|
Name |
Accession |
Description |
Interval |
E-value |
| GadA |
COG0076 |
Glutamate or tyrosine decarboxylase or a related PLP-dependent protein [Amino acid transport ... |
48-390 |
1.55e-117 |
|
Glutamate or tyrosine decarboxylase or a related PLP-dependent protein [Amino acid transport and metabolism]; Glutamate or tyrosine decarboxylase or a related PLP-dependent protein is part of the Pathway/BioSystem: Pantothenate/CoA biosynthesis
Pssm-ID: 439846 [Multi-domain] Cd Length: 460 Bit Score: 349.52 E-value: 1.55e-117
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1315690831 48 EPEELKQLLDLELQSQGESREQILER-CRTVIHYSVKTGHPRFFNQLFSGLDPHALAGRIITESLNTSQYTYEIAPVFVL 126
Cdd:COG0076 28 SPEELRAALDEPLPEEGLPPEEALAElEDLVLPGSVDWNHPRFLAFVTGGTTPAALAADLLASALNQNMGDWDTSPAATE 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1315690831 127 MEEEVLKKLRALVGW-NSGDGVFCPGGSISNMYAMNLARFQRYP-DCKQRGLRALPPLALFTSKECHYSITKGAAFLGLG 204
Cdd:COG0076 108 LEREVVRWLADLLGLpEGAGGVFTSGGTEANLLALLAARDRALArRVRAEGLPGAPRPRIVVSEEAHSSVDKAARLLGLG 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1315690831 205 TDSVRVVKADERGRMIPEDLERQIILAEAEGSVPFLVSATSGTTVLGAFDPLDAIADVCQRHGLWFHVDAAWGGSVLLSR 284
Cdd:COG0076 188 RDALRKVPVDEDGRMDPDALEAAIDEDRAAGLNPIAVVATAGTTNTGAIDPLAEIADIAREHGLWLHVDAAYGGFALPSP 267
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1315690831 285 THRHLLDGIQRADSVAWNPHKLLAAGLQCSALLLRDTSnLLKRCHGSQASYLFQQDkfyDVALDTGDKVVQCGRRVDCLK 364
Cdd:COG0076 268 ELRHLLDGIERADSITVDPHKWLYVPYGCGAVLVRDPE-LLREAFSFHASYLGPAD---DGVPNLGDYTLELSRRFRALK 343
|
330 340
....*....|....*....|....*.
gi 1315690831 365 LWLMWKAQGGQGLERRIDQAFALTRW 390
Cdd:COG0076 344 LWATLRALGREGYRELIERCIDLARY 369
|
|
| Pyridoxal_deC |
pfam00282 |
Pyridoxal-dependent decarboxylase conserved domain; |
49-382 |
3.15e-111 |
|
Pyridoxal-dependent decarboxylase conserved domain;
Pssm-ID: 395219 Cd Length: 373 Bit Score: 330.53 E-value: 3.15e-111
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1315690831 49 PEELKQLLDLELQSQGESREQILERCRTVIHYSVKTGH-PRFFNQLFSGLDPHALAGRIITESLNTSQYTYEIAPVFVLM 127
Cdd:pfam00282 1 PGYLKPLLPLAAPIIPEPELQIDGDIRRNLMPGVTTWHsPHFHAYMPTGNSYPSLLGDMLTDAINCNGFTWESSPACTEL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1315690831 128 EEEVLKKLRALVGW------NSGDGVFCPGGSISNMYAMNLARFQRYPDCKQRGLRALPP-----LALFTSKECHYSITK 196
Cdd:pfam00282 81 ENVVMNWLGEMLGLpaeflgQEGGGVLQPGSSESNLLALLAARTKWIKRMKAAGKPADSSgilakLVAYTSDQAHSSIEK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1315690831 197 GAAFLGLGtdsVRVVKADERGRMIPEDLERQIILAEAEGSVPFLVSATSGTTVLGAFDPLDAIADVCQRHGLWFHVDAAW 276
Cdd:pfam00282 161 AALYGGVK---LREIPSDDNGKMRGMDLEKAIEEDKENGLIPFFVVATLGTTGSGAFDDLQELGDICAKHNLWLHVDAAY 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1315690831 277 GGSVLLSRTHRHLLDGIQRADSVAWNPHKLLAAGLQCSALLLRDtSNLLKRCHGSQASYLFQQDKFYdvalDTGDKVVQC 356
Cdd:pfam00282 238 GGSAFICPEFRHWLFGIERADSITFNPHKWMLVLLDCSAVWVKD-KEALQQAFQFNPLYLGHTDSAY----DTGHKQIPL 312
|
330 340
....*....|....*....|....*.
gi 1315690831 357 GRRVDCLKLWLMWKAQGGQGLERRID 382
Cdd:pfam00282 313 SRRFRILKLWFVIRSLGVEGLQNQIR 338
|
|
| DOPA_deC_like |
cd06450 |
DOPA decarboxylase family. This family belongs to pyridoxal phosphate (PLP)-dependent ... |
89-390 |
1.17e-101 |
|
DOPA decarboxylase family. This family belongs to pyridoxal phosphate (PLP)-dependent aspartate aminotransferase superfamily (fold I). The major groups in this CD correspond to DOPA/tyrosine decarboxylase (DDC), histidine decarboxylase (HDC), and glutamate decarboxylase (GDC). DDC is active as a dimer and catalyzes the decarboxylation of tyrosine. GDC catalyzes the decarboxylation of glutamate and HDC catalyzes the decarboxylation of histidine.
