|
Name |
Accession |
Description |
Interval |
E-value |
| GadA |
COG0076 |
Glutamate or tyrosine decarboxylase or a related PLP-dependent protein [Amino acid transport ... |
17-486 |
1.15e-179 |
|
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: 511.30 E-value: 1.15e-179
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727188709 17 AYRQAIAQSSEAVVQWLQQ-PEMYQGKSVAELRERIQLDFTPQGLGNQAAIERAIEYFLKDSLSVHHPQCVAHLHCPSLV 95
Cdd:COG0076 1 EFRALLHQALDLAADYLAGlDRPVFGPSPEELRAALDEPLPEEGLPPEEALAELEDLVLPGSVDWNHPRFLAFVTGGTTP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727188709 96 ISQAAEVLINATNQSMDSWDQSPSATLIEMKLIEWLRAQVGYQPGDAGVFTSGGTQSNLMGLMLARDAFFARQghsVQQD 175
Cdd:COG0076 81 AALAADLLASALNQNMGDWDTSPAATELEREVVRWLADLLGLPEGAGGVFTSGGTEANLLALLAARDRALARR---VRAE 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727188709 176 GLVGdLRKLKVFCSENAHFSVQKNMALMGLGYQSVTLVKTDRFARMDVNDLAEKLAQAKANGEQVMALVATAGTTDAGAI 255
Cdd:COG0076 158 GLPG-APRPRIVVSEEAHSSVDKAARLLGLGRDALRKVPVDEDGRMDPDALEAAIDEDRAAGLNPIAVVATAGTTNTGAI 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727188709 256 DPLRDIARLAAEQKIWVHVDAAWGGALLLSEQYRDYLDGLELVDSITLDFHKQFFQTISCGAFLLKD-ERHYELMRYQAA 334
Cdd:COG0076 237 DPLAEIADIAREHGLWLHVDAAYGGFALPSPELRHLLDGIERADSITVDPHKWLYVPYGCGAVLVRDpELLREAFSFHAS 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727188709 335 YLNsefDEAQGVPNLVSKSLQTTRRFDALKLWMGLEALGQKQYAEIIDHGVSLAQQVARYIADQESLELVMQPQLASVLF 414
Cdd:COG0076 317 YLG---PADDGVPNLGDYTLELSRRFRALKLWATLRALGREGYRELIERCIDLARYLAEGIAALPGFELLAPPELNIVCF 393
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 727188709 415 RYRPAQLAAKGDaavalFNQRIGDALLESGRANVGVTEFDGVTCLKMTLLNPIVTLEDIKLLLALVEKTAQQ 486
Cdd:COG0076 394 RYKPAGLDEEDA-----LNYALRDRLRARGRAFLSPTKLDGRVVLRLVVLNPRTTEDDVDALLDDLREAAAE 460
|
|
| DOPA_deC_like |
cd06450 |
DOPA decarboxylase family. This family belongs to pyridoxal phosphate (PLP)-dependent ... |
85-482 |
5.68e-119 |
|
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: 352.66 E-value: 5.68e-119
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727188709 85 CVAHLHCPSLVISQAAEVLINATNQSMDSWDQSPSATLIEMKLIEWLRAQVGYQPGDA-GVFTSGGTQSNLMGLMLARDA 163
Cdd:cd06450 1 FLAGFVTTMDPPALLLEMLTSAKNAIDFTWDESPAATEMEAEVVNWLAKLFGLPSEDAdGVFTSGGSESNLLALLAARDR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727188709 164 FFARQghsvqQDGLVGDLRKLKVFCSENAHFSVQKNMALMGlgyQSVTLVKTDRFARMDVNDLAEKLAQAKANGEQVMAL 243
Cdd:cd06450 81 ARKRL-----KAGGGRGIDKLVIVCSDQAHVSVEKAAAYLD---VKVRLVPVDEDGRMDPEALEAAIDEDKAEGLNPIMV 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727188709 244 VATAGTTDAGAIDPLRDIARLAAEQKIWVHVDAAWGGALLLSEQYRDYLDGLELVDSITLDFHKQFFQTISCGAFLLKde 323
Cdd:cd06450 153 VATAGTTDTGAIDPLEEIADLAEKYDLWLHVDAAYGGFLLPFPEPRHLDFGIERVDSISVDPHKYGLVPLGCSAVLVR-- 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727188709 324 rhyelmryqaaylnsefdeaqgvpnlvskslqttrrfdALKLWMGLEALGQKQYAEIIDHGVSLAQQVARYIADQESLEL 403
Cdd:cd06450 231 --------------------------------------ALKLWATLRRFGRDGYGEHIDRIVDLAKYLAELIRADPGFEL 272
