|
Name |
Accession |
Description |
Interval |
E-value |
| GadA |
COG0076 |
Glutamate or tyrosine decarboxylase or a related PLP-dependent protein [Amino acid transport ... |
20-489 |
0e+00 |
|
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: 517.46 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2255892012 20 AYQQVIEQTSQAVVQWLKQ-PEMYQGKSVDELRERISLEFNEQGLGNQAAIDRAIEYFLKDSLSVHHPQCVAHLHCPSLV 98
Cdd:COG0076 1 EFRALLHQALDLAADYLAGlDRPVFGPSPEELRAALDEPLPEEGLPPEEALAELEDLVLPGSVDWNHPRFLAFVTGGTTP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2255892012 99 ISQAAEVLINATNQSMDSWDQSPSATIIEMKLIEWLRARVGFPAGDAGVFTSGGTQSNLMGLMLARDAFFARQghsIQQD 178
Cdd:COG0076 81 AALAADLLASALNQNMGDWDTSPAATELEREVVRWLADLLGLPEGAGGVFTSGGTEANLLALLAARDRALARR---VRAE 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2255892012 179 GLPGdIRKYKVLCSENAHFSVQKNMALMGLGYRSVTLVKTDEFARMDVSDLQAKIAQAQANGEQIMAIVATAGTTDAGAI 258
Cdd:COG0076 158 GLPG-APRPRIVVSEEAHSSVDKAARLLGLGRDALRKVPVDEDGRMDPDALEAAIDEDRAAGLNPIAVVATAGTTNTGAI 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2255892012 259 DPLRDIAGIAAEHQIWLHVDAAWGGALLLSKQYRDYLDGLELVDSVTLDFHKQFFQTISCGAFLLKDAR-HYELMRYQAA 337
Cdd:COG0076 237 DPLAEIADIAREHGLWLHVDAAYGGFALPSPELRHLLDGIERADSITVDPHKWLYVPYGCGAVLVRDPElLREAFSFHAS 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2255892012 338 YLNsefDEEHGVPNLVSKSLQTTRRFDALKLWMGLEALGQKQYAAIIDHGVTMAKNVAEYVKSQPTLELVMQPQLASVLF 417
Cdd:COG0076 317 YLG---PADDGVPNLGDYTLELSRRFRALKLWATLRALGREGYRELIERCIDLARYLAEGIAALPGFELLAPPELNIVCF 393
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2255892012 418 RSRPAQMAGSDAaaialLNQRVGDALLASGRANVGVTEHNGITCLKLTLLNPVVTLDDVKVLLNLVERTAQE 489
Cdd:COG0076 394 RYKPAGLDEEDA-----LNYALRDRLRARGRAFLSPTKLDGRVVLRLVVLNPRTTEDDVDALLDDLREAAAE 460
|
|
| DOPA_deC_like |
cd06450 |
DOPA decarboxylase family. This family belongs to pyridoxal phosphate (PLP)-dependent ... |
88-485 |
2.31e-118 |
|
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: 351.12 E-value: 2.31e-118
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2255892012 88 CVAHLHCPSLVISQAAEVLINATNQSMDSWDQSPSATIIEMKLIEWLRARVGFPAGDA-GVFTSGGTQSNLMGLMLARDA 166
Cdd:cd06450 1 FLAGFVTTMDPPALLLEMLTSAKNAIDFTWDESPAATEMEAEVVNWLAKLFGLPSEDAdGVFTSGGSESNLLALLAARDR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2255892012 167 FFARQghsiqQDGLPGDIRKYKVLCSENAHFSVQKNMALMGlgyRSVTLVKTDEFARMDVSDLQAKIAQAQANGEQIMAI 246
Cdd:cd06450 81 ARKRL-----KAGGGRGIDKLVIVCSDQAHVSVEKAAAYLD---VKVRLVPVDEDGRMDPEALEAAIDEDKAEGLNPIMV 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2255892012 247 VATAGTTDAGAIDPLRDIAGIAAEHQIWLHVDAAWGGALLLSKQYRDYLDGLELVDSVTLDFHKQFFQTISCGAFLLKda 326
Cdd:cd06450 153 VATAGTTDTGAIDPLEEIADLAEKYDLWLHVDAAYGGFLLPFPEPRHLDFGIERVDSISVDPHKYGLVPLGCSAVLVR-- 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2255892012 327 rhyelmryqaaylnsefdeehgvpnlvskslqttrrfdALKLWMGLEALGQKQYAAIIDHGVTMAKNVAEYVKSQPTLEL 406
Cdd:cd06450 231 --------------------------------------ALKLWATLRRFGRDGYGEHIDRIVDLAKYLAELIRADPGFEL 272
