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Conserved domains on  [gi|160420189|ref|NP_001104211|]
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dopa decarboxylase (aromatic L-amino acid decarboxylase) [Xenopus laevis]

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
DOPA_deC_like cd06450
DOPA decarboxylase family. This family belongs to pyridoxal phosphate (PLP)-dependent ...
76-470 2.88e-136

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  Cd Length: 345  Bit Score: 399.66  E-value: 2.88e-136
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160420189  76 FFAYFPTGNSYPALLADMLCGAIGCIGFSWASSPACTELETVMLDWLGKMIGLPEqflagnkGEGGGVIQGTASEATLMA 155
Cdd:cd06450    1 FLAGFVTTMDPPALLLEMLTSAKNAIDFTWDESPAATEMEAEVVNWLAKLFGLPS-------EDADGVFTSGGSESNLLA 73
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160420189 156 LLAARTKVTRRLQAENPKlteaeIVSRMVAYSSDQAHSSVERAGLISGVRMKKIPSDEKFVARGQALKKALEEDKAEGLI 235
Cdd:cd06450   74 LLAARDRARKRLKAGGGR-----GIDKLVIVCSDQAHVSVEKAAAYLDVKVRLVPVDEDGRMDPEALEAAIDEDKAEGLN 148
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160420189 236 PIFFCATLGTTNSCAFDNLMELGPVCNAENIWMHIDAAYAGSAFICPEFRYLMEGVEFADSFNFNPHKWLLVNFDCSAFW 315
Cdd:cd06450  149 PIMVVATAGTTDTGAIDPLEEIADLAEKYDLWLHVDAAYGGFLLPFPEPRHLDFGIERVDSISVDPHKYGLVPLGCSAVL 228
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160420189 316 VkkrsdligafkmdpvylqydqqesglvtdyrhwqiplgrrfRSLKLWFVFRIYGVKGLQAHIRKHVGLAHEFLECVKKD 395
Cdd:cd06450  229 V-----------------------------------------RALKLWATLRRFGRDGYGEHIDRIVDLAKYLAELIRAD 267
                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 160420189 396 ELFEICAPVILGLVCFRLKGS---NELNKALLQKINHSKKIHIVPCCLGDTFVLRFAVCARTVESSHVQFAWKHIKEL 470
Cdd:cd06450  268 PGFELLGEPNLSLVCFRLKPSvklDELNYDLSDRLNERGGWHVPATTLGGPNVLRFVVTNPLTTRDDADALLEDIERA 345
 
Name Accession Description Interval E-value
DOPA_deC_like cd06450
DOPA decarboxylase family. This family belongs to pyridoxal phosphate (PLP)-dependent ...
76-470 2.88e-136

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  Cd Length: 345  Bit Score: 399.66  E-value: 2.88e-136
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160420189  76 FFAYFPTGNSYPALLADMLCGAIGCIGFSWASSPACTELETVMLDWLGKMIGLPEqflagnkGEGGGVIQGTASEATLMA 155
Cdd:cd06450    1 FLAGFVTTMDPPALLLEMLTSAKNAIDFTWDESPAATEMEAEVVNWLAKLFGLPS-------EDADGVFTSGGSESNLLA 73
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160420189 156 LLAARTKVTRRLQAENPKlteaeIVSRMVAYSSDQAHSSVERAGLISGVRMKKIPSDEKFVARGQALKKALEEDKAEGLI 235
Cdd:cd06450   74 LLAARDRARKRLKAGGGR-----GIDKLVIVCSDQAHVSVEKAAAYLDVKVRLVPVDEDGRMDPEALEAAIDEDKAEGLN 148
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160420189 236 PIFFCATLGTTNSCAFDNLMELGPVCNAENIWMHIDAAYAGSAFICPEFRYLMEGVEFADSFNFNPHKWLLVNFDCSAFW 315
Cdd:cd06450  149 PIMVVATAGTTDTGAIDPLEEIADLAEKYDLWLHVDAAYGGFLLPFPEPRHLDFGIERVDSISVDPHKYGLVPLGCSAVL 228
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160420189 316 VkkrsdligafkmdpvylqydqqesglvtdyrhwqiplgrrfRSLKLWFVFRIYGVKGLQAHIRKHVGLAHEFLECVKKD 395
Cdd:cd06450  229 V-----------------------------------------RALKLWATLRRFGRDGYGEHIDRIVDLAKYLAELIRAD 267
                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 160420189 396 ELFEICAPVILGLVCFRLKGS---NELNKALLQKINHSKKIHIVPCCLGDTFVLRFAVCARTVESSHVQFAWKHIKEL 470
Cdd:cd06450  268 PGFELLGEPNLSLVCFRLKPSvklDELNYDLSDRLNERGGWHVPATTLGGPNVLRFVVTNPLTTRDDADALLEDIERA 345
Pyridoxal_deC pfam00282
Pyridoxal-dependent decarboxylase conserved domain;
35-414 0e+00

Pyridoxal-dependent decarboxylase conserved domain;