Pssm-ID: 99743 [Multi-domain] Cd Length: 345 Bit Score: 304.90 E-value: 1.17e-101
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1315690831 89 FFNQLFSGLDPHALAGRIITESLNTSQYTYEIAPVFVLMEEEVLKKLRALVGWNS--GDGVFCPGGSISNMYAMNLARFQ 166
Cdd:cd06450 1 FLAGFVTTMDPPALLLEMLTSAKNAIDFTWDESPAATEMEAEVVNWLAKLFGLPSedADGVFTSGGSESNLLALLAARDR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1315690831 167 RYPDCKQRGLRALPPLALFTSKECHYSITKGAAFLGlgtDSVRVVKADERGRMIPEDLERQIILAEAEGSVPFLVSATSG 246
Cdd:cd06450 81 ARKRLKAGGGRGIDKLVIVCSDQAHVSVEKAAAYLD---VKVRLVPVDEDGRMDPEALEAAIDEDKAEGLNPIMVVATAG 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1315690831 247 TTVLGAFDPLDAIADVCQRHGLWFHVDAAWGGSVLLSRTHRHLLDGIQRADSVAWNPHKLLAAGLQCSALLLRdtsnllk 326
Cdd:cd06450 158 TTDTGAIDPLEEIADLAEKYDLWLHVDAAYGGFLLPFPEPRHLDFGIERVDSISVDPHKYGLVPLGCSAVLVR------- 230
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1315690831 327 rchgsqasylfqqdkfydvaldtgdkvvqcgrrvdCLKLWLMWKAQGGQGLERRIDQAFALTRW 390
Cdd:cd06450 231 -----------------------------------ALKLWATLRRFGRDGYGEHIDRIVDLAKY 259
|
|
| NOD_PanD_pyr |
TIGR03799 |
putative pyridoxal-dependent aspartate 1-decarboxylase; This enzyme is proposed here to be a ... |
76-311 |
3.65e-44 |
|
putative pyridoxal-dependent aspartate 1-decarboxylase; This enzyme is proposed here to be a form of aspartate 1-decarboxylase, pyridoxal-dependent, that represents a non-orthologous displacement to the more widely distributed pyruvoyl-dependent form (TIGR00223). Aspartate 1-decarboxylase makes beta-alanine, used usually in pathothenate biosynthesis, by decarboxylation from asparatate. A number of species with the PanB and PanC enzymes, however, lack PanD. This protein family occurs in a number of Proteobacteria that lack PanD. This enzyme family appears to be a pyridoxal-dependent enzyme (see pfam00282). The family was identified by Partial Phylogenetic Profiling; members in Geobacter sulfurreducens, G. metallireducens, and Pseudoalteromonas atlantica are clustered with the genes for PanB and PanC. We suggest the gene symbol panP (panthothenate biosynthesis enzyme, Pyridoxal-dependent). [Biosynthesis of cofactors, prosthetic groups, and carriers, Pantothenate and coenzyme A]
Pssm-ID: 274791 Cd Length: 522 Bit Score: 160.29 E-value: 3.65e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1315690831 76 TVIHYSVKTGHPRFFNQLFSGLDPHALAGRIITESLNTSQYTYEIAPVFVLMEEEVLKKLRALV---------GW-NSGD 145
Cdd:TIGR03799 79 KLVAHSVHTASPSFIGHMTSALPYFLLPLSKLMVGLNQNLVKIETSKAFTPLERQVLGMMHHLVyqqddsfyrRWmHSAD 158
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1315690831 146 ---GVFCPGGSISNMYAMNLARFQRY-PDCKQRGL------RAL-----PPLALFTSKECHYSITKGAAFLGLGTDSVRV 210
Cdd:TIGR03799 159 hslGAFCSGGTVANITALWVARNRLLkADGDFRGIareglfAALrhygyDGLAILVSERGHYSLGKAADVLGIGRDNLVP 238
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1315690831 211 VKADERGRMIPEDLERQIILAEAEGSVPFLVSATSGTTVLGAFDPLDAIADVCQRHGLWFHVDAAWGGSVLLSRTHRHLL 290
Cdd:TIGR03799 239 VKTDENNRIRVDALRDKCLELAAQNIKPMAIVGVAGTTETGNIDPLDEMADIAQEAGCHFHVDAAWGGATLLSNTYRHLL 318
|
250 260
....*....|....*....|....*
gi 1315690831 291 DGIQRADSVAWNPHKLL----AAGL 311
Cdd:TIGR03799 319 KGIERADSVTIDAHKQMyvpmGAGM 343
|
|
| PLN02590 |
PLN02590 |
probable tyrosine decarboxylase |
48-381 |
3.16e-34 |
|
probable tyrosine decarboxylase
Pssm-ID: 178200 [Multi-domain] Cd Length: 539 Bit Score: 133.30 E-value: 3.16e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1315690831 48 EPEELKQLLDlelqsqgESREQILErcrTVIHYSvktgHPRFFNQLFSGLDPHALAGRIITESLNTSQYTYEIAPVFVLM 127
Cdd:PLN02590 106 RPESLKELLD-------DVSKKIMP---GITHWQ----SPSYFAYYASSTSVAGFLGEMLNAGLSVVGFTWLTSPAATEL 171
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1315690831 128 EEEVLKKLRALV-------GWNSGDGVFcPGGSISNMYAMNLARFQRYpdCKQRGLRALPPLALFTSKECHYSITKGAAF 200
Cdd:PLN02590 172 EIIVLDWLAKLLqlpdhflSTGNGGGVI-QGTGCEAVLVVVLAARDRI--LKKVGKTLLPQLVVYGSDQTHSSFRKACLI 248
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1315690831 201 LGLGTDSVRVVKADERGR--MIPEDLERQIILAEAEGSVPFLVSATSGTTVLGAFDPLDAIADVCQRHGLWFHVDAAWGG 278
Cdd:PLN02590 249 GGIHEENIRLLKTDSSTNygMPPESLEEAISHDLAKGFIPFFICATVGTTSSAAVDPLVPLGNIAKKYGIWLHVDAAYAG 328
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1315690831 279 SVLLSRTHRHLLDGIQRADSVAWNPHKLLAAGLQCSALLLRDTSNLLKRCHGSQASYLFQQDKfYDVALDTGDKVVQCGR 358
Cdd:PLN02590 329 NACICPEYRKFIDGIENADSFNMNAHKWLFANQTCSPLWVKDRYSLIDALKTNPEYLEFKVSK-KDTVVNYKDWQISLSR 407
|
330 340
....*....|....*....|...
