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Conserved domains on  [gi|1370477219|ref|XP_024308551|]
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glutamate decarboxylase 1 isoform X3 [Homo sapiens]

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) ...
 1-262 5.30e-134

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: 386.00  E-value: 5.30e-134
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370477219   1 MYSIMAARYKYFPEVKTKGMAAVP-----KLVLFTSEQSHYSIKKAGAALGFGtdnVILIKCNERGKIIPADFEAKILEA 75
Cdd:pfam00282 116 LLALLAARTKWIKRMKAAGKPADSsgilaKLVAYTSDQAHSSIEKAALYGGVK---LREIPSDDNGKMRGMDLEKAIEED 192

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370477219  76 KQKGYVPFYVNATAGTTVYGAFDPIQEIADICEKYNLWLHVDAAWGGGLLMSRKHRHKLNGIERANSVTWNPHKMMGVLL 155
Cdd:pfam00282 193 KENGLIPFFVVATLGTTGSGAFDDLQELGDICAKHNLWLHVDAAYGGSAFICPEFRHWLFGIERADSITFNPHKWMLVLL 272

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370477219 156 QCSAILVKEKGILQGCNQMCAGYLFQPDKqydvSYDTGDKAIQCGRHVDIFKFWLMWKAKGTVGFENQINKCLELAEYLY 235
Cdd:pfam00282 273 DCSAVWVKDKEALQQAFQFNPLYLGHTDS----AYDTGHKQIPLSRRFRILKLWFVIRSLGVEGLQNQIRRHVELAQYLE 348

                         250       260
                  ....*....|....*....|....*..
gi 1370477219 236 AKIKNREEFEMVFngEPEHTNVCFWYI 262
Cdd:pfam00282 349 ALIRKDGRFEICA--EVGLGLVCFRLK 373
 
Name Accession Description Interval E-value
Pyridoxal_deC pfam00282
Pyridoxal-dependent decarboxylase conserved domain;
1-262 5.30e-134

Pyridoxal-dependent decarboxylase conserved domain;


Pssm-ID: 395219  Cd Length: 373  Bit Score: 386.00  E-value: 5.30e-134
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370477219   1 MYSIMAARYKYFPEVKTKGMAAVP-----KLVLFTSEQSHYSIKKAGAALGFGtdnVILIKCNERGKIIPADFEAKILEA 75
Cdd:pfam00282 116 LLALLAARTKWIKRMKAAGKPADSsgilaKLVAYTSDQAHSSIEKAALYGGVK---LREIPSDDNGKMRGMDLEKAIEED 192

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370477219  76 KQKGYVPFYVNATAGTTVYGAFDPIQEIADICEKYNLWLHVDAAWGGGLLMSRKHRHKLNGIERANSVTWNPHKMMGVLL 155
Cdd:pfam00282 193 KENGLIPFFVVATLGTTGSGAFDDLQELGDICAKHNLWLHVDAAYGGSAFICPEFRHWLFGIERADSITFNPHKWMLVLL 272

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370477219 156 QCSAILVKEKGILQGCNQMCAGYLFQPDKqydvSYDTGDKAIQCGRHVDIFKFWLMWKAKGTVGFENQINKCLELAEYLY 235
Cdd:pfam00282 273 DCSAVWVKDKEALQQAFQFNPLYLGHTDS----AYDTGHKQIPLSRRFRILKLWFVIRSLGVEGLQNQIRRHVELAQYLE 348

                         250       260
                  ....*....|....*....|....*..
gi 1370477219 236 AKIKNREEFEMVFngEPEHTNVCFWYI 262
Cdd:pfam00282 349 ALIRKDGRFEICA--EVGLGLVCFRLK 373
DOPA_deC_like cd06450
DOPA decarboxylase family. This family belongs to pyridoxal phosphate (PLP)-dependent ...
 1-334 8.83e-127

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: 366.53  E-value: 8.83e-127
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370477219   1 MYSIMAARYKYFPEVKTKGMAAVPKLVLFTSEQSHYSIKKAGAALGfgtDNVILIKCNERGKIIPADFEAKILEAKQKGY 80
Cdd:cd06450    71 LLALLAARDRARKRLKAGGGRGIDKLVIVCSDQAHVSVEKAAAYLD---VKVRLVPVDEDGRMDPEALEAAIDEDKAEGL 147