Pssm-ID: 249739  Cd Length: 373  Bit Score: 591.66  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160420189   35 PGYLRPLIPDSAPEEGETYEDIIKDVERVIMPGVTHWHSPYFFAYFPTGNSYPALLADMLCGAIGCIGFSWASSPACTEL 114
Cdd:pfam00282   1 PGYLRPLLPEAAPIIPEPLLDILGDIRKNIMPGVTTWHSPNFHAYFPAGNSYPSLLGDMLSDAINCNGFTWESSPACTEL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160420189  115 ETVMLDWLGKMIGLPEQFLAgnKGEGGGVIQGTASEATLMALLAARTKVTRRLQAENPKLTEaeivsRMVAYSSDQAHSS 194
Cdd:pfam00282  81 ENVVMDWLAKMLGLPKEFLG--SGEGGGVLQGGSSESNLLALLAARTKWIRRMKAAGKPSLG-----KLVAYTSDQAHSS 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160420189  195 VERAGLISGVRMKKIPSDEKFVARGQALKKALEEDKAEGLIPIFFCATLGTTNSCAFDNLMELGPVCNAENIWMHIDAAY 274
Cdd:pfam00282 154 IEKAALIAGVELREIPTDENGKMRGMDLEKAIEEDKENGLIPFFVCATLGTTGSGAFDPLQELGDICNKYDLWLHVDAAY 233
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160420189  275 AGSAFICPEFRYLMEGVEFADSFNFNPHKWLLVNFDCSAFWVKKRSDLIGAFKMDPVYLQYDQQESGLVTDYRHWQIPLG 354
Cdd:pfam00282 234 AGSAFICPEFRHWLFGIERADSFSFNPHKWMLVLLDCSALWVRDKGALQQALQFNPEYLGHNDKQSDVAVDYGDWQIPLS 313
                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 160420189  355 RRFRSLKLWFVFRIYGVKGLQAHIRKHVGLAHEFLECVKKDELFEICAPVILGLVCFRLK 414
Cdd:pfam00282 314 RRFRILKLWFVLRSYGVEGLQNQIRRHVELAKYFEALVRKDSRFEICAERGLGLVCFRLK 373
PLN02880 PLN02880
tyrosine decarboxylase
1-475 0e+00

tyrosine decarboxylase


Pssm-ID: 215475  Cd Length: 490  Bit Score: 540.65  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160420189   1 MNASEFRKRGKDMVDYVADYLEQIESRQVFPDVEPGYLRPLIPDSAPEEGETYEDIIKDVERVIMPGVTHWHSPYFFAYF 80
Cdd:PLN02880  10 MDAEQLRECGHRMVDFIADYYKSIENFPVLSQVQPGYLRELLPDSAPNQPETLDQVLDDVQAKILPGVTHWQSPNYFAYY 89
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160420189  81 PTGNSYPALLADMLCGAIGCIGFSWASSPACTELETVMLDWLGKMIGLPEQFLAgnKGEGGGVIQGTASEATLMALLAAR 160
Cdd:PLN02880  90 PSNSSVAGFLGEMLSAGLNIVGFSWITSPAATELEMIVLDWLAKLLNLPEQFLS--TGNGGGVIQGTASEAVLVVLLAAR 167
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160420189 161 TKVTRRLQAENpklteaeiVSRMVAYSSDQAHSSVERAGLISG-----VRMKKIPSDEKFVARGQALKKALEEDKAEGLI 235
Cdd:PLN02880 168 DRVLRKVGKNA--------LEKLVVYASDQTHSALQKACQIAGihpenCRLLKTDSSTNYALAPELLSEAISTDLSSGLI 239
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160420189 236 PIFFCATLGTTNSCAFDNLMELGPVCNAENIWMHIDAAYAGSAFICPEFRYLMEGVEFADSFNFNPHKWLLVNFDCSAFW 315
Cdd:PLN02880 240 PFFLCATVGTTSSTAVDPLLELGKIAKSNGMWFHVDAAYAGSACICPEYRHYIDGVEEADSFNMNAHKWFLTNFDCSLLW 319
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160420189 316 VKKRSDLIGAFKMDPVYLQYDQQESGLVTDYRHWQIPLGRRFRSLKLWFVFRIYGVKGLQAHIRKHVGLAHEFLECVKKD 395
Cdd:PLN02880 320 VKDRNALIQSLSTNPEFLKNKASQANSVVDYKDWQIPLGRRFRSLKLWMVLRLYGVENLQSYIRNHIKLAKEFEQLVAQD 399
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160420189 396 ELFEICAPVILGLVCFRL-------KGSNELNKALLQKINHSKKIHIVPCCLGDTFVLRFAVCARTVESSHVQFAWKHIK 468
Cdd:PLN02880 400 SRFEVVTPRIFSLVCFRLvppknneDNGNKLNHDLLDAVNSSGKIFISHTVLSGKYVLRFAVGAPLTEERHVTAAWKVLQ 479

                 ....*..
gi 160420189 469 ELTTELL 475
Cdd:PLN02880 480 DEASKLL 486
GadB COG0076
Glutamate decarboxylase and related PLP-dependent proteins [Amino acid transport and ...
17-429 1.65e-74

