|
Name |
Accession |
Description |
Interval |
E-value |
| PLN02483 |
PLN02483 |
serine palmitoyltransferase |
1-489 |
0e+00 |
|
serine palmitoyltransferase
Pssm-ID: 178101 [Multi-domain] Cd Length: 489 Bit Score: 1068.61 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229023 1 MITIPYLTAVSTYFSYGLLFAFGQLRDYSRLIFDWWRTNNLQGYAPICLAHEDFYIRRLYHRIQDCFGRPISSAPDAWID 80
Cdd:PLN02483 1 MITIPYLTALTTYFSYGLLFAFGQLRDFFRAILDWWKTSNLQGYAPICLGLEDFYIRRLYLRIQDCFNRPIASAPDAWFD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229023 81 VVERVSDDNNKTLKRTTKTSRCLNLGSYNYLGFGSFDEYCTPRVIESLKKFSASTCSSRVDAGTTSVHAELEDCVAKYVG 160
Cdd:PLN02483 81 VVERVSNDNNKTLKRTTKTRRCLNLGSYNYLGFAAADEYCTPRVIESLKKYSASTCSSRVDGGTTKLHRELEELVARFVG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229023 161 QPAAVIFGMGYATNSAIIPVLIGKGGLIISDSLNHTSIVNGARGSGATIRVFQHNTPGHLEKVLKEQIAEGQPRTHRPWK 240
Cdd:PLN02483 161 KPAAIVFGMGYATNSTIIPALIGKGGLIISDSLNHNSIVNGARGSGATIRVFQHNTPSHLEEVLREQIAEGQPRTHRPWK 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229023 241 KIIVVVEGIYSMEGEICHLPEIVSICKKYKAYVYLDEAHSIGAIGKTGRGVCELLGVDTSDVDIMMGTFTKSFGSCGGYI 320
Cdd:PLN02483 241 KIIVIVEGIYSMEGELCKLPEIVAVCKKYKAYVYLDEAHSIGAVGKTGRGVCELLGVDPADVDIMMGTFTKSFGSCGGYI 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229023 321 AGSKDLIQYLKHQCPAHLYATSISTPSATQIISAIKVILGEDGSNRGAQKLARIRENSNFFRAELQKMGFEVLGDNDSPV 400
Cdd:PLN02483 321 AGSKELIQYLKRTCPAHLYATSMSPPAVQQVISAIKVILGEDGTNRGAQKLAQIRENSNFFRSELQKMGFEVLGDNDSPV 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229023 401 MPIMLYNPAKIPAFSRECLRENLAVVVVGFPATPLLLARARICISASHSREDLIKALQVISKAGDLTGIKYFPAAPKKQE 480
Cdd:PLN02483 401 MPIMLYNPAKIPAFSRECLKQNVAVVVVGFPATPLLLARARICISASHSREDLIKALEVISEVGDLVGIKYFPAEPKKQE 480
|
....*....
gi 15229023 481 VEKNGIKLD 489
Cdd:PLN02483 481 QVKKFIKLE 489
|
|
| KBL_like |
cd06454 |
KBL_like; this family belongs to the pyridoxal phosphate (PLP)-dependent aspartate ... |
100-464 |
2.15e-166 |
|
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: 473.59 E-value: 2.15e-166
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229023 100 SRCLNLGSYNYLGFgSFDEYCTPRVIESLKKFSASTCSSRVDAGTTSVHAELEDCVAKYVGQPAAVIFGMGYATNSAIIP 179
Cdd:cd06454 1 KKVLNFCSNDYLGL-ANHPEVIEAAKEALDKYGVGAGGSRLISGTSDLHEELEEELAEFHGKEAALVFSSGYAANDGVLS 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229023 180 VLIGKGGLIISDSLNHTSIVNGARGSGATIRVFQHNTPGHLEKVLKEQIaegqprthRPWKKIIVVVEGIYSMEGEICHL 259
Cdd:cd06454 80 TLAGKGDLIISDSLNHASIIDGIRLSGAKKRIFKHNDMEDLEKLLREAR--------RPYGKKLIVTEGVYSMDGDIAPL 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229023 260 PEIVSICKKYKAYVYLDEAHSIGAIGKTGRGVCElLGVDTSDVDIMMGTFTKSFGSCGGYIAGSKDLIQYLKHQCPAHLY 339
Cdd:cd06454 152 PELVDLAKKYGAILFVDEAHSVGVYGPHGRGVEE-FGGLTDDVDIIMGTLGKAFGAVGGYIAGSKELIDYLRSYARGFIF 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229023 340 ATSISTPSATQIISAIKVILGEDgsnrgaQKLARIRENSNFFRAELQKMGFEVLGDNDSPVMPIMLYNPAKIPAFSRECL 419
Cdd:cd06454 231 STSLPPAVAAAALAALEVLQGGP------ERRERLQENVRYLRRGLKELGFPVGGSPSHIIPPLIGDDPAKAVAFSDALL 304
|
330 340 350 360
....*....|....*....|....*....|....*....|....*
gi 15229023 420 RENLAVVVVGFPATPLLLARARICISASHSREDLIKALQVISKAG 464
Cdd:cd06454 305 ERGIYVQAIRYPTVPRGTARLRISLSAAHTKEDIDRLLEALKEVG 349
|
|
| BioF |
COG0156 |
7-keto-8-aminopelargonate synthetase or related enzyme [Coenzyme transport and metabolism]; ... |
69-465 |
3.28e-130 |
|
7-keto-8-aminopelargonate synthetase or related enzyme [Coenzyme transport and metabolism]; 7-keto-8-aminopelargonate synthetase or related enzyme is part of the Pathway/BioSystem: Biotin biosynthesis
Pssm-ID: 439926 [Multi-domain] Cd Length: 385 Bit Score: 382.86 E-value: 3.28e-130
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229023 69 RPISSAPDAWIDVVERvsddnnktlkrttktsRCLNLGSYNYLGFgSFDeyctPRVIE----SLKKFSASTCSSRVDAGT 144
Cdd:COG0156 22 RVLESPQGPRVTIDGR----------------EVLNFSSNDYLGL-ANH----PRVIEaaaeALDRYGTGSGGSRLVSGT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229023 145 TSVHAELEDCVAKYVGQPAAVIFGMGYATNSAIIPVLIGKGGLIISDSLNHTSIVNGARGSGATIRVFQHNTPGHLEKVL 224
Cdd:COG0156 81 TPLHEELEEELAEFLGKEAALLFSSGYAANLGVISALAGRGDLIFSDELNHASIIDGARLSGAKVVRFRHNDMDDLERLL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229023 225 KEqiaegqprtHRPWKKIIVVVEGIYSMEGEICHLPEIVSICKKYKAYVYLDEAHSIGAIGKTGRGVCELLGVdTSDVDI 304
Cdd:COG0156 161 KK---------ARAARRKLIVTDGVFSMDGDIAPLPEIVELAEKYGALLYVDDAHGTGVLGETGRGLVEHFGL-EDRVDI 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229023 305 MMGTFTKSFGSCGGYIAGSKDLIQYLKHQCPAHLYATSISTPSATQIISAIKVILGEDgsnrgaQKLARIRENSNFFRAE 384
Cdd:COG0156 231 IMGTLSKALGSSGGFVAGSKELIDYLRNRARPFIFSTALPPAVAAAALAALEILREEP------ELRERLWENIAYFREG 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229023 385 LQKMGFEvLGDNDSPVMPIMLYNPAKIPAFSRECLRENLAVVVVGFPATPLLLARARICISASHSREDLIKALQVISKAG 464
Cdd:COG0156 305 LKELGFD-LGPSESPIVPVIVGDAERALALADALLERGIYVSAIRPPTVPKGTARLRITLSAAHTEEDIDRLLEALAEVG 383
|
.
