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Conserved domains on  [gi|1622845112|ref|XP_028685348|]
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cysteine sulfinic acid decarboxylase isoform X4 [Macaca mulatta]

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) ...
 5-286 1.76e-86

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: 450240 [Multi-domain]  Cd Length: 345  Bit Score: 262.14  E-value: 1.76e-86
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622845112   5 RKEPVPPRrGKMVPEDLERQIGMAEAEGAVPFLVSATSGTTVLGAFDPLEAIADVCQRHGLWLHVDAAWGGSVLLSQTHR 84
Cdd:cd06450   120 RLVPVDED-GRMDPEALEAAIDEDKAEGLNPIMVVATAGTTDTGAIDPLEEIADLAEKYDLWLHVDAAYGGFLLPFPEPR 198

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622845112  85 HLLDGIQRADSVAWNPHKLLAAGLQCSALLLQdtsnllkrchgsqasylfqqdkfydvaldtgdkvvqcgrrvdCLKLWL 164
Cdd:cd06450   199 HLDFGIERVDSISVDPHKYGLVPLGCSAVLVR------------------------------------------ALKLWA 236

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622845112 165 MWKAQGDQGLERRIDQAFALARYLVEEIKKREGLELVMEPEFVNVCFWFVPPSlrgkqdspdyheRLSKVAPVLKERMVK 244
Cdd:cd06450   237 TLRRFGRDGYGEHIDRIVDLAKYLAELIRADPGFELLGEPNLSLVCFRLKPSV------------KLDELNYDLSDRLNE 304

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|..
gi 1622845112 245 EGSMMIGYQPHGTRgNFFRVVVANPALTCADMDFLLNELERL 286
Cdd:cd06450   305 RGGWHVPATTLGGP-NVLRFVVTNPLTTRDDADALLEDIERA 345
 
Name Accession Description Interval E-value
DOPA_deC_like cd06450
DOPA decarboxylase family. This family belongs to pyridoxal phosphate (PLP)-dependent ...
 5-286 1.76e-86

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: 262.14  E-value: 1.76e-86
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622845112   5 RKEPVPPRrGKMVPEDLERQIGMAEAEGAVPFLVSATSGTTVLGAFDPLEAIADVCQRHGLWLHVDAAWGGSVLLSQTHR 84
Cdd:cd06450   120 RLVPVDED-GRMDPEALEAAIDEDKAEGLNPIMVVATAGTTDTGAIDPLEEIADLAEKYDLWLHVDAAYGGFLLPFPEPR 198

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622845112  85 HLLDGIQRADSVAWNPHKLLAAGLQCSALLLQdtsnllkrchgsqasylfqqdkfydvaldtgdkvvqcgrrvdCLKLWL 164
Cdd:cd06450   199 HLDFGIERVDSISVDPHKYGLVPLGCSAVLVR------------------------------------------ALKLWA 236

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622845112 165 MWKAQGDQGLERRIDQAFALARYLVEEIKKREGLELVMEPEFVNVCFWFVPPSlrgkqdspdyheRLSKVAPVLKERMVK 244
Cdd:cd06450   237 TLRRFGRDGYGEHIDRIVDLAKYLAELIRADPGFELLGEPNLSLVCFRLKPSV------------KLDELNYDLSDRLNE 304

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|..
gi 1622845112 245 EGSMMIGYQPHGTRgNFFRVVVANPALTCADMDFLLNELERL 286
Cdd:cd06450   305 RGGWHVPATTLGGP-NVLRFVVTNPLTTRDDADALLEDIERA 345
GadA COG0076
Glutamate or tyrosine decarboxylase or a related PLP-dependent protein [Amino acid transport ...
 8-289 3.01e-81

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: 252.45  E-value: 3.01e-81
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622845112   8 PVPPRrGKMVPEDLERQIGMAEAEGAVPFLVSATSGTTVLGAFDPLEAIADVCQRHGLWLHVDAAWGGSVLLSQTHRHLL 87
Cdd:COG0076   195 PVDED-GRMDPDALEAAIDEDRAAGLNPIAVVATAGTTNTGAIDPLAEIADIAREHGLWLHVDAAYGGFALPSPELRHLL 273

