGIWLHVEGVNLATLALG-YVSSSVLAATKCDSMTLTPGLWLGLPA------------------VPA 310
Cdd:pfam00282 214 FDDLQELGDICAKHNLWLHVDAAYGGSAFICpEFRHWLFGIERADSITFNPHKWMLVLLdcsavwvkdkealqqafqFNP 293
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 201066344  311 VTLYKHDDPALTLIAGLTSNKpadKLRALPLWLSLQYLGLDGIVGRIKHACQLSQRLQESLKKVDHIKILVEDELssPVV 390
Cdd:pfam00282 294 LYLGHTDSAYDTGHKQIPLSR---RFRILKLWFVIRSLGVEGLQNQIRRHVELAQYLEALIRKDGRFEICAEVGL--GLV 368

                  ...
gi 201066344  391 VFR 393
Cdd:pfam00282 369 CFR 371
PRK13520 PRK13520
tyrosine decarboxylase MfnA;
212-393 4.58e-06

tyrosine decarboxylase MfnA;


Pssm-ID: 237409  Cd Length: 371  Bit Score: 49.50  E-value: 4.58e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 201066344 212 SQHQMDVAFLEKLIKDDVergrlpLLLVANAGTAAVGHTDKIGRLKELCEQYGIWLHVE----GVNLATLALGYVSSSVL 287
Cdd:PRK13520 135 DDYRVDVKAVEDLIDDNT------IGIVGIAGTTELGQVDPIPELSKIALENGIFLHVDaafgGFVIPFLDDPPNFDFSL 208
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 201066344 288 AATkcDSMTLTPGLwLGLPAVPA-VTLYKH---------DDPALTLI--AGLTSNKPAdkLRALPLWLSLQYLGLDGIVG 355
Cdd:PRK13520 209 PGV--DSITIDPHK-MGLAPIPAgGILFRDesyldalavDTPYLTSKkqATLTGTRSG--AGVAATYAVMKYLGREGYRK 283
                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 201066344 356 RIKHACQLSQRLQESLKKVDhIKILVEDELssPVVVFR 393
Cdd:PRK13520 284 VVERCMENTRWLAEELKERG-FEPVIEPVL--NIVAFD 318
PLN02590 PLN02590
probable tyrosine decarboxylase
221-394 1.92e-04

probable tyrosine decarboxylase


Pssm-ID: 178200  Cd Length: 539  Bit Score: 44.70  E-value: 1.92e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 201066344 221 LEKLIKDDVERGRLPLLLVANAGTAAVGHTDKIGRLKELCEQYGIWLHVEGVNLATLALGYVSSSVLAATK-CDSMTLTP 299
Cdd:PLN02590 274 LEEAISHDLAKGFIPFFICATVGTTSSAAVDPLVPLGNIAKKYGIWLHVDAAYAGNACICPEYRKFIDGIEnADSFNMNA 353
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 201066344 300 GLWLgLPAVPAVTLYKHDdpALTLIAGLTSNKP----------------------ADKLRALPLWLSLQYLGLDGIVGRI 357
Cdd:PLN02590 354 HKWL-FANQTCSPLWVKD--RYSLIDALKTNPEylefkvskkdtvvnykdwqislSRRFRSLKLWMVLRLYGSENLRNFI 430
                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 201066344 358 KHACQLSQRLQESLKKVDHIKILVEDELSspVVVFRF 394
Cdd:PLN02590 431 RDHVNLAKHFEDYVAQDPSFEVVTTRYFS--LVCFRL 465
PLN02880 PLN02880
tyrosine decarboxylase
193-369 8.08e-04

tyrosine decarboxylase


Pssm-ID: 215475  Cd Length: 490  Bit Score: 42.59  E-value: 8.08e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 201066344 193 QLGLPFPCLCRV---PCNTMFGSQHQMdvafLEKLIKDDVERGRLPLLLVANAGTAAVGHTDKIGRLKELCEQYGIWLHV 269
Cdd:PLN02880 199 QIAGIHPENCRLlktDSSTNYALAPEL----LSEAISTDLSSGLIPFFLCATVGTTSSTAVDPLLELGKIAKSNGMWFHV 274
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 201066344 270 EGvnlatlalGYVSSSVL---------AATKCDSMTLTPGLWLgLPAVPAVTLYKHDDPAltLIAGLTS------NKPAD 334
Cdd:PLN02880 275 DA--------AYAGSACIcpeyrhyidGVEEADSFNMNAHKWF-LTNFDCSLLWVKDRNA--LIQSLSTnpeflkNKASQ 343
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 201066344 335 ----------------KLRALPLWLSLQYLGLDGIVGRIKHACQLSQRLQE 369
Cdd:PLN02880 344 ansvvdykdwqiplgrRFRSLKLWMVLRLYGVENLQSYIRNHIKLAKEFEQ 394
 
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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