gi 15229023 465 D 465
Cdd:COG0156 384 K 384
|
|
| PRK05958 |
PRK05958 |
8-amino-7-oxononanoate synthase; Reviewed |
69-464 |
1.91e-92 |
|
8-amino-7-oxononanoate synthase; Reviewed
Pssm-ID: 235655 [Multi-domain] Cd Length: 385 Bit Score: 285.90 E-value: 1.91e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229023 69 RPISSAPDAWIDVVERvsddnnktlkrttktsRCLNLGSYNYLGFGSfdeycTPRVIE----SLKKFSASTCSSRVDAGT 144
Cdd:PRK05958 24 RPREGGAGRWLVVDGR----------------RMLNFASNDYLGLAR-----HPRLIAaaqqAARRYGAGSGGSRLVTGN 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229023 145 TSVHAELEDCVAKYVGQPAAVIFGMGYATNSAIIPVLIGKGGLIISDSLNHTSIVNGARGSGATIRVFQHNTPGHLEKVL 224
Cdd:PRK05958 83 SPAHEALEEELAEWFGAERALLFSSGYAANLAVLTALAGKGDLIVSDKLNHASLIDGARLSRARVRRYPHNDVDALEALL 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229023 225 KeqiaegQPRTHRPWkkiiVVVEGIYSMEGEICHLPEIVSICKKYKAYVYLDEAHSIGAIGKTGRGVCELLGVDTSDVDI 304
Cdd:PRK05958 163 A------KWRAGRAL----IVTESVFSMDGDLAPLAELVALARRHGAWLLVDEAHGTGVLGPQGRGLAAEAGLAGEPDVI 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229023 305 MMGTFTKSFGSCGGYIAGSKDLIQYLKHQCPAHLYATSIStPSATQIIS-AIKVILGEDgsnrgaQKLARIRENSNFFRA 383
Cdd:PRK05958 233 LVGTLGKALGSSGAAVLGSETLIDYLINRARPFIFTTALP-PAQAAAARaALRILRREP------ERRERLAALIARLRA 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229023 384 ELQKMGFEvLGDNDSPVMPIMLYNPAKIPAFSRECLRENLAVVVVGFPATPLLLARARICISASHSREDLIKALQVISKA 463
Cdd:PRK05958 306 GLRALGFQ-LMDSQSAIQPLIVGDNERALALAAALQEQGFWVGAIRPPTVPAGTSRLRITLTAAHTEADIDRLLEALAEA 384
|
.
gi 15229023 464 G 464
Cdd:PRK05958 385 L 385
|
|
| PRK06939 |
PRK06939 |
2-amino-3-ketobutyrate coenzyme A ligase; Provisional |
59-469 |
1.05e-86 |
|
2-amino-3-ketobutyrate coenzyme A ligase; Provisional
Pssm-ID: 235893 [Multi-domain] Cd Length: 397 Bit Score: 271.68 E-value: 1.05e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229023 59 LYHRIqdcfgRPISSAPDAWIDVvervsdDNNKTLkrttktsrcLNLGSYNYLGFGSfdeycTPRVI----ESLKKFSAS 134
Cdd:PRK06939 21 LYKEE-----RVITSPQGADITV------ADGKEV---------INFCANNYLGLAN-----HPELIaaakAALDSHGFG 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229023 135 TCSSRVDAGTTSVHAELEDCVAKYVGQPAAVIFGMGYATNSAIIPVLIGKGGLIISDSLNHTSIVNGARGSGATIRVFQH 214
Cdd:PRK06939 76 MASVRFICGTQDLHKELEEKLAKFLGTEDAILYSSCFDANGGLFETLLGKEDAIISDALNHASIIDGVRLCKAKRYRYAN 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229023 215 NTPGHLEKVLKEQIAEGQprthrpwKKIIVVVEGIYSMEGEICHLPEIVSICKKYKAYVYLDEAHSIGAIGKTGRGVCEL 294
Cdd:PRK06939 156 NDMADLEAQLKEAKEAGA-------RHKLIATDGVFSMDGDIAPLPEICDLADKYDALVMVDDSHAVGFVGENGRGTVEH 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229023 295 LGVDtSDVDIMMGTFTKSF-GSCGGYIAGSKDLIQYLKHQCPAHLYATSISTPSATQIISAIKvILGEDGSNRgaqklAR 373
Cdd:PRK06939 229 FGVM-DRVDIITGTLGKALgGASGGYTAGRKEVIDWLRQRSRPYLFSNSLAPAIVAASIKVLE-LLEESDELR-----DR 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229023 374 IRENSNFFRAELQKMGFEvLGDNDSPVMPIMLYNPAKIPAFSRECLRENLAVVVVGFPATPLLLARARICISASHSREDL 453
Cdd:PRK06939 302 LWENARYFREGMTAAGFT-LGPGEHPIIPVMLGDAKLAQEFADRLLEEGVYVIGFSFPVVPKGQARIRTQMSAAHTKEQL 380
|
410
....*....|....*.