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2255892012 407 VMQPQLASVLFRSRPAQMAGsdaaaiaLLNQRVGDALLASGRANVGVTEHNGITCLKLTLLNPVVTLDDVKVLLNLVER 485
Cdd:cd06450 273 LGEPNLSLVCFRLKPSVKLD-------ELNYDLSDRLNERGGWHVPATTLGGPNVLRFVVTNPLTTRDDADALLEDIER 344
|
|
| Pyridoxal_deC |
pfam00282 |
Pyridoxal-dependent decarboxylase conserved domain; |
69-418 |
4.55e-64 |
|
Pyridoxal-dependent decarboxylase conserved domain;
Pssm-ID: 395219 Cd Length: 373 Bit Score: 212.28 E-value: 4.55e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2255892012 69 IDRAIEYFLKDSlsvHHPQCVAHLHCPSLVISQAAEVLINATNQSMDSWDQSPSATIIEMKLIEWLRARVGFPAGD---- 144
Cdd:pfam00282 26 IRRNLMPGVTTW---HSPHFHAYMPTGNSYPSLLGDMLTDAINCNGFTWESSPACTELENVVMNWLGEMLGLPAEFlgqe 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2255892012 145 -AGVFTSGGTQSNLMGLMLARDAFFAR---QGHSIQQDGLPGDIRKYkvlCSENAHFSVQKNMALMGLGYRsvtLVKTDE 220
Cdd:pfam00282 103 gGGVLQPGSSESNLLALLAARTKWIKRmkaAGKPADSSGILAKLVAY---TSDQAHSSIEKAALYGGVKLR---EIPSDD 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2255892012 221 FARMDVSDLQAKIAQAQANGEQIMAIVATAGTTDAGAIDPLRDIAGIAAEHQIWLHVDAAWGGALLLSKQYRDYLDGLEL 300
Cdd:pfam00282 177 NGKMRGMDLEKAIEEDKENGLIPFFVVATLGTTGSGAFDDLQELGDICAKHNLWLHVDAAYGGSAFICPEFRHWLFGIER 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2255892012 301 VDSVTLDFHKQFFQTISCGAFLLKD--ARHYELmRYQAAYLNsefdEEHGVPNLVSKSLQTTRRFDALKLWMGLEALGQK 378
Cdd:pfam00282 257 ADSITFNPHKWMLVLLDCSAVWVKDkeALQQAF-QFNPLYLG----HTDSAYDTGHKQIPLSRRFRILKLWFVIRSLGVE 331
|
330 340 350 360
....*....|....*....|....*....|....*....|
gi 2255892012 379 QYAAIIDHGVTMAKNVAEYVKSQPTLELVMQPQLASVLFR 418
Cdd:pfam00282 332 GLQNQIRRHVELAQYLEALIRKDGRFEICAEVGLGLVCFR 371
|
|
| NOD_PanD_pyr |
TIGR03799 |
putative pyridoxal-dependent aspartate 1-decarboxylase; This enzyme is proposed here to be a ... |
146-472 |
5.81e-62 |
|
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: 210.76 E-value: 5.81e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2255892012 146 GVFTSGGTQSNLMGLMLARDAFFARQG--HSIQQDGLPGDIRKYK-----VLCSENAHFSVQKNMALMGLGYRSVTLVKT 218
Cdd:TIGR03799 162 GAFCSGGTVANITALWVARNRLLKADGdfRGIAREGLFAALRHYGydglaILVSERGHYSLGKAADVLGIGRDNLVPVKT 241
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2255892012 219 DEFARMDVSDLQAKIAQAQANGEQIMAIVATAGTTDAGAIDPLRDIAGIAAEHQIWLHVDAAWGGALLLSKQYRDYLDGL 298
Cdd:TIGR03799 242 DENNRIRVDALRDKCLELAAQNIKPMAIVGVAGTTETGNIDPLDEMADIAQEAGCHFHVDAAWGGATLLSNTYRHLLKGI 321
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2255892012 299 ELVDSVTLDFHKQFFQTISCGAFLLKDARHYELMRYQAAYLNSEfdeehGVPNLVSKSLQTTRRFDALKLWMGLEALGQK 378
Cdd:TIGR03799 322 ERADSVTIDAHKQMYVPMGAGMVLFKDPALTSAIEHHAEYILRK-----GSKDLGSHTLEGSRPGMAMLVYACLHIIGRK 396
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2255892012 379 QYAAIIDHGVTMAKNVAEYVKSQPTLELVMQPQLASVLFRSRPAQMAGSDAAAIALLNQRVGDALLA-----------SG 447
Cdd:TIGR03799 397 GYEMLINQSIDKAHYFANLIDQQPDFELVTEPELCLLTYRYVPENVKAALAIADEEQREKINDALNAltkfiqkrqreTG 476
|
330 340 350
....*....|....*....|....*....|..