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622845112  88 DGIQRADSVAWNPHKLLAAGLQCSALLLQDTSnLLKRCHGSQASYLFQQDkfyDVALDTGDKVVQCGRRVDCLKLWLMWK 167
Cdd:COG0076   274 DGIERADSITVDPHKWLYVPYGCGAVLVRDPE-LLREAFSFHASYLGPAD---DGVPNLGDYTLELSRRFRALKLWATLR 349

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622845112 168 AQGDQGLERRIDQAFALARYLVEEIKKREGLELVMEPEFVNVCFWFVPPSLrgkqdsPDYHERLSKVApvlkERMVKEGS 247
Cdd:COG0076   350 ALGREGYRELIERCIDLARYLAEGIAALPGFELLAPPELNIVCFRYKPAGL------DEEDALNYALR----DRLRARGR 419

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|..
gi 1622845112 248 MMIGYQPHGTRgNFFRVVVANPALTCADMDFLLNELERLGQD 289
Cdd:COG0076   420 AFLSPTKLDGR-VVLRLVVLNPRTTEDDVDALLDDLREAAAE 460
Pyridoxal_deC pfam00282
Pyridoxal-dependent decarboxylase conserved domain;
13-214 5.47e-72

Pyridoxal-dependent decarboxylase conserved domain;


Pssm-ID: 395219  Cd Length: 373  Bit Score: 226.15  E-value: 5.47e-72
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622845112  13 RGKMVPEDLERQIGMAEAEGAVPFLVSATSGTTVLGAFDPLEAIADVCQRHGLWLHVDAAWGGSVLLSQTHRHLLDGIQR 92
Cdd:pfam00282 177 NGKMRGMDLEKAIEEDKENGLIPFFVVATLGTTGSGAFDDLQELGDICAKHNLWLHVDAAYGGSAFICPEFRHWLFGIER 256

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622845112  93 ADSVAWNPHKLLAAGLQCSALLLQDtSNLLKRCHGSQASYLFQQDKFYdvalDTGDKVVQCGRRVDCLKLWLMWKAQGDQ 172
Cdd:pfam00282 257 ADSITFNPHKWMLVLLDCSAVWVKD-KEALQQAFQFNPLYLGHTDSAY----DTGHKQIPLSRRFRILKLWFVIRSLGVE 331

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 1622845112 173 GLERRIDQAFALARYLVEEIKKREGLELVMEPEFVNVCFWFV 214
Cdd:pfam00282 332 GLQNQIRRHVELAQYLEALIRKDGRFEICAEVGLGLVCFRLK 373
PLN02590 PLN02590
probable tyrosine decarboxylase
 16-215 2.66e-32

probable tyrosine decarboxylase


Pssm-ID: 178200 [Multi-domain]  Cd Length: 539  Bit Score: 124.82  E-value: 2.66e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622845112  16 MVPEDLERQIGMAEAEGAVPFLVSATSGTTVLGAFDPLEAIADVCQRHGLWLHVDAAWGGSVLLSQTHRHLLDGIQRADS 95
Cdd:PLN02590  269 MPPESLEEAISHDLAKGFIPFFICATVGTTSSAAVDPLVPLGNIAKKYGIWLHVDAAYAGNACICPEYRKFIDGIENADS 348

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622845112  96 VAWNPHKLLAAGLQCSALLLQDTSNLLKRCHGSQASYLFQQDKfYDVALDTGDKVVQCGRRVDCLKLWLMWKAQGDQGLE 175
Cdd:PLN02590  349 FNMNAHKWLFANQTCSPLWVKDRYSLIDALKTNPEYLEFKVSK-KDTVVNYKDWQISLSRRFRSLKLWMVLRLYGSENLR 427

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 1622845112 176 RRIDQAFALARYLVEEIKKREGLELVMEPEFVNVCFWFVP 215
Cdd:PLN02590  428 NFIRDHVNLAKHFEDYVAQDPSFEVVTTRYFSLVCFRLAP 467
 
Name Accession Description Interval E-value
DOPA_deC_like cd06450
DOPA decarboxylase family. This family belongs to pyridoxal phosphate (PLP)-dependent ...
 5-286 1.76e-86