gi 15229023 454 IKALQVISKAGDLTGI 469
Cdd:PRK06939 381 DRAIDAFEKVGKELGV 396
|
|
| PRK13392 |
PRK13392 |
5-aminolevulinate synthase; Provisional |
107-466 |
1.82e-53 |
|
5-aminolevulinate synthase; Provisional
Pssm-ID: 184023 [Multi-domain] Cd Length: 410 Bit Score: 185.44 E-value: 1.82e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229023 107 SYNYLGFGSfdeycTPRVI----ESLKKFSASTCSSRVDAGTTSVHAELEDCVAKYVGQPAAVIFGMGYATNSAIIPVLI 182
Cdd:PRK13392 53 SNDYLGMGQ-----HPDVIgamvDALDRYGAGAGGTRNISGTSHPHVLLERELADLHGKESALLFTSGYVSNDAALSTLG 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229023 183 GK--GGLIISDSLNHTSIVNGARGSGATIRVFQHNTPGHLEKVLKEQiaegqpRTHRPwkKIIvVVEGIYSMEGEICHLP 260
Cdd:PRK13392 128 KLlpGCVILSDALNHASMIEGIRRSGAEKQVFRHNDLADLEEQLASV------DPDRP--KLI-AFESVYSMDGDIAPIE 198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229023 261 EIVSICKKYKAYVYLDEAHSIGAIGKTGRGVCELLGVdTSDVDIMMGTFTKSFGSCGGYIAGSKDLIQYLKHQCPAHLYA 340
Cdd:PRK13392 199 AICDLADRYNALTYVDEVHAVGLYGARGGGIAERDGL-MDRIDMIQGTLAKAFGCLGGYIAASADLIDFVRSFAPGFIFT 277
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229023 341 TSISTPSATQIISAIKViLGEDGSNRGA--QKLARIrensnffRAELQKMGFEVLgDNDSPVMPIMLYNPAKIPAFSREC 418
Cdd:PRK13392 278 TALPPAVAAGATAAIRH-LKTSQTERDAhqDRVAAL-------KAKLNANGIPVM-PSPSHIVPVMVGDPTLCKAISDRL 348
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|..
gi 15229023 419 LREN-LAVVVVGFPATPLLLARARICISASHSRED---LIKALQVISKAGDL 466
Cdd:PRK13392 349 MSEHgIYIQPINYPTVPRGTERLRITPTPLHDDEDidaLVAALVAIWDRLEL 400
|
|
| PLN02822 |
PLN02822 |
serine palmitoyltransferase |
103-463 |
3.85e-50 |
|
serine palmitoyltransferase
Pssm-ID: 178417 [Multi-domain] Cd Length: 481 Bit Score: 178.01 E-value: 3.85e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229023 103 LNLGSYNYLGFGSfDEYCTPRVIESLKKFSASTCSSRVDAGTTSVHAELEDCVAKYVGQPAAVIFGMGYATNSAIIPVLI 182
Cdd:PLN02822 112 VNFASANYLGLIG-NEKIKESCTSALEKYGVGSCGPRGFYGTIDVHLDCETKIAKFLGTPDSILYSYGLSTIFSVIPAFC 190
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229023 183 GKGGLIISDSLNHTSIVNGARGSGATIRVFQHNTPGHLEKVLkEQIAEGQPRTHRPWKKIivVVEGIYSMEGEICHLPEI 262
Cdd:PLN02822 191 KKGDIIVADEGVHWGIQNGLYLSRSTIVYFKHNDMESLRNTL-EKLTAENKRKKKLRRYI--VVEAIYQNSGQIAPLDEI 267
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229023 263 VSICKKYKAYVYLDEAHSIGAIGKTGRGVCELLGVDTSDVDIMMGTFTKSFGSCGGYIAGSKDLIQYLKHQCPAHLYATS 342
Cdd:PLN02822 268 VRLKEKYRFRVLLDESNSFGVLGKSGRGLSEHFGVPIEKIDIITAAMGHALATEGGFCTGSARVVDHQRLSSSGYVFSAS 347
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229023 343 ISTPSATQIISAIKVIlgEDGSnrgaQKLARIRENSNFFRAELQKM-GFEVLGDNDSPVMPIMLYNP--------AKIPA 413
Cdd:PLN02822 348 LPPYLASAAITAIDVL--EDNP----SVLAKLKENIALLHKGLSDIpGLSIGSNTLSPIVFLHLEKStgsakedlSLLEH 421
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....