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370477219  81 VPFYVNATAGTTVYGAFDPIQEIADICEKYNLWLHVDAAWGGGLLMSRKHRHKLNGIERANSVTWNPHKMMGVLLQCSAI 160
Cdd:cd06450   148 NPIMVVATAGTTDTGAIDPLEEIADLAEKYDLWLHVDAAYGGFLLPFPEPRHLDFGIERVDSISVDPHKYGLVPLGCSAV 227

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370477219 161 LVKekgilqgcnqmcagylfqpdkqydvsydtgdkaiqcgrhvdIFKFWLMWKAKGTVGFENQINKCLELAEYLYAKIKN 240
Cdd:cd06450   228 LVR-----------------------------------------ALKLWATLRRFGRDGYGEHIDRIVDLAKYLAELIRA 266

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370477219 241 REEFEmvFNGEPEHTNVCFWYIPQSlrgvpdspqrreKLHKVAPKIKALMMESGTTMVGYQPQGDKaNFFRMVISNPAAT 320
Cdd:cd06450   267 DPGFE--LLGEPNLSLVCFRLKPSV------------KLDELNYDLSDRLNERGGWHVPATTLGGP-NVLRFVVTNPLTT 331

                         330
                  ....*....|....
gi 1370477219 321 QSDIDFLIEEIERL 334
Cdd:cd06450   332 RDDADALLEDIERA 345
GadA COG0076
Glutamate or tyrosine decarboxylase or a related PLP-dependent protein [Amino acid transport ...
 1-337 4.75e-105

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: 315.23  E-value: 4.75e-105
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370477219   1 MYSIMAARYKYFPE-VKTKGMAAVPKLVLFTSEQSHYSIKKAGAALGFGTDNVILIKCNERGKIIPADFEAKILEAKQKG 79
Cdd:COG0076   139 LLALLAARDRALARrVRAEGLPGAPRPRIVVSEEAHSSVDKAARLLGLGRDALRKVPVDEDGRMDPDALEAAIDEDRAAG 218

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370477219  80 YVPFYVNATAGTTVYGAFDPIQEIADICEKYNLWLHVDAAWGGGLLMSRKHRHKLNGIERANSVTWNPHKMMGVLLQCSA 159
Cdd:COG0076   219 LNPIAVVATAGTTNTGAIDPLAEIADIAREHGLWLHVDAAYGGFALPSPELRHLLDGIERADSITVDPHKWLYVPYGCGA 298

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370477219 160 ILVKEKGILQGCNQMCAGYLFQPDkqyDVSYDTGDKAIQCGRHVDIFKFWLMWKAKGTVGFENQINKCLELAEYLYAKIK 239
Cdd:COG0076   299 VLVRDPELLREAFSFHASYLGPAD---DGVPNLGDYTLELSRRFRALKLWATLRALGREGYRELIERCIDLARYLAEGIA 375

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370477219 240 NREEFEMVfnGEPEHTNVCFWYIPQSLRGVPDSPQRreklhkvapkIKALMMESGTTMVGYQPQGDKANfFRMVISNPAA 319
Cdd:COG0076   376 ALPGFELL--APPELNIVCFRYKPAGLDEEDALNYA----------LRDRLRARGRAFLSPTKLDGRVV-LRLVVLNPRT 442

                         330
                  ....*....|....*...
gi 1370477219 320 TQSDIDFLIEEIERLGQD 337
Cdd:COG0076   443 TEDDVDALLDDLREAAAE 460
PLN02880 PLN02880
tyrosine decarboxylase
 4-263 1.52e-31

tyrosine decarboxylase


Pssm-ID: 215475 [Multi-domain]  Cd Length: 490  Bit Score: 123.48  E-value: 1.52e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370477219   4 IMAARYKYfpeVKTKGMAAVPKLVLFTSEQSHYSIKKAGAALGFGTDNVILIK--CNERGKIIPADFEAKILEAKQKGYV 81
Cdd:PLN02880  163 LLAARDRV---LRKVGKNALEKLVVYASDQTHSALQKACQIAGIHPENCRLLKtdSSTNYALAPELLSEAISTDLSSGLI 239

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370477219  82 PFYVNATAGTTVYGAFDPIQEIADICEKYNLWLHVDAAWGGGLLMSRKHRHKLNGIERANSVTWNPHKMMGVLLQCSAIL 161
Cdd:PLN02880  240 PFFLCATVGTTSSTAVDPLLELGKIAKSNGMWFHVDAAYAGSACICPEYRHYIDGVEEADSFNMNAHKWFLTNFDCSLLW 319

