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Conserved domains on  [gi|1907112801|ref|XP_036015312|]
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cysteine sulfinic acid decarboxylase isoform X1 [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

 Zoom to residue level

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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 ...
 48-480 1.06e-135

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: 399.59  E-value: 1.06e-135
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907112801  48 EPEELKQLLDLELQSQGESREQILER-CRTVIHYSVKTGHPRFFNQLFSGLDPHALAGRIITESLNTSQYTYEIAPVFVL 126
Cdd:COG0076    28 SPEELRAALDEPLPEEGLPPEEALAElEDLVLPGSVDWNHPRFLAFVTGGTTPAALAADLLASALNQNMGDWDTSPAATE 107

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907112801 127 MEEEVLKKLRALVGW-NSGDGVFCPGGSISNMYAMNLARFQRYP-DCKQRGLRALPPLALFTSKECHYSITKGAAFLGLG 204
Cdd:COG0076   108 LEREVVRWLADLLGLpEGAGGVFTSGGTEANLLALLAARDRALArRVRAEGLPGAPRPRIVVSEEAHSSVDKAARLLGLG 187

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907112801 205 TDSVRVVKADERGRMIPEDLERQIILAEAEGSVPFLVSATSGTTVLGAFDPLDAIADVCQRHGLWFHVDAAWGGSVLLSR 284
Cdd:COG0076   188 RDALRKVPVDEDGRMDPDALEAAIDEDRAAGLNPIAVVATAGTTNTGAIDPLAEIADIAREHGLWLHVDAAYGGFALPSP 267

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907112801 285 THRHLLDGIQRADSVAWNPHKLLAAGLQCSALLLRDTSnLLKRCHGSQASYLFQQDkfyDVALDTGDKVVQCGRRVDCLK 364
Cdd:COG0076   268 ELRHLLDGIERADSITVDPHKWLYVPYGCGAVLVRDPE-LLREAFSFHASYLGPAD---DGVPNLGDYTLELSRRFRALK 343

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907112801 365 LWLMWKAQGGQGLERRIDQAFALTRYLVEEIKKREGFELVMEPEFVNVCFWFVPPslrGKKESPDYSQRLSqvapvlkER 444
Cdd:COG0076   344 LWATLRALGREGYRELIERCIDLARYLAEGIAALPGFELLAPPELNIVCFRYKPA---GLDEEDALNYALR-------DR 413

                         410       420       430
                  ....*....|....*....|....*....|....*.
gi 1907112801 445 MVKKGTMMIGYQPHGTRANfFRMVVANPILAQADID 480
Cdd:COG0076   414 LRARGRAFLSPTKLDGRVV-LRLVVLNPRTTEDDVD 448
 
Name Accession Description Interval E-value
GadA COG0076
Glutamate or tyrosine decarboxylase or a related PLP-dependent protein [Amino acid transport ...
 48-480 1.06e-135

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: 399.59  E-value: 1.06e-135
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907112801  48 EPEELKQLLDLELQSQGESREQILER-CRTVIHYSVKTGHPRFFNQLFSGLDPHALAGRIITESLNTSQYTYEIAPVFVL 126
Cdd:COG0076    28 SPEELRAALDEPLPEEGLPPEEALAElEDLVLPGSVDWNHPRFLAFVTGGTTPAALAADLLASALNQNMGDWDTSPAATE 107

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907112801 127 MEEEVLKKLRALVGW-NSGDGVFCPGGSISNMYAMNLARFQRYP-DCKQRGLRALPPLALFTSKECHYSITKGAAFLGLG 204
Cdd:COG0076   108 LEREVVRWLADLLGLpEGAGGVFTSGGTEANLLALLAARDRALArRVRAEGLPGAPRPRIVVSEEAHSSVDKAARLLGLG 187

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907112801 205 TDSVRVVKADERGRMIPEDLERQIILAEAEGSVPFLVSATSGTTVLGAFDPLDAIADVCQRHGLWFHVDAAWGGSVLLSR 284
Cdd:COG0076   188 RDALRKVPVDEDGRMDPDALEAAIDEDRAAGLNPIAVVATAGTTNTGAIDPLAEIADIAREHGLWLHVDAAYGGFALPSP 267

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907112801 285 THRHLLDGIQRADSVAWNPHKLLAAGLQCSALLLRDTSnLLKRCHGSQASYLFQQDkfyDVALDTGDKVVQCGRRVDCLK 364
Cdd:COG0076   268 ELRHLLDGIERADSITVDPHKWLYVPYGCGAVLVRDPE-LLREAFSFHASYLGPAD---DGVPNLGDYTLELSRRFRALK 343

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907112801 365 LWLMWKAQGGQGLERRIDQAFALTRYLVEEIKKREGFELVMEPEFVNVCFWFVPPslrGKKESPDYSQRLSqvapvlkER 444
Cdd:COG0076   344 LWATLRALGREGYRELIERCIDLARYLAEGIAALPGFELLAPPELNIVCFRYKPA---GLDEEDALNYALR-------DR 413

                         410       420       430
                  ....*....|....*....|....*....|....*.
gi 1907112801 445 MVKKGTMMIGYQPHGTRANfFRMVVANPILAQADID 480
Cdd:COG0076   414 LRARGRAFLSPTKLDGRVV-LRLVVLNPRTTEDDVD 448
DOPA_deC_like cd06450
DOPA decarboxylase family. This family belongs to pyridoxal phosphate (PLP)-dependent ...
 89-481 1.13e-130