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: 262.14  E-value: 1.76e-86
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622845112   5 RKEPVPPRrGKMVPEDLERQIGMAEAEGAVPFLVSATSGTTVLGAFDPLEAIADVCQRHGLWLHVDAAWGGSVLLSQTHR 84
Cdd:cd06450   120 RLVPVDED-GRMDPEALEAAIDEDKAEGLNPIMVVATAGTTDTGAIDPLEEIADLAEKYDLWLHVDAAYGGFLLPFPEPR 198

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622845112  85 HLLDGIQRADSVAWNPHKLLAAGLQCSALLLQdtsnllkrchgsqasylfqqdkfydvaldtgdkvvqcgrrvdCLKLWL 164
Cdd:cd06450   199 HLDFGIERVDSISVDPHKYGLVPLGCSAVLVR------------------------------------------ALKLWA 236

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622845112 165 MWKAQGDQGLERRIDQAFALARYLVEEIKKREGLELVMEPEFVNVCFWFVPPSlrgkqdspdyheRLSKVAPVLKERMVK 244
Cdd:cd06450   237 TLRRFGRDGYGEHIDRIVDLAKYLAELIRADPGFELLGEPNLSLVCFRLKPSV------------KLDELNYDLSDRLNE 304

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|..
gi 1622845112 245 EGSMMIGYQPHGTRgNFFRVVVANPALTCADMDFLLNELERL 286
Cdd:cd06450   305 RGGWHVPATTLGGP-NVLRFVVTNPLTTRDDADALLEDIERA 345
GadA COG0076
Glutamate or tyrosine decarboxylase or a related PLP-dependent protein [Amino acid transport ...
 8-289 3.01e-81

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: 252.45  E-value: 3.01e-81
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622845112   8 PVPPRrGKMVPEDLERQIGMAEAEGAVPFLVSATSGTTVLGAFDPLEAIADVCQRHGLWLHVDAAWGGSVLLSQTHRHLL 87
Cdd:COG0076   195 PVDED-GRMDPDALEAAIDEDRAAGLNPIAVVATAGTTNTGAIDPLAEIADIAREHGLWLHVDAAYGGFALPSPELRHLL 273

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622845112  88 DGIQRADSVAWNPHKLLAAGLQCSALLLQDTSnLLKRCHGSQASYLFQQDkfyDVALDTGDKVVQCGRRVDCLKLWLMWK 167
Cdd:COG0076   274 DGIERADSITVDPHKWLYVPYGCGAVLVRDPE-LLREAFSFHASYLGPAD---DGVPNLGDYTLELSRRFRALKLWATLR 349

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622845112 168 AQGDQGLERRIDQAFALARYLVEEIKKREGLELVMEPEFVNVCFWFVPPSLrgkqdsPDYHERLSKVApvlkERMVKEGS 247
Cdd:COG0076   350 ALGREGYRELIERCIDLARYLAEGIAALPGFELLAPPELNIVCFRYKPAGL------DEEDALNYALR----DRLRARGR 419

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|..
gi 1622845112 248 MMIGYQPHGTRgNFFRVVVANPALTCADMDFLLNELERLGQD 289
Cdd:COG0076   420 AFLSPTKLDGR-VVLRLVVLNPRTTEDDVDALLDDLREAAAE 460
Pyridoxal_deC pfam00282
Pyridoxal-dependent decarboxylase conserved domain;
13-214 5.47e-72

Pyridoxal-dependent decarboxylase conserved domain;


Pssm-ID: 395219  Cd Length: 373  Bit Score: 226.15  E-value: 5.47e-72
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622845112  13 RGKMVPEDLERQIGMAEAEGAVPFLVSATSGTTVLGAFDPLEAIADVCQRHGLWLHVDAAWGGSVLLSQTHRHLLDGIQR 92
Cdd:pfam00282 177 NGKMRGMDLEKAIEEDKENGLIPFFVVATLGTTGSGAFDDLQELGDICAKHNLWLHVDAAYGGSAFICPEFRHWLFGIER 256

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622845112  93 ADSVAWNPHKLLAAGLQCSALLLQDtSNLLKRCHGSQASYLFQQDKFYdvalDTGDKVVQCGRRVDCLKLWLMWKAQGDQ 172
Cdd:pfam00282 257 ADSITFNPHKWMLVLLDCSAVWVKD-KEALQQAFQFNPLYLGHTDSAY----DTGHKQIPLSRRFRILKLWFVIRSLGVE 331