gi 1315690831 359 RVDCLKLWLMWKAQGGQGLERRI 381
Cdd:PLN02590 408 RFRSLKLWMVLRLYGSENLRNFI 430
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| GadA |
COG0076 |
Glutamate or tyrosine decarboxylase or a related PLP-dependent protein [Amino acid transport ... |
48-390 |
1.55e-117 |
|
Glutamate or tyrosine decarboxylase or a related PLP-dependent protein [Amino acid transport and metabolism]; Glutamate or tyrosine decarboxylase or a related PLP-dependent protein is part of the Pathway/BioSystem: Pantothenate/CoA biosynthesis
Pssm-ID: 439846 [Multi-domain] Cd Length: 460 Bit Score: 349.52 E-value: 1.55e-117
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1315690831 48 EPEELKQLLDLELQSQGESREQILER-CRTVIHYSVKTGHPRFFNQLFSGLDPHALAGRIITESLNTSQYTYEIAPVFVL 126
Cdd:COG0076 28 SPEELRAALDEPLPEEGLPPEEALAElEDLVLPGSVDWNHPRFLAFVTGGTTPAALAADLLASALNQNMGDWDTSPAATE 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1315690831 127 MEEEVLKKLRALVGW-NSGDGVFCPGGSISNMYAMNLARFQRYP-DCKQRGLRALPPLALFTSKECHYSITKGAAFLGLG 204
Cdd:COG0076 108 LEREVVRWLADLLGLpEGAGGVFTSGGTEANLLALLAARDRALArRVRAEGLPGAPRPRIVVSEEAHSSVDKAARLLGLG 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1315690831 205 TDSVRVVKADERGRMIPEDLERQIILAEAEGSVPFLVSATSGTTVLGAFDPLDAIADVCQRHGLWFHVDAAWGGSVLLSR 284
Cdd:COG0076 188 RDALRKVPVDEDGRMDPDALEAAIDEDRAAGLNPIAVVATAGTTNTGAIDPLAEIADIAREHGLWLHVDAAYGGFALPSP 267
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1315690831 285 THRHLLDGIQRADSVAWNPHKLLAAGLQCSALLLRDTSnLLKRCHGSQASYLFQQDkfyDVALDTGDKVVQCGRRVDCLK 364
Cdd:COG0076 268 ELRHLLDGIERADSITVDPHKWLYVPYGCGAVLVRDPE-LLREAFSFHASYLGPAD---DGVPNLGDYTLELSRRFRALK 343
|
330 340
....*....|....*....|....*.
gi 1315690831 365 LWLMWKAQGGQGLERRIDQAFALTRW 390
Cdd:COG0076 344 LWATLRALGREGYRELIERCIDLARY 369
|
|
| Pyridoxal_deC |
pfam00282 |
Pyridoxal-dependent decarboxylase conserved domain; |
49-382 |
3.15e-111 |
|
Pyridoxal-dependent decarboxylase conserved domain;
Pssm-ID: 395219 Cd Length: 373 Bit Score: 330.53 E-value: 3.15e-111
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1315690831 49 PEELKQLLDLELQSQGESREQILERCRTVIHYSVKTGH-PRFFNQLFSGLDPHALAGRIITESLNTSQYTYEIAPVFVLM 127
Cdd:pfam00282 1 PGYLKPLLPLAAPIIPEPELQIDGDIRRNLMPGVTTWHsPHFHAYMPTGNSYPSLLGDMLTDAINCNGFTWESSPACTEL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1315690831 128 EEEVLKKLRALVGW------NSGDGVFCPGGSISNMYAMNLARFQRYPDCKQRGLRALPP-----LALFTSKECHYSITK 196
Cdd:pfam00282 81 ENVVMNWLGEMLGLpaeflgQEGGGVLQPGSSESNLLALLAARTKWIKRMKAAGKPADSSgilakLVAYTSDQAHSSIEK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1315690831 197 GAAFLGLGtdsVRVVKADERGRMIPEDLERQIILAEAEGSVPFLVSATSGTTVLGAFDPLDAIADVCQRHGLWFHVDAAW 276
Cdd:pfam00282 161 AALYGGVK---LREIPSDDNGKMRGMDLEKAIEEDKENGLIPFFVVATLGTTGSGAFDDLQELGDICAKHNLWLHVDAAY 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1315690831 277 GGSVLLSRTHRHLLDGIQRADSVAWNPHKLLAAGLQCSALLLRDtSNLLKRCHGSQASYLFQQDKFYdvalDTGDKVVQC 356
Cdd:pfam00282 238 GGSAFICPEFRHWLFGIERADSITFNPHKWMLVLLDCSAVWVKD-KEALQQAFQFNPLYLGHTDSAY----DTGHKQIPL 312
|
330 340
....*....|....*....|....*.