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: 382.71  E-value: 1.13e-130
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907112801  89 FFNQLFSGLDPHALAGRIITESLNTSQYTYEIAPVFVLMEEEVLKKLRALVGWNS--GDGVFCPGGSISNMYAMNLARFQ 166
Cdd:cd06450     1 FLAGFVTTMDPPALLLEMLTSAKNAIDFTWDESPAATEMEAEVVNWLAKLFGLPSedADGVFTSGGSESNLLALLAARDR 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907112801 167 RYPDCKQRGLRALPPLALFTSKECHYSITKGAAFLGlgtDSVRVVKADERGRMIPEDLERQIILAEAEGSVPFLVSATSG 246
Cdd:cd06450    81 ARKRLKAGGGRGIDKLVIVCSDQAHVSVEKAAAYLD---VKVRLVPVDEDGRMDPEALEAAIDEDKAEGLNPIMVVATAG 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907112801 247 TTVLGAFDPLDAIADVCQRHGLWFHVDAAWGGSVLLSRTHRHLLDGIQRADSVAWNPHKLLAAGLQCSALLLRdtsnllk 326
Cdd:cd06450   158 TTDTGAIDPLEEIADLAEKYDLWLHVDAAYGGFLLPFPEPRHLDFGIERVDSISVDPHKYGLVPLGCSAVLVR------- 230

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907112801 327 rchgsqasylfqqdkfydvaldtgdkvvqcgrrvdCLKLWLMWKAQGGQGLERRIDQAFALTRYLVEEIKKREGFELVME 406
Cdd:cd06450   231 -----------------------------------ALKLWATLRRFGRDGYGEHIDRIVDLAKYLAELIRADPGFELLGE 275

                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1907112801 407 PEFVNVCFWFVPPSlrgkkespdysqRLSQVAPVLKERMVKKGTMMIGYQPHGTRaNFFRMVVANPILAQADIDF 481
Cdd:cd06450   276 PNLSLVCFRLKPSV------------KLDELNYDLSDRLNERGGWHVPATTLGGP-NVLRFVVTNPLTTRDDADA 337
Pyridoxal_deC pfam00282
Pyridoxal-dependent decarboxylase conserved domain;
49-417 2.34e-123

Pyridoxal-dependent decarboxylase conserved domain;


Pssm-ID: 395219  Cd Length: 373  Bit Score: 365.20  E-value: 2.34e-123
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907112801  49 PEELKQLLDLELQSQGESREQILERCRTVIHYSVKTGH-PRFFNQLFSGLDPHALAGRIITESLNTSQYTYEIAPVFVLM 127
Cdd:pfam00282   1 PGYLKPLLPLAAPIIPEPELQIDGDIRRNLMPGVTTWHsPHFHAYMPTGNSYPSLLGDMLTDAINCNGFTWESSPACTEL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907112801 128 EEEVLKKLRALVGW------NSGDGVFCPGGSISNMYAMNLARFQRYPDCKQRGLRALPP-----LALFTSKECHYSITK 196
Cdd:pfam00282  81 ENVVMNWLGEMLGLpaeflgQEGGGVLQPGSSESNLLALLAARTKWIKRMKAAGKPADSSgilakLVAYTSDQAHSSIEK 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907112801 197 GAAFLGLGtdsVRVVKADERGRMIPEDLERQIILAEAEGSVPFLVSATSGTTVLGAFDPLDAIADVCQRHGLWFHVDAAW 276
Cdd:pfam00282 161 AALYGGVK---LREIPSDDNGKMRGMDLEKAIEEDKENGLIPFFVVATLGTTGSGAFDDLQELGDICAKHNLWLHVDAAY 237

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907112801 277 GGSVLLSRTHRHLLDGIQRADSVAWNPHKLLAAGLQCSALLLRDtSNLLKRCHGSQASYLFQQDKFYdvalDTGDKVVQC 356
Cdd:pfam00282 238 GGSAFICPEFRHWLFGIERADSITFNPHKWMLVLLDCSAVWVKD-KEALQQAFQFNPLYLGHTDSAY----DTGHKQIPL 312

                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1907112801 357 GRRVDCLKLWLMWKAQGGQGLERRIDQAFALTRYLVEEIKKREGFELVMEPEFVNVCFWFV 417
Cdd:pfam00282 313 SRRFRILKLWFVIRSLGVEGLQNQIRRHVELAQYLEALIRKDGRFEICAEVGLGLVCFRLK 373
NOD_PanD_pyr TIGR03799
putative pyridoxal-dependent aspartate 1-decarboxylase; This enzyme is proposed here to be a ...
 76-473 2.32e-52

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: 184.95  E-value: 2.32e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907112801  76 TVIHYSVKTGHPRFFNQLFSGLDPHALAGRIITESLNTSQYTYEIAPVFVLMEEEVLKKLRALV---------GW-NSGD 145
Cdd:TIGR03799  79 KLVAHSVHTASPSFIGHMTSALPYFLLPLSKLMVGLNQNLVKIETSKAFTPLERQVLGMMHHLVyqqddsfyrRWmHSAD 158

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907112801 146 ---GVFCPGGSISNMYAMNLARFQRY-PDCKQRGL------RAL-----PPLALFTSKECHYSITKGAAFLGLGTDSVRV 210
Cdd:TIGR03799 159 hslGAFCSGGTVANITALWVARNRLLkADGDFRGIareglfAALrhygyDGLAILVSERGHYSLGKAADVLGIGRDNLVP 238

