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Conserved domains on  [gi|1720384328|ref|XP_030104445|]
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cysteine sulfinic acid decarboxylase isoform X3 [Mus musculus]

Protein Classification

pyridoxal phosphate-dependent decarboxylase family protein( domain architecture ID 10000562)

pyridoxal phosphate-dependent decarboxylase family protein is primarily involved in the biosynthesis of amino acids and amino acid-derived metabolites, but it is also found in the biosynthetic pathways of amino sugars and in the synthesis or catabolism of neurotransmitters

CATH:  3.40.640.10
EC:  4.1.1.-
Gene Ontology:  GO:0016830|GO:0030170|GO:0019752
PubMed:  8690703|7748903
SCOP:  4003328

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
GadA COG0076
Glutamate or tyrosine decarboxylase or a related PLP-dependent protein [Amino acid transport ...
48-389 7.48e-117

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: 349.13  E-value: 7.48e-117
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720384328  48 EPEELKQLLDLELQSQGESREQILER-CRTVIHYSVKTGHPRFFNQLFSGLDPHALAGRIITESLNTSQYTYEIAPVFVL 126
Cdd:COG0076    28 SPEELRAALDEPLPEEGLPPEEALAElEDLVLPGSVDWNHPRFLAFVTGGTTPAALAADLLASALNQNMGDWDTSPAATE 107
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720384328 127 MEEEVLKKLRALVGW-NSGDGVFCPGGSISNMYAMNLARFQRYP-DCKQRGLRALPPLALFTSKECHYSITKGAAFLGLG 204
Cdd:COG0076   108 LEREVVRWLADLLGLpEGAGGVFTSGGTEANLLALLAARDRALArRVRAEGLPGAPRPRIVVSEEAHSSVDKAARLLGLG 187
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720384328 205 TDSVRVVKADERGRMIPEDLERQIILAEAEGSVPFLVSATSGTTVLGAFDPLDAIADVCQRHGLWFHVDAAWGGSVLLSR 284
Cdd:COG0076   188 RDALRKVPVDEDGRMDPDALEAAIDEDRAAGLNPIAVVATAGTTNTGAIDPLAEIADIAREHGLWLHVDAAYGGFALPSP 267
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720384328 285 THRHLLDGIQRADSVAWNPHKLLAAGLQCSALLLRDTSnLLKRCHGSQASYLFQQDkfyDVALDTGDKVVQCGRRVDCLK 364
Cdd:COG0076   268 ELRHLLDGIERADSITVDPHKWLYVPYGCGAVLVRDPE-LLREAFSFHASYLGPAD---DGVPNLGDYTLELSRRFRALK 343
                         330       340
                  ....*....|....*....|....*
gi 1720384328 365 LWLMWKAQGGQGLERRIDQAFALTR 389
Cdd:COG0076   344 LWATLRALGREGYRELIERCIDLAR 368
 
Name Accession Description Interval E-value
GadA COG0076
Glutamate or tyrosine decarboxylase or a related PLP-dependent protein [Amino acid transport ...
48-389 7.48e-117

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: 349.13  E-value: 7.48e-117
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720384328  48 EPEELKQLLDLELQSQGESREQILER-CRTVIHYSVKTGHPRFFNQLFSGLDPHALAGRIITESLNTSQYTYEIAPVFVL 126
Cdd:COG0076    28 SPEELRAALDEPLPEEGLPPEEALAElEDLVLPGSVDWNHPRFLAFVTGGTTPAALAADLLASALNQNMGDWDTSPAATE 107
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720384328 127 MEEEVLKKLRALVGW-NSGDGVFCPGGSISNMYAMNLARFQRYP-DCKQRGLRALPPLALFTSKECHYSITKGAAFLGLG 204
Cdd:COG0076   108 LEREVVRWLADLLGLpEGAGGVFTSGGTEANLLALLAARDRALArRVRAEGLPGAPRPRIVVSEEAHSSVDKAARLLGLG 187
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720384328 205 TDSVRVVKADERGRMIPEDLERQIILAEAEGSVPFLVSATSGTTVLGAFDPLDAIADVCQRHGLWFHVDAAWGGSVLLSR 284
Cdd:COG0076   188 RDALRKVPVDEDGRMDPDALEAAIDEDRAAGLNPIAVVATAGTTNTGAIDPLAEIADIAREHGLWLHVDAAYGGFALPSP 267
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720384328 285 THRHLLDGIQRADSVAWNPHKLLAAGLQCSALLLRDTSnLLKRCHGSQASYLFQQDkfyDVALDTGDKVVQCGRRVDCLK 364
Cdd:COG0076   268 ELRHLLDGIERADSITVDPHKWLYVPYGCGAVLVRDPE-LLREAFSFHASYLGPAD---DGVPNLGDYTLELSRRFRALK 343
                         330       340
                  ....*....|....*....|....*
gi 1720384328 365 LWLMWKAQGGQGLERRIDQAFALTR 389
Cdd:COG0076   344 LWATLRALGREGYRELIERCIDLAR 368
Pyridoxal_deC pfam00282
Pyridoxal-dependent decarboxylase conserved domain;
49-382 3.48e-111

Pyridoxal-dependent decarboxylase conserved domain;