Glutamate decarboxylase and related PLP-dependent proteins [Amino acid transport and metabolism]


Pssm-ID: 223154  Cd Length: 460  Bit Score: 244.20  E-value: 1.65e-74
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160420189  17 VADYLEQIESRQVFPDVEPGYLRPLIPDSAPEEGETYEDIIKDVER-VIMPGVTHWHSPYFFAYFPTGNSYPALLADMLC 95
Cdd:COG0076    4 LIDKDMLNSKRYSGDSLSPLFGALSDSRMAPEKGEPLEEVLDELAElLIKDELYLDGHPRANLAGFCPTRVPPVAAELLV 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160420189  96 GAIGCIGFSWASSPACTELETVMLDWLGKMIGLPEQFLagnkgeggGVIQGTASEATLMALLAARTKVTRRLQAENPKLT 175
Cdd:COG0076   84 SALNKNLGDPDESPAAAELEERVVNMLSDLLGAPEEAS--------GTFTSGGTEANLLALLAARERWRKRALAESGKPG 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160420189 176 EAEIVsrmvaYSSDQAHSSVERAGLISGVRMKKIPSDEKFVAR-GQALKKALEEDKAEGLIpiffCATLGTTNSCAFDNL 254
Cdd:COG0076  156 GKPNI-----VCSETAHFSFEKAARYLGLGLRRVPTVPTDYRIdVDALEEAIDENTIGGVV----VGTAGTTDTGSIDDI 226
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160420189 255 MELGPVCNAENIWMHIDAAYAGSAFICPEFRYLM-EGVEFADSFNFNPHKWLLVNFDCSAFWVKKRSDLIGAFKMDPVYL 333
Cdd:COG0076  227 EELADIAEEYGIWLHVDAAFGGFLLPFLEPDGRWdFGLEGVDSITVDGHKYGLAPIGCGVVLFRDEEALRRILIFADYYL 306
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160420189 334 QydqqeSGLVTDYRHWQIPLGRRfrSLKLWFVFRIYGVKGLQAHIRKHVGLAHEFLECVKKDELFEICAPVILGLVCFRL 413
Cdd:COG0076  307 P-----GGGIPNFTILGSRPGRQ--ALALYANLRRLGREGYRKLLDRTLELARYLAEELEKLGDFELVNEPELPIVAFRL 379
                        410
                 ....*....|....*.
gi 160420189 414 KGSNELNKALLQKINH 429
Cdd:COG0076  380 KDDEDTLADLSERLDR 395
NOD_PanD_pyr TIGR03799
putative pyridoxal-dependent aspartate 1-decarboxylase; This enzyme is proposed here to be a ...
141-438 9.60e-12

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: 163511  Cd Length: 522  Bit Score: 65.49  E-value: 9.60e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160420189  141 GGVIqgtaseATLMALLAARTKVtrrLQAEN--PKLTEAEIVSRMVAY--------SSDQAHSSVERAGLISGV---RMK 207
Cdd:TIGR03799 167 GGTV------ANITALWVARNRL---LKADGdfKGVAREGLFAALKHYgydglailVSERGHYSLGKAADVLGIgrdNLI 237
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160420189  208 KIPSDEKFVARGQALKKALEEDKAEGLIPIFFCATLGTTNSCAFDNLMELGPVCNAENIWMHIDAAYAGSAFICPEFRYL 287
Cdd:TIGR03799 238 AIKTDANNRIDVDALRDKCAELAEQNIKPLAIVGVAGTTETGNIDPLDEMADIAQELGCHFHVDAAWGGATLLSNTYRHL 317
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160420189  288 MEGVEFADSFNFNPHKWLLVNfdcsafwvkkrsdlIGA----FKmDPVYLQYDQQESGLVTdyRHWQIPLG-------RR 356
Cdd:TIGR03799 318 LKGIERADSVTIDAHKQLYVP--------------MGAgmvlFK-DPALMSAIEHHAEYIL--RKGSKDLGshtlegsRP 380
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160420189  357 FRSLKLWFVFRIYGVKGLQAHIRKHVGLAHEFLECVKKDELFEICAPVILGLVCFRLKGSNElnKALLQKINHSKKIHIV 436
Cdd:TIGR03799 381 GMAMLVYAGLHIIGRKGYELLIDQSIEKAKYFADLIQQQPDFELVTEPELCLLTYRYVPEEV--QQALAKADEEQREKIN 458

                  ..
gi 160420189  437 PC 438
Cdd:TIGR03799 459 EL 460
PRK13520 PRK13520
L-tyrosine decarboxylase; Provisional
109-338 1.14e-11