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907112801 211 VKADERGRMIPEDLERQIILAEAEGSVPFLVSATSGTTVLGAFDPLDAIADVCQRHGLWFHVDAAWGGSVLLSRTHRHLL 290
Cdd:TIGR03799 239 VKTDENNRIRVDALRDKCLELAAQNIKPMAIVGVAGTTETGNIDPLDEMADIAQEAGCHFHVDAAWGGATLLSNTYRHLL 318

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907112801 291 DGIQRADSVAWNPHKLLAAGLQCSALLLRDTSNLLKRCHgsQASYLFQQDkfydvALDTGDKVVQCGRRVDCLKLWLMWK 370
Cdd:TIGR03799 319 KGIERADSVTIDAHKQMYVPMGAGMVLFKDPALTSAIEH--HAEYILRKG-----SKDLGSHTLEGSRPGMAMLVYACLH 391

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907112801 371 AQGGQGLERRIDQAFALTRYLVEEIKKREGFELVMEPEFVNVCFWFVPPSLRGKKESPDYSQR------LSQVAPVLKER 444
Cdd:TIGR03799 392 IIGRKGYEMLINQSIDKAHYFANLIDQQPDFELVTEPELCLLTYRYVPENVKAALAIADEEQRekindaLNALTKFIQKR 471

                         410       420       430
                  ....*....|....*....|....*....|....*
gi 1907112801 445 MVKKG------TMMIGYQPHGTRANFFRMVVANPI 473
Cdd:TIGR03799 472 QRETGksfvsrTRLTPAQYDHQPTIVFRVVLANPL 506
PLN02880 PLN02880
tyrosine decarboxylase
 48-420 4.57e-39

tyrosine decarboxylase


Pssm-ID: 215475 [Multi-domain]  Cd Length: 490  Bit Score: 148.13  E-value: 4.57e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907112801  48 EPEELKQLLDLELQSQGESREQILERCRT-----VIHYSvktgHPRFFNQLFSGLDPHALAGRIITESLNTSQYTYEIAP 122
Cdd:PLN02880   43 QPGYLRELLPDSAPNQPETLDQVLDDVQAkilpgVTHWQ----SPNYFAYYPSNSSVAGFLGEMLSAGLNIVGFSWITSP 118

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907112801 123 VFVLMEEEVLKKLRALVGWNS-------GDGVFCPGGSISNMYAMNLARFQRYpdcKQRGLRALPPLALFTSKECHYSIT 195
Cdd:PLN02880  119 AATELEMIVLDWLAKLLNLPEqflstgnGGGVIQGTASEAVLVVLLAARDRVL---RKVGKNALEKLVVYASDQTHSALQ 195

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907112801 196 KGAAFLGLGTDSVRVVKADERGR--MIPEDLERQIILAEAEGSVPFLVSATSGTTVLGAFDPLDAIADVCQRHGLWFHVD 273
Cdd:PLN02880  196 KACQIAGIHPENCRLLKTDSSTNyaLAPELLSEAISTDLSSGLIPFFLCATVGTTSSTAVDPLLELGKIAKSNGMWFHVD 275

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907112801 274 AAWGGSVLLSRTHRHLLDGIQRADSVAWNPHKLLAAGLQCSALLLRDTSNLLKRChGSQASYLFQQDKFYDVALDTGDKV 353
Cdd:PLN02880  276 AAYAGSACICPEYRHYIDGVEEADSFNMNAHKWFLTNFDCSLLWVKDRNALIQSL-STNPEFLKNKASQANSVVDYKDWQ 354

                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1907112801 354 VQCGRRVDCLKLWLMWKAQGGQGLERRIDQAFALTRYLVEEIKKREGFELVMEPEFVNVCFWFVPPS 420
Cdd:PLN02880  355 IPLGRRFRSLKLWMVLRLYGVENLQSYIRNHIKLAKEFEQLVAQDSRFEVVTPRIFSLVCFRLVPPK 421
 
Name Accession Description Interval E-value
GadA COG0076
Glutamate or tyrosine decarboxylase or a related PLP-dependent protein [Amino acid transport ...
 48-480 1.06e-135

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: 399.59  E-value: 1.06e-135
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907112801  48 EPEELKQLLDLELQSQGESREQILER-CRTVIHYSVKTGHPRFFNQLFSGLDPHALAGRIITESLNTSQYTYEIAPVFVL 126
Cdd:COG0076    28 SPEELRAALDEPLPEEGLPPEEALAElEDLVLPGSVDWNHPRFLAFVTGGTTPAALAADLLASALNQNMGDWDTSPAATE 107

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907112801 127 MEEEVLKKLRALVGW-NSGDGVFCPGGSISNMYAMNLARFQRYP-DCKQRGLRALPPLALFTSKECHYSITKGAAFLGLG 204
Cdd:COG0076   108 LEREVVRWLADLLGLpEGAGGVFTSGGTEANLLALLAARDRALArRVRAEGLPGAPRPRIVVSEEAHSSVDKAARLLGLG 187

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907112801 205 TDSVRVVKADERGRMIPEDLERQIILAEAEGSVPFLVSATSGTTVLGAFDPLDAIADVCQRHGLWFHVDAAWGGSVLLSR 284
Cdd:COG0076   188 RDALRKVPVDEDGRMDPDALEAAIDEDRAAGLNPIAVVATAGTTNTGAIDPLAEIADIAREHGLWLHVDAAYGGFALPSP 267

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907112801 285 THRHLLDGIQRADSVAWNPHKLLAAGLQCSALLLRDTSnLLKRCHGSQASYLFQQDkfyDVALDTGDKVVQCGRRVDCLK 364
Cdd:COG0076   268 ELRHLLDGIERADSITVDPHKWLYVPYGCGAVLVRDPE-LLREAFSFHASYLGPAD---DGVPNLGDYTLELSRRFRALK 343