Pssm-ID: 395219  Cd Length: 373  Bit Score: 331.69  E-value: 3.48e-111
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720384328  49 PEELKQLLDLELQSQGESREQILERCRTVIHYSVKTGH-PRFFNQLFSGLDPHALAGRIITESLNTSQYTYEIAPVFVLM 127
Cdd:pfam00282   1 PGYLKPLLPLAAPIIPEPELQIDGDIRRNLMPGVTTWHsPHFHAYMPTGNSYPSLLGDMLTDAINCNGFTWESSPACTEL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720384328 128 EEEVLKKLRALVGW------NSGDGVFCPGGSISNMYAMNLARFQRYPDCKQRGLRALPP-----LALFTSKECHYSITK 196
Cdd:pfam00282  81 ENVVMNWLGEMLGLpaeflgQEGGGVLQPGSSESNLLALLAARTKWIKRMKAAGKPADSSgilakLVAYTSDQAHSSIEK 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720384328 197 GAAFLGLGtdsVRVVKADERGRMIPEDLERQIILAEAEGSVPFLVSATSGTTVLGAFDPLDAIADVCQRHGLWFHVDAAW 276
Cdd:pfam00282 161 AALYGGVK---LREIPSDDNGKMRGMDLEKAIEEDKENGLIPFFVVATLGTTGSGAFDDLQELGDICAKHNLWLHVDAAY 237
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720384328 277 GGSVLLSRTHRHLLDGIQRADSVAWNPHKLLAAGLQCSALLLRDtSNLLKRCHGSQASYLFQQDKFYdvalDTGDKVVQC 356
Cdd:pfam00282 238 GGSAFICPEFRHWLFGIERADSITFNPHKWMLVLLDCSAVWVKD-KEALQQAFQFNPLYLGHTDSAY----DTGHKQIPL 312
                         330       340
                  ....*....|....*....|....*.
gi 1720384328 357 GRRVDCLKLWLMWKAQGGQGLERRID 382
Cdd:pfam00282 313 SRRFRILKLWFVIRSLGVEGLQNQIR 338
DOPA_deC_like cd06450
DOPA decarboxylase family. This family belongs to pyridoxal phosphate (PLP)-dependent ...
89-389 3.17e-101

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: 304.90  E-value: 3.17e-101
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720384328  89 FFNQLFSGLDPHALAGRIITESLNTSQYTYEIAPVFVLMEEEVLKKLRALVGWNS--GDGVFCPGGSISNMYAMNLARFQ 166
Cdd:cd06450     1 FLAGFVTTMDPPALLLEMLTSAKNAIDFTWDESPAATEMEAEVVNWLAKLFGLPSedADGVFTSGGSESNLLALLAARDR 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720384328 167 RYPDCKQRGLRALPPLALFTSKECHYSITKGAAFLGlgtDSVRVVKADERGRMIPEDLERQIILAEAEGSVPFLVSATSG 246
Cdd:cd06450    81 ARKRLKAGGGRGIDKLVIVCSDQAHVSVEKAAAYLD---VKVRLVPVDEDGRMDPEALEAAIDEDKAEGLNPIMVVATAG 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720384328 247 TTVLGAFDPLDAIADVCQRHGLWFHVDAAWGGSVLLSRTHRHLLDGIQRADSVAWNPHKLLAAGLQCSALLLRdtsnllk 326
Cdd:cd06450   158 TTDTGAIDPLEEIADLAEKYDLWLHVDAAYGGFLLPFPEPRHLDFGIERVDSISVDPHKYGLVPLGCSAVLVR------- 230
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1720384328 327 rchgsqasylfqqdkfydvaldtgdkvvqcgrrvdCLKLWLMWKAQGGQGLERRIDQAFALTR 389
Cdd:cd06450   231 -----------------------------------ALKLWATLRRFGRDGYGEHIDRIVDLAK 258
NOD_PanD_pyr TIGR03799
putative pyridoxal-dependent aspartate 1-decarboxylase; This enzyme is proposed here to be a ...
76-311 3.72e-44

putative pyridoxal-dependent aspartate 1-decarboxylase; This enzyme is proposed here to be a form of aspartate 1-decarboxylase, pyridoxal-dependent, that represents a non-orthologous displacement to the more widely distributed pyruvoyl-dependent form (TIGR00223). Aspartate 1-decarboxylase makes beta-alanine, used usually in pathothenate biosynthesis, by decarboxylation from asparatate. A number of species with the PanB and PanC enzymes, however, lack PanD. This protein family occurs in a number of Proteobacteria that lack PanD. This enzyme family appears to be a pyridoxal-dependent enzyme (see pfam00282). The family was identified by Partial Phylogenetic Profiling; members in Geobacter sulfurreducens, G. metallireducens, and Pseudoalteromonas atlantica are clustered with the genes for PanB and PanC. We suggest the gene symbol panP (panthothenate biosynthesis enzyme, Pyridoxal-dependent). [Biosynthesis of cofactors, prosthetic groups, and carriers, Pantothenate and coenzyme A]