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 1622845112 173 GLERRIDQAFALARYLVEEIKKREGLELVMEPEFVNVCFWFV 214
Cdd:pfam00282 332 GLQNQIRRHVELAQYLEALIRKDGRFEICAEVGLGLVCFRLK 373
PLN02590 PLN02590
probable tyrosine decarboxylase
 16-215 2.66e-32

probable tyrosine decarboxylase


Pssm-ID: 178200 [Multi-domain]  Cd Length: 539  Bit Score: 124.82  E-value: 2.66e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622845112  16 MVPEDLERQIGMAEAEGAVPFLVSATSGTTVLGAFDPLEAIADVCQRHGLWLHVDAAWGGSVLLSQTHRHLLDGIQRADS 95
Cdd:PLN02590  269 MPPESLEEAISHDLAKGFIPFFICATVGTTSSAAVDPLVPLGNIAKKYGIWLHVDAAYAGNACICPEYRKFIDGIENADS 348

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622845112  96 VAWNPHKLLAAGLQCSALLLQDTSNLLKRCHGSQASYLFQQDKfYDVALDTGDKVVQCGRRVDCLKLWLMWKAQGDQGLE 175
Cdd:PLN02590  349 FNMNAHKWLFANQTCSPLWVKDRYSLIDALKTNPEYLEFKVSK-KDTVVNYKDWQISLSRRFRSLKLWMVLRLYGSENLR 427

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 1622845112 176 RRIDQAFALARYLVEEIKKREGLELVMEPEFVNVCFWFVP 215
Cdd:PLN02590  428 NFIRDHVNLAKHFEDYVAQDPSFEVVTTRYFSLVCFRLAP 467
PLN02880 PLN02880
tyrosine decarboxylase
 18-217 2.69e-32

tyrosine decarboxylase


Pssm-ID: 215475 [Multi-domain]  Cd Length: 490  Bit Score: 124.25  E-value: 2.69e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622845112  18 PEDLERQIGMAEAEGAVPFLVSATSGTTVLGAFDPLEAIADVCQRHGLWLHVDAAWGGSVLLSQTHRHLLDGIQRADSVA 97
Cdd:PLN02880  223 PELLSEAISTDLSSGLIPFFLCATVGTTSSTAVDPLLELGKIAKSNGMWFHVDAAYAGSACICPEYRHYIDGVEEADSFN 302

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622845112  98 WNPHKLLAAGLQCSALLLQDTSNLLKRChGSQASYLFQQDKFYDVALDTGDKVVQCGRRVDCLKLWLMWKAQGDQGLERR 177
Cdd:PLN02880  303 MNAHKWFLTNFDCSLLWVKDRNALIQSL-STNPEFLKNKASQANSVVDYKDWQIPLGRRFRSLKLWMVLRLYGVENLQSY 381

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 1622845112 178 IDQAFALARYLVEEIKKREGLELVMEPEFVNVCFWFVPPS 217
Cdd:PLN02880  382 IRNHIKLAKEFEQLVAQDSRFEVVTPRIFSLVCFRLVPPK 421
GLY1 COG2008
Threonine aldolase [Amino acid transport and metabolism];
8-73 7.23e-08

Threonine aldolase [Amino acid transport and metabolism];


Pssm-ID: 441611 [Multi-domain]  Cd Length: 333  Bit Score: 52.76  E-value: 7.23e-08
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1622845112   8 PVPPRRGKMVPEDLERQIGMAEAEGAVPFLVS---ATSGTTVLgAFDPLEAIADVCQRHGLWLHVDAAW 73
Cdd:COG2008   103 PVPGEDGKLTPEDLEAAIRPGDVHFPQPGLVSlenTTEGGTVY-PLEELRAIAAVAREHGLPLHLDGAR 170
LdcC COG1982
Arginine/lysine/ornithine decarboxylase [Amino acid transport and metabolism];
53-208 9.66e-08

Arginine/lysine/ornithine decarboxylase [Amino acid transport and metabolism];


Pssm-ID: 441585 [Multi-domain]  Cd Length: 486  Bit Score: 52.81  E-value: 9.66e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622845112  53 LEAIADVCQRHGLWLHVDAAWGGsvllsqtHRHLLDGIQR------ADSVAWNPHKLLAAGLQCSALLLQDT---SNLLK 123
Cdd:COG1982   179 LKAIAELAHEHGIPVLVDEAHGA-------HFGFHPDLPRsameagADLVVQSTHKTLGALTQSSMLHVKGGrvdHERVN 251