gi 2255892012 448 RANVGVTE-------HNGITCLKLTLLNPVVT 472
Cdd:TIGR03799 477 KSFVSRTRltpaqydHQPTIVFRVVLANPLTT 508
|
|
| PLN02590 |
PLN02590 |
probable tyrosine decarboxylase |
116-421 |
1.38e-38 |
|
probable tyrosine decarboxylase
Pssm-ID: 178200 [Multi-domain] Cd Length: 539 Bit Score: 147.55 E-value: 1.38e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2255892012 116 SWDQSPSATIIEMKLIEWLRARVGFP------AGDAGVFTSGGTQSNLMGLMLARDAFFARQGHSIqqdgLPgdirKYKV 189
Cdd:PLN02590 161 TWLTSPAATELEIIVLDWLAKLLQLPdhflstGNGGGVIQGTGCEAVLVVVLAARDRILKKVGKTL----LP----QLVV 232
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2255892012 190 LCSENAHFSVQKNMALMGLGYRSVTLVKTDEFAR--MDVSDLQAKIAQAQANGEQIMAIVATAGTTDAGAIDPLRDIAGI 267
Cdd:PLN02590 233 YGSDQTHSSFRKACLIGGIHEENIRLLKTDSSTNygMPPESLEEAISHDLAKGFIPFFICATVGTTSSAAVDPLVPLGNI 312
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2255892012 268 AAEHQIWLHVDAAWGGALLLSKQYRDYLDGLELVDSVTLDFHKQFFQTISCGAFLLKDarHYEL---MRYQAAYLNSEFD 344
Cdd:PLN02590 313 AKKYGIWLHVDAAYAGNACICPEYRKFIDGIENADSFNMNAHKWLFANQTCSPLWVKD--RYSLidaLKTNPEYLEFKVS 390
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2255892012 345 EEHGVPNLVSKSLQTTRRFDALKLWMGLEALGQKQYAAIIDHGVTMAKNVAEYVKSQPTLELVMQPQLASVLFRSRP 421
Cdd:PLN02590 391 KKDTVVNYKDWQISLSRRFRSLKLWMVLRLYGSENLRNFIRDHVNLAKHFEDYVAQDPSFEVVTTRYFSLVCFRLAP 467
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| GadA |
COG0076 |
Glutamate or tyrosine decarboxylase or a related PLP-dependent protein [Amino acid transport ... |
20-489 |
0e+00 |
|
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: 517.46 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2255892012 20 AYQQVIEQTSQAVVQWLKQ-PEMYQGKSVDELRERISLEFNEQGLGNQAAIDRAIEYFLKDSLSVHHPQCVAHLHCPSLV 98
Cdd:COG0076 1 EFRALLHQALDLAADYLAGlDRPVFGPSPEELRAALDEPLPEEGLPPEEALAELEDLVLPGSVDWNHPRFLAFVTGGTTP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2255892012 99 ISQAAEVLINATNQSMDSWDQSPSATIIEMKLIEWLRARVGFPAGDAGVFTSGGTQSNLMGLMLARDAFFARQghsIQQD 178
Cdd:COG0076 81 AALAADLLASALNQNMGDWDTSPAATELEREVVRWLADLLGLPEGAGGVFTSGGTEANLLALLAARDRALARR---VRAE 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2255892012 179 GLPGdIRKYKVLCSENAHFSVQKNMALMGLGYRSVTLVKTDEFARMDVSDLQAKIAQAQANGEQIMAIVATAGTTDAGAI 258
Cdd:COG0076 158 GLPG-APRPRIVVSEEAHSSVDKAARLLGLGRDALRKVPVDEDGRMDPDALEAAIDEDRAAGLNPIAVVATAGTTNTGAI 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2255892012 259 DPLRDIAGIAAEHQIWLHVDAAWGGALLLSKQYRDYLDGLELVDSVTLDFHKQFFQTISCGAFLLKDAR-HYELMRYQAA 337
Cdd:COG0076 237 DPLAEIADIAREHGLWLHVDAAYGGFALPSPELRHLLDGIERADSITVDPHKWLYVPYGCGAVLVRDPElLREAFSFHAS 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2255892012 338 YLNsefDEEHGVPNLVSKSLQTTRRFDALKLWMGLEALGQKQYAAIIDHGVTMAKNVAEYVKSQPTLELVMQPQLASVLF 417
Cdd:COG0076 317 YLG---PADDGVPNLGDYTLELSRRFRALKLWATLRALGREGYRELIERCIDLARYLAEGIAALPGFELLAPPELNIVCF 393
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2255892012 418 RSRPAQMAGSDAaaialLNQRVGDALLASGRANVGVTEHNGITCLKLTLLNPVVTLDDVKVLLNLVERTAQE 489