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 727188709 404 VMQPQLASVLFRYRPaqlaakgDAAVALFNQRIGDALLESGRANVGVTEFDGVTCLKMTLLNPIVTLEDIKLLLALVEK 482
Cdd:cd06450 273 LGEPNLSLVCFRLKP-------SVKLDELNYDLSDRLNERGGWHVPATTLGGPNVLRFVVTNPLTTRDDADALLEDIER 344
|
|
| NOD_PanD_pyr |
TIGR03799 |
putative pyridoxal-dependent aspartate 1-decarboxylase; This enzyme is proposed here to be a ... |
143-473 |
1.00e-61 |
|
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: 209.98 E-value: 1.00e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727188709 143 GVFTSGGTQSNLMGLMLARDAFFARQG--HSVQQDGLVGDLR-----KLKVFCSENAHFSVQKNMALMGLGYQSVTLVKT 215
Cdd:TIGR03799 162 GAFCSGGTVANITALWVARNRLLKADGdfRGIAREGLFAALRhygydGLAILVSERGHYSLGKAADVLGIGRDNLVPVKT 241
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727188709 216 DRFARMDVNDLAEKLAQAKANGEQVMALVATAGTTDAGAIDPLRDIARLAAEQKIWVHVDAAWGGALLLSEQYRDYLDGL 295
Cdd:TIGR03799 242 DENNRIRVDALRDKCLELAAQNIKPMAIVGVAGTTETGNIDPLDEMADIAQEAGCHFHVDAAWGGATLLSNTYRHLLKGI 321
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727188709 296 ELVDSITLDFHKQFFQTISCGAFLLKDERHYELMRYQAAYLNSefdeaQGVPNLVSKSLQTTRRFDALKLWMGLEALGQK 375
Cdd:TIGR03799 322 ERADSVTIDAHKQMYVPMGAGMVLFKDPALTSAIEHHAEYILR-----KGSKDLGSHTLEGSRPGMAMLVYACLHIIGRK 396
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727188709 376 QYAEIIDHGVSLAQQVARYIADQESLELVMQPQLASVLFRYRPAQLAAKGDAAVALFNQRIGDAL-----------LESG 444
Cdd:TIGR03799 397 GYEMLINQSIDKAHYFANLIDQQPDFELVTEPELCLLTYRYVPENVKAALAIADEEQREKINDALnaltkfiqkrqRETG 476
|
330 340 350
....*....|....*....|....*....|....*....
gi 727188709 445 RANVG-----VTEFDG--VTCLKMTLLNPIVT---LEDI 473
Cdd:TIGR03799 477 KSFVSrtrltPAQYDHqpTIVFRVVLANPLTTheiLQDI 515
|
|
| Pyridoxal_deC |
pfam00282 |
Pyridoxal-dependent decarboxylase conserved domain; |
66-417 |
8.33e-61 |
|
Pyridoxal-dependent decarboxylase conserved domain;
Pssm-ID: 395219 Cd Length: 373 Bit Score: 203.42 E-value: 8.33e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727188709 66 IERAIEYFLKDSlsvHHPQCVAHLHCPSLVISQAAEVLINATNQSMDSWDQSPSATLIEMKLIEWLRAQVGY------QP 139
Cdd:pfam00282 26 IRRNLMPGVTTW---HSPHFHAYMPTGNSYPSLLGDMLTDAINCNGFTWESSPACTELENVVMNWLGEMLGLpaeflgQE 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727188709 140 GDaGVFTSGGTQSNLMGLMLARDAFFAR---QGHSVQQDGLVGdlrKLKVFCSENAHFSVQKNMALMGLGyqsVTLVKTD 216
Cdd:pfam00282 103 GG-GVLQPGSSESNLLALLAARTKWIKRmkaAGKPADSSGILA---KLVAYTSDQAHSSIEKAALYGGVK---LREIPSD 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727188709 217 RFARMDVNDLAEKLAQAKANGEQVMALVATAGTTDAGAIDPLRDIARLAAEQKIWVHVDAAWGGALLLSEQYRDYLDGLE 296
Cdd:pfam00282 176 DNGKMRGMDLEKAIEEDKENGLIPFFVVATLGTTGSGAFDDLQELGDICAKHNLWLHVDAAYGGSAFICPEFRHWLFGIE 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727188709 297 LVDSITLDFHKQFFQTISCGAFLLKDER--HYELmRYQAAYLNSEfdeaQGVPNLVSKSLQTTRRFDALKLWMGLEALGQ 374
Cdd:pfam00282 256 RADSITFNPHKWMLVLLDCSAVWVKDKEalQQAF-QFNPLYLGHT----DSAYDTGHKQIPLSRRFRILKLWFVIRSLGV 330
|
330 340 350 360
....*....|....*....|....*....|....*....|...