gi 1315690831 357 GRRVDCLKLWLMWKAQGGQGLERRID 382
Cdd:pfam00282 313 SRRFRILKLWFVIRSLGVEGLQNQIR 338
|
|
| DOPA_deC_like |
cd06450 |
DOPA decarboxylase family. This family belongs to pyridoxal phosphate (PLP)-dependent ... |
89-390 |
1.17e-101 |
|
DOPA decarboxylase family. This family belongs to pyridoxal phosphate (PLP)-dependent aspartate aminotransferase superfamily (fold I). The major groups in this CD correspond to DOPA/tyrosine decarboxylase (DDC), histidine decarboxylase (HDC), and glutamate decarboxylase (GDC). DDC is active as a dimer and catalyzes the decarboxylation of tyrosine. GDC catalyzes the decarboxylation of glutamate and HDC catalyzes the decarboxylation of histidine.
Pssm-ID: 99743 [Multi-domain] Cd Length: 345 Bit Score: 304.90 E-value: 1.17e-101
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1315690831 89 FFNQLFSGLDPHALAGRIITESLNTSQYTYEIAPVFVLMEEEVLKKLRALVGWNS--GDGVFCPGGSISNMYAMNLARFQ 166
Cdd:cd06450 1 FLAGFVTTMDPPALLLEMLTSAKNAIDFTWDESPAATEMEAEVVNWLAKLFGLPSedADGVFTSGGSESNLLALLAARDR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1315690831 167 RYPDCKQRGLRALPPLALFTSKECHYSITKGAAFLGlgtDSVRVVKADERGRMIPEDLERQIILAEAEGSVPFLVSATSG 246
Cdd:cd06450 81 ARKRLKAGGGRGIDKLVIVCSDQAHVSVEKAAAYLD---VKVRLVPVDEDGRMDPEALEAAIDEDKAEGLNPIMVVATAG 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1315690831 247 TTVLGAFDPLDAIADVCQRHGLWFHVDAAWGGSVLLSRTHRHLLDGIQRADSVAWNPHKLLAAGLQCSALLLRdtsnllk 326
Cdd:cd06450 158 TTDTGAIDPLEEIADLAEKYDLWLHVDAAYGGFLLPFPEPRHLDFGIERVDSISVDPHKYGLVPLGCSAVLVR------- 230
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1315690831 327 rchgsqasylfqqdkfydvaldtgdkvvqcgrrvdCLKLWLMWKAQGGQGLERRIDQAFALTRW 390
Cdd:cd06450 231 -----------------------------------ALKLWATLRRFGRDGYGEHIDRIVDLAKY 259
|
|
| NOD_PanD_pyr |
TIGR03799 |
putative pyridoxal-dependent aspartate 1-decarboxylase; This enzyme is proposed here to be a ... |
76-311 |
3.65e-44 |
|
putative pyridoxal-dependent aspartate 1-decarboxylase; This enzyme is proposed here to be a form of aspartate 1-decarboxylase, pyridoxal-dependent, that represents a non-orthologous displacement to the more widely distributed pyruvoyl-dependent form (TIGR00223). Aspartate 1-decarboxylase makes beta-alanine, used usually in pathothenate biosynthesis, by decarboxylation from asparatate. A number of species with the PanB and PanC enzymes, however, lack PanD. This protein family occurs in a number of Proteobacteria that lack PanD. This enzyme family appears to be a pyridoxal-dependent enzyme (see pfam00282). The family was identified by Partial Phylogenetic Profiling; members in Geobacter sulfurreducens, G. metallireducens, and Pseudoalteromonas atlantica are clustered with the genes for PanB and PanC. We suggest the gene symbol panP (panthothenate biosynthesis enzyme, Pyridoxal-dependent). [Biosynthesis of cofactors, prosthetic groups, and carriers, Pantothenate and coenzyme A]
Pssm-ID: 274791 Cd Length: 522 Bit Score: 160.29 E-value: 3.65e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1315690831 76 TVIHYSVKTGHPRFFNQLFSGLDPHALAGRIITESLNTSQYTYEIAPVFVLMEEEVLKKLRALV---------GW-NSGD 145
Cdd:TIGR03799 79 KLVAHSVHTASPSFIGHMTSALPYFLLPLSKLMVGLNQNLVKIETSKAFTPLERQVLGMMHHLVyqqddsfyrRWmHSAD 158
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1315690831 146 ---GVFCPGGSISNMYAMNLARFQRY-PDCKQRGL------RAL-----PPLALFTSKECHYSITKGAAFLGLGTDSVRV 210
Cdd:TIGR03799 159 hslGAFCSGGTVANITALWVARNRLLkADGDFRGIareglfAALrhygyDGLAILVSERGHYSLGKAADVLGIGRDNLVP 238
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1315690831 211 VKADERGRMIPEDLERQIILAEAEGSVPFLVSATSGTTVLGAFDPLDAIADVCQRHGLWFHVDAAWGGSVLLSRTHRHLL 290
Cdd:TIGR03799 239 VKTDENNRIRVDALRDKCLELAAQNIKPMAIVGVAGTTETGNIDPLDEMADIAQEAGCHFHVDAAWGGATLLSNTYRHLL 318
|
250 260
....*....|....*....|....*
