NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|344031196|gb|AEM77227|]
View 

Ddc, partial [Drosophila prolongata]

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

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

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) ...
1-188 7.41e-84

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: 252.34  E-value: 7.41e-84
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 344031196    1 AIACIGFTWIASPACTELEVVMMDWLGKMLDLPAEFLSCSGGKgggVIQGTASESTLIALLGAKAKKVKEVKDLHPEWDE 80
Cdd:pfam00282  63 AINCNGFTWESSPACTELENVVMNWLGEMLGLPAEFLGQEGGG---VLQPGSSESNLLALLAARTKWIKRMKAAGKPADS 139
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 344031196   81 HTILGKLVGYCSDQAHSSVERAGLLGGVKLRSVIS-VNTRMHGDALEKAIEQDLAEGLIPFYAVVTLGTTNSCAFDRLDE 159
Cdd:pfam00282 140 SGILAKLVAYTSDQAHSSIEKAALYGGVKLREIPSdDNGKMRGMDLEKAIEEDKENGLIPFFVVATLGTTGSGAFDDLQE 219
                         170       180
                  ....*....|....*....|....*....
gi 344031196  160 CGPVGNRHNVWIHVDAAYAGSAFICPEYR 188
Cdd:pfam00282 220 LGDICAKHNLWLHVDAAYGGSAFICPEFR 248
 
Name Accession Description Interval E-value
Pyridoxal_deC pfam00282
Pyridoxal-dependent decarboxylase conserved domain;
1-188 7.41e-84

Pyridoxal-dependent decarboxylase conserved domain;


Pssm-ID: 395219  Cd Length: 373  Bit Score: 252.34  E-value: 7.41e-84
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 344031196    1 AIACIGFTWIASPACTELEVVMMDWLGKMLDLPAEFLSCSGGKgggVIQGTASESTLIALLGAKAKKVKEVKDLHPEWDE 80
Cdd:pfam00282  63 AINCNGFTWESSPACTELENVVMNWLGEMLGLPAEFLGQEGGG---VLQPGSSESNLLALLAARTKWIKRMKAAGKPADS 139
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 344031196   81 HTILGKLVGYCSDQAHSSVERAGLLGGVKLRSVIS-VNTRMHGDALEKAIEQDLAEGLIPFYAVVTLGTTNSCAFDRLDE 159
Cdd:pfam00282 140 SGILAKLVAYTSDQAHSSIEKAALYGGVKLREIPSdDNGKMRGMDLEKAIEEDKENGLIPFFVVATLGTTGSGAFDDLQE 219
                         170       180
                  ....*....|....*....|....*....
gi 344031196  160 CGPVGNRHNVWIHVDAAYAGSAFICPEYR 188
Cdd:pfam00282 220 LGDICAKHNLWLHVDAAYGGSAFICPEFR 248
DOPA_deC_like cd06450
DOPA decarboxylase family. This family belongs to pyridoxal phosphate (PLP)-dependent ...
1-188 3.16e-57

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: 183.17  E-value: 3.16e-57
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 344031196   1 AIACIGFTWIASPACTELEVVMMDWLGKMLDLPAEflscsggKGGGVIQGTASESTLIALLGAKAKKVKevkdlHPEWDE 80
Cdd:cd06450   22 AKNAIDFTWDESPAATEMEAEVVNWLAKLFGLPSE-------DADGVFTSGGSESNLLALLAARDRARK-----RLKAGG 89
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 344031196  81 HTILGKLVGYCSDQAHSSVERAGLLGGVKLRSV-ISVNTRMHGDALEKAIEQDLAEGLIPFYAVVTLGTTNSCAFDRLDE 159
Cdd:cd06450   90 GRGIDKLVIVCSDQAHVSVEKAAAYLDVKVRLVpVDEDGRMDPEALEAAIDEDKAEGLNPIMVVATAGTTDTGAIDPLEE 169
                        170       180
                 ....*....|....*....|....*....
gi 344031196 160 CGPVGNRHNVWIHVDAAYAGSAFICPEYR 188
Cdd:cd06450  170 IADLAEKYDLWLHVDAAYGGFLLPFPEPR 198
PLN02880 PLN02880
tyrosine decarboxylase
1-188 1.27e-52

tyrosine decarboxylase


Pssm-ID: 215475 [Multi-domain]  Cd Length: 490  Bit Score: 175.10  E-value: 1.27e-52
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 344031196   1 AIACIGFTWIASPACTELEVVMMDWLGKMLDLPAEFLSCSGGKGggVIQGTASESTLIALLGAKAKKVKEVKDlhpewde 80
Cdd:PLN02880 106 GLNIVGFSWITSPAATELEMIVLDWLAKLLNLPEQFLSTGNGGG--VIQGTASEAVLVVLLAARDRVLRKVGK------- 176
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 344031196  81 hTILGKLVGYCSDQAHSSVERAGLLGGVK------LRSVISVNTRMHGDALEKAIEQDLAEGLIPFYAVVTLGTTNSCAF 154
Cdd:PLN02880 177 -NALEKLVVYASDQTHSALQKACQIAGIHpencrlLKTDSSTNYALAPELLSEAISTDLSSGLIPFFLCATVGTTSSTAV 255
                        170       180       190
                 ....*....|....*....|....*....|....
gi 344031196 155 DRLDECGPVGNRHNVWIHVDAAYAGSAFICPEYR 188
Cdd:PLN02880 256 DPLLELGKIAKSNGMWFHVDAAYAGSACICPEYR 289
GadA COG0076
Glutamate or tyrosine decarboxylase or a related PLP-dependent protein [Amino acid transport ...
8-188 1.36e-41