gi 727188709 375 KQYAEIIDHGVSLAQQVARYIADQESLELVMQPQLASVLFRYR 417
Cdd:pfam00282 331 EGLQNQIRRHVELAQYLEALIRKDGRFEICAEVGLGLVCFRLK 373
|
|
| PLN02880 |
PLN02880 |
tyrosine decarboxylase |
101-487 |
1.70e-37 |
|
tyrosine decarboxylase
Pssm-ID: 215475 [Multi-domain] Cd Length: 490 Bit Score: 143.51 E-value: 1.70e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727188709 101 EVLINATNQSMDSWDQSPSATLIEMKLIEWLrAQVGYQPGD-------AGVFTSGGTQSNLMGLMLARDAFFARQGHSVq 173
Cdd:PLN02880 101 EMLSAGLNIVGFSWITSPAATELEMIVLDWL-AKLLNLPEQflstgngGGVIQGTASEAVLVVLLAARDRVLRKVGKNA- 178
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727188709 174 qdglvgdLRKLKVFCSENAHFSVQKNMALMGLGYQSVTLVKTDRFARMDV--NDLAEKLAQAKANGEQVMALVATAGTTD 251
Cdd:PLN02880 179 -------LEKLVVYASDQTHSALQKACQIAGIHPENCRLLKTDSSTNYALapELLSEAISTDLSSGLIPFFLCATVGTTS 251
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727188709 252 AGAIDPLRDIARLAAEQKIWVHVDAAWGGALLLSEQYRDYLDGLELVDSITLDFHKQFFQTISCGAFLLKDeRHYELmry 331
Cdd:PLN02880 252 STAVDPLLELGKIAKSNGMWFHVDAAYAGSACICPEYRHYIDGVEEADSFNMNAHKWFLTNFDCSLLWVKD-RNALI--- 327
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727188709 332 QAAYLNSEF-----DEAQGVPNLVSKSLQTTRRFDALKLWMGLEALGQKQYAEIIDHGVSLAQQVARYIADQESLELVMQ 406
Cdd:PLN02880 328 QSLSTNPEFlknkaSQANSVVDYKDWQIPLGRRFRSLKLWMVLRLYGVENLQSYIRNHIKLAKEFEQLVAQDSRFEVVTP 407
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727188709 407 PQLASVLFRYRPaqLAAKGDAAVALfNQRIGDALLESGRANVGVTEFDGVTCLKMTLLNPIVTLEDIKLLLALVEKTAQQ 486
Cdd:PLN02880 408 RIFSLVCFRLVP--PKNNEDNGNKL-NHDLLDAVNSSGKIFISHTVLSGKYVLRFAVGAPLTEERHVTAAWKVLQDEASK 484
|
.
gi 727188709 487 L 487
Cdd:PLN02880 485 L 485
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| GadA |
COG0076 |
Glutamate or tyrosine decarboxylase or a related PLP-dependent protein [Amino acid transport ... |
17-486 |
1.15e-179 |
|
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: 511.30 E-value: 1.15e-179
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727188709 17 AYRQAIAQSSEAVVQWLQQ-PEMYQGKSVAELRERIQLDFTPQGLGNQAAIERAIEYFLKDSLSVHHPQCVAHLHCPSLV 95
Cdd:COG0076 1 EFRALLHQALDLAADYLAGlDRPVFGPSPEELRAALDEPLPEEGLPPEEALAELEDLVLPGSVDWNHPRFLAFVTGGTTP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727188709 96 ISQAAEVLINATNQSMDSWDQSPSATLIEMKLIEWLRAQVGYQPGDAGVFTSGGTQSNLMGLMLARDAFFARQghsVQQD 175
Cdd:COG0076 81 AALAADLLASALNQNMGDWDTSPAATELEREVVRWLADLLGLPEGAGGVFTSGGTEANLLALLAARDRALARR---VRAE 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727188709 176 GLVGdLRKLKVFCSENAHFSVQKNMALMGLGYQSVTLVKTDRFARMDVNDLAEKLAQAKANGEQVMALVATAGTTDAGAI 255
Cdd:COG0076 158 GLPG-APRPRIVVSEEAHSSVDKAARLLGLGRDALRKVPVDEDGRMDPDALEAAIDEDRAAGLNPIAVVATAGTTNTGAI 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727188709 256 DPLRDIARLAAEQKIWVHVDAAWGGALLLSEQYRDYLDGLELVDSITLDFHKQFFQTISCGAFLLKD-ERHYELMRYQAA 334
Cdd:COG0076 237 DPLAEIADIAREHGLWLHVDAAYGGFALPSPELRHLLDGIERADSITVDPHKWLYVPYGCGAVLVRDpELLREAFSFHAS 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727188709 335 YLNsefDEAQGVPNLVSKSLQTTRRFDALKLWMGLEALGQKQYAEIIDHGVSLAQQVARYIADQESLELVMQPQLASVLF 414