Pssm-ID: 274791  Cd Length: 522  Bit Score: 161.06  E-value: 3.72e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720384328  76 TVIHYSVKTGHPRFFNQLFSGLDPHALAGRIITESLNTSQYTYEIAPVFVLMEEEVLKKLRALV---------GW-NSGD 145
Cdd:TIGR03799  79 KLVAHSVHTASPSFIGHMTSALPYFLLPLSKLMVGLNQNLVKIETSKAFTPLERQVLGMMHHLVyqqddsfyrRWmHSAD 158
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720384328 146 ---GVFCPGGSISNMYAMNLARFQRY-PDCKQRGL------RAL-----PPLALFTSKECHYSITKGAAFLGLGTDSVRV 210
Cdd:TIGR03799 159 hslGAFCSGGTVANITALWVARNRLLkADGDFRGIareglfAALrhygyDGLAILVSERGHYSLGKAADVLGIGRDNLVP 238
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720384328 211 VKADERGRMIPEDLERQIILAEAEGSVPFLVSATSGTTVLGAFDPLDAIADVCQRHGLWFHVDAAWGGSVLLSRTHRHLL 290
Cdd:TIGR03799 239 VKTDENNRIRVDALRDKCLELAAQNIKPMAIVGVAGTTETGNIDPLDEMADIAQEAGCHFHVDAAWGGATLLSNTYRHLL 318
                         250       260
                  ....*....|....*....|....*
gi 1720384328 291 DGIQRADSVAWNPHKLL----AAGL 311
Cdd:TIGR03799 319 KGIERADSVTIDAHKQMyvpmGAGM 343
PLN02590 PLN02590
probable tyrosine decarboxylase
48-381 5.56e-34

probable tyrosine decarboxylase


Pssm-ID: 178200 [Multi-domain]  Cd Length: 539  Bit Score: 133.30  E-value: 5.56e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720384328  48 EPEELKQLLDlelqsqgESREQILErcrTVIHYSvktgHPRFFNQLFSGLDPHALAGRIITESLNTSQYTYEIAPVFVLM 127
Cdd:PLN02590  106 RPESLKELLD-------DVSKKIMP---GITHWQ----SPSYFAYYASSTSVAGFLGEMLNAGLSVVGFTWLTSPAATEL 171
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720384328 128 EEEVLKKLRALV-------GWNSGDGVFcPGGSISNMYAMNLARFQRYpdCKQRGLRALPPLALFTSKECHYSITKGAAF 200
Cdd:PLN02590  172 EIIVLDWLAKLLqlpdhflSTGNGGGVI-QGTGCEAVLVVVLAARDRI--LKKVGKTLLPQLVVYGSDQTHSSFRKACLI 248
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720384328 201 LGLGTDSVRVVKADERGR--MIPEDLERQIILAEAEGSVPFLVSATSGTTVLGAFDPLDAIADVCQRHGLWFHVDAAWGG 278
Cdd:PLN02590  249 GGIHEENIRLLKTDSSTNygMPPESLEEAISHDLAKGFIPFFICATVGTTSSAAVDPLVPLGNIAKKYGIWLHVDAAYAG 328
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720384328 279 SVLLSRTHRHLLDGIQRADSVAWNPHKLLAAGLQCSALLLRDTSNLLKRCHGSQASYLFQQDKfYDVALDTGDKVVQCGR 358
Cdd:PLN02590  329 NACICPEYRKFIDGIENADSFNMNAHKWLFANQTCSPLWVKDRYSLIDALKTNPEYLEFKVSK-KDTVVNYKDWQISLSR 407
                         330       340
                  ....*....|....*....|...
gi 1720384328 359 RVDCLKLWLMWKAQGGQGLERRI 381
Cdd:PLN02590  408 RFRSLKLWMVLRLYGSENLRNFI 430
 
Name Accession Description Interval E-value
GadA COG0076
Glutamate or tyrosine decarboxylase or a related PLP-dependent protein [Amino acid transport ...
48-389 7.48e-117

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: 349.13  E-value: 7.48e-117
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720384328  48 EPEELKQLLDLELQSQGESREQILER-CRTVIHYSVKTGHPRFFNQLFSGLDPHALAGRIITESLNTSQYTYEIAPVFVL 126
Cdd:COG0076    28 SPEELRAALDEPLPEEGLPPEEALAElEDLVLPGSVDWNHPRFLAFVTGGTTPAALAADLLASALNQNMGDWDTSPAATE 107
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720384328 127 MEEEVLKKLRALVGW-NSGDGVFCPGGSISNMYAMNLARFQRYP-DCKQRGLRALPPLALFTSKECHYSITKGAAFLGLG 204
Cdd:COG0076   108 LEREVVRWLADLLGLpEGAGGVFTSGGTEANLLALLAARDRALArRVRAEGLPGAPRPRIVVSEEAHSSVDKAARLLGLG 187
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720384328 205 TDSVRVVKADERGRMIPEDLERQIILAEAEGSVPFLVSATSGTTVLGAFDPLDAIADVCQRHGLWFHVDAAWGGSVLLSR 284
Cdd:COG0076   188 RDALRKVPVDEDGRMDPDALEAAIDEDRAAGLNPIAVVATAGTTNTGAIDPLAEIADIAREHGLWLHVDAAYGGFALPSP 267
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720384328 285 THRHLLDGIQRADSVAWNPHKLLAAGLQCSALLLRDTSnLLKRCHGSQASYLFQQDkfyDVALDTGDKVVQCGRRVDCLK 364
Cdd:COG0076   268 ELRHLLDGIERADSITVDPHKWLYVPYGCGAVLVRDPE-LLREAFSFHASYLGPAD---DGVPNLGDYTLELSRRFRALK 343
                         330       340
                  ....*....|....*....|....*
gi 1720384328 365 LWLMWKAQGGQGLERRIDQAFALTR 389
Cdd:COG0076   344 LWATLRALGREGYRELIERCIDLAR 368
Pyridoxal_deC pfam00282
Pyridoxal-dependent decarboxylase conserved domain;
49-382 3.48e-111

Pyridoxal-dependent decarboxylase conserved domain;