gi 15229023 414 FSRECLRENlAVVVVGFPATPL----LLARARICISASHSREDLIKALQVISKA 463
Cdd:PLN02822 422 IADRMLKED-SVLVVVSKRSTLdkcrLPVGIRLFVSAGHTESDILKASESLKRV 474
|
|
| PLN03227 |
PLN03227 |
serine palmitoyltransferase-like protein; Provisional |
103-465 |
2.89e-47 |
|
serine palmitoyltransferase-like protein; Provisional
Pssm-ID: 178766 [Multi-domain] Cd Length: 392 Bit Score: 168.16 E-value: 2.89e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229023 103 LNLGSYNYLGFgSFDEYCTPRVIESLKKFSASTCSSRVDAGTTSVHAELEDCVAKYVGQPAAVIFGMGYATNSAIIPVLI 182
Cdd:PLN03227 1 LNFATHDFLST-SSSPTLRQTALESLSHYGCGSCGPRGFYGTIDAHLELEQCMAEFLGTESAILYSDGASTTSSTVAAFA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229023 183 GKGGLIISDSLNHTSIVNGARGSGATIRVFQHNTPGHLEKVLkEQIAEG--QPRTHRPWKKIIVVVEGIYSMEGEICHLP 260
Cdd:PLN03227 80 KRGDLLVVDRGVNEALLVGVSLSRANVRWFRHNDMKDLRRVL-EQVRAQdvALKRKPTDQRRFLVVEGLYKNTGTLAPLK 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229023 261 EIVSICKKYKAYVYLDEAHSIGAIGKTGRGVCELLGVD-TSDVDIMMGTFTKSFGSCGGYIAGSKDLIQYLKHQCPAHLY 339
Cdd:PLN03227 159 ELVALKEEFHYRLILDESFSFGTLGKSGRGSLEHAGLKpMVHAEIVTFSLENAFGSVGGMTVGSEEVVDHQRLSGSGYCF 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229023 340 ATSISTPSATQIISAIKVIL-GEDGSNRGAQKLARIRE---NSNFFRAELQKMGFEVLGDNDSPVMPIMLynpAKIPA-- 413
Cdd:PLN03227 239 SASAPPFLAKADATATAGELaGPQLLNRLHDSIANLYStltNSSHPYALKLRNRLVITSDPISPIIYLRL---SDQEAtr 315
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15229023 414 ----------FSRECLRENLAVVVVGFPATPLLLARA----RICISASHSREDLIKALQVISKAGD 465
Cdd:PLN03227 316 rtdetlildqIAHHSLSEGVAVVSTGGHVKKFLQLVPppclRVVANASHTREDIDKLLTVLGEAVE 381
|
|
| Aminotran_1_2 |
pfam00155 |
Aminotransferase class I and II; |
102-460 |
3.19e-45 |
|
Aminotransferase class I and II;
Pssm-ID: 395103 [Multi-domain] Cd Length: 351 Bit Score: 161.70 E-value: 3.19e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229023 102 CLNLGSYNYLGFgsfdeyCTPRVIESLKKFSAstCSSRVDAGTTSVHAELEDCVAKYVGQP--------AAVIFGMGYAT 173
Cdd:pfam00155 3 KINLGSNEYLGD------TLPAVAKAEKDALA--GGTRNLYGPTDGHPELREALAKFLGRSpvlkldreAAVVFGSGAGA 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229023 174 N-SAIIPVLIGKGGLIISDSLNHTSIVNGARGSGATIRVF-------QHNTPGHLEKVLKEqiaegqprthrpwKKIIVV 245
Cdd:pfam00155 75 NiEALIFLLANPGDAILVPAPTYASYIRIARLAGGEVVRYplydsndFHLDFDALEAALKE-------------KPKVVL 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229023 246 VEGIYSMEGEIC---HLPEIVSICKKYKAYVYLDEAHSIGAIGkTGRGVCELLGVDTSDVDIMMGTFTKSFGSCG---GY 319
Cdd:pfam00155 142 HTSPHNPTGTVAtleELEKLLDLAKEHNILLLVDEAYAGFVFG-SPDAVATRALLAEGPNLLVVGSFSKAFGLAGwrvGY 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229023 320 IAGSKDLIQYLKhQCPAHLYATSISTPSATQIISAIKVILGEDGSNRgaqklARIRENSNFFRAELQKMGFEVLgDNDSP 399
Cdd:pfam00155 221 ILGNAAVISQLR-KLARPFYSSTHLQAAAAAALSDPLLVASELEEMR-----QRIKERRDYLRDGLQAAGLSVL-PSQAG 293
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15229023 400 VMPIMLYNPAKIPAFSREcLRENLAVVVVGFpATPLLLARARICIsASHSREDLIKALQVI 460
Cdd:pfam00155 294 FFLLTGLDPETAKELAQV-LLEEVGVYVTPG-SSPGVPGWLRITV-AGGTEEELEELLEAI 351
|
|
| PRK07179 |
PRK07179 |
quorum-sensing autoinducer synthase; |
151-475 |
3.37e-34 |
|
quorum-sensing autoinducer synthase;
Pssm-ID: 180866 [Multi-domain] Cd Length: 407 Bit Score: 132.83 E-value: 3.37e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229023 151 LEDCVAKYVGQPAAVIFGMGYATNSAIIPVLIGKGGLIISDSLNHTSIVNGARGSGATIRVFQHNTPGHLEKvlkeQIAE 230
Cdd:PRK07179 104 FEKKLAAFTGFESCLLCQSGWAANVGLLQTIADPNTPVYIDFFAHMSLWEGVRAAGAQAHPFRHNDVDHLRR----QIER 179
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229023 231 gqprtHRPWkkiIVVVEGIYSMEGEICHLPEIVSICKKYKAYVYLDEAHSIGAIGKTGRGVCELLGVdTSDVDIMMGTFT 310
Cdd:PRK07179 180 -----HGPG---IIVVDSVYSTTGTIAPLADIVDIAEEFGCVLVVDESHSLGTHGPQGAGLVAELGL-TSRVHFITASLA 250
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229023 311 KSFGSCGGYIAGSKDLIQYLKHQC-PAHLYAT----SISTPSATqiisaIKVILGEDgsnrgaQKLARIRENSNFFRAEL 385
Cdd:PRK07179 251 KAFAGRAGIITCPRELAEYVPFVSyPAIFSSTllphEIAGLEAT-----LEVIESAD------DRRARLHANARFLREGL 319
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229023 386 QKMGFEVLGdnDSPVMPIMLYNPAKIPAFSRECLRENLAVVVVGFPATPLLLARARICISASHSREDLIKALQVISKAGD 465
Cdd:PRK07179 320 SELGYNIRS--ESQIIALETGSERNTEVLRDALEERNVFGAVFCAPATPKNRNLIRLSLNADLTASDLDRVLEVCREARD 397
|
330
....*....|
gi 15229023 466 LTGIKYFPAA 475
Cdd:PRK07179 398 EVDLWFWKST 407
|
|
| PLN02955 |
PLN02955 |
8-amino-7-oxononanoate synthase |
95-474 |
1.10e-31 |
|
8-amino-7-oxononanoate synthase
Pssm-ID: 178541 [Multi-domain] Cd Length: 476 Bit Score: 127.10 E-value: 1.10e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229023 95 RTTKTSRCLNLGSYNYLGFGSFDEyCTPRVIESLKKFSASTCSSRVDAGTTSVHAELEDCVAKYVGQPAAVIFGMGYATN 174
Cdd:PLN02955 97 RKGRFKKLLLFSGNDYLGLSSHPT-ISNAAANAAKEYGMGPKGSALICGYTTYHRLLESSLADLKKKEDCLVCPTGFAAN 175
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229023 175 SAIIPVLIGKGGL--------------IISDSLNHTSIVNGAR-----GSgATIRVFQHNTPGHLEKVLkeqiaegqprT 235
Cdd:PLN02955 176 MAAMVAIGSVASLlaasgkplknekvaIFSDALNHASIIDGVRlaerqGN-VEVFVYRHCDMYHLNSLL----------S 244
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229023 236 HRPWKKIIVVVEGIYSMEGEICHLPEIVSICKKYKAYVYLDEAHSIGAIGKTGRGVCELLGVDtSDVDIMMGTFTKSFGS 315
Cdd:PLN02955 245 SCKMKRKVVVTDSLFSMDGDFAPMEELSQLRKKYGFLLVIDDAHGTFVCGENGGGVAEEFNCE-ADVDLCVGTLSKAAGC 323
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229023 316 CGGYIAGSKDLIQYLKHQCPAHLYATSISTPSATQIISAikVILGEDGSNRGAQKLARIREnsnfFRaelqkmgfEVLG- 394
Cdd:PLN02955 324 HGGFIACSKKWKQLIQSRGRSFIFSTAIPVPMAAAAYAA--VVVARKEKWRRKAIWERVKE----FK--------ALSGv 389
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229023 395 DNDSPVMPIMLYNPAKIPAFSRECLRENLAVVVVGFPATPLLLARARICISASHSREDLIKALQVISKAGDLTGIK-YFP 473
Cdd:PLN02955 390 DISSPIISLVVGNQEKALKASRYLLKSGFHVMAIRPPTVPPNSCRLRVTLSAAHTTEDVKKLITALSSCLDFDNTAtYIP 469
|
.
