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Conserved domains on  [gi|5006769|gb|AAD37625|]
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dopa decarboxylase, partial [Gluphisia septentrionis]

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) ...
1-211 1.01e-96

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 pfam00282:

Pssm-ID: 450240  Cd Length: 373  Bit Score: 286.24  E-value: 1.01e-96
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5006769      1 LGLPDSFLARSGGeagGVIQGTASEATLVALLGAKSRMMHRVKEQHPEWSDTEIISKLVGYCNKQAHSSVERAGLLGGVK 80
Cdd:pfam00282  92 LGLPAEFLGQEGG---GVLQPGSSESNLLALLAARTKWIKRMKAAGKPADSSGILAKLVAYTSDQAHSSIEKAALYGGVK 168
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5006769     81 LRSLKPDGKRRLRGETLQEAIEEDIRNGLIPFYAVATLGTTSS*TFDALDEIGDVCRSNGI**HV*A*YAG*AFICPEYR 160
Cdd:pfam00282 169 LREIPSDDNGKMRGMDLEKAIEEDKENGLIPFFVVATLGTTGSGAFDDLQELGDICAKHNLWLHVDAAYGGSAFICPEFR 248
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 5006769    161 YLMKGVEKADSFNFNPHKWLLVNFDCSAMWLKEPRWIVDAFNVDPLYLKHD 211
Cdd:pfam00282 249 HWLFGIERADSITFNPHKWMLVLLDCSAVWVKDKEALQQAFQFNPLYLGHT 299
 
Name Accession Description Interval E-value
Pyridoxal_deC pfam00282
Pyridoxal-dependent decarboxylase conserved domain;
1-211 1.01e-96

Pyridoxal-dependent decarboxylase conserved domain;


Pssm-ID: 395219  Cd Length: 373  Bit Score: 286.24  E-value: 1.01e-96
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5006769      1 LGLPDSFLARSGGeagGVIQGTASEATLVALLGAKSRMMHRVKEQHPEWSDTEIISKLVGYCNKQAHSSVERAGLLGGVK 80
Cdd:pfam00282  92 LGLPAEFLGQEGG---GVLQPGSSESNLLALLAARTKWIKRMKAAGKPADSSGILAKLVAYTSDQAHSSIEKAALYGGVK 168
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5006769     81 LRSLKPDGKRRLRGETLQEAIEEDIRNGLIPFYAVATLGTTSS*TFDALDEIGDVCRSNGI**HV*A*YAG*AFICPEYR 160
Cdd:pfam00282 169 LREIPSDDNGKMRGMDLEKAIEEDKENGLIPFFVVATLGTTGSGAFDDLQELGDICAKHNLWLHVDAAYGGSAFICPEFR 248
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 5006769    161 YLMKGVEKADSFNFNPHKWLLVNFDCSAMWLKEPRWIVDAFNVDPLYLKHD 211
Cdd:pfam00282 249 HWLFGIERADSITFNPHKWMLVLLDCSAVWVKDKEALQQAFQFNPLYLGHT 299
PLN02880 PLN02880
tyrosine decarboxylase
1-210 2.55e-66