Cdd:COG0076 317 YLG---PADDGVPNLGDYTLELSRRFRALKLWATLRALGREGYRELIERCIDLARYLAEGIAALPGFELLAPPELNIVCF 393
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 727188709 415 RYRPAQLAAKGDaavalFNQRIGDALLESGRANVGVTEFDGVTCLKMTLLNPIVTLEDIKLLLALVEKTAQQ 486
Cdd:COG0076 394 RYKPAGLDEEDA-----LNYALRDRLRARGRAFLSPTKLDGRVVLRLVVLNPRTTEDDVDALLDDLREAAAE 460
|
|
| DOPA_deC_like |
cd06450 |
DOPA decarboxylase family. This family belongs to pyridoxal phosphate (PLP)-dependent ... |
85-482 |
5.68e-119 |
|
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: 352.66 E-value: 5.68e-119
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727188709 85 CVAHLHCPSLVISQAAEVLINATNQSMDSWDQSPSATLIEMKLIEWLRAQVGYQPGDA-GVFTSGGTQSNLMGLMLARDA 163
Cdd:cd06450 1 FLAGFVTTMDPPALLLEMLTSAKNAIDFTWDESPAATEMEAEVVNWLAKLFGLPSEDAdGVFTSGGSESNLLALLAARDR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727188709 164 FFARQghsvqQDGLVGDLRKLKVFCSENAHFSVQKNMALMGlgyQSVTLVKTDRFARMDVNDLAEKLAQAKANGEQVMAL 243
Cdd:cd06450 81 ARKRL-----KAGGGRGIDKLVIVCSDQAHVSVEKAAAYLD---VKVRLVPVDEDGRMDPEALEAAIDEDKAEGLNPIMV 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727188709 244 VATAGTTDAGAIDPLRDIARLAAEQKIWVHVDAAWGGALLLSEQYRDYLDGLELVDSITLDFHKQFFQTISCGAFLLKde 323
Cdd:cd06450 153 VATAGTTDTGAIDPLEEIADLAEKYDLWLHVDAAYGGFLLPFPEPRHLDFGIERVDSISVDPHKYGLVPLGCSAVLVR-- 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727188709 324 rhyelmryqaaylnsefdeaqgvpnlvskslqttrrfdALKLWMGLEALGQKQYAEIIDHGVSLAQQVARYIADQESLEL 403
Cdd:cd06450 231 --------------------------------------ALKLWATLRRFGRDGYGEHIDRIVDLAKYLAELIRADPGFEL 272
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 727188709 404 VMQPQLASVLFRYRPaqlaakgDAAVALFNQRIGDALLESGRANVGVTEFDGVTCLKMTLLNPIVTLEDIKLLLALVEK 482
Cdd:cd06450 273 LGEPNLSLVCFRLKP-------SVKLDELNYDLSDRLNERGGWHVPATTLGGPNVLRFVVTNPLTTRDDADALLEDIER 344
|
|
| NOD_PanD_pyr |
TIGR03799 |
putative pyridoxal-dependent aspartate 1-decarboxylase; This enzyme is proposed here to be a ... |
143-473 |
1.00e-61 |
|
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: 209.98 E-value: 1.00e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727188709 143 GVFTSGGTQSNLMGLMLARDAFFARQG--HSVQQDGLVGDLR-----KLKVFCSENAHFSVQKNMALMGLGYQSVTLVKT 215
Cdd:TIGR03799 162 GAFCSGGTVANITALWVARNRLLKADGdfRGIAREGLFAALRhygydGLAILVSERGHYSLGKAADVLGIGRDNLVPVKT 241
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727188709 216 DRFARMDVNDLAEKLAQAKANGEQVMALVATAGTTDAGAIDPLRDIARLAAEQKIWVHVDAAWGGALLLSEQYRDYLDGL 295
Cdd:TIGR03799 242 DENNRIRVDALRDKCLELAAQNIKPMAIVGVAGTTETGNIDPLDEMADIAQEAGCHFHVDAAWGGATLLSNTYRHLLKGI 321
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727188709 296 ELVDSITLDFHKQFFQTISCGAFLLKDERHYELMRYQAAYLNSefdeaQGVPNLVSKSLQTTRRFDALKLWMGLEALGQK 375
Cdd:TIGR03799 322 ERADSVTIDAHKQMYVPMGAGMVLFKDPALTSAIEHHAEYILR-----KGSKDLGSHTLEGSRPGMAMLVYACLHIIGRK 396
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727188709 376 QYAEIIDHGVSLAQQVARYIADQESLELVMQPQLASVLFRYRPAQLAAKGDAAVALFNQRIGDAL-----------LESG 444
Cdd:TIGR03799 397 GYEMLINQSIDKAHYFANLIDQQPDFELVTEPELCLLTYRYVPENVKAALAIADEEQREKINDALnaltkfiqkrqRETG 476
|
330 340 350
....*....|....*....|....*....|....*....