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622845112 124 RC---HGS-QASYLFqqdkfydVA-LDTgdkvvqcGRRvdclklwlMWKAQGdqglERRIDQAFALARYLVEEIKKREGL 198
Cdd:COG1982   252 EAlmlLQStSPSYLL-------MAsLDV-------ARR--------QMAGEG----EELLDEALELAIEARKEINKIPGL 305

                         170
                  ....*....|
gi 1622845112 199 ElVMEPEFVN 208
Cdd:COG1982   306 Y-VFGPEDLG 314
PRK02769 PRK02769
histidine decarboxylase; Provisional
 14-196 1.25e-07

histidine decarboxylase; Provisional


Pssm-ID: 235068 [Multi-domain]  Cd Length: 380  Bit Score: 52.35  E-value: 1.25e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622845112  14 GKMVPEDLERQIgmaEAEGAVPFLVSATSGTTVLGAFDPLEAIADVCQRHGL---WLHVDAAWGGSVLLSQTHRHLLDGI 90
Cdd:PRK02769  143 GEIDYDDLISKI---KENKNQPPIIFANIGTTMTGAIDNIKEIQEILKKIGIddyYIHADAALSGMILPFVNNPPPFSFA 219

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622845112  91 QRADSVAWNPHKLLAAGLQCSALllqdtsnLLKRCHGSQASylfqqdkfYDVA-LDTGDKVVQCGRR-VDCLKLWLMWKA 168
Cdd:PRK02769  220 DGIDSIAISGHKFIGSPMPCGIV-------LAKKKYVERIS--------VDVDyIGSRDQTISGSRNgHTALLLWAAIRS 284

                         170       180
                  ....*....|....*....|....*...
gi 1622845112 169 QGDQGLERRIDQAFALARYLVEEIKKRE 196
Cdd:PRK02769  285 LGSKGLRQRVQHCLDMAQYAVDRLQANG 312
AAT_I cd01494
Aspartate aminotransferase (AAT) superfamily (fold type I) of pyridoxal phosphate (PLP) ...
 35-106 1.26e-06

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: 47.38  E-value: 1.26e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1622845112  35 PFLVSATSGTTVLGAFDPLEAIADVCQRHGLWLHVDAAWGGsvlLSQTHRHLLDGIQRADSVAWNPHKLLAA 106
Cdd:cd01494    93 VALIVITPNTTSGGVLVPLKEIRKIAKEYGILLLVDAASAG---GASPAPGVLIPEGGADVVTFSLHKNLGG 161
TA_like cd06502
Low-specificity threonine aldolase (TA). This family belongs to pyridoxal phosphate (PLP) ...
 8-72 5.03e-06

Low-specificity threonine aldolase (TA). This family belongs to pyridoxal phosphate (PLP)-dependent aspartate aminotransferase superfamily (fold I). TA catalyzes the conversion of L-threonine or L-allo-threonine to glycine and acetaldehyde in a secondary glycine biosynthetic pathway.


Pssm-ID: 99748 [Multi-domain]  Cd Length: 338  Bit Score: 47.33  E-value: 5.03e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1622845112   8 PVPPRRGKMVPEDLERQI-GMAEAEGAVPFLVSATSgTTVLGAFDPLE---AIADVCQRHGLWLHVDAA 72
Cdd:cd06502   100 PVPGENGKLTPEDLEAAIrPRDDIHFPPPSLVSLEN-TTEGGTVYPLDelkAISALAKENGLPLHLDGA 167
Aminotran_5 pfam00266
Aminotransferase class-V; This domain is found in amino transferases, and other enzymes ...
 37-105 9.70e-05

Aminotransferase class-V; This domain is found in amino transferases, and other enzymes including cysteine desulphurase EC:4.4.1.-.