tyrosine decarboxylase


Pssm-ID: 215475 [Multi-domain]  Cd Length: 490  Bit Score: 211.69  E-value: 2.55e-66
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5006769     1 LGLPDSFLarSGGEAGGVIQGTASEATLVALLGAKSRMMHRVKEQHPEwsdteiisKLVGYCNKQAHSSVERAGLLGGV- 79
Cdd:PLN02880 135 LNLPEQFL--STGNGGGVIQGTASEAVLVVLLAARDRVLRKVGKNALE--------KLVVYASDQTHSALQKACQIAGIh 204
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5006769    80 --KLRSLKPDGKRR--LRGETLQEAIEEDIRNGLIPFYAVATLGTTSS*TFDALDEIGDVCRSNGI**HV*A*YAG*AFI 155
Cdd:PLN02880 205 peNCRLLKTDSSTNyaLAPELLSEAISTDLSSGLIPFFLCATVGTTSSTAVDPLLELGKIAKSNGMWFHVDAAYAGSACI 284
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 5006769   156 CPEYRYLMKGVEKADSFNFNPHKWLLVNFDCSAMWLKEPRWIVDAFNVDPLYLKH 210
Cdd:PLN02880 285 CPEYRHYIDGVEEADSFNMNAHKWFLTNFDCSLLWVKDRNALIQSLSTNPEFLKN 339
DOPA_deC_like cd06450
DOPA decarboxylase family. This family belongs to pyridoxal phosphate (PLP)-dependent ...
13-192 5.21e-66

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: 207.06  E-value: 5.21e-66
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5006769   13 GEAGGVIQGTASEATLVALLGAKSRMMHRVKEQHPEwsdteIISKLVGYCNKQAHSSVERAGLLGGVKLRSLKPDGKRRL 92
Cdd:cd06450  56 EDADGVFTSGGSESNLLALLAARDRARKRLKAGGGR-----GIDKLVIVCSDQAHVSVEKAAAYLDVKVRLVPVDEDGRM 130
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5006769   93 RGETLQEAIEEDIRNGLIPFYAVATLGTTSS*TFDALDEIGDVCRSNGI**HV*A*YAG*AFICPEYRYLMKGVEKADSF 172
Cdd:cd06450 131 DPEALEAAIDEDKAEGLNPIMVVATAGTTDTGAIDPLEEIADLAEKYDLWLHVDAAYGGFLLPFPEPRHLDFGIERVDSI 210
                       170       180
                ....*....|....*....|
gi 5006769  173 NFNPHKWLLVNFDCSAMWLK 192
Cdd:cd06450 211 SVDPHKYGLVPLGCSAVLVR 230
GadA COG0076
Glutamate or tyrosine decarboxylase or a related PLP-dependent protein [Amino acid transport ...
1-215 1.57e-55

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: 183.11  E-value: 1.57e-55
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5006769    1 LGLPDsflarsggEAGGVIQGTASEATLVALLGAKSRMMHRVKEQHPEWSdteiISKLVGYCNKQAHSSVERAGLLGGVK 80
Cdd:COG0076 120 LGLPE--------GAGGVFTSGGTEANLLALLAARDRALARRVRAEGLPG----APRPRIVVSEEAHSSVDKAARLLGLG 187
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5006769   81 ---LRSLKPDGKRRLRGETLQEAIEEDIRNGLIPFYAVATLGTTSS*TFDALDEIGDVCRSNGI**HV*A*YAG*AFICP 157
Cdd:COG0076 188 rdaLRKVPVDEDGRMDPDALEAAIDEDRAAGLNPIAVVATAGTTNTGAIDPLAEIADIAREHGLWLHVDAAYGGFALPSP 267
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 5006769  158 EYRYLMKGVEKADSFNFNPHKWLLVNFDCSAMWLKEPRWIVDAFNVDPLYLKHDQQGS 215
Cdd:COG0076 268 ELRHLLDGIERADSITVDPHKWLYVPYGCGAVLVRDPELLREAFSFHASYLGPADDGV 325
 
Name Accession Description Interval E-value
Pyridoxal_deC pfam00282
Pyridoxal-dependent decarboxylase conserved domain;
1-211 1.01e-96

Pyridoxal-dependent decarboxylase conserved domain;