L-tyrosine decarboxylase; Provisional


Pssm-ID: 237409  Cd Length: 371  Bit Score: 64.90  E-value: 1.14e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160420189 109 PACTELETVMLDWLGKMIGLPEqflagnkgeGGGVIQGTASEATLMALLAARtkvtRRLQAENPKLteaeivsrmVAYSS 188
Cdd:PRK13520  55 PGTAKLEEEAVEMLGELLHLPD---------AYGYITSGGTEANIQAVRAAR----NLAKAEKPNI---------VVPES 112
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160420189 189 dqAHSSVERAGLISGVRMKKIPSDEKFVARGQALKKALEEDKAeGLIPIffcatLGTTNSCAFDNLMELGPVCNAENIWM 268
Cdd:PRK13520 113 --AHFSFDKAADMLGVELRRAPLDDDYRVDVKAVEDLIDDNTI-GIVGI-----AGTTELGQVDPIPELSKIALENGIFL 184
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 160420189 269 HIDAAYAGsaFICP------EFRYLMEGVefaDSFNFNPHKWLLVNFDCSAFWVKKRSDLiGAFKMDPVYLQYDQQ 338
Cdd:PRK13520 185 HVDAAFGG--FVIPflddppNFDFSLPGV---DSITIDPHKMGLAPIPAGGILFRDESYL-DALAVDTPYLTSKKQ 254
 
Name Accession Description Interval E-value
DOPA_deC_like cd06450
DOPA decarboxylase family. This family belongs to pyridoxal phosphate (PLP)-dependent ...
76-470 2.88e-136

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  Cd Length: 345  Bit Score: 399.66  E-value: 2.88e-136
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160420189  76 FFAYFPTGNSYPALLADMLCGAIGCIGFSWASSPACTELETVMLDWLGKMIGLPEqflagnkGEGGGVIQGTASEATLMA 155
Cdd:cd06450    1 FLAGFVTTMDPPALLLEMLTSAKNAIDFTWDESPAATEMEAEVVNWLAKLFGLPS-------EDADGVFTSGGSESNLLA 73
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160420189 156 LLAARTKVTRRLQAENPKlteaeIVSRMVAYSSDQAHSSVERAGLISGVRMKKIPSDEKFVARGQALKKALEEDKAEGLI 235
Cdd:cd06450   74 LLAARDRARKRLKAGGGR-----GIDKLVIVCSDQAHVSVEKAAAYLDVKVRLVPVDEDGRMDPEALEAAIDEDKAEGLN 148
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160420189 236 PIFFCATLGTTNSCAFDNLMELGPVCNAENIWMHIDAAYAGSAFICPEFRYLMEGVEFADSFNFNPHKWLLVNFDCSAFW 315
Cdd:cd06450  149 PIMVVATAGTTDTGAIDPLEEIADLAEKYDLWLHVDAAYGGFLLPFPEPRHLDFGIERVDSISVDPHKYGLVPLGCSAVL 228
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160420189 316 VkkrsdligafkmdpvylqydqqesglvtdyrhwqiplgrrfRSLKLWFVFRIYGVKGLQAHIRKHVGLAHEFLECVKKD 395
Cdd:cd06450  229 V-----------------------------------------RALKLWATLRRFGRDGYGEHIDRIVDLAKYLAELIRAD 267
                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 160420189 396 ELFEICAPVILGLVCFRLKGS---NELNKALLQKINHSKKIHIVPCCLGDTFVLRFAVCARTVESSHVQFAWKHIKEL 470
Cdd:cd06450  268 PGFELLGEPNLSLVCFRLKPSvklDELNYDLSDRLNERGGWHVPATTLGGPNVLRFVVTNPLTTRDDADALLEDIERA 345
Pyridoxal_deC pfam00282
Pyridoxal-dependent decarboxylase conserved domain;
35-414 0e+00

Pyridoxal-dependent decarboxylase conserved domain;


Pssm-ID: 249739  Cd Length: 373  Bit Score: 591.66  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160420189   35 PGYLRPLIPDSAPEEGETYEDIIKDVERVIMPGVTHWHSPYFFAYFPTGNSYPALLADMLCGAIGCIGFSWASSPACTEL 114
Cdd:pfam00282   1 PGYLRPLLPEAAPIIPEPLLDILGDIRKNIMPGVTTWHSPNFHAYFPAGNSYPSLLGDMLSDAINCNGFTWESSPACTEL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160420189  115 ETVMLDWLGKMIGLPEQFLAgnKGEGGGVIQGTASEATLMALLAARTKVTRRLQAENPKLTEaeivsRMVAYSSDQAHSS 194
Cdd:pfam00282  81 ENVVMDWLAKMLGLPKEFLG--SGEGGGVLQGGSSESNLLALLAARTKWIRRMKAAGKPSLG-----KLVAYTSDQAHSS 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160420189  195 VERAGLISGVRMKKIPSDEKFVARGQALKKALEEDKAEGLIPIFFCATLGTTNSCAFDNLMELGPVCNAENIWMHIDAAY 274
Cdd:pfam00282 154 IEKAALIAGVELREIPTDENGKMRGMDLEKAIEEDKENGLIPFFVCATLGTTGSGAFDPLQELGDICNKYDLWLHVDAAY 233
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160420189  275 AGSAFICPEFRYLMEGVEFADSFNFNPHKWLLVNFDCSAFWVKKRSDLIGAFKMDPVYLQYDQQESGLVTDYRHWQIPLG 354
Cdd:pfam00282 234 AGSAFICPEFRHWLFGIERADSFSFNPHKWMLVLLDCSALWVRDKGALQQALQFNPEYLGHNDKQSDVAVDYGDWQIPLS 313
                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 160420189  355 RRFRSLKLWFVFRIYGVKGLQAHIRKHVGLAHEFLECVKKDELFEICAPVILGLVCFRLK 414
Cdd:pfam00282 314 RRFRILKLWFVLRSYGVEGLQNQIRRHVELAKYFEALVRKDSRFEICAERGLGLVCFRLK 373
PLN02880 PLN02880
tyrosine decarboxylase
1-475 0e+00