Cdd:COG0076 394 RYKPAGLDEEDA-----LNYALRDRLRARGRAFLSPTKLDGRVVLRLVVLNPRTTEDDVDALLDDLREAAAE 460
|
|
| DOPA_deC_like |
cd06450 |
DOPA decarboxylase family. This family belongs to pyridoxal phosphate (PLP)-dependent ... |
88-485 |
2.31e-118 |
|
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: 351.12 E-value: 2.31e-118
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2255892012 88 CVAHLHCPSLVISQAAEVLINATNQSMDSWDQSPSATIIEMKLIEWLRARVGFPAGDA-GVFTSGGTQSNLMGLMLARDA 166
Cdd:cd06450 1 FLAGFVTTMDPPALLLEMLTSAKNAIDFTWDESPAATEMEAEVVNWLAKLFGLPSEDAdGVFTSGGSESNLLALLAARDR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2255892012 167 FFARQghsiqQDGLPGDIRKYKVLCSENAHFSVQKNMALMGlgyRSVTLVKTDEFARMDVSDLQAKIAQAQANGEQIMAI 246
Cdd:cd06450 81 ARKRL-----KAGGGRGIDKLVIVCSDQAHVSVEKAAAYLD---VKVRLVPVDEDGRMDPEALEAAIDEDKAEGLNPIMV 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2255892012 247 VATAGTTDAGAIDPLRDIAGIAAEHQIWLHVDAAWGGALLLSKQYRDYLDGLELVDSVTLDFHKQFFQTISCGAFLLKda 326
Cdd:cd06450 153 VATAGTTDTGAIDPLEEIADLAEKYDLWLHVDAAYGGFLLPFPEPRHLDFGIERVDSISVDPHKYGLVPLGCSAVLVR-- 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2255892012 327 rhyelmryqaaylnsefdeehgvpnlvskslqttrrfdALKLWMGLEALGQKQYAAIIDHGVTMAKNVAEYVKSQPTLEL 406
Cdd:cd06450 231 --------------------------------------ALKLWATLRRFGRDGYGEHIDRIVDLAKYLAELIRADPGFEL 272
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2255892012 407 VMQPQLASVLFRSRPAQMAGsdaaaiaLLNQRVGDALLASGRANVGVTEHNGITCLKLTLLNPVVTLDDVKVLLNLVER 485
Cdd:cd06450 273 LGEPNLSLVCFRLKPSVKLD-------ELNYDLSDRLNERGGWHVPATTLGGPNVLRFVVTNPLTTRDDADALLEDIER 344
|
|
| Pyridoxal_deC |
pfam00282 |
Pyridoxal-dependent decarboxylase conserved domain; |
69-418 |
4.55e-64 |
|
Pyridoxal-dependent decarboxylase conserved domain;
Pssm-ID: 395219 Cd Length: 373 Bit Score: 212.28 E-value: 4.55e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2255892012 69 IDRAIEYFLKDSlsvHHPQCVAHLHCPSLVISQAAEVLINATNQSMDSWDQSPSATIIEMKLIEWLRARVGFPAGD---- 144
Cdd:pfam00282 26 IRRNLMPGVTTW---HSPHFHAYMPTGNSYPSLLGDMLTDAINCNGFTWESSPACTELENVVMNWLGEMLGLPAEFlgqe 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2255892012 145 -AGVFTSGGTQSNLMGLMLARDAFFAR---QGHSIQQDGLPGDIRKYkvlCSENAHFSVQKNMALMGLGYRsvtLVKTDE 220
Cdd:pfam00282 103 gGGVLQPGSSESNLLALLAARTKWIKRmkaAGKPADSSGILAKLVAY---TSDQAHSSIEKAALYGGVKLR---EIPSDD 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2255892012 221 FARMDVSDLQAKIAQAQANGEQIMAIVATAGTTDAGAIDPLRDIAGIAAEHQIWLHVDAAWGGALLLSKQYRDYLDGLEL 300
Cdd:pfam00282 177 NGKMRGMDLEKAIEEDKENGLIPFFVVATLGTTGSGAFDDLQELGDICAKHNLWLHVDAAYGGSAFICPEFRHWLFGIER 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2255892012 301 VDSVTLDFHKQFFQTISCGAFLLKD--ARHYELmRYQAAYLNsefdEEHGVPNLVSKSLQTTRRFDALKLWMGLEALGQK 378
Cdd:pfam00282 257 ADSITFNPHKWMLVLLDCSAVWVKDkeALQQAF-QFNPLYLG----HTDSAYDTGHKQIPLSRRFRILKLWFVIRSLGVE 331
|
330 340 350 360
....*....|....*....|....*....|....*....|