Pssm-ID: 395219  Cd Length: 373  Bit Score: 331.69  E-value: 3.48e-111
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720384328  49 PEELKQLLDLELQSQGESREQILERCRTVIHYSVKTGH-PRFFNQLFSGLDPHALAGRIITESLNTSQYTYEIAPVFVLM 127
Cdd:pfam00282   1 PGYLKPLLPLAAPIIPEPELQIDGDIRRNLMPGVTTWHsPHFHAYMPTGNSYPSLLGDMLTDAINCNGFTWESSPACTEL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720384328 128 EEEVLKKLRALVGW------NSGDGVFCPGGSISNMYAMNLARFQRYPDCKQRGLRALPP-----LALFTSKECHYSITK 196
Cdd:pfam00282  81 ENVVMNWLGEMLGLpaeflgQEGGGVLQPGSSESNLLALLAARTKWIKRMKAAGKPADSSgilakLVAYTSDQAHSSIEK 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720384328 197 GAAFLGLGtdsVRVVKADERGRMIPEDLERQIILAEAEGSVPFLVSATSGTTVLGAFDPLDAIADVCQRHGLWFHVDAAW 276
Cdd:pfam00282 161 AALYGGVK---LREIPSDDNGKMRGMDLEKAIEEDKENGLIPFFVVATLGTTGSGAFDDLQELGDICAKHNLWLHVDAAY 237
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720384328 277 GGSVLLSRTHRHLLDGIQRADSVAWNPHKLLAAGLQCSALLLRDtSNLLKRCHGSQASYLFQQDKFYdvalDTGDKVVQC 356
Cdd:pfam00282 238 GGSAFICPEFRHWLFGIERADSITFNPHKWMLVLLDCSAVWVKD-KEALQQAFQFNPLYLGHTDSAY----DTGHKQIPL 312
                         330       340
                  ....*....|....*....|....*.
gi 1720384328 357 GRRVDCLKLWLMWKAQGGQGLERRID 382
Cdd:pfam00282 313 SRRFRILKLWFVIRSLGVEGLQNQIR 338
DOPA_deC_like cd06450
DOPA decarboxylase family. This family belongs to pyridoxal phosphate (PLP)-dependent ...
89-389 3.17e-101

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: 304.90  E-value: 3.17e-101
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720384328  89 FFNQLFSGLDPHALAGRIITESLNTSQYTYEIAPVFVLMEEEVLKKLRALVGWNS--GDGVFCPGGSISNMYAMNLARFQ 166
Cdd:cd06450     1 FLAGFVTTMDPPALLLEMLTSAKNAIDFTWDESPAATEMEAEVVNWLAKLFGLPSedADGVFTSGGSESNLLALLAARDR 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720384328 167 RYPDCKQRGLRALPPLALFTSKECHYSITKGAAFLGlgtDSVRVVKADERGRMIPEDLERQIILAEAEGSVPFLVSATSG 246
Cdd:cd06450    81 ARKRLKAGGGRGIDKLVIVCSDQAHVSVEKAAAYLD---VKVRLVPVDEDGRMDPEALEAAIDEDKAEGLNPIMVVATAG 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720384328 247 TTVLGAFDPLDAIADVCQRHGLWFHVDAAWGGSVLLSRTHRHLLDGIQRADSVAWNPHKLLAAGLQCSALLLRdtsnllk 326
Cdd:cd06450   158 TTDTGAIDPLEEIADLAEKYDLWLHVDAAYGGFLLPFPEPRHLDFGIERVDSISVDPHKYGLVPLGCSAVLVR------- 230
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1720384328 327 rchgsqasylfqqdkfydvaldtgdkvvqcgrrvdCLKLWLMWKAQGGQGLERRIDQAFALTR 389
Cdd:cd06450   231 -----------------------------------ALKLWATLRRFGRDGYGEHIDRIVDLAK 258
NOD_PanD_pyr TIGR03799
putative pyridoxal-dependent aspartate 1-decarboxylase; This enzyme is proposed here to be a ...
76-311 3.72e-44

putative pyridoxal-dependent aspartate 1-decarboxylase; This enzyme is proposed here to be a form of aspartate 1-decarboxylase, pyridoxal-dependent, that represents a non-orthologous displacement to the more widely distributed pyruvoyl-dependent form (TIGR00223). Aspartate 1-decarboxylase makes beta-alanine, used usually in pathothenate biosynthesis, by decarboxylation from asparatate. A number of species with the PanB and PanC enzymes, however, lack PanD. This protein family occurs in a number of Proteobacteria that lack PanD. This enzyme family appears to be a pyridoxal-dependent enzyme (see pfam00282). The family was identified by Partial Phylogenetic Profiling; members in Geobacter sulfurreducens, G. metallireducens, and Pseudoalteromonas atlantica are clustered with the genes for PanB and PanC. We suggest the gene symbol panP (panthothenate biosynthesis enzyme, Pyridoxal-dependent). [Biosynthesis of cofactors, prosthetic groups, and carriers, Pantothenate and coenzyme A]