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370477219 162 VKEKGILQGCNQMCAGYLFQPDKQYDVSYDTGDKAIQCGRHVDIFKFWLMWKAKGTVGFENQINKCLELAEYLYAKIKNR 241
Cdd:PLN02880  320 VKDRNALIQSLSTNPEFLKNKASQANSVVDYKDWQIPLGRRFRSLKLWMVLRLYGVENLQSYIRNHIKLAKEFEQLVAQD 399

                         250       260
                  ....*....|....*....|..
gi 1370477219 242 EEFEMVfnGEPEHTNVCFWYIP 263
Cdd:PLN02880  400 SRFEVV--TPRIFSLVCFRLVP 419
 
Name Accession Description Interval E-value
Pyridoxal_deC pfam00282
Pyridoxal-dependent decarboxylase conserved domain;
1-262 5.30e-134

Pyridoxal-dependent decarboxylase conserved domain;


Pssm-ID: 395219  Cd Length: 373  Bit Score: 386.00  E-value: 5.30e-134
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370477219   1 MYSIMAARYKYFPEVKTKGMAAVP-----KLVLFTSEQSHYSIKKAGAALGFGtdnVILIKCNERGKIIPADFEAKILEA 75
Cdd:pfam00282 116 LLALLAARTKWIKRMKAAGKPADSsgilaKLVAYTSDQAHSSIEKAALYGGVK---LREIPSDDNGKMRGMDLEKAIEED 192

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370477219  76 KQKGYVPFYVNATAGTTVYGAFDPIQEIADICEKYNLWLHVDAAWGGGLLMSRKHRHKLNGIERANSVTWNPHKMMGVLL 155
Cdd:pfam00282 193 KENGLIPFFVVATLGTTGSGAFDDLQELGDICAKHNLWLHVDAAYGGSAFICPEFRHWLFGIERADSITFNPHKWMLVLL 272

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370477219 156 QCSAILVKEKGILQGCNQMCAGYLFQPDKqydvSYDTGDKAIQCGRHVDIFKFWLMWKAKGTVGFENQINKCLELAEYLY 235
Cdd:pfam00282 273 DCSAVWVKDKEALQQAFQFNPLYLGHTDS----AYDTGHKQIPLSRRFRILKLWFVIRSLGVEGLQNQIRRHVELAQYLE 348

                         250       260
                  ....*....|....*....|....*..
gi 1370477219 236 AKIKNREEFEMVFngEPEHTNVCFWYI 262
Cdd:pfam00282 349 ALIRKDGRFEICA--EVGLGLVCFRLK 373
DOPA_deC_like cd06450
DOPA decarboxylase family. This family belongs to pyridoxal phosphate (PLP)-dependent ...
 1-334 8.83e-127

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: 366.53  E-value: 8.83e-127
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370477219   1 MYSIMAARYKYFPEVKTKGMAAVPKLVLFTSEQSHYSIKKAGAALGfgtDNVILIKCNERGKIIPADFEAKILEAKQKGY 80
Cdd:cd06450    71 LLALLAARDRARKRLKAGGGRGIDKLVIVCSDQAHVSVEKAAAYLD---VKVRLVPVDEDGRMDPEALEAAIDEDKAEGL 147

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370477219  81 VPFYVNATAGTTVYGAFDPIQEIADICEKYNLWLHVDAAWGGGLLMSRKHRHKLNGIERANSVTWNPHKMMGVLLQCSAI 160
Cdd:cd06450   148 NPIMVVATAGTTDTGAIDPLEEIADLAEKYDLWLHVDAAYGGFLLPFPEPRHLDFGIERVDSISVDPHKYGLVPLGCSAV 227

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370477219 161 LVKekgilqgcnqmcagylfqpdkqydvsydtgdkaiqcgrhvdIFKFWLMWKAKGTVGFENQINKCLELAEYLYAKIKN 240
Cdd:cd06450   228 LVR-----------------------------------------ALKLWATLRRFGRDGYGEHIDRIVDLAKYLAELIRA 266