gi 2255892012 379 QYAAIIDHGVTMAKNVAEYVKSQPTLELVMQPQLASVLFR 418
Cdd:pfam00282 332 GLQNQIRRHVELAQYLEALIRKDGRFEICAEVGLGLVCFR 371
|
|
| NOD_PanD_pyr |
TIGR03799 |
putative pyridoxal-dependent aspartate 1-decarboxylase; This enzyme is proposed here to be a ... |
146-472 |
5.81e-62 |
|
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: 210.76 E-value: 5.81e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2255892012 146 GVFTSGGTQSNLMGLMLARDAFFARQG--HSIQQDGLPGDIRKYK-----VLCSENAHFSVQKNMALMGLGYRSVTLVKT 218
Cdd:TIGR03799 162 GAFCSGGTVANITALWVARNRLLKADGdfRGIAREGLFAALRHYGydglaILVSERGHYSLGKAADVLGIGRDNLVPVKT 241
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2255892012 219 DEFARMDVSDLQAKIAQAQANGEQIMAIVATAGTTDAGAIDPLRDIAGIAAEHQIWLHVDAAWGGALLLSKQYRDYLDGL 298
Cdd:TIGR03799 242 DENNRIRVDALRDKCLELAAQNIKPMAIVGVAGTTETGNIDPLDEMADIAQEAGCHFHVDAAWGGATLLSNTYRHLLKGI 321
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2255892012 299 ELVDSVTLDFHKQFFQTISCGAFLLKDARHYELMRYQAAYLNSEfdeehGVPNLVSKSLQTTRRFDALKLWMGLEALGQK 378
Cdd:TIGR03799 322 ERADSVTIDAHKQMYVPMGAGMVLFKDPALTSAIEHHAEYILRK-----GSKDLGSHTLEGSRPGMAMLVYACLHIIGRK 396
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2255892012 379 QYAAIIDHGVTMAKNVAEYVKSQPTLELVMQPQLASVLFRSRPAQMAGSDAAAIALLNQRVGDALLA-----------SG 447
Cdd:TIGR03799 397 GYEMLINQSIDKAHYFANLIDQQPDFELVTEPELCLLTYRYVPENVKAALAIADEEQREKINDALNAltkfiqkrqreTG 476
|
330 340 350
....*....|....*....|....*....|..
gi 2255892012 448 RANVGVTE-------HNGITCLKLTLLNPVVT 472
Cdd:TIGR03799 477 KSFVSRTRltpaqydHQPTIVFRVVLANPLTT 508
|
|
| PLN02590 |
PLN02590 |
probable tyrosine decarboxylase |
116-421 |
1.38e-38 |
|
probable tyrosine decarboxylase
Pssm-ID: 178200 [Multi-domain] Cd Length: 539 Bit Score: 147.55 E-value: 1.38e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2255892012 116 SWDQSPSATIIEMKLIEWLRARVGFP------AGDAGVFTSGGTQSNLMGLMLARDAFFARQGHSIqqdgLPgdirKYKV 189
Cdd:PLN02590 161 TWLTSPAATELEIIVLDWLAKLLQLPdhflstGNGGGVIQGTGCEAVLVVVLAARDRILKKVGKTL----LP----QLVV 232
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2255892012 190 LCSENAHFSVQKNMALMGLGYRSVTLVKTDEFAR--MDVSDLQAKIAQAQANGEQIMAIVATAGTTDAGAIDPLRDIAGI 267
Cdd:PLN02590 233 YGSDQTHSSFRKACLIGGIHEENIRLLKTDSSTNygMPPESLEEAISHDLAKGFIPFFICATVGTTSSAAVDPLVPLGNI 312
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2255892012 268 AAEHQIWLHVDAAWGGALLLSKQYRDYLDGLELVDSVTLDFHKQFFQTISCGAFLLKDarHYEL---MRYQAAYLNSEFD 344
Cdd:PLN02590 313 AKKYGIWLHVDAAYAGNACICPEYRKFIDGIENADSFNMNAHKWLFANQTCSPLWVKD--RYSLidaLKTNPEYLEFKVS 390
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2255892012 345 EEHGVPNLVSKSLQTTRRFDALKLWMGLEALGQKQYAAIIDHGVTMAKNVAEYVKSQPTLELVMQPQLASVLFRSRP 421
Cdd:PLN02590 391 KKDTVVNYKDWQISLSRRFRSLKLWMVLRLYGSENLRNFIRDHVNLAKHFEDYVAQDPSFEVVTTRYFSLVCFRLAP 467
|
|
| PLN02880 |
PLN02880 |
tyrosine decarboxylase |
104-493 |
5.37e-38 |
|
tyrosine decarboxylase