Pssm-ID: 274791  Cd Length: 522  Bit Score: 161.06  E-value: 3.72e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720384328  76 TVIHYSVKTGHPRFFNQLFSGLDPHALAGRIITESLNTSQYTYEIAPVFVLMEEEVLKKLRALV---------GW-NSGD 145
Cdd:TIGR03799  79 KLVAHSVHTASPSFIGHMTSALPYFLLPLSKLMVGLNQNLVKIETSKAFTPLERQVLGMMHHLVyqqddsfyrRWmHSAD 158
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720384328 146 ---GVFCPGGSISNMYAMNLARFQRY-PDCKQRGL------RAL-----PPLALFTSKECHYSITKGAAFLGLGTDSVRV 210
Cdd:TIGR03799 159 hslGAFCSGGTVANITALWVARNRLLkADGDFRGIareglfAALrhygyDGLAILVSERGHYSLGKAADVLGIGRDNLVP 238
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720384328 211 VKADERGRMIPEDLERQIILAEAEGSVPFLVSATSGTTVLGAFDPLDAIADVCQRHGLWFHVDAAWGGSVLLSRTHRHLL 290
Cdd:TIGR03799 239 VKTDENNRIRVDALRDKCLELAAQNIKPMAIVGVAGTTETGNIDPLDEMADIAQEAGCHFHVDAAWGGATLLSNTYRHLL 318
                         250       260
                  ....*....|....*....|....*
gi 1720384328 291 DGIQRADSVAWNPHKLL----AAGL 311
Cdd:TIGR03799 319 KGIERADSVTIDAHKQMyvpmGAGM 343
PLN02590 PLN02590
probable tyrosine decarboxylase
48-381 5.56e-34

probable tyrosine decarboxylase


Pssm-ID: 178200 [Multi-domain]  Cd Length: 539  Bit Score: 133.30  E-value: 5.56e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720384328  48 EPEELKQLLDlelqsqgESREQILErcrTVIHYSvktgHPRFFNQLFSGLDPHALAGRIITESLNTSQYTYEIAPVFVLM 127
Cdd:PLN02590  106 RPESLKELLD-------DVSKKIMP---GITHWQ----SPSYFAYYASSTSVAGFLGEMLNAGLSVVGFTWLTSPAATEL 171
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720384328 128 EEEVLKKLRALV-------GWNSGDGVFcPGGSISNMYAMNLARFQRYpdCKQRGLRALPPLALFTSKECHYSITKGAAF 200
Cdd:PLN02590  172 EIIVLDWLAKLLqlpdhflSTGNGGGVI-QGTGCEAVLVVVLAARDRI--LKKVGKTLLPQLVVYGSDQTHSSFRKACLI 248
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720384328 201 LGLGTDSVRVVKADERGR--MIPEDLERQIILAEAEGSVPFLVSATSGTTVLGAFDPLDAIADVCQRHGLWFHVDAAWGG 278
Cdd:PLN02590  249 GGIHEENIRLLKTDSSTNygMPPESLEEAISHDLAKGFIPFFICATVGTTSSAAVDPLVPLGNIAKKYGIWLHVDAAYAG 328
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720384328 279 SVLLSRTHRHLLDGIQRADSVAWNPHKLLAAGLQCSALLLRDTSNLLKRCHGSQASYLFQQDKfYDVALDTGDKVVQCGR 358
Cdd:PLN02590  329 NACICPEYRKFIDGIENADSFNMNAHKWLFANQTCSPLWVKDRYSLIDALKTNPEYLEFKVSK-KDTVVNYKDWQISLSR 407
                         330       340
                  ....*....|....*....|...
gi 1720384328 359 RVDCLKLWLMWKAQGGQGLERRI 381
Cdd:PLN02590  408 RFRSLKLWMVLRLYGSENLRNFI 430
PLN02880 PLN02880
tyrosine decarboxylase
48-381 3.51e-32

tyrosine decarboxylase


Pssm-ID: 215475 [Multi-domain]  Cd Length: 490  Bit Score: 127.33  E-value: 3.51e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720384328  48 EPEELKQLLDLELQSQGESREQILERCRT-----VIHYSvktgHPRFFNQLFSGLDPHALAGRIITESLNTSQYTYEIAP 122
Cdd:PLN02880   43 QPGYLRELLPDSAPNQPETLDQVLDDVQAkilpgVTHWQ----SPNYFAYYPSNSSVAGFLGEMLSAGLNIVGFSWITSP 118
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720384328 123 VFVLMEEEVLKKLRALVGWNS-------GDGVFCPGGSISNMYAMNLARFQRYpdcKQRGLRALPPLALFTSKECHYSIT 195
Cdd:PLN02880  119 AATELEMIVLDWLAKLLNLPEqflstgnGGGVIQGTASEAVLVVLLAARDRVL---RKVGKNALEKLVVYASDQTHSALQ 195
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720384328 196 KGAAFLGLGTDSVRVVKADERGR--MIPEDLERQIILAEAEGSVPFLVSATSGTTVLGAFDPLDAIADVCQRHGLWFHVD 273
Cdd:PLN02880  196 KACQIAGIHPENCRLLKTDSSTNyaLAPELLSEAISTDLSSGLIPFFLCATVGTTSSTAVDPLLELGKIAKSNGMWFHVD 275
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720384328 274 AAWGGSVLLSRTHRHLLDGIQRADSVAWNPHKLLAAGLQCSALLLRDTSNLLKRChGSQASYLFQQDKFYDVALDTGDKV 353
Cdd:PLN02880  276 AAYAGSACICPEYRHYIDGVEEADSFNMNAHKWFLTNFDCSLLWVKDRNALIQSL-STNPEFLKNKASQANSVVDYKDWQ 354
                         330       340
                  ....*....|....*....|....*...
gi 1720384328 354 VQCGRRVDCLKLWLMWKAQGGQGLERRI 381
Cdd:PLN02880  355 IPLGRRFRSLKLWMVLRLYGVENLQSYI 382
PRK02769 PRK02769
histidine decarboxylase; Provisional
68-319 4.41e-15