gi 1315690831 291 DGIQRADSVAWNPHKLL----AAGL 311
Cdd:TIGR03799 319 KGIERADSVTIDAHKQMyvpmGAGM 343
|
|
| PLN02590 |
PLN02590 |
probable tyrosine decarboxylase |
48-381 |
3.16e-34 |
|
probable tyrosine decarboxylase
Pssm-ID: 178200 [Multi-domain] Cd Length: 539 Bit Score: 133.30 E-value: 3.16e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1315690831 48 EPEELKQLLDlelqsqgESREQILErcrTVIHYSvktgHPRFFNQLFSGLDPHALAGRIITESLNTSQYTYEIAPVFVLM 127
Cdd:PLN02590 106 RPESLKELLD-------DVSKKIMP---GITHWQ----SPSYFAYYASSTSVAGFLGEMLNAGLSVVGFTWLTSPAATEL 171
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1315690831 128 EEEVLKKLRALV-------GWNSGDGVFcPGGSISNMYAMNLARFQRYpdCKQRGLRALPPLALFTSKECHYSITKGAAF 200
Cdd:PLN02590 172 EIIVLDWLAKLLqlpdhflSTGNGGGVI-QGTGCEAVLVVVLAARDRI--LKKVGKTLLPQLVVYGSDQTHSSFRKACLI 248
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1315690831 201 LGLGTDSVRVVKADERGR--MIPEDLERQIILAEAEGSVPFLVSATSGTTVLGAFDPLDAIADVCQRHGLWFHVDAAWGG 278
Cdd:PLN02590 249 GGIHEENIRLLKTDSSTNygMPPESLEEAISHDLAKGFIPFFICATVGTTSSAAVDPLVPLGNIAKKYGIWLHVDAAYAG 328
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1315690831 279 SVLLSRTHRHLLDGIQRADSVAWNPHKLLAAGLQCSALLLRDTSNLLKRCHGSQASYLFQQDKfYDVALDTGDKVVQCGR 358
Cdd:PLN02590 329 NACICPEYRKFIDGIENADSFNMNAHKWLFANQTCSPLWVKDRYSLIDALKTNPEYLEFKVSK-KDTVVNYKDWQISLSR 407
|
330 340
....*....|....*....|...
gi 1315690831 359 RVDCLKLWLMWKAQGGQGLERRI 381
Cdd:PLN02590 408 RFRSLKLWMVLRLYGSENLRNFI 430
|
|
| PLN02880 |
PLN02880 |
tyrosine decarboxylase |
48-381 |
2.69e-32 |
|
tyrosine decarboxylase
Pssm-ID: 215475 [Multi-domain] Cd Length: 490 Bit Score: 127.33 E-value: 2.69e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1315690831 48 EPEELKQLLDLELQSQGESREQILERCRT-----VIHYSvktgHPRFFNQLFSGLDPHALAGRIITESLNTSQYTYEIAP 122
Cdd:PLN02880 43 QPGYLRELLPDSAPNQPETLDQVLDDVQAkilpgVTHWQ----SPNYFAYYPSNSSVAGFLGEMLSAGLNIVGFSWITSP 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1315690831 123 VFVLMEEEVLKKLRALVGWNS-------GDGVFCPGGSISNMYAMNLARFQRYpdcKQRGLRALPPLALFTSKECHYSIT 195
Cdd:PLN02880 119 AATELEMIVLDWLAKLLNLPEqflstgnGGGVIQGTASEAVLVVLLAARDRVL---RKVGKNALEKLVVYASDQTHSALQ 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1315690831 196 KGAAFLGLGTDSVRVVKADERGR--MIPEDLERQIILAEAEGSVPFLVSATSGTTVLGAFDPLDAIADVCQRHGLWFHVD 273
Cdd:PLN02880 196 KACQIAGIHPENCRLLKTDSSTNyaLAPELLSEAISTDLSSGLIPFFLCATVGTTSSTAVDPLLELGKIAKSNGMWFHVD 275
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1315690831 274 AAWGGSVLLSRTHRHLLDGIQRADSVAWNPHKLLAAGLQCSALLLRDTSNLLKRChGSQASYLFQQDKFYDVALDTGDKV 353
Cdd:PLN02880 276 AAYAGSACICPEYRHYIDGVEEADSFNMNAHKWFLTNFDCSLLWVKDRNALIQSL-STNPEFLKNKASQANSVVDYKDWQ 354
|
330 340
....*....|....*....|....*...
gi 1315690831 354 VQCGRRVDCLKLWLMWKAQGGQGLERRI 381
Cdd:PLN02880 355 IPLGRRFRSLKLWMVLRLYGVENLQSYI 382
|
|
| PRK02769 |
PRK02769 |
histidine decarboxylase; Provisional |
68-319 |
3.59e-15 |
|
histidine decarboxylase; Provisional
Pssm-ID: 235068 [Multi-domain] Cd Length: 380 Bit Score: 76.23 E-value: 3.59e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1315690831 68 EQILERCRtvIHYSVKTGHPrfFNQLFSgldpHALAGRIITESLNTSQYTYEiAPVFVL----MEEEVLKKLRALVG--W 141
Cdd:PRK02769 12 EDFWLYLR--HNQYFNVGYP--EAADFD----YSALKRFFSFSINNCGDPYS-KSNYPLnsfdFERDVMNFFAELFKipF 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1315690831 142 NSGDGVFCPGGSISNMYAMNLARfQRYPDCkqrglralpplALFTSKECHYSITKGAAFLGLGTdsvRVVKADERGRMIP 221
Cdd:PRK02769 83 NESWGYITNGGTEGNLYGCYLAR-ELFPDG-----------TLYYSKDTHYSVSKIARLLRIKS---RVITSLPNGEIDY 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1315690831 222 EDLERQIilaEAEGSVPFLVSATSGTTVLGAFDPLDAIADVCQRHGL---WFHVDAAWGGSVLLSRTHRHLLDGIQRADS 298
Cdd:PRK02769 148 DDLISKI---KENKNQPPIIFANIGTTMTGAIDNIKEIQEILKKIGIddyYIHADAALSGMILPFVNNPPPFSFADGIDS 224
|
250 260
....*....|....*....|.