Pssm-ID: 215475 [Multi-domain] Cd Length: 490 Bit Score: 145.05 E-value: 5.37e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2255892012 104 EVLINATNQSMDSWDQSPSATIIEMKLIEWLRARVGFP------AGDAGVFTSGGTQSNLMGLMLARDAFFARQGHSiqq 177
Cdd:PLN02880 101 EMLSAGLNIVGFSWITSPAATELEMIVLDWLAKLLNLPeqflstGNGGGVIQGTASEAVLVVLLAARDRVLRKVGKN--- 177
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2255892012 178 dglpgDIRKYKVLCSENAHFSVQKNMALMGLGYRSVTLVKTDEFARMDVSD--LQAKIAQAQANGEQIMAIVATAGTTDA 255
Cdd:PLN02880 178 -----ALEKLVVYASDQTHSALQKACQIAGIHPENCRLLKTDSSTNYALAPelLSEAISTDLSSGLIPFFLCATVGTTSS 252
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2255892012 256 GAIDPLRDIAGIAAEHQIWLHVDAAWGGALLLSKQYRDYLDGLELVDSVTLDFHKQFFQTISCGAFLLKDaRHYELmryQ 335
Cdd:PLN02880 253 TAVDPLLELGKIAKSNGMWFHVDAAYAGSACICPEYRHYIDGVEEADSFNMNAHKWFLTNFDCSLLWVKD-RNALI---Q 328
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2255892012 336 AAYLNSEF-----DEEHGVPNLVSKSLQTTRRFDALKLWMGLEALGQKQYAAIIDHGVTMAKNVAEYVKSQPTLELVMQP 410
Cdd:PLN02880 329 SLSTNPEFlknkaSQANSVVDYKDWQIPLGRRFRSLKLWMVLRLYGVENLQSYIRNHIKLAKEFEQLVAQDSRFEVVTPR 408
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2255892012 411 QLASVLFRSRPAQmagSDAAAIALLNQRVGDALLASGRANVGVTEHNGITCLKLTLLNPVVTLDDVKVLLNLVERTAQEL 490
Cdd:PLN02880 409 IFSLVCFRLVPPK---NNEDNGNKLNHDLLDAVNSSGKIFISHTVLSGKYVLRFAVGAPLTEERHVTAAWKVLQDEASKL 485
|
...
gi 2255892012 491 LAQ 493
Cdd:PLN02880 486 LGK 488
|
|
| PRK02769 |
PRK02769 |
histidine decarboxylase; Provisional |
146-329 |
3.23e-18 |
|
histidine decarboxylase; Provisional
Pssm-ID: 235068 [Multi-domain] Cd Length: 380 Bit Score: 86.25 E-value: 3.23e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2255892012 146 GVFTSGGTQSNLMGLMLARDAFfarqghsiqqdglPGDIRKYkvlcSENAHFSVQKNMALMGLGYRSVTLVKTDEfarMD 225
Cdd:PRK02769 87 GYITNGGTEGNLYGCYLARELF-------------PDGTLYY----SKDTHYSVSKIARLLRIKSRVITSLPNGE---ID 146
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2255892012 226 VSDLQAKIaqaQANGEQIMAIVATAGTTDAGAIDPLRDIAGIAAEHQI---WLHVDAAWGGALLL---SKQYRDYLDGle 299
Cdd:PRK02769 147 YDDLISKI---KENKNQPPIIFANIGTTMTGAIDNIKEIQEILKKIGIddyYIHADAALSGMILPfvnNPPPFSFADG-- 221
|
170 180 190
....*....|....*....|....*....|
gi 2255892012 300 lVDSVTLDFHKQFFQTISCGAFLLKdaRHY 329
Cdd:PRK02769 222 -IDSIAISGHKFIGSPMPCGIVLAK--KKY 248
|
|
| AAT_I |
cd01494 |
Aspartate aminotransferase (AAT) superfamily (fold type I) of pyridoxal phosphate (PLP) ... |
129-312 |
6.54e-16 |
|
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: 75.50 E-value: 6.54e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2255892012 129 KLIEWLRaRVGFPAGDAGVFTSGGTQSNLMGLMLARdaffarqghsiqqdglpgdIRKYKVLCSENAHFSVQKNMALMGl 208
Cdd:cd01494 4 ELEEKLA-RLLQPGNDKAVFVPSGTGANEAALLALL-------------------GPGDEVIVDANGHGSRYWVAAELA- 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2255892012 209 GYRSVTLVKTDEFARmdvsDLQAKIAQAQANGEQIMAIVATAGTTDAGAIDPLRDIAGIAAEHQIWLHVDAAWGGALLLS 288
Cdd:cd01494 63 GAKPVPVPVDDAGYG----GLDVAILEELKAKPNVALIVITPNTTSGGVLVPLKEIRKIAKEYGILLLVDAASAGGASPA 138
|
170 180
....*....|....*....|....