tyrosine decarboxylase


Pssm-ID: 215475  Cd Length: 490  Bit Score: 540.65  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160420189   1 MNASEFRKRGKDMVDYVADYLEQIESRQVFPDVEPGYLRPLIPDSAPEEGETYEDIIKDVERVIMPGVTHWHSPYFFAYF 80
Cdd:PLN02880  10 MDAEQLRECGHRMVDFIADYYKSIENFPVLSQVQPGYLRELLPDSAPNQPETLDQVLDDVQAKILPGVTHWQSPNYFAYY 89
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160420189  81 PTGNSYPALLADMLCGAIGCIGFSWASSPACTELETVMLDWLGKMIGLPEQFLAgnKGEGGGVIQGTASEATLMALLAAR 160
Cdd:PLN02880  90 PSNSSVAGFLGEMLSAGLNIVGFSWITSPAATELEMIVLDWLAKLLNLPEQFLS--TGNGGGVIQGTASEAVLVVLLAAR 167
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160420189 161 TKVTRRLQAENpklteaeiVSRMVAYSSDQAHSSVERAGLISG-----VRMKKIPSDEKFVARGQALKKALEEDKAEGLI 235
Cdd:PLN02880 168 DRVLRKVGKNA--------LEKLVVYASDQTHSALQKACQIAGihpenCRLLKTDSSTNYALAPELLSEAISTDLSSGLI 239
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160420189 236 PIFFCATLGTTNSCAFDNLMELGPVCNAENIWMHIDAAYAGSAFICPEFRYLMEGVEFADSFNFNPHKWLLVNFDCSAFW 315
Cdd:PLN02880 240 PFFLCATVGTTSSTAVDPLLELGKIAKSNGMWFHVDAAYAGSACICPEYRHYIDGVEEADSFNMNAHKWFLTNFDCSLLW 319
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160420189 316 VKKRSDLIGAFKMDPVYLQYDQQESGLVTDYRHWQIPLGRRFRSLKLWFVFRIYGVKGLQAHIRKHVGLAHEFLECVKKD 395
Cdd:PLN02880 320 VKDRNALIQSLSTNPEFLKNKASQANSVVDYKDWQIPLGRRFRSLKLWMVLRLYGVENLQSYIRNHIKLAKEFEQLVAQD 399
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160420189 396 ELFEICAPVILGLVCFRL-------KGSNELNKALLQKINHSKKIHIVPCCLGDTFVLRFAVCARTVESSHVQFAWKHIK 468
Cdd:PLN02880 400 SRFEVVTPRIFSLVCFRLvppknneDNGNKLNHDLLDAVNSSGKIFISHTVLSGKYVLRFAVGAPLTEERHVTAAWKVLQ 479

                 ....*..
gi 160420189 469 ELTTELL 475
Cdd:PLN02880 480 DEASKLL 486
PLN02590 PLN02590
probable tyrosine decarboxylase
1-477 8.90e-153