gi 1315690831 299 VAWNPHKLLAAGLQCSALLLR 319
Cdd:PRK02769 225 IAISGHKFIGSPMPCGIVLAK 245
|
|
| AAT_I |
cd01494 |
Aspartate aminotransferase (AAT) superfamily (fold type I) of pyridoxal phosphate (PLP) ... |
128-309 |
1.43e-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: 1.43e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1315690831 128 EEEVLKKLRALVGWNSGDGVFCPGGSISN-MYAMNLArfqrypdckQRGLRALPPLALFTSkecHYSITKGAAFLGlgtd 206
Cdd:cd01494 2 LEELEEKLARLLQPGNDKAVFVPSGTGANeAALLALL---------GPGDEVIVDANGHGS---RYWVAAELAGAK---- 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1315690831 207 sVRVVKADERGRMIpedLERQIILAEAEGSVPFLVSATSGTTVLGAFDPLDAIADVCQRHGLWFHVDAAWGGsvlLSRTH 286
Cdd:cd01494 66 -PVPVPVDDAGYGG---LDVAILEELKAKPNVALIVITPNTTSGGVLVPLKEIRKIAKEYGILLLVDAASAG---GASPA 138
|
170 180
....*....|....*....|...
gi 1315690831 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 |
2.78e-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: 2.78e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1315690831 129 EEVLKKLRALVGWNSGDG-VFCPGGSIS-NMYAMNLARFQRYPDCkqrglralpplALFTSKEcHYSITKGAAFLG--LG 204
Cdd:pfam00266 46 EEAREKVAEFINAPSNDEiIFTSGTTEAiNLVALSLGRSLKPGDE-----------IVITEME-HHANLVPWQELAkrTG 113
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1315690831 205 TDsVRVVKADERGRMIPEDLERQIilaeAEGSVpfLVSATSGTTVLGAFDPLDAIADVCQRHGLWFHVDAA 275
Cdd:pfam00266 114 AR-VRVLPLDEDGLLDLDELEKLI----TPKTK--LVAITHVSNVTGTIQPVPEIGKLAHQYGALVLVDAA 177
|
|
| PLN03032 |
PLN03032 |
serine decarboxylase; Provisional |
175-319 |
2.62e-06 |
|
serine decarboxylase; Provisional
Pssm-ID: 166673 [Multi-domain] Cd Length: 374 Bit Score: 49.05 E-value: 2.62e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1315690831 175 GLRALPPLALFTSKECHYSITKGAAFLGLGTDSVRVVkadERGRMIPEDLERQIilAEAEGSvPFLVSATSGTTVLGAFD 254
Cdd:PLN03032 105 GREVFPDGILYASRESHYSVFKAARMYRMEAVKVPTL---PSGEIDYDDLERAL--AKNRDK-PAILNVNIGTTVKGAVD 178
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1315690831 255 PLDAIADVCQRHG-----LWFHVDAAWGGSVLLSRTHRHLLDGIQRADSVAWNPHKLLAAGLQCSALLLR 319
Cdd:PLN03032 179 DLDRILRILKELGytedrFYIHCDGALFGLMMPFVSRAPEVTFRKPIGSVSVSGHKFLGCPMPCGVALTR 248
|
|
| CsdA |
COG0520 |
Selenocysteine lyase/Cysteine desulfurase [Amino acid transport and metabolism]; |
208-308 |
3.10e-06 |
|
Selenocysteine lyase/Cysteine desulfurase [Amino acid transport and metabolism];
Pssm-ID: 440286 [Multi-domain] Cd Length: 396 Bit Score: 48.98 E-value: 3.10e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1315690831 208 VRVVKADERGRMIPEDLERQIilaeaeGSVPFLVSATSGTTVLGAFDPLDAIADVCQRHGLWFHVDAAwgGSVllsrTHR 287
Cdd:COG0520 131 VRVIPLDEDGELDLEALEALL------TPRTKLVAVTHVSNVTGTVNPVKEIAALAHAHGALVLVDGA--QSV----PHL 198
|
90 100
....*....|....*....|....*
gi 1315690831 288 HL----LDgiqrADSVAWNPHKLLA 308
Cdd:COG0520 199 PVdvqaLG----CDFYAFSGHKLYG 219
|
|
| TA_like |
cd06502 |
Low-specificity threonine aldolase (TA). This family belongs to pyridoxal phosphate (PLP) ... |
128-275 |
1.51e-05 |
|
Low-specificity threonine aldolase (TA). This family belongs to pyridoxal phosphate (PLP)-dependent aspartate aminotransferase superfamily (fold I). TA catalyzes the conversion of L-threonine or L-allo-threonine to glycine and acetaldehyde in a secondary glycine biosynthetic pathway.