gi 727188709 445 RANVG-----VTEFDG--VTCLKMTLLNPIVT---LEDI 473
Cdd:TIGR03799 477 KSFVSrtrltPAQYDHqpTIVFRVVLANPLTTheiLQDI 515
|
|
| Pyridoxal_deC |
pfam00282 |
Pyridoxal-dependent decarboxylase conserved domain; |
66-417 |
8.33e-61 |
|
Pyridoxal-dependent decarboxylase conserved domain;
Pssm-ID: 395219 Cd Length: 373 Bit Score: 203.42 E-value: 8.33e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727188709 66 IERAIEYFLKDSlsvHHPQCVAHLHCPSLVISQAAEVLINATNQSMDSWDQSPSATLIEMKLIEWLRAQVGY------QP 139
Cdd:pfam00282 26 IRRNLMPGVTTW---HSPHFHAYMPTGNSYPSLLGDMLTDAINCNGFTWESSPACTELENVVMNWLGEMLGLpaeflgQE 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727188709 140 GDaGVFTSGGTQSNLMGLMLARDAFFAR---QGHSVQQDGLVGdlrKLKVFCSENAHFSVQKNMALMGLGyqsVTLVKTD 216
Cdd:pfam00282 103 GG-GVLQPGSSESNLLALLAARTKWIKRmkaAGKPADSSGILA---KLVAYTSDQAHSSIEKAALYGGVK---LREIPSD 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727188709 217 RFARMDVNDLAEKLAQAKANGEQVMALVATAGTTDAGAIDPLRDIARLAAEQKIWVHVDAAWGGALLLSEQYRDYLDGLE 296
Cdd:pfam00282 176 DNGKMRGMDLEKAIEEDKENGLIPFFVVATLGTTGSGAFDDLQELGDICAKHNLWLHVDAAYGGSAFICPEFRHWLFGIE 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727188709 297 LVDSITLDFHKQFFQTISCGAFLLKDER--HYELmRYQAAYLNSEfdeaQGVPNLVSKSLQTTRRFDALKLWMGLEALGQ 374
Cdd:pfam00282 256 RADSITFNPHKWMLVLLDCSAVWVKDKEalQQAF-QFNPLYLGHT----DSAYDTGHKQIPLSRRFRILKLWFVIRSLGV 330
|
330 340 350 360
....*....|....*....|....*....|....*....|...
gi 727188709 375 KQYAEIIDHGVSLAQQVARYIADQESLELVMQPQLASVLFRYR 417
Cdd:pfam00282 331 EGLQNQIRRHVELAQYLEALIRKDGRFEICAEVGLGLVCFRLK 373
|
|
| PLN02880 |
PLN02880 |
tyrosine decarboxylase |
101-487 |
1.70e-37 |
|
tyrosine decarboxylase
Pssm-ID: 215475 [Multi-domain] Cd Length: 490 Bit Score: 143.51 E-value: 1.70e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727188709 101 EVLINATNQSMDSWDQSPSATLIEMKLIEWLrAQVGYQPGD-------AGVFTSGGTQSNLMGLMLARDAFFARQGHSVq 173
Cdd:PLN02880 101 EMLSAGLNIVGFSWITSPAATELEMIVLDWL-AKLLNLPEQflstgngGGVIQGTASEAVLVVLLAARDRVLRKVGKNA- 178
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727188709 174 qdglvgdLRKLKVFCSENAHFSVQKNMALMGLGYQSVTLVKTDRFARMDV--NDLAEKLAQAKANGEQVMALVATAGTTD 251
Cdd:PLN02880 179 -------LEKLVVYASDQTHSALQKACQIAGIHPENCRLLKTDSSTNYALapELLSEAISTDLSSGLIPFFLCATVGTTS 251
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727188709 252 AGAIDPLRDIARLAAEQKIWVHVDAAWGGALLLSEQYRDYLDGLELVDSITLDFHKQFFQTISCGAFLLKDeRHYELmry 331
Cdd:PLN02880 252 STAVDPLLELGKIAKSNGMWFHVDAAYAGSACICPEYRHYIDGVEEADSFNMNAHKWFLTNFDCSLLWVKD-RNALI--- 327
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727188709 332 QAAYLNSEF-----DEAQGVPNLVSKSLQTTRRFDALKLWMGLEALGQKQYAEIIDHGVSLAQQVARYIADQESLELVMQ 406
Cdd:PLN02880 328 QSLSTNPEFlknkaSQANSVVDYKDWQIPLGRRFRSLKLWMVLRLYGVENLQSYIRNHIKLAKEFEQLVAQDSRFEVVTP 407
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727188709 407 PQLASVLFRYRPaqLAAKGDAAVALfNQRIGDALLESGRANVGVTEFDGVTCLKMTLLNPIVTLEDIKLLLALVEKTAQQ 486
Cdd:PLN02880 408 RIFSLVCFRLVP--PKNNEDNGNKL-NHDLLDAVNSSGKIFISHTVLSGKYVLRFAVGAPLTEERHVTAAWKVLQDEASK 484
|
.