gi 2255892012 289 KQYRDYLDGlelVDSVTLDFHKQF 312
Cdd:cd01494 139 PGVLIPEGG---ADVVTFSLHKNL 159
|
|
| Beta_elim_lyase |
pfam01212 |
Beta-eliminating lyase; |
129-350 |
1.18e-08 |
|
Beta-eliminating lyase;
Pssm-ID: 426128 [Multi-domain] Cd Length: 288 Bit Score: 56.07 E-value: 1.18e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2255892012 129 KLIEWLRARVGFpagDAGVFTSGGTQSNLMGLMLardafFARQGHSiqqdglpgdirkykVLCSENAHFSVQKNMALMGL 208
Cdd:pfam01212 36 RLEDRVAELFGK---EAALFVPSGTAANQLALMA-----HCQRGDE--------------VICGEPAHIHFDETGGHAEL 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2255892012 209 GYRSVTLVKTDEFARMDVSDLQAKIAQAQANGEQIMAIVATAGTTDAGA-----IDPLRDIAGIAAEHQIWLHVDAA--W 281
Cdd:pfam01212 94 GGVQPRPLDGDEAGNMDLEDLEAAIREVGADIFPPTGLISLENTHNSAGgqvvsLENLREIAALAREHGIPVHLDGArfA 173
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2255892012 282 GGALLLSKQYRDYLDGlelVDSVTLDFHKQFFQTIscGAFLLKDARHYELMRYQAAYLNSEFDeEHGVP 350
Cdd:pfam01212 174 NAAVALGVIVKEITSY---ADSVTMCLSKGLGAPV--GSVLAGSDDFIAKAIRQRKYLGGGLR-QAGVL 236
|
|
| NifS |
COG1104 |
Cysteine desulfurase/Cysteine sulfinate desulfinase IscS or related enzyme, NifS family [Amino ... |
147-280 |
3.36e-08 |
|
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: 55.44 E-value: 3.36e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2255892012 147 VFTSGGTQSNLMGLMLARDAFFARQGHsiqqdglpgdirkykVLCSENAHFSVQKNM-ALMGLGYRsVTLVKTDEFARMD 225
Cdd:COG1104 66 IFTSGGTEANNLAIKGAARAYRKKGKH---------------IITSAIEHPAVLETArFLEKEGFE-VTYLPVDEDGRVD 129
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2255892012 226 VSDLQAKIAQA-------QANGEqimaivatagtTdaGAIDPLRDIAGIAAEHQIWLHVDAA 280
Cdd:COG1104 130 LEALEAALRPDtalvsvmHANNE-----------T--GTIQPIAEIAEIAKEHGVLFHTDAV 178
|
|
| PLN03032 |
PLN03032 |
serine decarboxylase; Provisional |
146-341 |
5.34e-06 |
|
serine decarboxylase; Provisional
Pssm-ID: 166673 [Multi-domain] Cd Length: 374 Bit Score: 48.67 E-value: 5.34e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2255892012 146 GVFTSGGTQSNLMGLMLARDAFfarqghsiqQDGLpgdirkykVLCSENAHFSVQKnMALMglgYR-SVTLVKTDEFARM 224
Cdd:PLN03032 88 GYITTCGTEGNLHGILVGREVF---------PDGI--------LYASRESHYSVFK-AARM---YRmEAVKVPTLPSGEI 146
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2255892012 225 DVSDLQAKIAQaqaNGEQIMAIVATAGTTDAGAIDPLRDI------AGIaAEHQIWLHVDAAWGGALLLSKQYRDYLDGL 298
Cdd:PLN03032 147 DYDDLERALAK---NRDKPAILNVNIGTTVKGAVDDLDRIlrilkeLGY-TEDRFYIHCDGALFGLMMPFVSRAPEVTFR 222
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 2255892012 299 ELVDSVTLDFHKQFFQTISCGAFLLKdARHYELMRYQAAYLNS 341
Cdd:PLN03032 223 KPIGSVSVSGHKFLGCPMPCGVALTR-KKHVKALSQNVEYLNS 264
|
|
| TA_like |
cd06502 |
Low-specificity threonine aldolase (TA). This family belongs to pyridoxal phosphate (PLP) ... |
145-405 |
6.72e-06 |
|
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: 48.10 E-value: 6.72e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2255892012 145 AGVFTSGGTQSNLMGLMLardafFARQGHSiqqdglpgdirkykVLCSENAHFSVQKNMALMGLGYRSVTLVKTDEfARM 224
Cdd:cd06502 49 AALFVPSGTAANQLALAA-----HTQPGGS--------------VICHETAHIYTDEAGAPEFLSGVKLLPVPGEN-GKL 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2255892012 225 DVSDLQAKIAQAQANGEQIMAIVATAGTTDAGAIDP---LRDIAGIAAEHQIWLHVD--------AAWGGALLLSKQYrd 293
Cdd:cd06502 109 TPEDLEAAIRPRDDIHFPPPSLVSLENTTEGGTVYPldeLKAISALAKENGLPLHLDgarlanaaAALGVALKTYKSG-- 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2255892012 294 yldglelVDSVTLDFHKQ---FFQTISCG-AFLLKDARHYelmRYQAAylnsefdeehgvpNLVSKSlqttrRFDALKlw 369
Cdd:cd06502 187 -------VDSVSFCLSKGggaPVGAVVVGnRDFIARARRR---RKQAG-------------GGMRQS-----GFLAAA-- 236
|
250 260 270
....*....|....*....|....*....|....*.