Pssm-ID: 99748 [Multi-domain] Cd Length: 338 Bit Score: 46.56 E-value: 1.51e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1315690831 128 EEEVLKKLRALVGWNSGD--GVFCPGGSISNmyamnlarfqrypdckQRGLRAL--PPLALFTSKECHYSI--TKGAAFL 201
Cdd:cd06502 30 EDPTTAKLEARAAELFGKeaALFVPSGTAAN----------------QLALAAHtqPGGSVICHETAHIYTdeAGAPEFL 93
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1315690831 202 GlgtdSVRVVKAD-ERGRMIPEDLERQIILAEAEGSV-PFLVSATSgTTVLGAFDPLD---AIADVCQRHGLWFHVDAA 275
Cdd:cd06502 94 S----GVKLLPVPgENGKLTPEDLEAAIRPRDDIHFPpPSLVSLEN-TTEGGTVYPLDelkAISALAKENGLPLHLDGA 167
|
|
| GLY1 |
COG2008 |
Threonine aldolase [Amino acid transport and metabolism]; |
134-276 |
3.65e-05 |
|
Threonine aldolase [Amino acid transport and metabolism];
Pssm-ID: 441611 [Multi-domain] Cd Length: 333 Bit Score: 45.44 E-value: 3.65e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1315690831 134 KLRALVGwnSGDGVFCPGGSISNMyamnLArfqrypdckqrgLRAL-PPL-ALFTSKECHYSI--TKGAAFL-GLgtdSV 208
Cdd:COG2008 43 RVAELFG--KEAALFVPSGTMANQ----LA------------LRAHtRPGdEVICHETAHIYVdeGGAPEALsGV---KL 101
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1315690831 209 RVVkADERGRMIPEDLERQIILAEAEGSVPFLVS---ATSGTTVLgAFDPLDAIADVCQRHGLWFHVDAAW 276
Cdd:COG2008 102 LPV-PGEDGKLTPEDLEAAIRPGDVHFPQPGLVSlenTTEGGTVY-PLEELRAIAAVAREHGLPLHLDGAR 170
|
|
| NifS |
COG1104 |
Cysteine desulfurase/Cysteine sulfinate desulfinase IscS or related enzyme, NifS family [Amino ... |
129-275 |
8.09e-05 |
|
Cysteine desulfurase/Cysteine sulfinate desulfinase IscS or related enzyme, NifS family [Amino acid transport and metabolism];
Pssm-ID: 440721 [Multi-domain] Cd Length: 381 Bit Score: 44.27 E-value: 8.09e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1315690831 129 EEVLKKLRALVGWNSGDGVFCPGGSISNmyamNLA---RFQRYPDCKQRglralpplaLFTSK-EcHYSITKGAAFL-GL 203
Cdd:COG1104 48 EEAREQVAALLGADPEEIIFTSGGTEAN----NLAikgAARAYRKKGKH---------IITSAiE-HPAVLETARFLeKE 113
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1315690831 204 GTDsVRVVKADERGRMIPEDLERQIilaeAEGSVpfLVSATSGTTVLGAFDPLDAIADVCQRHGLWFHVDAA 275
Cdd:COG1104 114 GFE-VTYLPVDEDGRVDLEALEAAL----RPDTA--LVSVMHANNETGTIQPIAEIAEIAKEHGVLFHTDAV 178
|
|
| PLN02263 |
PLN02263 |
serine decarboxylase |
175-278 |
1.01e-04 |
|
serine decarboxylase
Pssm-ID: 177904 [Multi-domain] Cd Length: 470 Bit Score: 44.42 E-value: 1.01e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1315690831 175 GLRALPPLALFTSKECHYSITKGAAFLglgtdSVRVVKAD--ERGRMIPEDLERQIIlaeAEGSVPFLVSATSGTTVLGA 252
Cdd:PLN02263 172 GREVFPDGILYASRESHYSVFKAARMY-----RMECVKVDtlVSGEIDCADFKAKLL---ANKDKPAIINVNIGTTVKGA 243
|
90 100 110
....*....|....*....|....*....|.
gi 1315690831 253 FDPLDAIADVCQRHG-----LWFHVDAAWGG 278
Cdd:PLN02263 244 VDDLDLVIKTLEECGfsqdrFYIHCDGALFG 274
|
|
| Orn_deC_like |
cd00615 |
Ornithine decarboxylase family. This family belongs to pyridoxal phosphate (PLP)-dependent ... |
256-338 |
4.24e-04 |
|
Ornithine decarboxylase family. This family belongs to pyridoxal phosphate (PLP)-dependent aspartate aminotransferase superfamily (fold I). The major groups in this CD corresponds to ornithine decarboxylase (ODC), arginine decarboxylase (ADC) and lysine decarboxylase (LDC). ODC is a dodecamer composed of six homodimers and catalyzes the decarboxylation of tryptophan. ADC catalyzes the decarboxylation of arginine and LDC catalyzes the decarboxylation of lysine. Members of this family are widely found in all three forms of life.