histidine decarboxylase; Provisional


Pssm-ID: 235068 [Multi-domain]  Cd Length: 380  Bit Score: 76.23  E-value: 4.41e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720384328  68 EQILERCRtvIHYSVKTGHPrfFNQLFSgldpHALAGRIITESLNTSQYTYEiAPVFVL----MEEEVLKKLRALVG--W 141
Cdd:PRK02769   12 EDFWLYLR--HNQYFNVGYP--EAADFD----YSALKRFFSFSINNCGDPYS-KSNYPLnsfdFERDVMNFFAELFKipF 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720384328 142 NSGDGVFCPGGSISNMYAMNLARfQRYPDCkqrglralpplALFTSKECHYSITKGAAFLGLGTdsvRVVKADERGRMIP 221
Cdd:PRK02769   83 NESWGYITNGGTEGNLYGCYLAR-ELFPDG-----------TLYYSKDTHYSVSKIARLLRIKS---RVITSLPNGEIDY 147
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720384328 222 EDLERQIilaEAEGSVPFLVSATSGTTVLGAFDPLDAIADVCQRHGL---WFHVDAAWGGSVLLSRTHRHLLDGIQRADS 298
Cdd:PRK02769  148 DDLISKI---KENKNQPPIIFANIGTTMTGAIDNIKEIQEILKKIGIddyYIHADAALSGMILPFVNNPPPFSFADGIDS 224
                         250       260
                  ....*....|....*....|.
gi 1720384328 299 VAWNPHKLLAAGLQCSALLLR 319
Cdd:PRK02769  225 IAISGHKFIGSPMPCGIVLAK 245
AAT_I cd01494
Aspartate aminotransferase (AAT) superfamily (fold type I) of pyridoxal phosphate (PLP) ...
128-309 1.58e-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: 59.70  E-value: 1.58e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720384328 128 EEEVLKKLRALVGWNSGDGVFCPGGSISN-MYAMNLArfqrypdckQRGLRALPPLALFTSkecHYSITKGAAFLGlgtd 206
Cdd:cd01494     2 LEELEEKLARLLQPGNDKAVFVPSGTGANeAALLALL---------GPGDEVIVDANGHGS---RYWVAAELAGAK---- 65
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720384328 207 sVRVVKADERGRMIpedLERQIILAEAEGSVPFLVSATSGTTVLGAFDPLDAIADVCQRHGLWFHVDAAWGGsvlLSRTH 286
Cdd:cd01494    66 -PVPVPVDDAGYGG---LDVAILEELKAKPNVALIVITPNTTSGGVLVPLKEIRKIAKEYGILLLVDAASAG---GASPA 138
                         170       180
                  ....*....|....*....|...
gi 1720384328 287 RHLLDGIQRADSVAWNPHKLLAA 309
Cdd:cd01494   139 PGVLIPEGGADVVTFSLHKNLGG 161
Aminotran_5 pfam00266
Aminotransferase class-V; This domain is found in amino transferases, and other enzymes ...
129-275 3.21e-09

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: 58.41  E-value: 3.21e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720384328 129 EEVLKKLRALVGWNSGDG-VFCPGGSIS-NMYAMNLARFQRYPDCkqrglralpplALFTSKEcHYSITKGAAFLG--LG 204
Cdd:pfam00266  46 EEAREKVAEFINAPSNDEiIFTSGTTEAiNLVALSLGRSLKPGDE-----------IVITEME-HHANLVPWQELAkrTG 113
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1720384328 205 TDsVRVVKADERGRMIPEDLERQIilaeAEGSVpfLVSATSGTTVLGAFDPLDAIADVCQRHGLWFHVDAA 275
Cdd:pfam00266 114 AR-VRVLPLDEDGLLDLDELEKLI----TPKTK--LVAITHVSNVTGTIQPVPEIGKLAHQYGALVLVDAA 177
PLN03032 PLN03032
serine decarboxylase; Provisional
175-319 2.42e-06

serine decarboxylase; Provisional


Pssm-ID: 166673 [Multi-domain]  Cd Length: 374  Bit Score: 49.44  E-value: 2.42e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720384328 175 GLRALPPLALFTSKECHYSITKGAAFLGLGTDSVRVVkadERGRMIPEDLERQiiLAEAEGSvPFLVSATSGTTVLGAFD 254
Cdd:PLN03032  105 GREVFPDGILYASRESHYSVFKAARMYRMEAVKVPTL---PSGEIDYDDLERA--LAKNRDK-PAILNVNIGTTVKGAVD 178
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720384328 255 PLDAIADVCQRHG-----LWFHVDAAWGGSVLLSRTHRHLLDGIQRADSVAWNPHKLLAAGLQCSALLLR 319
Cdd:PLN03032  179 DLDRILRILKELGytedrFYIHCDGALFGLMMPFVSRAPEVTFRKPIGSVSVSGHKFLGCPMPCGVALTR 248
CsdA COG0520
Selenocysteine lyase/Cysteine desulfurase [Amino acid transport and metabolism];
208-308 2.78e-06

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


Pssm-ID: 440286 [Multi-domain]  Cd Length: 396  Bit Score: 49.37  E-value: 2.78e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720384328 208 VRVVKADERGRMIPEDLERQIilaeaeGSVPFLVSATSGTTVLGAFDPLDAIADVCQRHGLWFHVDAAwgGSVllsrTHR 287
Cdd:COG0520   131 VRVIPLDEDGELDLEALEALL------TPRTKLVAVTHVSNVTGTVNPVKEIAALAHAHGALVLVDGA--QSV----PHL 198
                          90       100
                  ....*....|....*....|....*
gi 1720384328 288 HL----LDgiqrADSVAWNPHKLLA 308
Cdd:COG0520   199 PVdvqaLG----CDFYAFSGHKLYG 219
TA_like cd06502
Low-specificity threonine aldolase (TA). This family belongs to pyridoxal phosphate (PLP) ...
128-275 1.58e-05