gi 15229023 474 A 474
Cdd:PLN02955 470 S 470
|
|
| PRK07505 |
PRK07505 |
hypothetical protein; Provisional |
64-465 |
3.48e-24 |
|
hypothetical protein; Provisional
Pssm-ID: 181006 [Multi-domain] Cd Length: 402 Bit Score: 104.29 E-value: 3.48e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229023 64 QDCFGRPISSAPDAWiDVVE-------RVSDDNNKTLkRTTKTSRCLNLGSYNYLGFGSfdeycTPRVIE----SLKKF- 131
Cdd:PRK07505 5 YRNNKKRINRAEKFW-DAAYdeglnglTVGEREGILI-TLADGHTFVNFVSCSYLGLDT-----HPAIIEgavdALKRTg 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229023 132 SASTCSSRVdAGTTSVHAELEDCVAKYVgQPAAVIFGMGYATNSAIIPvLIGKGGL-------IISDSLNHTSIvNGARG 204
Cdd:PRK07505 78 SLHLSSSRT-RVRSQILKDLEEALSELF-GASVLTFTSCSAAHLGILP-LLASGHLtggvpphMVFDKNAHASL-NILKG 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229023 205 SGAT---IRVFQHNTPGHLEKVLKEQiaegqprthrpwKKIIVVVEGIYSMeGEICHLPEIVSICKKYKAYVYLDEAHSI 281
Cdd:PRK07505 154 ICADeteVETIDHNDLDALEDICKTN------------KTVAYVADGVYSM-GGIAPVKELLRLQEKYGLFLYIDDAHGL 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229023 282 GAIGKTGRG-VCELLGVDTSDVDIMMGTFTKSFGSCGGYIA-GSKDLIQYLKHQCPAHLYATSISTPSATQIISAIKVIL 359
Cdd:PRK07505 221 SIYGKNGEGyVRSELDYRLNERTIIAASLGKAFGASGGVIMlGDAEQIELILRYAGPLAFSQSLNVAALGAILASAEIHL 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229023 360 GEDGSNRgaQKlaRIRENSNFFRAELQKMGFEvlgdNDSPVMPIMLYNPAKIPAFSRECLRENLAVVVVGFPATPLLLAR 439
Cdd:PRK07505 301 SEELDQL--QQ--KLQNNIALFDSLIPTEQSG----SFLPIRLIYIGDEDTAIKAAKQLLDRGFYTSPVFFPVVAKGRAG 372
|
410 420
....*....|....*....|....*.
gi 15229023 440 ARICISASHSREDLIKALQVISKAGD 465
Cdd:PRK07505 373 LRIMFRASHTNDEIKRLCSLLKEILD 398
|
|
| PRK05937 |
PRK05937 |
8-amino-7-oxononanoate synthase; Provisional |
136-436 |
6.92e-24 |
|
8-amino-7-oxononanoate synthase; Provisional
Pssm-ID: 102071 [Multi-domain] Cd Length: 370 Bit Score: 102.94 E-value: 6.92e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229023 136 CSSRVDAGTTSVHAELEDCVAKYVGQPAAVIFGMGYATNSAIIPVLIGKGGLIISDSLNHTSIVNGARGSGATIRVFQHN 215
Cdd:PRK05937 46 GGSRAILGPSSLLDDLEHKIAHFHGAPEAFIVPSGYMANLGLCAHLSSVTDYVLWDEQVHISVVYSLSVISGWHQSFRHN 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229023 216 TPGHLEKVLKEQIAEGQPRthrpwkkIIVVVEGIYSMEGEICHLPEIVSICKKYKAYVYLDEAHSIGAIGKTGRGVCELL 295
Cdd:PRK05937 126 DLDHLESLLESCRQRSFGR-------IFIFVCSVYSFKGTLAPLEQIIALSKKYHAHLIVDEAHAMGIFGDDGKGFCHSL 198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229023 296 GVDtsDVDIMMGTFTKSFGSCGGYIAGSKDLIQYLKHQCPAHLYATSISTPSATQIISAIKVILGEDGSNRgaQKLARIR 375
Cdd:PRK05937 199 GYE--NFYAVLVTYSKALGSMGAALLSSSEVKQDLMLNSPPLRYSTGLPPHLLISIQVAYDFLSQEGELAR--KQLFRLK 274
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15229023 376 EnsnFFRaelQKMGFEVLGdndsPVMPIMLynpakiPAFSRECLRE-----NLAVVVVGFPATPLL 436
Cdd:PRK05937 275 E---YFA---QKFSSAAPG----CVQPIFL------PGISEQELYSklvetGIRVGVVCFPTGPFL 324
|
|
| AAT_like |
cd00609 |
Aspartate aminotransferase family. This family belongs to pyridoxal phosphate (PLP)-dependent ... |
111-462 |
1.73e-14 |
|
Aspartate aminotransferase family. This family belongs to pyridoxal phosphate (PLP)-dependent aspartate aminotransferase superfamily (fold I). Pyridoxal phosphate 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. The major groups in this CD corresponds to Aspartate aminotransferase a, b and c, Tyrosine, Alanine, Aromatic-amino-acid, Glutamine phenylpyruvate, 1-Aminocyclopropane-1-carboxylate synthase, Histidinol-phosphate, gene products of malY and cobC, Valine-pyruvate aminotransferase and Rhizopine catabolism regulatory protein.