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907112801 365 LWLMWKAQGGQGLERRIDQAFALTRYLVEEIKKREGFELVMEPEFVNVCFWFVPPslrGKKESPDYSQRLSqvapvlkER 444
Cdd:COG0076   344 LWATLRALGREGYRELIERCIDLARYLAEGIAALPGFELLAPPELNIVCFRYKPA---GLDEEDALNYALR-------DR 413

                         410       420       430
                  ....*....|....*....|....*....|....*.
gi 1907112801 445 MVKKGTMMIGYQPHGTRANfFRMVVANPILAQADID 480
Cdd:COG0076   414 LRARGRAFLSPTKLDGRVV-LRLVVLNPRTTEDDVD 448
DOPA_deC_like cd06450
DOPA decarboxylase family. This family belongs to pyridoxal phosphate (PLP)-dependent ...
 89-481 1.13e-130

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: 382.71  E-value: 1.13e-130
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907112801  89 FFNQLFSGLDPHALAGRIITESLNTSQYTYEIAPVFVLMEEEVLKKLRALVGWNS--GDGVFCPGGSISNMYAMNLARFQ 166
Cdd:cd06450     1 FLAGFVTTMDPPALLLEMLTSAKNAIDFTWDESPAATEMEAEVVNWLAKLFGLPSedADGVFTSGGSESNLLALLAARDR 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907112801 167 RYPDCKQRGLRALPPLALFTSKECHYSITKGAAFLGlgtDSVRVVKADERGRMIPEDLERQIILAEAEGSVPFLVSATSG 246
Cdd:cd06450    81 ARKRLKAGGGRGIDKLVIVCSDQAHVSVEKAAAYLD---VKVRLVPVDEDGRMDPEALEAAIDEDKAEGLNPIMVVATAG 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907112801 247 TTVLGAFDPLDAIADVCQRHGLWFHVDAAWGGSVLLSRTHRHLLDGIQRADSVAWNPHKLLAAGLQCSALLLRdtsnllk 326
Cdd:cd06450   158 TTDTGAIDPLEEIADLAEKYDLWLHVDAAYGGFLLPFPEPRHLDFGIERVDSISVDPHKYGLVPLGCSAVLVR------- 230

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907112801 327 rchgsqasylfqqdkfydvaldtgdkvvqcgrrvdCLKLWLMWKAQGGQGLERRIDQAFALTRYLVEEIKKREGFELVME 406
Cdd:cd06450   231 -----------------------------------ALKLWATLRRFGRDGYGEHIDRIVDLAKYLAELIRADPGFELLGE 275

                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1907112801 407 PEFVNVCFWFVPPSlrgkkespdysqRLSQVAPVLKERMVKKGTMMIGYQPHGTRaNFFRMVVANPILAQADIDF 481
Cdd:cd06450   276 PNLSLVCFRLKPSV------------KLDELNYDLSDRLNERGGWHVPATTLGGP-NVLRFVVTNPLTTRDDADA 337
Pyridoxal_deC pfam00282
Pyridoxal-dependent decarboxylase conserved domain;
49-417 2.34e-123

Pyridoxal-dependent decarboxylase conserved domain;


Pssm-ID: 395219  Cd Length: 373  Bit Score: 365.20  E-value: 2.34e-123
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907112801  49 PEELKQLLDLELQSQGESREQILERCRTVIHYSVKTGH-PRFFNQLFSGLDPHALAGRIITESLNTSQYTYEIAPVFVLM 127
Cdd:pfam00282   1 PGYLKPLLPLAAPIIPEPELQIDGDIRRNLMPGVTTWHsPHFHAYMPTGNSYPSLLGDMLTDAINCNGFTWESSPACTEL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907112801 128 EEEVLKKLRALVGW------NSGDGVFCPGGSISNMYAMNLARFQRYPDCKQRGLRALPP-----LALFTSKECHYSITK 196
Cdd:pfam00282  81 ENVVMNWLGEMLGLpaeflgQEGGGVLQPGSSESNLLALLAARTKWIKRMKAAGKPADSSgilakLVAYTSDQAHSSIEK 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907112801 197 GAAFLGLGtdsVRVVKADERGRMIPEDLERQIILAEAEGSVPFLVSATSGTTVLGAFDPLDAIADVCQRHGLWFHVDAAW 276
Cdd:pfam00282 161 AALYGGVK---LREIPSDDNGKMRGMDLEKAIEEDKENGLIPFFVVATLGTTGSGAFDDLQELGDICAKHNLWLHVDAAY 237

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907112801 277 GGSVLLSRTHRHLLDGIQRADSVAWNPHKLLAAGLQCSALLLRDtSNLLKRCHGSQASYLFQQDKFYdvalDTGDKVVQC 356
Cdd:pfam00282 238 GGSAFICPEFRHWLFGIERADSITFNPHKWMLVLLDCSAVWVKD-KEALQQAFQFNPLYLGHTDSAY----DTGHKQIPL 312

                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1907112801 357 GRRVDCLKLWLMWKAQGGQGLERRIDQAFALTRYLVEEIKKREGFELVMEPEFVNVCFWFV 417
Cdd:pfam00282 313 SRRFRILKLWFVIRSLGVEGLQNQIRRHVELAQYLEALIRKDGRFEICAEVGLGLVCFRLK 373
NOD_PanD_pyr TIGR03799
putative pyridoxal-dependent aspartate 1-decarboxylase; This enzyme is proposed here to be a ...
 76-473 2.32e-52