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370477219 241 REEFEmvFNGEPEHTNVCFWYIPQSlrgvpdspqrreKLHKVAPKIKALMMESGTTMVGYQPQGDKaNFFRMVISNPAAT 320
Cdd:cd06450   267 DPGFE--LLGEPNLSLVCFRLKPSV------------KLDELNYDLSDRLNERGGWHVPATTLGGP-NVLRFVVTNPLTT 331

                         330
                  ....*....|....
gi 1370477219 321 QSDIDFLIEEIERL 334
Cdd:cd06450   332 RDDADALLEDIERA 345
GadA COG0076
Glutamate or tyrosine decarboxylase or a related PLP-dependent protein [Amino acid transport ...
 1-337 4.75e-105

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: 315.23  E-value: 4.75e-105
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370477219   1 MYSIMAARYKYFPE-VKTKGMAAVPKLVLFTSEQSHYSIKKAGAALGFGTDNVILIKCNERGKIIPADFEAKILEAKQKG 79
Cdd:COG0076   139 LLALLAARDRALARrVRAEGLPGAPRPRIVVSEEAHSSVDKAARLLGLGRDALRKVPVDEDGRMDPDALEAAIDEDRAAG 218

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370477219  80 YVPFYVNATAGTTVYGAFDPIQEIADICEKYNLWLHVDAAWGGGLLMSRKHRHKLNGIERANSVTWNPHKMMGVLLQCSA 159
Cdd:COG0076   219 LNPIAVVATAGTTNTGAIDPLAEIADIAREHGLWLHVDAAYGGFALPSPELRHLLDGIERADSITVDPHKWLYVPYGCGA 298

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370477219 160 ILVKEKGILQGCNQMCAGYLFQPDkqyDVSYDTGDKAIQCGRHVDIFKFWLMWKAKGTVGFENQINKCLELAEYLYAKIK 239
Cdd:COG0076   299 VLVRDPELLREAFSFHASYLGPAD---DGVPNLGDYTLELSRRFRALKLWATLRALGREGYRELIERCIDLARYLAEGIA 375

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370477219 240 NREEFEMVfnGEPEHTNVCFWYIPQSLRGVPDSPQRreklhkvapkIKALMMESGTTMVGYQPQGDKANfFRMVISNPAA 319
Cdd:COG0076   376 ALPGFELL--APPELNIVCFRYKPAGLDEEDALNYA----------LRDRLRARGRAFLSPTKLDGRVV-LRLVVLNPRT 442

                         330
                  ....*....|....*...
gi 1370477219 320 TQSDIDFLIEEIERLGQD 337
Cdd:COG0076   443 TEDDVDALLDDLREAAAE 460
PLN02880 PLN02880
tyrosine decarboxylase
 4-263 1.52e-31

tyrosine decarboxylase


Pssm-ID: 215475 [Multi-domain]  Cd Length: 490  Bit Score: 123.48  E-value: 1.52e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370477219   4 IMAARYKYfpeVKTKGMAAVPKLVLFTSEQSHYSIKKAGAALGFGTDNVILIK--CNERGKIIPADFEAKILEAKQKGYV 81
Cdd:PLN02880  163 LLAARDRV---LRKVGKNALEKLVVYASDQTHSALQKACQIAGIHPENCRLLKtdSSTNYALAPELLSEAISTDLSSGLI 239

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370477219  82 PFYVNATAGTTVYGAFDPIQEIADICEKYNLWLHVDAAWGGGLLMSRKHRHKLNGIERANSVTWNPHKMMGVLLQCSAIL 161
Cdd:PLN02880  240 PFFLCATVGTTSSTAVDPLLELGKIAKSNGMWFHVDAAYAGSACICPEYRHYIDGVEEADSFNMNAHKWFLTNFDCSLLW 319

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370477219 162 VKEKGILQGCNQMCAGYLFQPDKQYDVSYDTGDKAIQCGRHVDIFKFWLMWKAKGTVGFENQINKCLELAEYLYAKIKNR 241
Cdd:PLN02880  320 VKDRNALIQSLSTNPEFLKNKASQANSVVDYKDWQIPLGRRFRSLKLWMVLRLYGVENLQSYIRNHIKLAKEFEQLVAQD 399