Pssm-ID: 99734 [Multi-domain] Cd Length: 350 Bit Score: 74.69 E-value: 1.73e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229023 111 LGFGSFDEYCTPRVIESLKKFSAStcSSRVDAGTTSVHAELEDCVAKYVGQ-------PAAVIFGMGyATN--SAIIPVL 181
Cdd:cd00609 3 LSIGEPDFPPPPEVLEALAAAALR--AGLLGYYPDPGLPELREAIAEWLGRrggvdvpPEEIVVTNG-AQEalSLLLRAL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229023 182 IGKGGLIISDSLNHTSIVNGARGSGATIRVFQHNTPGHLEKVLKEQIAEGQPRThrpwkKIIVVV-----EG-IYSMEge 255
Cdd:cd00609 80 LNPGDEVLVPDPTYPGYEAAARLAGAEVVPVPLDEEGGFLLDLELLEAAKTPKT-----KLLYLNnpnnpTGaVLSEE-- 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229023 256 icHLPEIVSICKKYKAYVYLDEAHSigAIGKTGRGVCELLGVDTSDVDIMMGTFTKSFGSCG---GYIAGSKDLIqylKH 332
Cdd:cd00609 153 --ELEELAELAKKHGILIISDEAYA--ELVYDGEPPPALALLDAYERVIVLRSFSKTFGLPGlriGYLIAPPEEL---LE 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229023 333 QCPAHLYATSISTPSATQIIsAIKVILGEDGSNRGAQKlaRIRENSNFFRAELQKMGFEVlgdndsPVMP-----IML-Y 406
Cdd:cd00609 226 RLKKLLPYTTSGPSTLSQAA-AAAALDDGEEHLEELRE--RYRRRRDALLEALKELGPLV------VVKPsggffLWLdL 296
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*.
gi 15229023 407 NPAKIPAFSRECLRENLAVVVVGFPATPLLLARARICISAshSREDLIKALQVISK 462
Cdd:cd00609 297 PEGDDEEFLERLLLEAGVVVRPGSAFGEGGEGFVRLSFAT--PEEELEEALERLAE 350
|
|
| AAT_I |
cd01494 |
Aspartate aminotransferase (AAT) superfamily (fold type I) of pyridoxal phosphate (PLP) ... |
148-318 |
3.34e-12 |
|
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: 64.71 E-value: 3.34e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229023 148 HAELEDCVAKY--VGQPAAVIFGMGYATNSAIIPVLIGKGGLIISDSLNHTS-IVNGARGSGATIRVFQHNTPGHLEkvl 224
Cdd:cd01494 2 LEELEEKLARLlqPGNDKAVFVPSGTGANEAALLALLGPGDEVIVDANGHGSrYWVAAELAGAKPVPVPVDDAGYGG--- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229023 225 kEQIAEGQPRTHRPWKKIIVVVEGIYSMEGEIcHLPEIVSICKKYKAYVYLDEAHSIGAIGktgrgvCELLGVDTSDVDI 304
Cdd:cd01494 79 -LDVAILEELKAKPNVALIVITPNTTSGGVLV-PLKEIRKIAKEYGILLLVDAASAGGASP------APGVLIPEGGADV 150
|
170
....*....|....
gi 15229023 305 MMGTFTKSFGSCGG 318
Cdd:cd01494 151 VTFSLHKNLGGEGG 164
|
|
| Beta_elim_lyase |
pfam01212 |
Beta-eliminating lyase; |
150-334 |
3.36e-09 |
|
Beta-eliminating lyase;
Pssm-ID: 426128 [Multi-domain] Cd Length: 288 Bit Score: 58.00 E-value: 3.36e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229023 150 ELEDCVAKYVGQPAAVIFGMGYATNSAIIPVLIGKGGLIISDSLNHT--------SIVNGARGSGATIRVFQHNTPGHLE 221
Cdd:pfam01212 36 RLEDRVAELFGKEAALFVPSGTAANQLALMAHCQRGDEVICGEPAHIhfdetgghAELGGVQPRPLDGDEAGNMDLEDLE 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229023 222 KVLKEQIAEGQPRThrpwkKIIVV-----VEG--IYSMEgeicHLPEIVSICKKYKAYVYLDEAHSIGAIGKTGRGVCEL 294
Cdd:pfam01212 116 AAIREVGADIFPPT-----GLISLenthnSAGgqVVSLE----NLREIAALAREHGIPVHLDGARFANAAVALGVIVKEI 186
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 15229023 295 lgvdTSDVDIMMGTFTKSFGS-CGGYIAGSKDLIQYLKHQC 334
Cdd:pfam01212 187 ----TSYADSVTMCLSKGLGApVGSVLAGSDDFIAKAIRQR 223
|
|
| Orn_deC_like |
cd00615 |
Ornithine decarboxylase family. This family belongs to pyridoxal phosphate (PLP)-dependent ... |
145-279 |
7.86e-06 |
|
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: 47.63 E-value: 7.86e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229023 145 TSVHAELEDCVAKYVGQPAAvIFGMGYATNS--AIIPVLIGKGGLIISDSLNHTSIVNGARGSGAT-----------IRV 211
Cdd:cd00615 58 TGPIKEAQELAARAFGAKHT-FFLVNGTSSSnkAVILAVCGPGDKILIDRNCHKSVINGLVLSGAVpvylkpernpyYGI 136
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15229023 212 FQHNTPGHLEKVLKEqiaegqprthRPWKKIIVVVEGIYsmEGEICHLPEIVSICKKYKAYVYLDEAH 279
Cdd:cd00615 137 AGGIPPETFKKALIE----------HPDAKAAVITNPTY--YGICYNLRKIVEEAHHRGLPVLVDEAH 192
|
|
| TA_like |
cd06502 |
Low-specificity threonine aldolase (TA). This family belongs to pyridoxal phosphate (PLP) ... |
121-457 |
4.58e-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: 45.40 E-value: 4.58e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229023 121 TPRVIESLKKFSASTCSSRVDAGTtsvhAELEDCVAKYVGQPAAVIFGMGYATNSAIIPVLIGKGGLIISDSLNHtSIVN 200
Cdd:cd06502 11 TPEMLEAMAAANVGDDVYGEDPTT----AKLEARAAELFGKEAALFVPSGTAANQLALAAHTQPGGSVICHETAH-IYTD 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229023 201 GARGSGATIRVFQHNTPGHLEKVLKEQIAE---GQPRTHRPWKKIIVV-----VEGIYSMEgeicHLPEIVSICKKYKAY 272