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: 184.95  E-value: 2.32e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907112801  76 TVIHYSVKTGHPRFFNQLFSGLDPHALAGRIITESLNTSQYTYEIAPVFVLMEEEVLKKLRALV---------GW-NSGD 145
Cdd:TIGR03799  79 KLVAHSVHTASPSFIGHMTSALPYFLLPLSKLMVGLNQNLVKIETSKAFTPLERQVLGMMHHLVyqqddsfyrRWmHSAD 158

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907112801 146 ---GVFCPGGSISNMYAMNLARFQRY-PDCKQRGL------RAL-----PPLALFTSKECHYSITKGAAFLGLGTDSVRV 210
Cdd:TIGR03799 159 hslGAFCSGGTVANITALWVARNRLLkADGDFRGIareglfAALrhygyDGLAILVSERGHYSLGKAADVLGIGRDNLVP 238

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907112801 211 VKADERGRMIPEDLERQIILAEAEGSVPFLVSATSGTTVLGAFDPLDAIADVCQRHGLWFHVDAAWGGSVLLSRTHRHLL 290
Cdd:TIGR03799 239 VKTDENNRIRVDALRDKCLELAAQNIKPMAIVGVAGTTETGNIDPLDEMADIAQEAGCHFHVDAAWGGATLLSNTYRHLL 318

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907112801 291 DGIQRADSVAWNPHKLLAAGLQCSALLLRDTSNLLKRCHgsQASYLFQQDkfydvALDTGDKVVQCGRRVDCLKLWLMWK 370
Cdd:TIGR03799 319 KGIERADSVTIDAHKQMYVPMGAGMVLFKDPALTSAIEH--HAEYILRKG-----SKDLGSHTLEGSRPGMAMLVYACLH 391

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907112801 371 AQGGQGLERRIDQAFALTRYLVEEIKKREGFELVMEPEFVNVCFWFVPPSLRGKKESPDYSQR------LSQVAPVLKER 444
Cdd:TIGR03799 392 IIGRKGYEMLINQSIDKAHYFANLIDQQPDFELVTEPELCLLTYRYVPENVKAALAIADEEQRekindaLNALTKFIQKR 471

                         410       420       430
                  ....*....|....*....|....*....|....*
gi 1907112801 445 MVKKG------TMMIGYQPHGTRANFFRMVVANPI 473
Cdd:TIGR03799 472 QRETGksfvsrTRLTPAQYDHQPTIVFRVVLANPL 506
PLN02880 PLN02880
tyrosine decarboxylase
 48-420 4.57e-39

tyrosine decarboxylase


Pssm-ID: 215475 [Multi-domain]  Cd Length: 490  Bit Score: 148.13  E-value: 4.57e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907112801  48 EPEELKQLLDLELQSQGESREQILERCRT-----VIHYSvktgHPRFFNQLFSGLDPHALAGRIITESLNTSQYTYEIAP 122
Cdd:PLN02880   43 QPGYLRELLPDSAPNQPETLDQVLDDVQAkilpgVTHWQ----SPNYFAYYPSNSSVAGFLGEMLSAGLNIVGFSWITSP 118

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907112801 123 VFVLMEEEVLKKLRALVGWNS-------GDGVFCPGGSISNMYAMNLARFQRYpdcKQRGLRALPPLALFTSKECHYSIT 195
Cdd:PLN02880  119 AATELEMIVLDWLAKLLNLPEqflstgnGGGVIQGTASEAVLVVLLAARDRVL---RKVGKNALEKLVVYASDQTHSALQ 195

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907112801 196 KGAAFLGLGTDSVRVVKADERGR--MIPEDLERQIILAEAEGSVPFLVSATSGTTVLGAFDPLDAIADVCQRHGLWFHVD 273
Cdd:PLN02880  196 KACQIAGIHPENCRLLKTDSSTNyaLAPELLSEAISTDLSSGLIPFFLCATVGTTSSTAVDPLLELGKIAKSNGMWFHVD 275

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907112801 274 AAWGGSVLLSRTHRHLLDGIQRADSVAWNPHKLLAAGLQCSALLLRDTSNLLKRChGSQASYLFQQDKFYDVALDTGDKV 353
Cdd:PLN02880  276 AAYAGSACICPEYRHYIDGVEEADSFNMNAHKWFLTNFDCSLLWVKDRNALIQSL-STNPEFLKNKASQANSVVDYKDWQ 354

                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1907112801 354 VQCGRRVDCLKLWLMWKAQGGQGLERRIDQAFALTRYLVEEIKKREGFELVMEPEFVNVCFWFVPPS 420
Cdd:PLN02880  355 IPLGRRFRSLKLWMVLRLYGVENLQSYIRNHIKLAKEFEQLVAQDSRFEVVTPRIFSLVCFRLVPPK 421
PLN02590 PLN02590
probable tyrosine decarboxylase
 48-418 8.17e-39

probable tyrosine decarboxylase


Pssm-ID: 178200 [Multi-domain]  Cd Length: 539  Bit Score: 148.32  E-value: 8.17e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907112801  48 EPEELKQLLDlelqsqgESREQILErcrTVIHYSvktgHPRFFNQLFSGLDPHALAGRIITESLNTSQYTYEIAPVFVLM 127
Cdd:PLN02590  106 RPESLKELLD-------DVSKKIMP---GITHWQ----SPSYFAYYASSTSVAGFLGEMLNAGLSVVGFTWLTSPAATEL 171