Pssm-ID: 99739 [Multi-domain] Cd Length: 294 Bit Score: 41.85 E-value: 4.24e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1315690831 256 LDAIADVCQRHGLWFHVDAAWGGsvllsrtHRHLLDGIQR------ADSVAWNPHKLLAAGLQCSALLLRDtsNLLKRCH 329
Cdd:cd00615 172 LRKIVEEAHHRGLPVLVDEAHGA-------HFRFHPILPSsaamagADIVVQSTHKTLPALTQGSMIHVKG--DLVNPDR 242
|
....*....
gi 1315690831 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 |
4.84e-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: 4.84e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1315690831 207 SVRVVKADERGRMIPEDLERQIilaeaeGSVPFLVSATSGTTVLGAFDPLDAIADVCQRHGLWFHVDAA 275
Cdd:cd06453 115 KLKVVPVDDDGQLDLEALEKLL------TERTKLVAVTHVSNVLGTINPVKEIGEIAHEAGVPVLVDGA 177
|
|
| Beta_elim_lyase |
pfam01212 |
Beta-eliminating lyase; |
118-275 |
8.38e-04 |
|
Beta-eliminating lyase;
Pssm-ID: 426128 [Multi-domain] Cd Length: 288 Bit Score: 41.05 E-value: 8.38e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1315690831 118 YEIAPVFVLMEEEVlkklRALVGWNSGdgVFCPGGSISNmyamnlarfqrypdckQRGLRAL--PPLALFTSKECHYSI- 194
Cdd:pfam01212 28 YGGDPTVNRLEDRV----AELFGKEAA--LFVPSGTAAN----------------QLALMAHcqRGDEVICGEPAHIHFd 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1315690831 195 -TKGAAFLGLGTdsVRVVKADERGRMIPEDLERQIILAEAEGSVPF-LVSAT-----SGTTVLgAFDPLDAIADVCQRHG 267
Cdd:pfam01212 86 eTGGHAELGGVQ--PRPLDGDEAGNMDLEDLEAAIREVGADIFPPTgLISLEnthnsAGGQVV-SLENLREIAALAREHG 162
|
....*...
gi 1315690831 268 LWFHVDAA 275
Cdd:pfam01212 163 IPVHLDGA 170
|
|
| PLN02721 |
PLN02721 |
threonine aldolase |
146-299 |
9.99e-04 |
|
threonine aldolase
Pssm-ID: 178323 [Multi-domain] Cd Length: 353 Bit Score: 40.83 E-value: 9.99e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1315690831 146 GVFCPGGSISNMYAMNLarfqrypDCKQRGLRALpplalfTSKECHYSITKGAAFLGLGTDSVRVVKADERGRMIPEDLE 225
Cdd:PLN02721 58 ALFVPSGTMGNLISVLV-------HCDVRGSEVI------LGDNSHIHLYENGGISTLGGVHPRTVKNNEDGTMDLDAIE 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1315690831 226 RQIilaEAEGSVPFLVS---------ATSGTTVLGAfDPLDAIADVCQRHGLWFHVDAA--WGGSVLLSRTHRHLLdgiQ 294
Cdd:PLN02721 125 AAI---RPKGDDHFPTTrliclenthANCGGRCLSV-EYTDKVGELAKRHGLKLHIDGAriFNASVALGVPVHRLV---K 197
|
....*
gi 1315690831 295 RADSV 299
Cdd:PLN02721 198 AADSV 202
|
|
| LdcC |
COG1982 |
Arginine/lysine/ornithine decarboxylase [Amino acid transport and metabolism]; |
256-320 |
2.14e-03 |
|
Arginine/lysine/ornithine decarboxylase [Amino acid transport and metabolism];
Pssm-ID: 441585 [Multi-domain] Cd Length: 486 Bit Score: 40.09 E-value: 2.14e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1315690831 256 LDAIADVCQRHGLWFHVDAAWGGsvllsrtHRHLLDGIQR------ADSVAWNPHKLLAAGLQCSALLLRD 320
Cdd:COG1982 179 LKAIAELAHEHGIPVLVDEAHGA-------HFGFHPDLPRsameagADLVVQSTHKTLGALTQSSMLHVKG 242
|
|
| PLN02651 |
PLN02651 |
cysteine desulfurase |
129-275 |
3.65e-03 |
|
cysteine desulfurase
Pssm-ID: 178257 [Multi-domain] Cd Length: 364 Bit Score: 39.25 E-value: 3.65e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1315690831 129 EEVLKKLR----ALVGWNSGDGVFCPGGSISNMYAMNLArfqrypdckQRGLRALPPLALFTSKEcHYSITKGAAFLGLG 204
Cdd:PLN02651 42 EDAVEKARaqvaALIGADPKEIIFTSGATESNNLAIKGV---------MHFYKDKKKHVITTQTE-HKCVLDSCRHLQQE 111
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1315690831 205 TDSVRVVKADERGRMIPEDLERQIILAEAegsvpfLVSATSGTTVLGAFDPLDAIADVCQRHGLWFHVDAA 275
Cdd:PLN02651 112 GFEVTYLPVKSDGLVDLDELAAAIRPDTA------LVSVMAVNNEIGVIQPVEEIGELCREKKVLFHTDAA 176
|
|
| PRK02948 |
PRK02948 |
IscS subfamily cysteine desulfurase; |
133-274 |
3.85e-03 |
|
IscS subfamily cysteine desulfurase;
Pssm-ID: 179511 [Multi-domain] Cd Length: 381 Bit Score: 38.94 E-value: 3.85e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1315690831 133 KKLRALVGwNSGDGV-FCPGGSISNMYAMNlARFQRYPDCKQRglralpplaLFTSKECHYSITKGAAFLGLGTDSVRVV 211
Cdd:PRK02948 50 KTFAEMIG-GEEQGIyFTSGGTESNYLAIQ-SLLNALPQNKKH---------IITTPMEHASIHSYFQSLESQGYTVTEI 118
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1315690831 212 KADERGRMIPEDLERQIilaeAEGSVpfLVSATSGTTVLGAFDPLDAIADVCQRHGLWFHVDA 274
Cdd:PRK02948 119 PVDKSGLIRLVDLERAI----TPDTV--LASIQHANSEIGTIQPIAEIGALLKKYNVLFHSDC 175
|
|
| |