Cdd:cd06502 86 EAGAPEFLSGVKLLPVPGENGKLTPEDLEAairPRDDIHFPPPSLVSLentteGGTVYPLD----ELKAISALAKENGLP 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229023 273 VYLDEAHSIGAIGKTGRGVCELlgvdTSDVDIMMGTFTKSFGSCGGYI-AGSKDLIQYLKHQCPA--HLYATSistpsat 349
Cdd:cd06502 162 LHLDGARLANAAAALGVALKTY----KSGVDSVSFCLSKGGGAPVGAVvVGNRDFIARARRRRKQagGGMRQS------- 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229023 350 QIISAIKVILGEDGSNRgaQKLARIRENSNFFRAELQKMGfevlGDNDSPVMPIMLYNPAKIPA----FSRECLRENLAV 425
Cdd:cd06502 231 GFLAAAGLAALENDLWL--RRLRHDHEMARRLAEALEELG----GLESEVQTNIVLLDPVEANAvfveLSKEAIERRGEG 304
|
330 340 350
....*....|....*....|....*....|..
gi 15229023 426 VVVGFpatpLLLARARICISASHSREDLIKAL 457
Cdd:cd06502 305 VLFYA----WGEGGVRFVTHWDTTEEDVDELL 332
|
|
| DegT_DnrJ_EryC1 |
pfam01041 |
DegT/DnrJ/EryC1/StrS aminotransferase family; The members of this family are probably all ... |
150-294 |
4.63e-05 |
|
DegT/DnrJ/EryC1/StrS aminotransferase family; The members of this family are probably all pyridoxal-phosphate-dependent aminotransferase enzymes with a variety of molecular functions. The family includes StsA, StsC and StsS. The aminotransferase activity was demonstrated for purified StsC protein as the L-glutamine:scyllo-inosose aminotransferase EC:2.6.1.50, which catalyzes the first amino transfer in the biosynthesis of the streptidine subunit of streptomycin.
Pssm-ID: 395827 Cd Length: 360 Bit Score: 45.35 E-value: 4.63e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229023 150 ELEDCVAKYVGQPAAVIFGMGYATNSAIIPVL-IGKGGLIISDSLNHTSIVNGARGSGATIrVF------QHN-TPGHLE 221
Cdd:pfam01041 28 EFERAFAAYLGVKHAIAVSSGTAALHLALRALgVGPGDEVITPSFTFVATANAALRLGAKP-VFvdidpdTYNiDPEAIE 106
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15229023 222 KVLkeqiaegQPRThrpwKKIIVVvegiySMEGEICHLPEIVSICKKYKAYVYLDEAHSIGAIGKtGRGVCEL 294
Cdd:pfam01041 107 AAI-------TPRT----KAIIPV-----HLYGQPADMDAIRAIAARHGLPVIEDAAHALGATYQ-GKKVGTL 162
|
|
| HisC |
COG0079 |
Histidinol-phosphate/aromatic aminotransferase or cobyric acid decarboxylase [Amino acid ... |
304-394 |
6.74e-04 |
|
Histidinol-phosphate/aromatic aminotransferase or cobyric acid decarboxylase [Amino acid transport and metabolism]; Histidinol-phosphate/aromatic aminotransferase or cobyric acid decarboxylase is part of the Pathway/BioSystem: Cobalamine/B12 biosynthesis
Pssm-ID: 439849 [Multi-domain] Cd Length: 341 Bit Score: 41.66 E-value: 6.74e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229023 304 IMMGTFTKSFGSCG---GYIAGSKDLIQYLKHQCPAHlyatSISTPS---ATQIISAIKVIlgedgsnrgAQKLARIREN 377
Cdd:COG0079 198 VVLRTFSKAYGLAGlrlGYAIASPELIAALRRVRGPW----NVNSLAqaaALAALEDRAYL---------EETRARLRAE 264
|
90
....*....|....*..
gi 15229023 378 SNFFRAELQKMGFEVLG 394
Cdd:COG0079 265 RERLAAALRALGLTVYP 281
|
|
| Aminotran_5 |
pfam00266 |
Aminotransferase class-V; This domain is found in amino transferases, and other enzymes ... |
122-332 |
8.94e-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: 41.46 E-value: 8.94e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229023 122 PRVIESLKKFS----ASTCSSRVDAG--TTSVHAELEDCVAKYVGQPAA--VIF--GMGYATNSAIIPVL--IGKGGLII 189
Cdd:pfam00266 13 QEVLDAIQEYYtdynGNVHRGVHTLGkeATQAYEEAREKVAEFINAPSNdeIIFtsGTTEAINLVALSLGrsLKPGDEIV 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229023 190 SDSLNHTSIVNG----ARGSGATIRVFQHNTPGHLE-KVLKEQIAegqPRTHrpwkkiIVVVEGIYSMEGEICHLPEIVS 264
Cdd:pfam00266 93 ITEMEHHANLVPwqelAKRTGARVRVLPLDEDGLLDlDELEKLIT---PKTK------LVAITHVSNVTGTIQPVPEIGK 163
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15229023 265 ICKKYKAYVYLDEAHSIGAIgktgrgvcellGVDTSDVDIMMGTFT--KSFGSCG-GYIAGSKDLIQYLKH 332
Cdd:pfam00266 164 LAHQYGALVLVDAAQAIGHR-----------PIDVQKLGVDFLAFSghKLYGPTGiGVLYGRRDLLEKMPP 223
|
|
| OAT_like |
cd00610 |
Acetyl ornithine aminotransferase family. This family belongs to pyridoxal phosphate (PLP) ... |
259-463 |
9.69e-04 |
|
Acetyl ornithine aminotransferase family. This family belongs to pyridoxal phosphate (PLP)-dependent aspartate aminotransferase superfamily (fold I). The major groups in this CD correspond to ornithine aminotransferase, acetylornithine aminotransferase, alanine-glyoxylate aminotransferase, dialkylglycine decarboxylase, 4-aminobutyrate aminotransferase, beta-alanine-pyruvate aminotransferase, adenosylmethionine-8-amino-7-oxononanoate aminotransferase, and glutamate-1-semialdehyde 2,1-aminomutase. All the enzymes belonging to this family act on basic amino acids and their derivatives are involved in transamination or decarboxylation.