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907112801 128 EEEVLKKLRALV-------GWNSGDGVFcPGGSISNMYAMNLARFQRYpdCKQRGLRALPPLALFTSKECHYSITKGAAF 200
Cdd:PLN02590  172 EIIVLDWLAKLLqlpdhflSTGNGGGVI-QGTGCEAVLVVVLAARDRI--LKKVGKTLLPQLVVYGSDQTHSSFRKACLI 248

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907112801 201 LGLGTDSVRVVKADERGR--MIPEDLERQIILAEAEGSVPFLVSATSGTTVLGAFDPLDAIADVCQRHGLWFHVDAAWGG 278
Cdd:PLN02590  249 GGIHEENIRLLKTDSSTNygMPPESLEEAISHDLAKGFIPFFICATVGTTSSAAVDPLVPLGNIAKKYGIWLHVDAAYAG 328

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907112801 279 SVLLSRTHRHLLDGIQRADSVAWNPHKLLAAGLQCSALLLRDTSNLLKRCHGSQASYLFQQDKfYDVALDTGDKVVQCGR 358
Cdd:PLN02590  329 NACICPEYRKFIDGIENADSFNMNAHKWLFANQTCSPLWVKDRYSLIDALKTNPEYLEFKVSK-KDTVVNYKDWQISLSR 407

                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907112801 359 RVDCLKLWLMWKAQGGQGLERRIDQAFALTRYLVEEIKKREGFELVMEPEFVNVCFWFVP 418
Cdd:PLN02590  408 RFRSLKLWMVLRLYGSENLRNFIRDHVNLAKHFEDYVAQDPSFEVVTTRYFSLVCFRLAP 467
PRK02769 PRK02769
histidine decarboxylase; Provisional
 68-399 7.88e-16

histidine decarboxylase; Provisional


Pssm-ID: 235068 [Multi-domain]  Cd Length: 380  Bit Score: 78.93  E-value: 7.88e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907112801  68 EQILERCRtvIHYSVKTGHPrfFNQLFSgldpHALAGRIITESLNTSQYTYEiAPVFVL----MEEEVLKKLRALVG--W 141
Cdd:PRK02769   12 EDFWLYLR--HNQYFNVGYP--EAADFD----YSALKRFFSFSINNCGDPYS-KSNYPLnsfdFERDVMNFFAELFKipF 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907112801 142 NSGDGVFCPGGSISNMYAMNLARfQRYPDCkqrglralpplALFTSKECHYSITKGAAFLGLGTdsvRVVKADERGRMIP 221
Cdd:PRK02769   83 NESWGYITNGGTEGNLYGCYLAR-ELFPDG-----------TLYYSKDTHYSVSKIARLLRIKS---RVITSLPNGEIDY 147

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907112801 222 EDLERQIilaEAEGSVPFLVSATSGTTVLGAFDPLDAIADVCQRHGL---WFHVDAAWGGSVLLSRTHRHLLDGIQRADS 298
Cdd:PRK02769  148 DDLISKI---KENKNQPPIIFANIGTTMTGAIDNIKEIQEILKKIGIddyYIHADAALSGMILPFVNNPPPFSFADGIDS 224

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907112801 299 VAWNPHKLLAAGLQCSALllrdtsnLLKRCHGSQASylfqqdkfYDVA-LDTGDKVVQCGRR-VDCLKLWLMWKAQGGQG 376
Cdd:PRK02769  225 IAISGHKFIGSPMPCGIV-------LAKKKYVERIS--------VDVDyIGSRDQTISGSRNgHTALLLWAAIRSLGSKG 289

                         330       340
                  ....*....|....*....|...
gi 1907112801 377 LERRIDQAFALTRYLVEEIKKRE 399
Cdd:PRK02769  290 LRQRVQHCLDMAQYAVDRLQANG 312
AAT_I cd01494
Aspartate aminotransferase (AAT) superfamily (fold type I) of pyridoxal phosphate (PLP) ...
 128-309 1.91e-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: 1.91e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907112801 128 EEEVLKKLRALVGWNSGDGVFCPGGSISN-MYAMNLArfqrypdckQRGLRALPPLALFTSkecHYSITKGAAFLGlgtd 206
Cdd:cd01494     2 LEELEEKLARLLQPGNDKAVFVPSGTGANeAALLALL---------GPGDEVIVDANGHGS---RYWVAAELAGAK---- 65

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907112801 207 sVRVVKADERGRMIpedLERQIILAEAEGSVPFLVSATSGTTVLGAFDPLDAIADVCQRHGLWFHVDAAWGGsvlLSRTH 286
Cdd:cd01494    66 -PVPVPVDDAGYGG---LDVAILEELKAKPNVALIVITPNTTSGGVLVPLKEIRKIAKEYGILLLVDAASAG---GASPA 138

                         170       180
                  ....*....|....*....|...
gi 1907112801 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 4.13e-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: 4.13e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907112801 129 EEVLKKLRALVGWNSGDG-VFCPGGSIS-NMYAMNLARFQRYPDCkqrglralpplALFTSKEcHYSITKGAAFLG--LG 204
Cdd:pfam00266  46 EEAREKVAEFINAPSNDEiIFTSGTTEAiNLVALSLGRSLKPGDE-----------IVITEME-HHANLVPWQELAkrTG 113

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1907112801 205 TDsVRVVKADERGRMIPEDLERQIilaeAEGSVpfLVSATSGTTVLGAFDPLDAIADVCQRHGLWFHVDAA 275
Cdd:pfam00266 114 AR-VRVLPLDEDGLLDLDELEKLI----TPKTK--LVAITHVSNVTGTIQPVPEIGKLAHQYGALVLVDAA 177
CsdA COG0520
Selenocysteine lyase/Cysteine desulfurase [Amino acid transport and metabolism];
208-308 3.50e-06