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: 46.56  E-value: 1.58e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720384328 128 EEEVLKKLRALVGWNSGD--GVFCPGGSISNmyamnlarfqrypdckQRGLRAL--PPLALFTSKECHYSI--TKGAAFL 201
Cdd:cd06502    30 EDPTTAKLEARAAELFGKeaALFVPSGTAAN----------------QLALAAHtqPGGSVICHETAHIYTdeAGAPEFL 93
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1720384328 202 GlgtdSVRVVKAD-ERGRMIPEDLERQIILAEAEGSV-PFLVSATSgTTVLGAFDPLD---AIADVCQRHGLWFHVDAA 275
Cdd:cd06502    94 S----GVKLLPVPgENGKLTPEDLEAAIRPRDDIHFPpPSLVSLEN-TTEGGTVYPLDelkAISALAKENGLPLHLDGA 167
GLY1 COG2008
Threonine aldolase [Amino acid transport and metabolism];
134-276 3.75e-05

Threonine aldolase [Amino acid transport and metabolism];


Pssm-ID: 441611 [Multi-domain]  Cd Length: 333  Bit Score: 45.44  E-value: 3.75e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720384328 134 KLRALVGwnSGDGVFCPGGSISNMyamnLArfqrypdckqrgLRAL-PPL-ALFTSKECHYSI--TKGAAFL-GLgtdSV 208
Cdd:COG2008    43 RVAELFG--KEAALFVPSGTMANQ----LA------------LRAHtRPGdEVICHETAHIYVdeGGAPEALsGV---KL 101
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1720384328 209 RVVkADERGRMIPEDLERQIILAEAEGSVPFLVS---ATSGTTVLgAFDPLDAIADVCQRHGLWFHVDAAW 276
Cdd:COG2008   102 LPV-PGEDGKLTPEDLEAAIRPGDVHFPQPGLVSlenTTEGGTVY-PLEELRAIAAVAREHGLPLHLDGAR 170
NifS COG1104
Cysteine desulfurase/Cysteine sulfinate desulfinase IscS or related enzyme, NifS family [Amino ...
129-275 8.86e-05

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: 44.27  E-value: 8.86e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720384328 129 EEVLKKLRALVGWNSGDGVFCPGGSISNmyamNLA---RFQRYPDCKQRglralpplaLFTSK-EcHYSITKGAAFL-GL 203
Cdd:COG1104    48 EEAREQVAALLGADPEEIIFTSGGTEAN----NLAikgAARAYRKKGKH---------IITSAiE-HPAVLETARFLeKE 113
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1720384328 204 GTDsVRVVKADERGRMIPEDLERQIilaeAEGSVpfLVSATSGTTVLGAFDPLDAIADVCQRHGLWFHVDAA 275
Cdd:COG1104   114 GFE-VTYLPVDEDGRVDLEALEAAL----RPDTA--LVSVMHANNETGTIQPIAEIAEIAKEHGVLFHTDAV 178
PLN02263 PLN02263
serine decarboxylase
175-278 1.13e-04

serine decarboxylase


Pssm-ID: 177904 [Multi-domain]  Cd Length: 470  Bit Score: 44.42  E-value: 1.13e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720384328 175 GLRALPPLALFTSKECHYSITKGAAFLglgtdSVRVVKAD--ERGRMIPEDLERQIIlaeAEGSVPFLVSATSGTTVLGA 252
Cdd:PLN02263  172 GREVFPDGILYASRESHYSVFKAARMY-----RMECVKVDtlVSGEIDCADFKAKLL---ANKDKPAIINVNIGTTVKGA 243
                          90       100       110
                  ....*....|....*....|....*....|.
gi 1720384328 253 FDPLDAIADVCQRHG-----LWFHVDAAWGG 278
Cdd:PLN02263  244 VDDLDLVIKTLEECGfsqdrFYIHCDGALFG 274
Orn_deC_like cd00615
Ornithine decarboxylase family. This family belongs to pyridoxal phosphate (PLP)-dependent ...
256-338 4.73e-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: 41.85  E-value: 4.73e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720384328 256 LDAIADVCQRHGLWFHVDAAWGGsvllsrtHRHLLDGIQR------ADSVAWNPHKLLAAGLQCSALLLRDtsNLLKRCH 329
Cdd:cd00615   172 LRKIVEEAHHRGLPVLVDEAHGA-------HFRFHPILPSsaamagADIVVQSTHKTLPALTQGSMIHVKG--DLVNPDR 242

                  ....*....
gi 1720384328 330 GSQASYLFQ 338
Cdd:cd00615   243 VNEALNLHQ 251
SufS_like cd06453
Cysteine desulfurase (SufS)-like. This family belongs to the pyridoxal phosphate (PLP) ...
207-275 5.27e-04

Cysteine desulfurase (SufS)-like. This family belongs to the pyridoxal phosphate (PLP)-dependent aspartate aminotransferase superfamily (fold I). The major groups in this CD correspond to cysteine desulfurase (SufS) and selenocysteine lyase. SufS catalyzes the removal of elemental sulfur and selenium atoms from L-cysteine, L-cystine, L-selenocysteine, and L-selenocystine to produce L-alanine; and selenocysteine lyase catalyzes the decomposition of L-selenocysteine.