probable tyrosine decarboxylase


Pssm-ID: 178200  Cd Length: 539  Bit Score: 449.16  E-value: 8.90e-153
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160420189   1 MNASEFRKRGKDMVDYVADYLEQIE-SRQVFP---DVEPGYLRPLIPDSAPEEGETYEDIIKDVERVIMPGVTHWHSPYF 76
Cdd:PLN02590  54 MDSELLREQGHIMVDFIADYYKNLQdSPQDFPvlsQVQPGYLRDMLPDSAPERPESLKELLDDVSKKIMPGITHWQSPSY 133
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160420189  77 FAYFPTGNSYPALLADMLCGAIGCIGFSWASSPACTELETVMLDWLGKMIGLPEQFLAgnKGEGGGVIQGTASEATLMAL 156
Cdd:PLN02590 134 FAYYASSTSVAGFLGEMLNAGLSVVGFTWLTSPAATELEIIVLDWLAKLLQLPDHFLS--TGNGGGVIQGTGCEAVLVVV 211
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160420189 157 LAARTKVTRRLQAEnpklteaeIVSRMVAYSSDQAHSSVERAGLISGV-----RMKKIPSDEKFVARGQALKKALEEDKA 231
Cdd:PLN02590 212 LAARDRILKKVGKT--------LLPQLVVYGSDQTHSSFRKACLIGGIheeniRLLKTDSSTNYGMPPESLEEAISHDLA 283
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160420189 232 EGLIPIFFCATLGTTNSCAFDNLMELGPVCNAENIWMHIDAAYAGSAFICPEFRYLMEGVEFADSFNFNPHKWLLVNFDC 311
Cdd:PLN02590 284 KGFIPFFICATVGTTSSAAVDPLVPLGNIAKKYGIWLHVDAAYAGNACICPEYRKFIDGIENADSFNMNAHKWLFANQTC 363
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160420189 312 SAFWVKKRSDLIGAFKMDPVYLQYDQQESGLVTDYRHWQIPLGRRFRSLKLWFVFRIYGVKGLQAHIRKHVGLAHEFLEC 391
Cdd:PLN02590 364 SPLWVKDRYSLIDALKTNPEYLEFKVSKKDTVVNYKDWQISLSRRFRSLKLWMVLRLYGSENLRNFIRDHVNLAKHFEDY 443
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160420189 392 VKKDELFEICAPVILGLVCFRL-------KGSNELNKALLQKINHSKKIHIVPCCLGDTFVLRFAVCARTVESSHVQFAW 464
Cdd:PLN02590 444 VAQDPSFEVVTTRYFSLVCFRLapvdgdeDQCNERNRELLAAVNSTGKIFISHTALSGKFVLRFAVGAPLTEEKHVTEAW 523
                        490
                 ....*....|...
gi 160420189 465 KHIKELTTELLNN 477
Cdd:PLN02590 524 QIIQKHASKFTRN 536
GadB COG0076
Glutamate decarboxylase and related PLP-dependent proteins [Amino acid transport and ...
17-429 1.65e-74

Glutamate decarboxylase and related PLP-dependent proteins [Amino acid transport and metabolism]


Pssm-ID: 223154  Cd Length: 460  Bit Score: 244.20  E-value: 1.65e-74
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160420189  17 VADYLEQIESRQVFPDVEPGYLRPLIPDSAPEEGETYEDIIKDVER-VIMPGVTHWHSPYFFAYFPTGNSYPALLADMLC 95
Cdd:COG0076    4 LIDKDMLNSKRYSGDSLSPLFGALSDSRMAPEKGEPLEEVLDELAElLIKDELYLDGHPRANLAGFCPTRVPPVAAELLV 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160420189  96 GAIGCIGFSWASSPACTELETVMLDWLGKMIGLPEQFLagnkgeggGVIQGTASEATLMALLAARTKVTRRLQAENPKLT 175
Cdd:COG0076   84 SALNKNLGDPDESPAAAELEERVVNMLSDLLGAPEEAS--------GTFTSGGTEANLLALLAARERWRKRALAESGKPG 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160420189 176 EAEIVsrmvaYSSDQAHSSVERAGLISGVRMKKIPSDEKFVAR-GQALKKALEEDKAEGLIpiffCATLGTTNSCAFDNL 254
Cdd:COG0076  156 GKPNI-----VCSETAHFSFEKAARYLGLGLRRVPTVPTDYRIdVDALEEAIDENTIGGVV----VGTAGTTDTGSIDDI 226
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160420189 255 MELGPVCNAENIWMHIDAAYAGSAFICPEFRYLM-EGVEFADSFNFNPHKWLLVNFDCSAFWVKKRSDLIGAFKMDPVYL 333
Cdd:COG0076  227 EELADIAEEYGIWLHVDAAFGGFLLPFLEPDGRWdFGLEGVDSITVDGHKYGLAPIGCGVVLFRDEEALRRILIFADYYL 306
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160420189 334 QydqqeSGLVTDYRHWQIPLGRRfrSLKLWFVFRIYGVKGLQAHIRKHVGLAHEFLECVKKDELFEICAPVILGLVCFRL 413
Cdd:COG0076  307 P-----GGGIPNFTILGSRPGRQ--ALALYANLRRLGREGYRKLLDRTLELARYLAEELEKLGDFELVNEPELPIVAFRL 379
                        410
                 ....*....|....*.
gi 160420189 414 KGSNELNKALLQKINH 429
Cdd:COG0076  380 KDDEDTLADLSERLDR 395
AAT_I cd01494
Aspartate aminotransferase (AAT) superfamily (fold type I) of pyridoxal phosphate (PLP) ...
136-317 7.92e-19

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  Cd Length: 170  Bit Score: 83.59  E-value: 7.92e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160420189 136 NKGEGGGVIQGTASEATLMALLAARTKvtrrlqaenpklteaeivsRMVAYSSDQAHSSVER-AGLISGVRMKKIPSDEK 214
Cdd:cd01494   14 QPGNDKAVFVPSGTGANEAALLALLGP-------------------GDEVIVDANGHGSRYWvAAELAGAKPVPVPVDDA 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160420189 215 FVARgqaLKKALEEDKAEGLIPIFFCATLGTTNSCAFDNLMELGPVCNAENIWMHIDAAYAGSAFICPEFRylmEGVEFA 294
Cdd:cd01494   75 GYGG---LDVAILEELKAKPNVALIVITPNTTSGGVLVPLKEIRKIAKEYGILLLVDAASAGGASPAPGVL---IPEGGA 148
                        170       180
                 ....*....|....*....|...
gi 160420189 295 DSFNFNPHKWLLVNfDCSAFWVK 317
Cdd:cd01494  149 DVVTFSLHKNLGGE-GGGVVIVK 170
NOD_PanD_pyr TIGR03799
putative pyridoxal-dependent aspartate 1-decarboxylase; This enzyme is proposed here to be a ...
141-438 9.60e-12