                         250       260
                  ....*....|....*....|..
gi 1370477219 242 EEFEMVfnGEPEHTNVCFWYIP 263
Cdd:PLN02880  400 SRFEVV--TPRIFSLVCFRLVP 419
PLN02590 PLN02590
probable tyrosine decarboxylase
 4-263 2.46e-30

probable tyrosine decarboxylase


Pssm-ID: 178200 [Multi-domain]  Cd Length: 539  Bit Score: 120.59  E-value: 2.46e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370477219   4 IMAARYKYFPEVktkGMAAVPKLVLFTSEQSHYSIKKAGAALGFGTDNVILIKCNERGK--IIPADFEAKILEAKQKGYV 81
Cdd:PLN02590  211 VLAARDRILKKV---GKTLLPQLVVYGSDQTHSSFRKACLIGGIHEENIRLLKTDSSTNygMPPESLEEAISHDLAKGFI 287

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370477219  82 PFYVNATAGTTVYGAFDPIQEIADICEKYNLWLHVDAAWGGGLLMSRKHRHKLNGIERANSVTWNPHKMMGVLLQCSAIL 161
Cdd:PLN02590  288 PFFICATVGTTSSAAVDPLVPLGNIAKKYGIWLHVDAAYAGNACICPEYRKFIDGIENADSFNMNAHKWLFANQTCSPLW 367

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370477219 162 VKEKGILQGCNQMCAGYLFQPDKQYDVSYDTGDKAIQCGRHVDIFKFWLMWKAKGTVGFENQINKCLELAEYLYAKIKNR 241
Cdd:PLN02590  368 VKDRYSLIDALKTNPEYLEFKVSKKDTVVNYKDWQISLSRRFRSLKLWMVLRLYGSENLRNFIRDHVNLAKHFEDYVAQD 447

                         250       260
                  ....*....|....*....|..
gi 1370477219 242 EEFEMVFNgePEHTNVCFWYIP 263
Cdd:PLN02590  448 PSFEVVTT--RYFSLVCFRLAP 467
PRK02769 PRK02769
histidine decarboxylase; Provisional
 1-242 4.76e-23

histidine decarboxylase; Provisional


Pssm-ID: 235068 [Multi-domain]  Cd Length: 380  Bit Score: 98.19  E-value: 4.76e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370477219   1 MYSIMAARyKYFPEVktkgmaavpklVLFTSEQSHYSIKKAGAALGFgTDNVILIKCNerGKIIPADFEAKILEAKQKGY 80
Cdd:PRK02769   98 LYGCYLAR-ELFPDG-----------TLYYSKDTHYSVSKIARLLRI-KSRVITSLPN--GEIDYDDLISKIKENKNQPP 162

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370477219  81 VpfyVNATAGTTVYGAFDPIQEIADICEKYNL---WLHVDAAWGGGLLMSRKHRHKLNGIERANSVTWNPHKMMGVLLQC 157
Cdd:PRK02769  163 I---IFANIGTTMTGAIDNIKEIQEILKKIGIddyYIHADAALSGMILPFVNNPPPFSFADGIDSIAISGHKFIGSPMPC 239

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370477219 158 SAILVKEKGIlqgcnqmcagylfqpDKQY-DVSY-DTGDKAIQCGR--HVDIfkfwLMWKA---KGTVGFENQINKCLEL 230
Cdd:PRK02769  240 GIVLAKKKYV---------------ERISvDVDYiGSRDQTISGSRngHTAL----LLWAAirsLGSKGLRQRVQHCLDM 300

                         250
                  ....*....|..
gi 1370477219 231 AEYLYAKIKNRE 242
Cdd:PRK02769  301 AQYAVDRLQANG 312
PLN02263 PLN02263
serine decarboxylase
 24-240 4.84e-13

serine decarboxylase


Pssm-ID: 177904 [Multi-domain]  Cd Length: 470  Bit Score: 69.46  E-value: 4.84e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370477219  24 PKLVLFTSEQSHYSIKKAGAALGFGtdnVILIKCNERGKIIPADFEAKILEAKQKgyvPFYVNATAGTTVYGAFDPIQEI 103
Cdd:PLN02263  177 PDGILYASRESHYSVFKAARMYRME---CVKVDTLVSGEIDCADFKAKLLANKDK---PAIINVNIGTTVKGAVDDLDLV 250

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370477219 104 ADICEKY-----NLWLHVDAAWGGGLLMSRKHRHKLNGIERANSVTWNPHKMMGVLLQCSAILVKEKGIlqgcNQMCAgy 178
Cdd:PLN02263  251 IKTLEECgfsqdRFYIHCDGALFGLMMPFVKRAPKVTFKKPIGSVSVSGHKFVGCPMPCGVQITRMEHI----NVLSS-- 324