Pssm-ID: 395219  Cd Length: 373  Bit Score: 286.24  E-value: 1.01e-96
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5006769      1 LGLPDSFLARSGGeagGVIQGTASEATLVALLGAKSRMMHRVKEQHPEWSDTEIISKLVGYCNKQAHSSVERAGLLGGVK 80
Cdd:pfam00282  92 LGLPAEFLGQEGG---GVLQPGSSESNLLALLAARTKWIKRMKAAGKPADSSGILAKLVAYTSDQAHSSIEKAALYGGVK 168
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5006769     81 LRSLKPDGKRRLRGETLQEAIEEDIRNGLIPFYAVATLGTTSS*TFDALDEIGDVCRSNGI**HV*A*YAG*AFICPEYR 160
Cdd:pfam00282 169 LREIPSDDNGKMRGMDLEKAIEEDKENGLIPFFVVATLGTTGSGAFDDLQELGDICAKHNLWLHVDAAYGGSAFICPEFR 248
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 5006769    161 YLMKGVEKADSFNFNPHKWLLVNFDCSAMWLKEPRWIVDAFNVDPLYLKHD 211
Cdd:pfam00282 249 HWLFGIERADSITFNPHKWMLVLLDCSAVWVKDKEALQQAFQFNPLYLGHT 299
PLN02880 PLN02880
tyrosine decarboxylase
1-210 2.55e-66

tyrosine decarboxylase


Pssm-ID: 215475 [Multi-domain]  Cd Length: 490  Bit Score: 211.69  E-value: 2.55e-66
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5006769     1 LGLPDSFLarSGGEAGGVIQGTASEATLVALLGAKSRMMHRVKEQHPEwsdteiisKLVGYCNKQAHSSVERAGLLGGV- 79
Cdd:PLN02880 135 LNLPEQFL--STGNGGGVIQGTASEAVLVVLLAARDRVLRKVGKNALE--------KLVVYASDQTHSALQKACQIAGIh 204
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5006769    80 --KLRSLKPDGKRR--LRGETLQEAIEEDIRNGLIPFYAVATLGTTSS*TFDALDEIGDVCRSNGI**HV*A*YAG*AFI 155
Cdd:PLN02880 205 peNCRLLKTDSSTNyaLAPELLSEAISTDLSSGLIPFFLCATVGTTSSTAVDPLLELGKIAKSNGMWFHVDAAYAGSACI 284
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 5006769   156 CPEYRYLMKGVEKADSFNFNPHKWLLVNFDCSAMWLKEPRWIVDAFNVDPLYLKH 210
Cdd:PLN02880 285 CPEYRHYIDGVEEADSFNMNAHKWFLTNFDCSLLWVKDRNALIQSLSTNPEFLKN 339
DOPA_deC_like cd06450
DOPA decarboxylase family. This family belongs to pyridoxal phosphate (PLP)-dependent ...
13-192 5.21e-66

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: 207.06  E-value: 5.21e-66
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5006769   13 GEAGGVIQGTASEATLVALLGAKSRMMHRVKEQHPEwsdteIISKLVGYCNKQAHSSVERAGLLGGVKLRSLKPDGKRRL 92
Cdd:cd06450  56 EDADGVFTSGGSESNLLALLAARDRARKRLKAGGGR-----GIDKLVIVCSDQAHVSVEKAAAYLDVKVRLVPVDEDGRM 130
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5006769   93 RGETLQEAIEEDIRNGLIPFYAVATLGTTSS*TFDALDEIGDVCRSNGI**HV*A*YAG*AFICPEYRYLMKGVEKADSF 172
Cdd:cd06450 131 DPEALEAAIDEDKAEGLNPIMVVATAGTTDTGAIDPLEEIADLAEKYDLWLHVDAAYGGFLLPFPEPRHLDFGIERVDSI 210
                       170       180
                ....*....|....*....|
gi 5006769  173 NFNPHKWLLVNFDCSAMWLK 192
Cdd:cd06450 211 SVDPHKYGLVPLGCSAVLVR 230
GadA COG0076
Glutamate or tyrosine decarboxylase or a related PLP-dependent protein [Amino acid transport ...
1-215 1.57e-55