gi 727188709 487 L 487
Cdd:PLN02880 485 L 485
|
|
| PLN02590 |
PLN02590 |
probable tyrosine decarboxylase |
113-418 |
2.34e-37 |
|
probable tyrosine decarboxylase
Pssm-ID: 178200 [Multi-domain] Cd Length: 539 Bit Score: 144.08 E-value: 2.34e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727188709 113 SWDQSPSATLIEMKLIEWLrAQVGYQP-------GDAGVFTSGGTQSNLMGLMLARDAFFARQGHSVqqdglvgdLRKLK 185
Cdd:PLN02590 161 TWLTSPAATELEIIVLDWL-AKLLQLPdhflstgNGGGVIQGTGCEAVLVVVLAARDRILKKVGKTL--------LPQLV 231
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727188709 186 VFCSENAHFSVQKNMALMGLGYQSVTLVKTDRFAR--MDVNDLAEKLAQAKANGEQVMALVATAGTTDAGAIDPLRDIAR 263
Cdd:PLN02590 232 VYGSDQTHSSFRKACLIGGIHEENIRLLKTDSSTNygMPPESLEEAISHDLAKGFIPFFICATVGTTSSAAVDPLVPLGN 311
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727188709 264 LAAEQKIWVHVDAAWGGALLLSEQYRDYLDGLELVDSITLDFHKQFFQTISCGAFLLKDErhYEL---MRYQAAYLNSEF 340
Cdd:PLN02590 312 IAKKYGIWLHVDAAYAGNACICPEYRKFIDGIENADSFNMNAHKWLFANQTCSPLWVKDR--YSLidaLKTNPEYLEFKV 389
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 727188709 341 DEAQGVPNLVSKSLQTTRRFDALKLWMGLEALGQKQYAEIIDHGVSLAQQVARYIADQESLELVMQPQLASVLFRYRP 418
Cdd:PLN02590 390 SKKDTVVNYKDWQISLSRRFRSLKLWMVLRLYGSENLRNFIRDHVNLAKHFEDYVAQDPSFEVVTTRYFSLVCFRLAP 467
|
|
| PRK02769 |
PRK02769 |
histidine decarboxylase; Provisional |
143-389 |
2.61e-16 |
|
histidine decarboxylase; Provisional
Pssm-ID: 235068 [Multi-domain] Cd Length: 380 Bit Score: 80.47 E-value: 2.61e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727188709 143 GVFTSGGTQSNLMGLMLARDAFfarqghsvqQDGLvgdlrklkVFCSENAHFSVQKNMALMGLGYQsvtLVKTDRFARMD 222
Cdd:PRK02769 87 GYITNGGTEGNLYGCYLARELF---------PDGT--------LYYSKDTHYSVSKIARLLRIKSR---VITSLPNGEID 146
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727188709 223 VNDLAEKLaqaKANGEQVMALVATAGTTDAGAIDPLRDIARLAAEQKI---WVHVDAAWGGALLL---SEQYRDYLDGle 296
Cdd:PRK02769 147 YDDLISKI---KENKNQPPIIFANIGTTMTGAIDNIKEIQEILKKIGIddyYIHADAALSGMILPfvnNPPPFSFADG-- 221
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727188709 297 lVDSITLDFHKQFFQTISCGAFLLKDErHYELMRYQAAYLNSEFDEAQGVPNLVSkslqttrrfdALKLWMGLEALGQKQ 376
Cdd:PRK02769 222 -IDSIAISGHKFIGSPMPCGIVLAKKK-YVERISVDVDYIGSRDQTISGSRNGHT----------ALLLWAAIRSLGSKG 289
|
250
....*....|...