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1370477219 179 lfqpdkqyDVSY-DTGDKAIQCGR--HVDIFkFWLMWKAKGTVGFENQINKCLELAEYLYAKIKN 240
Cdd:PLN02263  325 --------NVEYlASRDATIMGSRngHAPIF-LWYTLNRKGYRGFQKEVQKCLRNAHYLKDRLRE 380
PLN03032 PLN03032
serine decarboxylase; Provisional
 24-239 7.05e-12

serine decarboxylase; Provisional


Pssm-ID: 166673 [Multi-domain]  Cd Length: 374  Bit Score: 65.62  E-value: 7.05e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370477219  24 PKLVLFTSEQSHYSIKKAGAALGFGTDNVILIkcnERGKIIPADFEAKILEAKQKgyvPFYVNATAGTTVYGAFDPIQEI 103
Cdd:PLN03032  110 PDGILYASRESHYSVFKAARMYRMEAVKVPTL---PSGEIDYDDLERALAKNRDK---PAILNVNIGTTVKGAVDDLDRI 183

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370477219 104 ADICEKYN-----LWLHVDAAWGGGLLMSRKHRHKLNGIERANSVTWNPHKMMGVLLQCSAILVKEKGILQgcnqmcagy 178
Cdd:PLN03032  184 LRILKELGytedrFYIHCDGALFGLMMPFVSRAPEVTFRKPIGSVSVSGHKFLGCPMPCGVALTRKKHVKA--------- 254

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1370477219 179 lFQPDKQYDVSYDTGDKAIQCGrHVDIFkFWLMWKAKGTVGFENQINKCLELAEYLYAKIK 239
Cdd:PLN03032  255 -LSQNVEYLNSRDATIMGSRNG-HAPLY-LWYTLRRKGYRGIKRDVQHCMRNAHYLKDRLT 312
AAT_I cd01494
Aspartate aminotransferase (AAT) superfamily (fold type I) of pyridoxal phosphate (PLP) ...
 24-163 1.25e-09

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: 56.62  E-value: 1.25e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370477219  24 PKLVLFTSEQSHYSIKKAGAALGFGTDNVILIKCNERGKIipadfEAKILEAKQKGYVPFYVNATAGTTVYGAFDPIQEI 103
Cdd:cd01494    40 PGDEVIVDANGHGSRYWVAAELAGAKPVPVPVDDAGYGGL-----DVAILEELKAKPNVALIVITPNTTSGGVLVPLKEI 114

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370477219 104 ADICEKYNLWLHVDAAWGGGLLMSRKHrhkLNGIERANSVTWNPHKMMGVlLQCSAILVK 163
Cdd:cd01494   115 RKIAKEYGILLLVDAASAGGASPAPGV---LIPEGGADVVTFSLHKNLGG-EGGGVVIVK 170
Orn_deC_like cd00615
Ornithine decarboxylase family. This family belongs to pyridoxal phosphate (PLP)-dependent ...
 92-164 1.11e-06

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: 49.55  E-value: 1.11e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1370477219  92 TVYGAFDPIQEIADICEKYNLWLHVDAAWGGGLLMS---RKHRHKLNGIERANSVtwnpHKMMGVLLQCSAILVKE 164
Cdd:cd00615   164 TYYGICYNLRKIVEEAHHRGLPVLVDEAHGAHFRFHpilPSSAAMAGADIVVQST----HKTLPALTQGSMIHVKG 235
Aminotran_5 pfam00266
Aminotransferase class-V; This domain is found in amino transferases, and other enzymes ...
 30-258 2.21e-06

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: 48.78  E-value: 2.21e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370477219  30 TSEQSHYSIKKAGAALG-FGTDNVILIKCNERGKIIPADFEAKILEaKQKgyvpfYVNATAGTTVYGAFDPIQEIADICE 108
Cdd:pfam00266  93 ITEMEHHANLVPWQELAkRTGARVRVLPLDEDGLLDLDELEKLITP-KTK-----LVAITHVSNVTGTIQPVPEIGKLAH 166

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370477219 109 KYNLWLHVDAAWGGGllmsrkHRH----KLNgierANSVTWNPHKMM-----GVLLQCSAILVKEKGILQGcnqmcAGYL 179
Cdd:pfam00266 167 QYGALVLVDAAQAIG------HRPidvqKLG----VDFLAFSGHKLYgptgiGVLYGRRDLLEKMPPLLGG-----GGMI 231