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: 145.36  E-value: 1.36e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 344031196   8 TWIASPACTELEVVMMDWLGKMLDLPAEFlscsggkgGGVIQGTASESTLIALLgakaKKVKEVKDLHPEWDEHTILGKL 87
Cdd:COG0076   98 DWDTSPAATELEREVVRWLADLLGLPEGA--------GGVFTSGGTEANLLALL----AARDRALARRVRAEGLPGAPRP 165
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 344031196  88 VGYCSDQAHSSVERAGLLGGVKLRSVISVNT----RMHGDALEKAIEQDLAEGLIPFYAVVTLGTTNSCAFDRLDECGPV 163
Cdd:COG0076  166 RIVVSEEAHSSVDKAARLLGLGRDALRKVPVdedgRMDPDALEAAIDEDRAAGLNPIAVVATAGTTNTGAIDPLAEIADI 245
                        170       180
                 ....*....|....*....|....*
gi 344031196 164 GNRHNVWIHVDAAYAGSAFICPEYR 188
Cdd:COG0076  246 AREHGLWLHVDAAYGGFALPSPELR 270
 
Name Accession Description Interval E-value
Pyridoxal_deC pfam00282
Pyridoxal-dependent decarboxylase conserved domain;
1-188 7.41e-84

Pyridoxal-dependent decarboxylase conserved domain;


Pssm-ID: 395219  Cd Length: 373  Bit Score: 252.34  E-value: 7.41e-84
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 344031196    1 AIACIGFTWIASPACTELEVVMMDWLGKMLDLPAEFLSCSGGKgggVIQGTASESTLIALLGAKAKKVKEVKDLHPEWDE 80
Cdd:pfam00282  63 AINCNGFTWESSPACTELENVVMNWLGEMLGLPAEFLGQEGGG---VLQPGSSESNLLALLAARTKWIKRMKAAGKPADS 139
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 344031196   81 HTILGKLVGYCSDQAHSSVERAGLLGGVKLRSVIS-VNTRMHGDALEKAIEQDLAEGLIPFYAVVTLGTTNSCAFDRLDE 159
Cdd:pfam00282 140 SGILAKLVAYTSDQAHSSIEKAALYGGVKLREIPSdDNGKMRGMDLEKAIEEDKENGLIPFFVVATLGTTGSGAFDDLQE 219
                         170       180
                  ....*....|....*....|....*....
gi 344031196  160 CGPVGNRHNVWIHVDAAYAGSAFICPEYR 188
Cdd:pfam00282 220 LGDICAKHNLWLHVDAAYGGSAFICPEFR 248
DOPA_deC_like cd06450
DOPA decarboxylase family. This family belongs to pyridoxal phosphate (PLP)-dependent ...
1-188 3.16e-57

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: 183.17  E-value: 3.16e-57
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 344031196   1 AIACIGFTWIASPACTELEVVMMDWLGKMLDLPAEflscsggKGGGVIQGTASESTLIALLGAKAKKVKevkdlHPEWDE 80
Cdd:cd06450   22 AKNAIDFTWDESPAATEMEAEVVNWLAKLFGLPSE-------DADGVFTSGGSESNLLALLAARDRARK-----RLKAGG 89
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 344031196  81 HTILGKLVGYCSDQAHSSVERAGLLGGVKLRSV-ISVNTRMHGDALEKAIEQDLAEGLIPFYAVVTLGTTNSCAFDRLDE 159
Cdd:cd06450   90 GRGIDKLVIVCSDQAHVSVEKAAAYLDVKVRLVpVDEDGRMDPEALEAAIDEDKAEGLNPIMVVATAGTTDTGAIDPLEE 169
                        170       180
                 ....*....|....*....|....*....
gi 344031196 160 CGPVGNRHNVWIHVDAAYAGSAFICPEYR 188
Cdd:cd06450  170 IADLAEKYDLWLHVDAAYGGFLLPFPEPR 198
PLN02880 PLN02880
tyrosine decarboxylase
1-188 1.27e-52