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: 183.11  E-value: 1.57e-55
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5006769    1 LGLPDsflarsggEAGGVIQGTASEATLVALLGAKSRMMHRVKEQHPEWSdteiISKLVGYCNKQAHSSVERAGLLGGVK 80
Cdd:COG0076 120 LGLPE--------GAGGVFTSGGTEANLLALLAARDRALARRVRAEGLPG----APRPRIVVSEEAHSSVDKAARLLGLG 187
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5006769   81 ---LRSLKPDGKRRLRGETLQEAIEEDIRNGLIPFYAVATLGTTSS*TFDALDEIGDVCRSNGI**HV*A*YAG*AFICP 157
Cdd:COG0076 188 rdaLRKVPVDEDGRMDPDALEAAIDEDRAAGLNPIAVVATAGTTNTGAIDPLAEIADIAREHGLWLHVDAAYGGFALPSP 267
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 5006769  158 EYRYLMKGVEKADSFNFNPHKWLLVNFDCSAMWLKEPRWIVDAFNVDPLYLKHDQQGS 215
Cdd:COG0076 268 ELRHLLDGIERADSITVDPHKWLYVPYGCGAVLVRDPELLREAFSFHASYLGPADDGV 325
PLN02590 PLN02590
probable tyrosine decarboxylase
1-209 1.75e-54

probable tyrosine decarboxylase


Pssm-ID: 178200 [Multi-domain]  Cd Length: 539  Bit Score: 182.22  E-value: 1.75e-54
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5006769     1 LGLPDSFLarSGGEAGGVIQGTASEATLVALLGAKSRMMHRVKEQhpewsdteIISKLVGYCNKQAHSSVERAGLLGGV- 79
Cdd:PLN02590 183 LQLPDHFL--STGNGGGVIQGTGCEAVLVVVLAARDRILKKVGKT--------LLPQLVVYGSDQTHSSFRKACLIGGIh 252
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5006769    80 --KLRSLKPDGKRR--LRGETLQEAIEEDIRNGLIPFYAVATLGTTSS*TFDALDEIGDVCRSNGI**HV*A*YAG*AFI 155
Cdd:PLN02590 253 eeNIRLLKTDSSTNygMPPESLEEAISHDLAKGFIPFFICATVGTTSSAAVDPLVPLGNIAKKYGIWLHVDAAYAGNACI 332
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 5006769   156 CPEYRYLMKGVEKADSFNFNPHKWLLVNFDCSAMWLKEPRWIVDAFNVDPLYLK 209
Cdd:PLN02590 333 CPEYRKFIDGIENADSFNMNAHKWLFANQTCSPLWVKDRYSLIDALKTNPEYLE 386
AAT_I cd01494
Aspartate aminotransferase (AAT) superfamily (fold type I) of pyridoxal phosphate (PLP) ...
12-192 1.93e-15

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: 70.87  E-value: 1.93e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5006769   12 GGEAGGVIQGTASEATLVALLGAKSRmmhrvkeqhpewsDTEIISKLVGYcnkqaHSSVERAGLLGGVKLRSL--KPDGK 89
Cdd:cd01494  15 PGNDKAVFVPSGTGANEAALLALLGP-------------GDEVIVDANGH-----GSRYWVAAELAGAKPVPVpvDDAGY 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5006769   90 RRLRGetlqeAIEEDIRNGLIPFYAVATLGTTSS*TFDALDEIGDVCRSNGI**HV*A*YAG*AFICPEYRylmKGVEKA 169
Cdd:cd01494  77 GGLDV-----AILEELKAKPNVALIVITPNTTSGGVLVPLKEIRKIAKEYGILLLVDAASAGGASPAPGVL---IPEGGA 148
                       170       180
                ....*....|....*....|...
gi 5006769  170 DSFNFNPHKWLLVNfDCSAMWLK 192
Cdd:cd01494 149 DVVTFSLHKNLGGE-GGGVVIVK 170
 
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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