gi 2255892012 370 mGLEALGQKQYAAIIDHGVTMAKNVAEYVKSQPTLE 405
Cdd:cd06502 237 -GLAALENDLWLRRLRHDHEMARRLAEALEELGGLE 271
|
|
| PRK02948 |
PRK02948 |
IscS subfamily cysteine desulfurase; |
148-279 |
1.09e-05 |
|
IscS subfamily cysteine desulfurase;
Pssm-ID: 179511 [Multi-domain] Cd Length: 381 Bit Score: 47.42 E-value: 1.09e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2255892012 148 FTSGGTQSNLMGLmlardaffarqgHSIQQdGLPGdiRKYKVLCSENAHFSVQKNMA-LMGLGYrSVTLVKTDEFARMDV 226
Cdd:PRK02948 65 FTSGGTESNYLAI------------QSLLN-ALPQ--NKKHIITTPMEHASIHSYFQsLESQGY-TVTEIPVDKSGLIRL 128
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 2255892012 227 SDLQAKIAQaqangEQIMAIVATAgTTDAGAIDPLRDIAGIAAEHQIWLHVDA 279
Cdd:PRK02948 129 VDLERAITP-----DTVLASIQHA-NSEIGTIQPIAEIGALLKKYNVLFHSDC 175
|
|
| PLN02651 |
PLN02651 |
cysteine desulfurase |
147-280 |
5.64e-05 |
|
cysteine desulfurase
Pssm-ID: 178257 [Multi-domain] Cd Length: 364 Bit Score: 45.42 E-value: 5.64e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2255892012 147 VFTSGGTQSNLMGLMLARDAFFARQGHsiqqdglpgdirkykVLCSENAHFSVQKNMALMGLGYRSVTLVKTDEFARMDV 226
Cdd:PLN02651 64 IFTSGATESNNLAIKGVMHFYKDKKKH---------------VITTQTEHKCVLDSCRHLQQEGFEVTYLPVKSDGLVDL 128
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 2255892012 227 SDLQAKIAQAQAngeqIMAIVATagTTDAGAIDPLRDIAGIAAEHQIWLHVDAA 280
Cdd:PLN02651 129 DELAAAIRPDTA----LVSVMAV--NNEIGVIQPVEEIGELCREKKVLFHTDAA 176
|
|
| Aminotran_5 |
pfam00266 |
Aminotransferase class-V; This domain is found in amino transferases, and other enzymes ... |
147-280 |
7.39e-04 |
|
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: 41.85 E-value: 7.39e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2255892012 147 VFTSGGTQS-NLMGLMLardaffarqGHSIQqdglPGDirkyKVLCSENAHFS--VQKNMALMGLGYRsVTLVKTDEFAR 223
Cdd:pfam00266 65 IFTSGTTEAiNLVALSL---------GRSLK----PGD----EIVITEMEHHAnlVPWQELAKRTGAR-VRVLPLDEDGL 126
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 2255892012 224 MDVSDLQAKIAQaqanGEQIMAIvaTAGTTDAGAIDPLRDIAGIAAEHQIWLHVDAA 280
Cdd:pfam00266 127 LDLDELEKLITP----KTKLVAI--THVSNVTGTIQPVPEIGKLAHQYGALVLVDAA 177
|
|
| PLN02263 |
PLN02263 |
serine decarboxylase |
146-286 |
3.16e-03 |
|
serine decarboxylase
Pssm-ID: 177904 [Multi-domain] Cd Length: 470 Bit Score: 39.80 E-value: 3.16e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2255892012 146 GVFTSGGTQSNLMGLMLARDAFfarqghsiqQDGLpgdirkykVLCSENAHFSVQKnMALMglgYRsVTLVKTD--EFAR 223
Cdd:PLN02263 155 GYITNCGTEGNLHGILVGREVF---------PDGI--------LYASRESHYSVFK-AARM---YR-MECVKVDtlVSGE 212
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2255892012 224 MDVSDLQAKIAqaqANGEQIMAIVATAGTTDAGAIDPLRDI------AGIaAEHQIWLHVDAAWGGALL 286
Cdd:PLN02263 213 IDCADFKAKLL---ANKDKPAIINVNIGTTVKGAVDDLDLViktleeCGF-SQDRFYIHCDGALFGLMM 277
|
|
| |