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


Pssm-ID: 440286 [Multi-domain]  Cd Length: 396  Bit Score: 49.37  E-value: 3.50e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907112801 208 VRVVKADERGRMIPEDLERQIilaeaeGSVPFLVSATSGTTVLGAFDPLDAIADVCQRHGLWFHVDAAwgGSVllsrTHR 287
Cdd:COG0520   131 VRVIPLDEDGELDLEALEALL------TPRTKLVAVTHVSNVTGTVNPVKEIAALAHAHGALVLVDGA--QSV----PHL 198

                          90       100
                  ....*....|....*....|....*
gi 1907112801 288 HL----LDgiqrADSVAWNPHKLLA 308
Cdd:COG0520   199 PVdvqaLG----CDFYAFSGHKLYG 219
PLN03032 PLN03032
serine decarboxylase; Provisional
 175-319 4.32e-06

serine decarboxylase; Provisional


Pssm-ID: 166673 [Multi-domain]  Cd Length: 374  Bit Score: 48.67  E-value: 4.32e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907112801 175 GLRALPPLALFTSKECHYSITKGAAFLGLGTDSVRVVkadERGRMIPEDLERQiiLAEAEGSvPFLVSATSGTTVLGAFD 254
Cdd:PLN03032  105 GREVFPDGILYASRESHYSVFKAARMYRMEAVKVPTL---PSGEIDYDDLERA--LAKNRDK-PAILNVNIGTTVKGAVD 178

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907112801 255 PLDAIADVCQRHG-----LWFHVDAAWGGSVLLSRTHRHLLDGIQRADSVAWNPHKLLAAGLQCSALLLR 319
Cdd:PLN03032  179 DLDRILRILKELGytedrFYIHCDGALFGLMMPFVSRAPEVTFRKPIGSVSVSGHKFLGCPMPCGVALTR 248
TA_like cd06502
Low-specificity threonine aldolase (TA). This family belongs to pyridoxal phosphate (PLP) ...
 128-275 1.41e-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: 46.94  E-value: 1.41e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907112801 128 EEEVLKKLRALVGWNSGD--GVFCPGGSISNmyamnlarfqrypdckQRGLRAL--PPLALFTSKECHYSI--TKGAAFL 201
Cdd:cd06502    30 EDPTTAKLEARAAELFGKeaALFVPSGTAAN----------------QLALAAHtqPGGSVICHETAHIYTdeAGAPEFL 93

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1907112801 202 GlgtdSVRVVKAD-ERGRMIPEDLERQIILAEAEGSV-PFLVSATSgTTVLGAFDPLD---AIADVCQRHGLWFHVDAA 275
Cdd:cd06502    94 S----GVKLLPVPgENGKLTPEDLEAAIRPRDDIHFPpPSLVSLEN-TTEGGTVYPLDelkAISALAKENGLPLHLDGA 167
LdcC COG1982
Arginine/lysine/ornithine decarboxylase [Amino acid transport and metabolism];
256-411 2.15e-05

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


Pssm-ID: 441585 [Multi-domain]  Cd Length: 486  Bit Score: 47.03  E-value: 2.15e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907112801 256 LDAIADVCQRHGLWFHVDAAWGGsvllsrtHRHLLDGIQR------ADSVAWNPHKLLAAGLQCSALLLRDT---SNLLK 326
Cdd:COG1982   179 LKAIAELAHEHGIPVLVDEAHGA-------HFGFHPDLPRsameagADLVVQSTHKTLGALTQSSMLHVKGGrvdHERVN 251

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907112801 327 RC---HGS-QASYLFqqdkfydVA-LDTgdkvvqcGRRvdclklwlMWKAQGgqglERRIDQAFALTRYLVEEIKKREGF 401
Cdd:COG1982   252 EAlmlLQStSPSYLL-------MAsLDV-------ARR--------QMAGEG----EELLDEALELAIEARKEINKIPGL 305

                         170
                  ....*....|
gi 1907112801 402 ElVMEPEFVN 411
Cdd:COG1982   306 Y-VFGPEDLG 314
GLY1 COG2008
Threonine aldolase [Amino acid transport and metabolism];
134-276 3.35e-05

Threonine aldolase [Amino acid transport and metabolism];


Pssm-ID: 441611 [Multi-domain]  Cd Length: 333  Bit Score: 45.83  E-value: 3.35e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907112801 134 KLRALVGwnSGDGVFCPGGSISNMyamnLArfqrypdckqrgLRAL-PPL-ALFTSKECHysI----TKGAAFL-GLgtd 206
Cdd:COG2008    43 RVAELFG--KEAALFVPSGTMANQ----LA------------LRAHtRPGdEVICHETAH--IyvdeGGAPEALsGV--- 99

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1907112801 207 SVRVVkADERGRMIPEDLERQIILAEAEGSVPFLVS---ATSGTTVLgAFDPLDAIADVCQRHGLWFHVDAAW 276
Cdd:COG2008   100 KLLPV-PGEDGKLTPEDLEAAIRPGDVHFPQPGLVSlenTTEGGTVY-PLEELRAIAAVAREHGLPLHLDGAR 170
NifS COG1104
Cysteine desulfurase/Cysteine sulfinate desulfinase IscS or related enzyme, NifS family [Amino ...
 129-275 8.52e-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: 44.65  E-value: 8.52e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907112801 129 EEVLKKLRALVGWNSGDGVFCPGGSISNmyamNLA---RFQRYPDCKQRglralpplaLFTSK-EcHYSITKGAAFL-GL 203
Cdd:COG1104    48 EEAREQVAALLGADPEEIIFTSGGTEAN----NLAikgAARAYRKKGKH---------IITSAiE-HPAVLETARFLeKE 113