gi 727188709 377 YAEIIDHGVSLAQ 389
Cdd:PRK02769 290 LRQRVQHCLDMAQ 302
|
|
| AAT_I |
cd01494 |
Aspartate aminotransferase (AAT) superfamily (fold type I) of pyridoxal phosphate (PLP) ... |
126-309 |
3.82e-13 |
|
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: 67.41 E-value: 3.82e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727188709 126 KLIEWLRAQvgYQPG-DAGVFTSGGTQSNLMGLMlardafFARQGHSVqqdglvgdlrklkVFCSENAHFSVQKNMALMG 204
Cdd:cd01494 4 ELEEKLARL--LQPGnDKAVFVPSGTGANEAALL------ALLGPGDE-------------VIVDANGHGSRYWVAAELA 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727188709 205 lGYQSVTLVKTDRFARMDVNDLAEKLAqakaNGEQVMALVATAGTTDAGAIDPLRDIARLAAEQKIWVHVDAAWGGALLL 284
Cdd:cd01494 63 -GAKPVPVPVDDAGYGGLDVAILEELK----AKPNVALIVITPNTTSGGVLVPLKEIRKIAKEYGILLLVDAASAGGASP 137
|
170 180
....*....|....*....|....*
gi 727188709 285 SEQYRDYLDGlelVDSITLDFHKQF 309
Cdd:cd01494 138 APGVLIPEGG---ADVVTFSLHKNL 159
|
|
| Beta_elim_lyase |
pfam01212 |
Beta-eliminating lyase; |
126-347 |
6.46e-08 |
|
Beta-eliminating lyase;
Pssm-ID: 426128 [Multi-domain] Cd Length: 288 Bit Score: 54.14 E-value: 6.46e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727188709 126 KLIEWLRAQVGYqpgDAGVFTSGGTQSNLMGLMLardafFARQGHSVqqdglvgdlrklkvFCSENAH--FSVQKNMALM 203
Cdd:pfam01212 36 RLEDRVAELFGK---EAALFVPSGTAANQLALMA-----HCQRGDEV--------------ICGEPAHihFDETGGHAEL 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727188709 204 GlGYQSVTlVKTDRFARMDVNDLAEKLAQAKANGEQVMALVATAGTTDAGA-----IDPLRDIARLAAEQKIWVHVDAA- 277
Cdd:pfam01212 94 G-GVQPRP-LDGDEAGNMDLEDLEAAIREVGADIFPPTGLISLENTHNSAGgqvvsLENLREIAALAREHGIPVHLDGAr 171
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 727188709 278 -WGGALLLSEQYRDYLDGlelVDSITLDFHKQFFQTIscGAFLLKDERHYELMRYQAAYLNSEFDEAqGVP 347
Cdd:pfam01212 172 fANAAVALGVIVKEITSY---ADSVTMCLSKGLGAPV--GSVLAGSDDFIAKAIRQRKYLGGGLRQA-GVL 236
|
|
| PLN03032 |
PLN03032 |
serine decarboxylase; Provisional |
143-428 |
7.18e-07 |
|
serine decarboxylase; Provisional
Pssm-ID: 166673 [Multi-domain] Cd Length: 374 Bit Score: 51.37 E-value: 7.18e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727188709 143 GVFTSGGTQSNLMGLMLARDAFfarqghsvqQDGLvgdlrklkVFCSENAHFSVQKNMALMGLGYQSvtlVKTDRFARMD 222
Cdd:PLN03032 88 GYITTCGTEGNLHGILVGREVF---------PDGI--------LYASRESHYSVFKAARMYRMEAVK---VPTLPSGEID 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727188709 223 VNDLAEKLAQakaNGEQVMALVATAGTTDAGAIDPLRDIARLA-----AEQKIWVHVDAAWGGALLLSEQYRDYLDGLEL 297
Cdd:PLN03032 148 YDDLERALAK---NRDKPAILNVNIGTTVKGAVDDLDRILRILkelgyTEDRFYIHCDGALFGLMMPFVSRAPEVTFRKP 224
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727188709 298 VDSITLDFHKQFFQTISCGAFLLKDErHYELMRYQAAYLNSefdeaqgvpnlVSKSLQTTRRFDA-LKLWMGLEALGQKQ 376
Cdd:PLN03032 225 IGSVSVSGHKFLGCPMPCGVALTRKK-HVKALSQNVEYLNS-----------RDATIMGSRNGHApLYLWYTLRRKGYRG 292
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 727188709 377 YAEIIDHgvslAQQVARYIAD--QESLELVMQPQLASVLFRYRPA--------QLAAKGDAA 428
Cdd:PLN03032 293 IKRDVQH----CMRNAHYLKDrlTEAGLTCRLNELSSTVVFERPMdeafikkwQLACEGDIA 350
|
|
| PLN02651 |
PLN02651 |
cysteine desulfurase |
128-277 |
9.37e-05 |
|
cysteine desulfurase
Pssm-ID: 178257 [Multi-domain] Cd Length: 364 Bit Score: 44.65 E-value: 9.37e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727188709 128 IEWLRAQVGY---QPGDAGVFTSGGTQSNLMGLMLARDAFFARQGHsvqqdglvgdlrklkVFCSENAHFSVQKNMALMG 204
Cdd:PLN02651 45 VEKARAQVAAligADPKEIIFTSGATESNNLAIKGVMHFYKDKKKH---------------VITTQTEHKCVLDSCRHLQ 109
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 727188709 205 LGYQSVTLVKTDRFARMDVNDLAEKLAQAKAngeqvmaLVAT-AGTTDAGAIDPLRDIARLAAEQKIWVHVDAA 277
Cdd:PLN02651 110 QEGFEVTYLPVKSDGLVDLDELAAAIRPDTA-------LVSVmAVNNEIGVIQPVEEIGELCREKKVLFHTDAA 176
|
|
| KBL_like |
cd06454 |
KBL_like; this family belongs to the pyridoxal phosphate (PLP)-dependent aspartate ... |
217-334 |
1.42e-03 |
|
KBL_like; this family belongs to the pyridoxal phosphate (PLP)-dependent aspartate aminotransferase superfamily (fold I). The major groups in this CD corresponds to serine palmitoyltransferase (SPT), 5-aminolevulinate synthase (ALAS), 8-amino-7-oxononanoate synthase (AONS), and 2-amino-3-ketobutyrate CoA ligase (KBL). SPT is responsible for the condensation of L-serine with palmitoyl-CoA to produce 3-ketodihydrospingosine, the reaction of the first step in sphingolipid biosynthesis. ALAS is involved in heme biosynthesis; it catalyzes the synthesis of 5-aminolevulinic acid from glycine and succinyl-coenzyme A. AONS catalyses the decarboxylative condensation of l-alanine and pimeloyl-CoA in the first committed step of biotin biosynthesis. KBL catalyzes the second reaction step of the metabolic degradation pathway for threonine converting 2-amino-3-ketobutyrate, to glycine and acetyl-CoA. The members of this CD are widely found in all three forms of life.