Pssm-ID: 99735 [Multi-domain] Cd Length: 413 Bit Score: 41.40 E-value: 9.69e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229023 259 LPEIVSICKKYKAYVYLDEAHSigAIGKTGR-GVCELLGVdtsDVDIMmgTFTKSFGscGGY----IAGSKDLIQYLKHQ 333
Cdd:cd00610 214 LKALRELCRKHGILLIADEVQT--GFGRTGKmFAFEHFGV---EPDIV--TLGKGLG--GGLplgaVLGREEIMDAFPAG 284
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229023 334 CPAHLYATSISTPSATQIISAIKVILGEDgsnrgaqKLARIRENSNFFRAELQKM-----------------GFEVLGDN 396
Cdd:cd00610 285 PGLHGGTFGGNPLACAAALAVLEVLEEEG-------LLENAAELGEYLRERLRELaekhplvgdvrgrglmiGIELVKDR 357
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15229023 397 DSpvmpiMLYNPAKIPAFSRECLRENLAVvvvgFPATPLLLaraRICISASHSREDLIKALQVISKA 463
Cdd:cd00610 358 AT-----KPPDKELAAKIIKAALERGLLL----RPSGGNVI---RLLPPLIITEEEIDEGLDALDEA 412
|
|
| OKR_DC_1 |
pfam01276 |
Orn/Lys/Arg decarboxylase, major domain; |
131-279 |
1.36e-03 |
|
Orn/Lys/Arg decarboxylase, major domain;
Pssm-ID: 396025 [Multi-domain] Cd Length: 417 Bit Score: 40.95 E-value: 1.36e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229023 131 FSASTCSSRVDAGT----TSVHAELEDCVAKYVGQPAAVIFGMGYAT-NSAIIPVLIGKGGLIISDSLNHTSIVNGARGS 205
Cdd:pfam01276 47 LRIDVCIEDVELGDlldhEGAIKEAQKYAARVFGADKSYFVVNGTSGsNKTVGMAVCTPGDTILIDRNCHKSIHHALMLS 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229023 206 GATiRVFQHNT------PGHL------EKVLKEQIAEGQPRThrpWKKIIVVVEGIYsmEGEICHLPEIVSICKKYKAYV 273
Cdd:pfam01276 127 GAT-PVYLEPSrnaygiIGGIplhefqEETLKEAIAEVPDAK---GPRLAVITNPTY--DGVLYNAKEIVDTLHHLSDPI 200
|
....*.
gi 15229023 274 YLDEAH 279
Cdd:pfam01276 201 LFDSAW 206
|
|
| AHBA_syn |
cd00616 |
3-amino-5-hydroxybenzoic acid synthase family (AHBA_syn). AHBA_syn family belongs to pyridoxal ... |
148-291 |
2.28e-03 |
|
3-amino-5-hydroxybenzoic acid synthase family (AHBA_syn). AHBA_syn family belongs to pyridoxal phosphate (PLP)-dependent aspartate aminotransferase superfamily (fold I). The members of this CD are involved in various biosynthetic pathways for secondary metabolites. Some well studied proteins in this CD are AHBA_synthase, protein product of pleiotropic regulatory gene degT, Arnb aminotransferase and pilin glycosylation protein. The prototype of this family, the AHBA_synthase, is a dimeric PLP dependent enzyme. AHBA_syn is the terminal enzyme of 3-amino-5-hydroxybenzoic acid (AHBA) formation which is involved in the biosynthesis of ansamycin antibiotics, including rifamycin B. Some members of this CD are involved in 4-amino-6-deoxy-monosaccharide D-perosamine synthesis. Perosamine is an important element in the glycosylation of several cell products, such as antibiotics and lipopolysaccharides of gram-positive and gram-negative bacteria. The pilin glycosylation protein encoded by gene pglA, is a galactosyltransferase involved in pilin glycosylation. Additionally, this CD consists of ArnB (PmrH) aminotransferase, a 4-amino-4-deoxy-L-arabinose lipopolysaccharide-modifying enzyme. This CD also consists of several predicted pyridoxal phosphate-dependent enzymes apparently involved in regulation of cell wall biogenesis. The catalytic lysine which is present in all characterized PLP dependent enzymes is replaced by histidine in some members of this CD.
Pssm-ID: 99740 [Multi-domain] Cd Length: 352 Bit Score: 40.22 E-value: 2.28e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229023 148 HAELEDCVAKYVGQPAAVifgmgyATNSA----IIPVL---IGKGGLIISDSLNHTSIVNGARGSGATIrVF-------Q 213
Cdd:cd00616 20 VREFEKAFAEYLGVKYAV------AVSSGtaalHLALRalgIGPGDEVIVPSFTFVATANAILLLGATP-VFvdidpdtY 92
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15229023 214 HNTPGHLEKVLKeqiaegqPRThrpwkKIIVVVEgiysMEGEICHLPEIVSICKKYKAYVYLDEAHSIGAIGKtGRGV 291
Cdd:cd00616 93 NIDPELIEAAIT-------PRT-----KAIIPVH----LYGNPADMDAIMAIAKRHGLPVIEDAAQALGATYK-GRKV 153
|
|
| |