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: 163511  Cd Length: 522  Bit Score: 65.49  E-value: 9.60e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160420189  141 GGVIqgtaseATLMALLAARTKVtrrLQAEN--PKLTEAEIVSRMVAY--------SSDQAHSSVERAGLISGV---RMK 207
Cdd:TIGR03799 167 GGTV------ANITALWVARNRL---LKADGdfKGVAREGLFAALKHYgydglailVSERGHYSLGKAADVLGIgrdNLI 237
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160420189  208 KIPSDEKFVARGQALKKALEEDKAEGLIPIFFCATLGTTNSCAFDNLMELGPVCNAENIWMHIDAAYAGSAFICPEFRYL 287
Cdd:TIGR03799 238 AIKTDANNRIDVDALRDKCAELAEQNIKPLAIVGVAGTTETGNIDPLDEMADIAQELGCHFHVDAAWGGATLLSNTYRHL 317
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160420189  288 MEGVEFADSFNFNPHKWLLVNfdcsafwvkkrsdlIGA----FKmDPVYLQYDQQESGLVTdyRHWQIPLG-------RR 356
Cdd:TIGR03799 318 LKGIERADSVTIDAHKQLYVP--------------MGAgmvlFK-DPALMSAIEHHAEYIL--RKGSKDLGshtlegsRP 380
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160420189  357 FRSLKLWFVFRIYGVKGLQAHIRKHVGLAHEFLECVKKDELFEICAPVILGLVCFRLKGSNElnKALLQKINHSKKIHIV 436
Cdd:TIGR03799 381 GMAMLVYAGLHIIGRKGYELLIDQSIEKAKYFADLIQQQPDFELVTEPELCLLTYRYVPEEV--QQALAKADEEQREKIN 458

                  ..
gi 160420189  437 PC 438
Cdd:TIGR03799 459 EL 460
tyr_de_CO2_Arch TIGR03812
tyrosine decarboxylase MnfA; Members of this protein family are the archaeal form, MnfA, of ...
109-426 1.01e-11

tyrosine decarboxylase MnfA; Members of this protein family are the archaeal form, MnfA, of tyrosine decarboxylase, and are involved in methanofuran biosynthesis. Members show clear homology to the Enterococcus form, Tdc, that is involved in tyrosine decarboxylation for resistance to acidic conditions [Biosynthesis of cofactors, prosthetic groups, and carriers, Other].


Pssm-ID: 234361  Cd Length: 373  Bit Score: 65.06  E-value: 1.01e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160420189  109 PACTELETVMLDWLGKMIGLPEqflagnkgeGGGVIQGTASEATLMALLAARTKVTrrlqAENPKlteAEIVSrmvaysS 188
Cdd:TIGR03812  55 PGTKKIEEEVVGSLGNLLHLPD---------AYGYIVSGGTEANIQAVRAAKNLAR----EEKRT---PNIIV------P 112
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160420189  189 DQAHSSVERAGLISGVRMKKIPSDEKFVARGQALKKALEeDKAEGLIPIffcatLGTTNSCAFDNLMELGPVCNAENIWM 268
Cdd:TIGR03812 113 ESAHFSFEKAAEMLGLELRYAPLDEDYTVDVKDVEDLID-DNTIGIVGI-----AGTTELGQIDDIEELSKIALENGIYL 186
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160420189  269 HIDAAYAGsaFICPefrYLMEGVEFADsFNF----------NPHKWLLVNFDCSAFwVKKRSDLIGAFKMDPVYLQYDQQ 338
Cdd:TIGR03812 187 HVDAAFGG--FVIP---FLKKGYNPPP-FDFslpgvqsitiDPHKMGLSPIPAGGI-LFRSKSYLKYLSVDAPYLTVKKQ 259
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160420189  339 ESglvtdyrhwqiPLGRR--FRSLKLWFVFRIYGVKGLQAHIRKHVGLAHEFLECVKKDELFEICAPViLGLVCFRLKGS 416
Cdd:TIGR03812 260 AT-----------ITGTRsgASAAATYAVIKYLGREGYRKIVAECMENTRYLVEELKKIGFEPVIEPV-LNIVAFEVDDP 327
                         330
                  ....*....|
gi 160420189  417 NELNKALLQK 426
Cdd:TIGR03812 328 EEVRKKLRDR 337
PRK13520 PRK13520
L-tyrosine decarboxylase; Provisional
109-338 1.14e-11