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1907112801 204 GTDsVRVVKADERGRMIPEDLERQIilaeAEGSVpfLVSATSGTTVLGAFDPLDAIADVCQRHGLWFHVDAA 275
Cdd:COG1104   114 GFE-VTYLPVDEDGRVDLEALEAAL----RPDTA--LVSVMHANNETGTIQPIAEIAEIAKEHGVLFHTDAV 178
PLN02263 PLN02263
serine decarboxylase
 175-278 1.41e-04

serine decarboxylase


Pssm-ID: 177904 [Multi-domain]  Cd Length: 470  Bit Score: 44.42  E-value: 1.41e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907112801 175 GLRALPPLALFTSKECHYSITKGAAFLglgtdSVRVVKAD--ERGRMIPEDLERQIIlaeAEGSVPFLVSATSGTTVLGA 252
Cdd:PLN02263  172 GREVFPDGILYASRESHYSVFKAARMY-----RMECVKVDtlVSGEIDCADFKAKLL---ANKDKPAIINVNIGTTVKGA 243

                          90       100       110
                  ....*....|....*....|....*....|.
gi 1907112801 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 5.78e-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: 5.78e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907112801 256 LDAIADVCQRHGLWFHVDAAWGGsvllsrtHRHLLDGIQR------ADSVAWNPHKLLAAGLQCSALLLRDtsNLLKRCH 329
Cdd:cd00615   172 LRKIVEEAHHRGLPVLVDEAHGA-------HFRFHPILPSsaamagADIVVQSTHKTLPALTQGSMIHVKG--DLVNPDR 242


                  ....*....
gi 1907112801 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 6.61e-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: 6.61e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1907112801 207 SVRVVKADERGRMIPEDLERQIilaeaeGSVPFLVSATSGTTVLGAFDPLDAIADVCQRHGLWFHVDAA 275
Cdd:cd06453   115 KLKVVPVDDDGQLDLEALEKLL------TERTKLVAVTHVSNVLGTINPVKEIGEIAHEAGVPVLVDGA 177
Beta_elim_lyase pfam01212
Beta-eliminating lyase;
118-275 1.04e-03

Beta-eliminating lyase;


Pssm-ID: 426128 [Multi-domain]  Cd Length: 288  Bit Score: 41.05  E-value: 1.04e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907112801 118 YEIAPVFVLMEEEVlkklRALVGWNSGdgVFCPGGSISNmyamnlarfqrypdckQRGLRAL--PPLALFTSKECHYSI- 194
Cdd:pfam01212  28 YGGDPTVNRLEDRV----AELFGKEAA--LFVPSGTAAN----------------QLALMAHcqRGDEVICGEPAHIHFd 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907112801 195 -TKGAAFLGLGTdsVRVVKADERGRMIPEDLERQIILAEAEGSVPF-LVSAT-----SGTTVLgAFDPLDAIADVCQRHG 267
Cdd:pfam01212  86 eTGGHAELGGVQ--PRPLDGDEAGNMDLEDLEAAIREVGADIFPPTgLISLEnthnsAGGQVV-SLENLREIAALAREHG 162


                  ....*...
gi 1907112801 268 LWFHVDAA 275
Cdd:pfam01212 163 IPVHLDGA 170
PLN02721 PLN02721
threonine aldolase
 146-299 1.17e-03

threonine aldolase


Pssm-ID: 178323 [Multi-domain]  Cd Length: 353  Bit Score: 41.21  E-value: 1.17e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907112801 146 GVFCPGGSISNMYAMNLarfqrypDCKQRGLRALpplalfTSKECHYSITKGAAFLGLGTDSVRVVKADERGRMIPEDLE 225
Cdd:PLN02721   58 ALFVPSGTMGNLISVLV-------HCDVRGSEVI------LGDNSHIHLYENGGISTLGGVHPRTVKNNEDGTMDLDAIE 124

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907112801 226 RQIilaEAEGSVPFLVS---------ATSGTTVLGAfDPLDAIADVCQRHGLWFHVDAA--WGGSVLLSRTHRHLLdgiQ 294
Cdd:PLN02721  125 AAI---RPKGDDHFPTTrliclenthANCGGRCLSV-EYTDKVGELAKRHGLKLHIDGAriFNASVALGVPVHRLV---K 197


                  ....*
gi 1907112801 295 RADSV 299
Cdd:PLN02721  198 AADSV 202
PLN02651 PLN02651
cysteine desulfurase
 129-275 4.96e-03

cysteine desulfurase


Pssm-ID: 178257 [Multi-domain]  Cd Length: 364  Bit Score: 39.25  E-value: 4.96e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907112801 129 EEVLKKLR----ALVGWNSGDGVFCPGGSISNMYAMNLArfqrypdckQRGLRALPPLALFTSKEcHYSITKGAAFLGLG 204
Cdd:PLN02651   42 EDAVEKARaqvaALIGADPKEIIFTSGATESNNLAIKGV---------MHFYKDKKKHVITTQTE-HKCVLDSCRHLQQE 111

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1907112801 205 TDSVRVVKADERGRMIPEDLERQIILAEAegsvpfLVSATSGTTVLGAFDPLDAIADVCQRHGLWFHVDAA 275
Cdd:PLN02651  112 GFEVTYLPVKSDGLVDLDELAAAIRPDTA------LVSVMAVNNEIGVIQPVEEIGELCREKKVLFHTDAA 176
 
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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