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370477219 180 FQPDKQYDVSYDTGDK----------AIQCGRHVDifkfWLMwkakgTVGFENQINKCLELAEYLYAKIKNREEFEmvFN 249
Cdd:pfam00266 232 ETVSLQESTFADAPWKfeagtpniagIIGLGAALE----YLS-----EIGLEAIEKHEHELAQYLYERLLSLPGIR--LY 300


                  ....*....
gi 1370477219 250 GEPEHTNVC 258
Cdd:pfam00266 301 GPERRASII 309
LdcC COG1982
Arginine/lysine/ornithine decarboxylase [Amino acid transport and metabolism];
92-167 5.48e-04

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


Pssm-ID: 441585 [Multi-domain]  Cd Length: 486  Bit Score: 41.64  E-value: 5.48e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370477219  92 TVYGAFDPIQEIADICEKYNLWLHVDAAWGG---------------GLLMSrkhrhklngierANSVtwnpHKMMGVLLQ 156
Cdd:COG1982   171 TYYGVCYDLKAIAELAHEHGIPVLVDEAHGAhfgfhpdlprsameaGADLV------------VQST----HKTLGALTQ 234

                          90
                  ....*....|.
gi 1370477219 157 CSAILVKEKGI 167
Cdd:COG1982   235 SSMLHVKGGRV 245
Beta_elim_lyase pfam01212
Beta-eliminating lyase;
31-119 2.36e-03

Beta-eliminating lyase;


Pssm-ID: 426128 [Multi-domain]  Cd Length: 288  Bit Score: 39.12  E-value: 2.36e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370477219  31 SEQSHYSIKKAGAALGFGTDNVILIKCNERGKIIPADFEAKILEAKQKGYVPFYV------NATAGTTVYgAFDPIQEIA 104
Cdd:pfam01212  77 GEPAHIHFDETGGHAELGGVQPRPLDGDEAGNMDLEDLEAAIREVGADIFPPTGLislentHNSAGGQVV-SLENLREIA 155

                          90
                  ....*....|....*
gi 1370477219 105 DICEKYNLWLHVDAA 119
Cdd:pfam01212 156 ALAREHGIPVHLDGA 170
TA_like cd06502
Low-specificity threonine aldolase (TA). This family belongs to pyridoxal phosphate (PLP) ...
 29-119 2.63e-03

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: 39.24  E-value: 2.63e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370477219  29 FTSEQSHYSIKKAGAALGFGTDNVILIKcNERGKIIPADFEAKILEAKQKGYVPFYV----NATAGTTVYgafdPIQEIA 104
Cdd:cd06502    75 ICHETAHIYTDEAGAPEFLSGVKLLPVP-GENGKLTPEDLEAAIRPRDDIHFPPPSLvsleNTTEGGTVY----PLDELK 149

                          90
                  ....*....|....*...
gi 1370477219 105 DICE---KYNLWLHVDAA 119
Cdd:cd06502   150 AISAlakENGLPLHLDGA 167
KBL_like cd06454
KBL_like; this family belongs to the pyridoxal phosphate (PLP)-dependent aspartate ...
 65-125 3.51e-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: 38.70  E-value: 3.51e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1370477219  65 PADFEAKILEAKQKgYVPFYVnATAGttVY---GAFDPIQEIADICEKYNLWLHVDAAWGGGLL 125
Cdd:cd06454   117 MEDLEKLLREARRP-YGKKLI-VTEG--VYsmdGDIAPLPELVDLAKKYGAILFVDEAHSVGVY 176
NifS COG1104
Cysteine desulfurase/Cysteine sulfinate desulfinase IscS or related enzyme, NifS family [Amino ...
 99-119 4.73e-03

Cysteine desulfurase/Cysteine sulfinate desulfinase IscS or related enzyme, NifS family [Amino acid transport and metabolism];


Pssm-ID: 440721 [Multi-domain]  Cd Length: 381  Bit Score: 38.49  E-value: 4.73e-03
                          10        20
                  ....*....|....*....|.
gi 1370477219  99 PIQEIADICEKYNLWLHVDAA 119
Cdd:COG1104   158 PIAEIAEIAKEHGVLFHTDAV 178
 
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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