L-tyrosine decarboxylase; Provisional


Pssm-ID: 237409  Cd Length: 371  Bit Score: 64.90  E-value: 1.14e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160420189 109 PACTELETVMLDWLGKMIGLPEqflagnkgeGGGVIQGTASEATLMALLAARtkvtRRLQAENPKLteaeivsrmVAYSS 188
Cdd:PRK13520  55 PGTAKLEEEAVEMLGELLHLPD---------AYGYITSGGTEANIQAVRAAR----NLAKAEKPNI---------VVPES 112
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160420189 189 dqAHSSVERAGLISGVRMKKIPSDEKFVARGQALKKALEEDKAeGLIPIffcatLGTTNSCAFDNLMELGPVCNAENIWM 268
Cdd:PRK13520 113 --AHFSFDKAADMLGVELRRAPLDDDYRVDVKAVEDLIDDNTI-GIVGI-----AGTTELGQVDPIPELSKIALENGIFL 184
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 160420189 269 HIDAAYAGsaFICP------EFRYLMEGVefaDSFNFNPHKWLLVNFDCSAFWVKKRSDLiGAFKMDPVYLQYDQQ 338
Cdd:PRK13520 185 HVDAAFGG--FVIPflddppNFDFSLPGV---DSITIDPHKMGLAPIPAGGILFRDESYL-DALAVDTPYLTSKKQ 254
PRK02769 PRK02769
histidine decarboxylase; Provisional
184-305 1.14e-04

histidine decarboxylase; Provisional


Pssm-ID: 235068  Cd Length: 380  Bit Score: 43.11  E-value: 1.14e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160420189 184 VAYSSDQAHSSVERAGLISGVRMKKIPSDEKFVARGQALKKALEEDKAEGliPIFFcATLGTTNSCAFDNLMELGPVC-- 261
Cdd:PRK02769 112 TLYYSKDTHYSVSKIARLLRIKSRVITSLPNGEIDYDDLISKIKENKNQP--PIIF-ANIGTTMTGAIDNIKEIQEILkk 188
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 160420189 262 -NAENIWMHIDAAYAGS--AFICPEFRYLMEgvEFADSFNFNPHKWL 305
Cdd:PRK02769 189 iGIDDYYIHADAALSGMilPFVNNPPPFSFA--DGIDSIAISGHKFI 233
Glu-decarb-GAD TIGR01788
glutamate decarboxylase; This model represents the pyridoxal phosphate-dependent glutamate ...
109-425 1.67e-03

glutamate decarboxylase; This model represents the pyridoxal phosphate-dependent glutamate (alpha) decarboxylase found in bacteria (low and hi-GC gram positive, proteobacteria and cyanobacteria), plants, fungi and at least one archaon (Methanosarcina). The product of the enzyme is gamma-aminobutyrate (GABA).


Pssm-ID: 130848  Cd Length: 431  Bit Score: 39.31  E-value: 1.67e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160420189  109 PACTELETVMLDWLGKMIGLPeqflaGNKGEGGGVIQGTASEATLMALLAARTKVTRRLQAENPKLTEAEIVSrmvaysS 188
Cdd:TIGR01788  76 PQTAEIENRCVNMLADLWHAP-----AKDAEAVGTSTIGSSEAIMLGGLAMKWRWRKRMEAAGKPTDKPNLVM------G 144
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160420189  189 DQAHSSVERAGLISGVRMKKIPSD-EKFVARGQALKKALEEDKaeglipIFFCATLGTTNSCAFDNLMELGPVC---NAE 264
Cdd:TIGR01788 145 SNVQVCWEKFARYFDVELREVPMDpGRYVIDPEQVVEAVDENT------IGVVCILGTTYTGEYEDVKALNDALdeyNAK 218
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160420189  265 ---NIWMHIDAAYAGsaFICPeFRYLMEGVEF----ADSFNFNPHKWLLVNFDCSafWVKKRS------DLIgaFKMDpv 331
Cdd:TIGR01788 219 tgwDIPIHVDAASGG--FIAP-FVYPDLEWDFrlprVKSINVSGHKYGLVYPGVG--WVIWRDeealpeELI--FHVN-- 289
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160420189  332 YLQYDQQESGLVTDYRHWQIpLGRRFRSLKLWFvfriYGVKGLQAHIRKhvgLAHEFLECVKKDELFEI-CAPVILGLVC 410
Cdd:TIGR01788 290 YLGGDEPTFTLNFSRPANQV-IAQYYNFLRLGR----EGYRKIMQNSLD---VARYLAEEIAKLGPFEIiSDGSGIPLVA 361
                         330
                  ....*....|....*
gi 160420189  411 FRLKGSNELNKALLQ 425
Cdd:TIGR01788 362 FKLKDDADPGYTLYD 376
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.11
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Marchler-Bauer A et al. (2011), "CDD: a Conserved Domain Database for the functional annotation of proteins.", Nucleic Acids Res.39(D)225-9.
  • Marchler-Bauer A et al. (2009), "CDD: specific functional annotation with the Conserved Domain Database.", Nucleic Acids Res.37(D)205-10.
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