Pssm-ID: 425567 [Multi-domain]  Cd Length: 368  Bit Score: 43.39  E-value: 9.70e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1622845112  37 LVSATSGTTVLGAFDPLEAIADVCQRHGLWLHVDAAwggsvllsQT--HRHlLDgIQR--ADSVAWNPHKLLA 105
Cdd:pfam00266 142 LVAITHVSNVTGTIQPVPEIGKLAHQYGALVLVDAA--------QAigHRP-ID-VQKlgVDFLAFSGHKLYG 204
Orn_deC_like cd00615
Ornithine decarboxylase family. This family belongs to pyridoxal phosphate (PLP)-dependent ...
 53-135 5.13e-04

Ornithine decarboxylase family. This family belongs to pyridoxal phosphate (PLP)-dependent aspartate aminotransferase superfamily (fold I). The major groups in this CD corresponds to ornithine decarboxylase (ODC), arginine decarboxylase (ADC) and lysine decarboxylase (LDC). ODC is a dodecamer composed of six homodimers and catalyzes the decarboxylation of tryptophan. ADC catalyzes the decarboxylation of arginine and LDC catalyzes the decarboxylation of lysine. Members of this family are widely found in all three forms of life.


Pssm-ID: 99739 [Multi-domain]  Cd Length: 294  Bit Score: 40.69  E-value: 5.13e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622845112  53 LEAIADVCQRHGLWLHVDAAWGGsvllsqtHRHLLDGIQR------ADSVAWNPHKLLAAGLQCSALLLQDtsNLLKRCH 126
Cdd:cd00615   172 LRKIVEEAHHRGLPVLVDEAHGA-------HFRFHPILPSsaamagADIVVQSTHKTLPALTQGSMIHVKG--DLVNPDR 242


                  ....*....
gi 1622845112 127 GSQASYLFQ 135
Cdd:cd00615   243 VNEALNLHQ 251
CsdA COG0520
Selenocysteine lyase/Cysteine desulfurase [Amino acid transport and metabolism];
12-105 6.24e-04

Selenocysteine lyase/Cysteine desulfurase [Amino acid transport and metabolism];


Pssm-ID: 440286 [Multi-domain]  Cd Length: 396  Bit Score: 40.89  E-value: 6.24e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622845112  12 RRG---KMVPEDLERQIGMAEAEGAV---PFLVSATSGTTVLGAFDPLEAIADVCQRHGLWLHVDAAwggsvllsQT--H 83
Cdd:COG0520   126 RTGaevRVIPLDEDGELDLEALEALLtprTKLVAVTHVSNVTGTVNPVKEIAALAHAHGALVLVDGA--------QSvpH 197

                          90       100
                  ....*....|....*....|....*.
gi 1622845112  84 RHL----LDgiqrADSVAWNPHKLLA 105
Cdd:COG0520   198 LPVdvqaLG----CDFYAFSGHKLYG 219
KBL_like cd06454
KBL_like; this family belongs to the pyridoxal phosphate (PLP)-dependent aspartate ...
 18-72 1.48e-03

KBL_like; this family belongs to the pyridoxal phosphate (PLP)-dependent aspartate aminotransferase superfamily (fold I). The major groups in this CD corresponds to serine palmitoyltransferase (SPT), 5-aminolevulinate synthase (ALAS), 8-amino-7-oxononanoate synthase (AONS), and 2-amino-3-ketobutyrate CoA ligase (KBL). SPT is responsible for the condensation of L-serine with palmitoyl-CoA to produce 3-ketodihydrospingosine, the reaction of the first step in sphingolipid biosynthesis. ALAS is involved in heme biosynthesis; it catalyzes the synthesis of 5-aminolevulinic acid from glycine and succinyl-coenzyme A. AONS catalyses the decarboxylative condensation of l-alanine and pimeloyl-CoA in the first committed step of biotin biosynthesis. KBL catalyzes the second reaction step of the metabolic degradation pathway for threonine converting 2-amino-3-ketobutyrate, to glycine and acetyl-CoA. The members of this CD are widely found in all three forms of life.


Pssm-ID: 99747 [Multi-domain]  Cd Length: 349  Bit Score: 39.47  E-value: 1.48e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1622845112  18 PEDLERQIgmAEA-EGAVPFLVSATSGTTVLGAFDPLEAIADVCQRHGLWLHVDAA 72
Cdd:cd06454   117 MEDLEKLL--REArRPYGKKLIVTEGVYSMDGDIAPLPELVDLAKKYGAILFVDEA 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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