Pssm-ID: 99747 [Multi-domain] Cd Length: 349 Bit Score: 40.62 E-value: 1.42e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727188709 217 RFARMDVNDLAEKLAQAKANGEQVmaLVATAG--TTDaGAIDPLRDIARLAAEQKIWVHVDAAWG-GALLLSEQYRDYLD 293
Cdd:cd06454 111 IFKHNDMEDLEKLLREARRPYGKK--LIVTEGvySMD-GDIAPLPELVDLAKKYGAILFVDEAHSvGVYGPHGRGVEEFG 187
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 727188709 294 GL-ELVDSITLDFHKQFFqtiSCGAFLLKDERHYELMRYQAA 334
Cdd:cd06454 188 GLtDDVDIIMGTLGKAFG---AVGGYIAGSKELIDYLRSYAR 226
|
|
| TA_like |
cd06502 |
Low-specificity threonine aldolase (TA). This family belongs to pyridoxal phosphate (PLP) ... |
142-482 |
2.25e-03 |
|
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: 40.01 E-value: 2.25e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727188709 142 AGVFTSGGTQSNLMGLMLardafFARQGHSvqqdglvgdlrklkVFCSENAHFSVQKNMALMGLGYQSVTLVKTDRfARM 221
Cdd:cd06502 49 AALFVPSGTAANQLALAA-----HTQPGGS--------------VICHETAHIYTDEAGAPEFLSGVKLLPVPGEN-GKL 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727188709 222 DVNDLAEKLAQAKANGEQVMALVATAGTTDAGAIDP---LRDIARLAAEQKIWVHVD--------AAWGGALllsEQYRD 290
Cdd:cd06502 109 TPEDLEAAIRPRDDIHFPPPSLVSLENTTEGGTVYPldeLKAISALAKENGLPLHLDgarlanaaAALGVAL---KTYKS 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727188709 291 YldglelVDSITLDFHKQFFQTIscGAFLLKDERHYELMRYqaaylnseFDEAQGvpNLVSKSlqttrRFDALKlwmGLE 370
Cdd:cd06502 186 G------VDSVSFCLSKGGGAPV--GAVVVGNRDFIARARR--------RRKQAG--GGMRQS-----GFLAAA---GLA 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727188709 371 ALGQKQYAEIIDHGVSLAQQVARYIadqESLELVMQPQLASVLFryrpaqLAAKGDAAVALfnqRIGDALLESGRANVGV 450
Cdd:cd06502 240 ALENDLWLRRLRHDHEMARRLAEAL---EELGGLESEVQTNIVL------LDPVEANAVFV---ELSKEAIERRGEGVLF 307
|
330 340 350
....*....|....*....|....*....|..
gi 727188709 451 TEFDGVTCLKMTLLNpiVTLEDIKLLLALVEK 482
Cdd:cd06502 308 YAWGEGGVRFVTHWD--TTEEDVDELLSALKA 337
|
|
| PLN02263 |
PLN02263 |
serine decarboxylase |
143-283 |
8.48e-03 |
|
serine decarboxylase
Pssm-ID: 177904 [Multi-domain] Cd Length: 470 Bit Score: 38.64 E-value: 8.48e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727188709 143 GVFTSGGTQSNLMGLMLARDAFfarqghsvqQDGLvgdlrklkVFCSENAHFSVQKNMALMGLGYQSV-TLVKtdrfARM 221
Cdd:PLN02263 155 GYITNCGTEGNLHGILVGREVF---------PDGI--------LYASRESHYSVFKAARMYRMECVKVdTLVS----GEI 213
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 727188709 222 DVNDLAEKLAqakANGEQVMALVATAGTTDAGAIDPLRDIARLAAE-----QKIWVHVDAAWGGALL 283
Cdd:PLN02263 214 DCADFKAKLL---ANKDKPAIINVNIGTTVKGAVDDLDLVIKTLEEcgfsqDRFYIHCDGALFGLMM 277
|
|
| |