Pssm-ID: 99746 [Multi-domain]  Cd Length: 373  Bit Score: 42.07  E-value: 5.27e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1720384328 207 SVRVVKADERGRMIPEDLERQIilaeaeGSVPFLVSATSGTTVLGAFDPLDAIADVCQRHGLWFHVDAA 275
Cdd:cd06453   115 KLKVVPVDDDGQLDLEALEKLL------TERTKLVAVTHVSNVLGTINPVKEIGEIAHEAGVPVLVDGA 177
Beta_elim_lyase pfam01212
Beta-eliminating lyase;
118-275 9.33e-04

Beta-eliminating lyase;


Pssm-ID: 426128 [Multi-domain]  Cd Length: 288  Bit Score: 41.05  E-value: 9.33e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720384328 118 YEIAPVFVLMEEEVlkklRALVGWNSGdgVFCPGGSISNmyamnlarfqrypdckQRGLRAL--PPLALFTSKECHYSI- 194
Cdd:pfam01212  28 YGGDPTVNRLEDRV----AELFGKEAA--LFVPSGTAAN----------------QLALMAHcqRGDEVICGEPAHIHFd 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720384328 195 -TKGAAFLGLGTdsVRVVKADERGRMIPEDLERQIILAEAEGSVPF-LVSAT-----SGTTVLgAFDPLDAIADVCQRHG 267
Cdd:pfam01212  86 eTGGHAELGGVQ--PRPLDGDEAGNMDLEDLEAAIREVGADIFPPTgLISLEnthnsAGGQVV-SLENLREIAALAREHG 162

                  ....*...
gi 1720384328 268 LWFHVDAA 275
Cdd:pfam01212 163 IPVHLDGA 170
PLN02721 PLN02721
threonine aldolase
146-299 1.23e-03

threonine aldolase


Pssm-ID: 178323 [Multi-domain]  Cd Length: 353  Bit Score: 40.83  E-value: 1.23e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720384328 146 GVFCPGGSISNMYAMNLarfqrypDCKQRGLRALpplalfTSKECHYSITKGAAFLGLGTDSVRVVKADERGRMIPEDLE 225
Cdd:PLN02721   58 ALFVPSGTMGNLISVLV-------HCDVRGSEVI------LGDNSHIHLYENGGISTLGGVHPRTVKNNEDGTMDLDAIE 124
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720384328 226 RQIilaEAEGSVPFLVS---------ATSGTTVLGAfDPLDAIADVCQRHGLWFHVDAA--WGGSVLLSRTHRHLLdgiQ 294
Cdd:PLN02721  125 AAI---RPKGDDHFPTTrliclenthANCGGRCLSV-EYTDKVGELAKRHGLKLHIDGAriFNASVALGVPVHRLV---K 197

                  ....*
gi 1720384328 295 RADSV 299
Cdd:PLN02721  198 AADSV 202
LdcC COG1982
Arginine/lysine/ornithine decarboxylase [Amino acid transport and metabolism];
256-320 2.39e-03

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


Pssm-ID: 441585 [Multi-domain]  Cd Length: 486  Bit Score: 40.09  E-value: 2.39e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1720384328 256 LDAIADVCQRHGLWFHVDAAWGGsvllsrtHRHLLDGIQR------ADSVAWNPHKLLAAGLQCSALLLRD 320
Cdd:COG1982   179 LKAIAELAHEHGIPVLVDEAHGA-------HFGFHPDLPRsameagADLVVQSTHKTLGALTQSSMLHVKG 242
PLN02651 PLN02651
cysteine desulfurase
129-275 4.06e-03

cysteine desulfurase


Pssm-ID: 178257 [Multi-domain]  Cd Length: 364  Bit Score: 39.25  E-value: 4.06e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720384328 129 EEVLKKLR----ALVGWNSGDGVFCPGGSISNMYAMNLArfqrypdckQRGLRALPPLALFTSKEcHYSITKGAAFLGLG 204
Cdd:PLN02651   42 EDAVEKARaqvaALIGADPKEIIFTSGATESNNLAIKGV---------MHFYKDKKKHVITTQTE-HKCVLDSCRHLQQE 111
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1720384328 205 TDSVRVVKADERGRMIPEDLERQIILAEAegsvpfLVSATSGTTVLGAFDPLDAIADVCQRHGLWFHVDAA 275
Cdd:PLN02651  112 GFEVTYLPVKSDGLVDLDELAAAIRPDTA------LVSVMAVNNEIGVIQPVEEIGELCREKKVLFHTDAA 176
PRK02948 PRK02948
IscS subfamily cysteine desulfurase;
133-274 4.29e-03

IscS subfamily cysteine desulfurase;


Pssm-ID: 179511 [Multi-domain]  Cd Length: 381  Bit Score: 38.94  E-value: 4.29e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720384328 133 KKLRALVGwNSGDGV-FCPGGSISNMYAMNlARFQRYPDCKQRglralpplaLFTSKECHYSITKGAAFLGLGTDSVRVV 211
Cdd:PRK02948   50 KTFAEMIG-GEEQGIyFTSGGTESNYLAIQ-SLLNALPQNKKH---------IITTPMEHASIHSYFQSLESQGYTVTEI 118
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1720384328 212 KADERGRMIPEDLERQIilaeAEGSVpfLVSATSGTTVLGAFDPLDAIADVCQRHGLWFHVDA 274
Cdd:PRK02948  119 PVDKSGLIRLVDLERAI----TPDTV--LASIQHANSEIGTIQPIAEIGALLKKYNVLFHSDC 175
 
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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