tyrosine decarboxylase


Pssm-ID: 215475 [Multi-domain]  Cd Length: 490  Bit Score: 175.10  E-value: 1.27e-52
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 344031196   1 AIACIGFTWIASPACTELEVVMMDWLGKMLDLPAEFLSCSGGKGggVIQGTASESTLIALLGAKAKKVKEVKDlhpewde 80
Cdd:PLN02880 106 GLNIVGFSWITSPAATELEMIVLDWLAKLLNLPEQFLSTGNGGG--VIQGTASEAVLVVLLAARDRVLRKVGK------- 176
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 344031196  81 hTILGKLVGYCSDQAHSSVERAGLLGGVK------LRSVISVNTRMHGDALEKAIEQDLAEGLIPFYAVVTLGTTNSCAF 154
Cdd:PLN02880 177 -NALEKLVVYASDQTHSALQKACQIAGIHpencrlLKTDSSTNYALAPELLSEAISTDLSSGLIPFFLCATVGTTSSTAV 255
                        170       180       190
                 ....*....|....*....|....*....|....
gi 344031196 155 DRLDECGPVGNRHNVWIHVDAAYAGSAFICPEYR 188
Cdd:PLN02880 256 DPLLELGKIAKSNGMWFHVDAAYAGSACICPEYR 289
PLN02590 PLN02590
probable tyrosine decarboxylase
1-188 1.01e-48

probable tyrosine decarboxylase


Pssm-ID: 178200 [Multi-domain]  Cd Length: 539  Bit Score: 165.65  E-value: 1.01e-48
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 344031196   1 AIACIGFTWIASPACTELEVVMMDWLGKMLDLPAEFLSCSGGKGggVIQGTASESTLIALLGAKAKKVKEVKDlhpewde 80
Cdd:PLN02590 154 GLSVVGFTWLTSPAATELEIIVLDWLAKLLQLPDHFLSTGNGGG--VIQGTGCEAVLVVVLAARDRILKKVGK------- 224
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 344031196  81 hTILGKLVGYCSDQAHSSVERAGLLGGVK------LRSVISVNTRMHGDALEKAIEQDLAEGLIPFYAVVTLGTTNSCAF 154
Cdd:PLN02590 225 -TLLPQLVVYGSDQTHSSFRKACLIGGIHeenirlLKTDSSTNYGMPPESLEEAISHDLAKGFIPFFICATVGTTSSAAV 303
                        170       180       190
                 ....*....|....*....|....*....|....
gi 344031196 155 DRLDECGPVGNRHNVWIHVDAAYAGSAFICPEYR 188
Cdd:PLN02590 304 DPLVPLGNIAKKYGIWLHVDAAYAGNACICPEYR 337
GadA COG0076
Glutamate or tyrosine decarboxylase or a related PLP-dependent protein [Amino acid transport ...
8-188 1.36e-41

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: 145.36  E-value: 1.36e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 344031196   8 TWIASPACTELEVVMMDWLGKMLDLPAEFlscsggkgGGVIQGTASESTLIALLgakaKKVKEVKDLHPEWDEHTILGKL 87
Cdd:COG0076   98 DWDTSPAATELEREVVRWLADLLGLPEGA--------GGVFTSGGTEANLLALL----AARDRALARRVRAEGLPGAPRP 165
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 344031196  88 VGYCSDQAHSSVERAGLLGGVKLRSVISVNT----RMHGDALEKAIEQDLAEGLIPFYAVVTLGTTNSCAFDRLDECGPV 163
Cdd:COG0076  166 RIVVSEEAHSSVDKAARLLGLGRDALRKVPVdedgRMDPDALEAAIDEDRAAGLNPIAVVATAGTTNTGAIDPLAEIADI 245
                        170       180
                 ....*....|....*....|....*
gi 344031196 164 GNRHNVWIHVDAAYAGSAFICPEYR 188
Cdd:COG0076  246 AREHGLWLHVDAAYGGFALPSPELR 270
AAT_I cd01494
Aspartate aminotransferase (AAT) superfamily (fold type I) of pyridoxal phosphate (PLP) ...
92-188 1.57e-10

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: 57.01  E-value: 1.57e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 344031196  92 SDQAHSSVER-AGLLGGVKLRSVisVNTRMHGDALEKAIEQDLAEGLIPFYAVVTLGTTNSCAFDRLDECGPVGNRHNVW 170
Cdd:cd01494   47 DANGHGSRYWvAAELAGAKPVPV--PVDDAGYGGLDVAILEELKAKPNVALIVITPNTTSGGVLVPLKEIRKIAKEYGIL 124
                         90
                 ....*....|....*...
gi 344031196 171 IHVDAAYAGSAFICPEYR 188
Cdd:cd01494  125 LLVDAASAGGASPAPGVL 142
PRK02769 PRK02769
histidine decarboxylase; Provisional
90-179 1.26e-03

histidine decarboxylase; Provisional


Pssm-ID: 235068 [Multi-domain]  Cd Length: 380  Bit Score: 38.48  E-value: 1.26e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 344031196  90 YCSDQAHSSVERAGLLGGVKLRSVISV-NTRMHGDALEKAIEQDLAEGLIPFyavVTLGTTNSCAFDRLDECGPVGNRH- 167
Cdd:PRK02769 114 YYSKDTHYSVSKIARLLRIKSRVITSLpNGEIDYDDLISKIKENKNQPPIIF---ANIGTTMTGAIDNIKEIQEILKKIg 190
                         90
                 ....*....|....
gi 344031196 168 --NVWIHVDAAYAG 179
Cdd:PRK02769 191 idDYYIHADAALSG 204
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH