|
Name |
Accession |
Description |
Interval |
E-value |
| PRK05958 |
PRK05958 |
8-amino-7-oxononanoate synthase; Reviewed |
1-382 |
0e+00 |
|
8-amino-7-oxononanoate synthase; Reviewed
Pssm-ID: 235655 [Multi-domain] Cd Length: 385 Bit Score: 541.29 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446041004 1 MSWQEKINAALDARRTADALRRRYPVAQGAGRWLVADECQYLNFSSNDYLGLSHHPDIIRAWKQGAEQFGVGSGGSGHVS 80
Cdd:PRK05958 1 MSWLDRLEAALAQRRAAGLYRSLRPREGGAGRWLVVDGRRMLNFASNDYLGLARHPRLIAAAQQAARRYGAGSGGSRLVT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446041004 81 GYSVAHQALEEELAEWLGYSRALLFISGFAANQAVITAMMAKEDRIVADRLSHASLLEAASLSPAQLRRFTHNDVAHLAR 160
Cdd:PRK05958 81 GNSPAHEALEEELAEWFGAERALLFSSGYAANLAVLTALAGKGDLIVSDKLNHASLIDGARLSRARVRRYPHNDVDALEA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446041004 161 LLASPCPGQQLVVTEGVFSMDGDRAPLAEIQQVTQQHNGWLVVDDAHGTGVIGEQGRGSCWQ---QQVKPELLVVTFGKG 237
Cdd:PRK05958 161 LLAKWRAGRALIVTESVFSMDGDLAPLAELVALARRHGAWLLVDEAHGTGVLGPQGRGLAAEaglAGEPDVILVGTLGKA 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446041004 238 FGVSGAAVLCSNTVADYLLQFARHLIYSTSMPPAQAQALRASLAVIRGEegDARREKLAVLITRFRAGLQGLPFTLADSR 317
Cdd:PRK05958 241 LGSSGAAVLGSETLIDYLINRARPFIFTTALPPAQAAAARAALRILRRE--PERRERLAALIARLRAGLRALGFQLMDSQ 318
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446041004 318 SAIQPLIVGDNARALHLAEKLRQQGCWVTAIRPPTVPAGTARLRLTLTAAHETQDIDLLLEVLHG 382
Cdd:PRK05958 319 SAIQPLIVGDNERALALAAALQEQGFWVGAIRPPTVPAGTSRLRITLTAAHTEADIDRLLEALAE 383
|
|
| BioF |
COG0156 |
7-keto-8-aminopelargonate synthetase or related enzyme [Coenzyme transport and metabolism]; ... |
3-381 |
5.25e-174 |
|
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: 489.95 E-value: 5.25e-174
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446041004 3 WQEKINAALDARRTADALRRRYPVAQGAGRWLVADECQYLNFSSNDYLGLSHHPDIIRAWKQGAEQFGVGSGGSGHVSGY 82
Cdd:COG0156 1 LLDRLEAELAALKAAGLYRYLRVLESPQGPRVTIDGREVLNFSSNDYLGLANHPRVIEAAAEALDRYGTGSGGSRLVSGT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446041004 83 SVAHQALEEELAEWLGYSRALLFISGFAANQAVITAMMAKEDRIVADRLSHASLLEAASLSPAQLRRFTHNDVAHLARLL 162
Cdd:COG0156 81 TPLHEELEEELAEFLGKEAALLFSSGYAANLGVISALAGRGDLIFSDELNHASIIDGARLSGAKVVRFRHNDMDDLERLL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446041004 163 A-SPCPGQQLVVTEGVFSMDGDRAPLAEIQQVTQQHNGWLVVDDAHGTGVIGEQGRGSCWQQQVKPE--LLVVTFGKGFG 239
Cdd:COG0156 161 KkARAARRKLIVTDGVFSMDGDIAPLPEIVELAEKYGALLYVDDAHGTGVLGETGRGLVEHFGLEDRvdIIMGTLSKALG 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446041004 240 VSGAAVLCSNTVADYLLQFARHLIYSTSMPPAQAQALRASLAVIRGEegDARREKLAVLITRFRAGLQGLPFTLADSRSA 319
Cdd:COG0156 241 SSGGFVAGSKELIDYLRNRARPFIFSTALPPAVAAAALAALEILREE--PELRERLWENIAYFREGLKELGFDLGPSESP 318
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446041004 320 IQPLIVGDNARALHLAEKLRQQGCWVTAIRPPTVPAGTARLRLTLTAAHETQDIDLLLEVLH 381
Cdd:COG0156 319 IVPVIVGDAERALALADALLERGIYVSAIRPPTVPKGTARLRITLSAAHTEEDIDRLLEALA 380
|
|
| bioF |
TIGR00858 |
8-amino-7-oxononanoate synthase; 7-keto-8-aminopelargonic acid synthetase is an alternate name. ... |
24-381 |
1.78e-172 |
|
8-amino-7-oxononanoate synthase; 7-keto-8-aminopelargonic acid synthetase is an alternate name. This model represents 8-amino-7-oxononanoate synthase, the BioF protein of biotin biosynthesis. This model is based on a careful phylogenetic analysis to separate members of this family from 2-amino-3-ketobutyrate and other related pyridoxal phosphate-dependent enzymes. In several species, including Staphylococcus and Coxiella, a candidate 8-amino-7-oxononanoate synthase is confirmed by location in the midst of a biotin biosynthesis operon but scores below the trusted cutoff of this model. [Biosynthesis of cofactors, prosthetic groups, and carriers, Biotin]
Pssm-ID: 273303 [Multi-domain] Cd Length: 360 Bit Score: 484.85 E-value: 1.78e-172
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446041004 24 YPVAQGAGRWLVADECQYLNFSSNDYLGLSHHPDIIRAWKQGAEQFGVGSGGSGHVSGYSVAHQALEEELAEWLGYSRAL 103
Cdd:TIGR00858 1 RPLDRGPGPEVVRDGRRLLNFSSNDYLGLASHPEVIQAAQQGAEQYGAGSTASRLVSGNSPLHEELEEELAEWKGTEAAL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446041004 104 LFISGFAANQAVITAMMAKEDRIVADRLSHASLLEAASLSPAQLRRFTHNDVAHLARLLASPC-PGQQLVVTEGVFSMDG 182
Cdd:TIGR00858 81 LFSSGYLANVGVISALVGKGDLILSDALNHASLIDGCRLSGARVRRYRHNDVEHLERLLEKNRgERRKLIVTDGVFSMDG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446041004 183 DRAPLAEIQQVTQQHNGWLVVDDAHGTGVIGEQGRGSCWQQQVKPE---LLVVTFGKGFGVSGAAVLCSNTVADYLLQFA 259
Cdd:TIGR00858 161 DIAPLPQLVALAERYGAWLMVDDAHGTGVLGEDGRGTLEHFGLKPEpvdIQVGTLSKALGSYGAYVAGSQALIDYLINRA 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446041004 260 RHLIYSTSMPPAQAQALRASLAVIrgEEGDARREKLAVLITRFRAGLQGLPFTLADSRSAIQPLIVGDNARALHLAEKLR 339
Cdd:TIGR00858 241 RTLIFSTALPPAVAAAALAALELI--QEEPWRREKLLALIARLRAGLEALGFTLMPSCTPIVPVIIGDNASALALAEELQ 318
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 446041004 340 QQGCWVTAIRPPTVPAGTARLRLTLTAAHETQDIDLLLEVLH 381
Cdd:TIGR00858 319 QQGIFVGAIRPPTVPAGTSRLRLTLSAAHTPGDIDRLAEALK 360
|
|
| KBL_like |
cd06454 |
KBL_like; this family belongs to the pyridoxal phosphate (PLP)-dependent aspartate ... |
40-384 |
6.87e-148 |
|
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: 422.35 E-value: 6.87e-148
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446041004 40 QYLNFSSNDYLGLSHHPDIIRAWKQGAEQFGVGSGGSGHVSGYSVAHQALEEELAEWLGYSRALLFISGFAANQAVITAM 119
Cdd:cd06454 2 KVLNFCSNDYLGLANHPEVIEAAKEALDKYGVGAGGSRLISGTSDLHEELEEELAEFHGKEAALVFSSGYAANDGVLSTL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446041004 120 MAKEDRIVADRLSHASLLEAASLSPAQLRRFTHNDVAHLARLLASP--CPGQQLVVTEGVFSMDGDRAPLAEIQQVTQQH 197
Cdd:cd06454 82 AGKGDLIISDSLNHASIIDGIRLSGAKKRIFKHNDMEDLEKLLREArrPYGKKLIVTEGVYSMDGDIAPLPELVDLAKKY 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446041004 198 NGWLVVDDAHGTGVIGEQGRGSC--WQQQVKPELLVVTFGKGFGVSGAAVLCSNTVADYLLQFARHLIYSTSMPPAQAQA 275
Cdd:cd06454 162 GAILFVDEAHSVGVYGPHGRGVEefGGLTDDVDIIMGTLGKAFGAVGGYIAGSKELIDYLRSYARGFIFSTSLPPAVAAA 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446041004 276 LRASLAVIRGeeGDARREKLAVLITRFRAGLQGLPFTLADSRS-AIQPLIVGDNARALHLAEKLRQQGCWVTAIRPPTVP 354
Cdd:cd06454 242 ALAALEVLQG--GPERRERLQENVRYLRRGLKELGFPVGGSPShIIPPLIGDDPAKAVAFSDALLERGIYVQAIRYPTVP 319
|
330 340 350
....*....|....*....|....*....|
gi 446041004 355 AGTARLRLTLTAAHETQDIDLLLEVLHGNG 384
Cdd:cd06454 320 RGTARLRISLSAAHTKEDIDRLLEALKEVG 349
|
|
| Aminotran_1_2 |
pfam00155 |
Aminotransferase class I and II; |
42-380 |
1.28e-59 |
|
Aminotransferase class I and II;
Pssm-ID: 395103 [Multi-domain] Cd Length: 351 Bit Score: 196.76 E-value: 1.28e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446041004 42 LNFSSNDYLGlshhpDIIRAWKQgAEQFGVGSGGSGHVSGYSVaHQALEEELAEWLGYS--------RALLFISGFAANQ 113
Cdd:pfam00155 4 INLGSNEYLG-----DTLPAVAK-AEKDALAGGTRNLYGPTDG-HPELREALAKFLGRSpvlkldreAAVVFGSGAGANI 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446041004 114 AVITAMMA-KEDRIVADRLSHASLLEAASLSPAQLRRFT-------HNDVAHLARLLASPCpgqQLVVTEGVFSMDGDRA 185
Cdd:pfam00155 77 EALIFLLAnPGDAILVPAPTYASYIRIARLAGGEVVRYPlydsndfHLDFDALEAALKEKP---KVVLHTSPHNPTGTVA 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446041004 186 PLAEIQQV---TQQHNGWLVVDDAHGTGVIGEQGRGSCWQQ-QVKPELLVV-TFGKGFGVSG---AAVLCSNTVADYLLQ 257
Cdd:pfam00155 154 TLEELEKLldlAKEHNILLLVDEAYAGFVFGSPDAVATRALlAEGPNLLVVgSFSKAFGLAGwrvGYILGNAAVISQLRK 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446041004 258 FARHLIYSTSMPPAQAQALRASLAVIrgEEGDARREKLAVLITRFRAGLQGLPFTLADSRSAIQPLIVGDNARALHLAEK 337
Cdd:pfam00155 234 LARPFYSSTHLQAAAAAALSDPLLVA--SELEEMRQRIKERRDYLRDGLQAAGLSVLPSQAGFFLLTGLDPETAKELAQV 311
|
330 340 350 360
....*....|....*....|....*....|....*....|....
gi 446041004 338 LRQQ-GCWVTAIRPPTVPagtARLRLTLtAAHETQDIDLLLEVL 380
Cdd:pfam00155 312 LLEEvGVYVTPGSSPGVP---GWLRITV-AGGTEEELEELLEAI 351
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| PRK05958 |
PRK05958 |
8-amino-7-oxononanoate synthase; Reviewed |
1-382 |
0e+00 |
|
8-amino-7-oxononanoate synthase; Reviewed
Pssm-ID: 235655 [Multi-domain] Cd Length: 385 Bit Score: 541.29 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446041004 1 MSWQEKINAALDARRTADALRRRYPVAQGAGRWLVADECQYLNFSSNDYLGLSHHPDIIRAWKQGAEQFGVGSGGSGHVS 80
Cdd:PRK05958 1 MSWLDRLEAALAQRRAAGLYRSLRPREGGAGRWLVVDGRRMLNFASNDYLGLARHPRLIAAAQQAARRYGAGSGGSRLVT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446041004 81 GYSVAHQALEEELAEWLGYSRALLFISGFAANQAVITAMMAKEDRIVADRLSHASLLEAASLSPAQLRRFTHNDVAHLAR 160
Cdd:PRK05958 81 GNSPAHEALEEELAEWFGAERALLFSSGYAANLAVLTALAGKGDLIVSDKLNHASLIDGARLSRARVRRYPHNDVDALEA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446041004 161 LLASPCPGQQLVVTEGVFSMDGDRAPLAEIQQVTQQHNGWLVVDDAHGTGVIGEQGRGSCWQ---QQVKPELLVVTFGKG 237
Cdd:PRK05958 161 LLAKWRAGRALIVTESVFSMDGDLAPLAELVALARRHGAWLLVDEAHGTGVLGPQGRGLAAEaglAGEPDVILVGTLGKA 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446041004 238 FGVSGAAVLCSNTVADYLLQFARHLIYSTSMPPAQAQALRASLAVIRGEegDARREKLAVLITRFRAGLQGLPFTLADSR 317
Cdd:PRK05958 241 LGSSGAAVLGSETLIDYLINRARPFIFTTALPPAQAAAARAALRILRRE--PERRERLAALIARLRAGLRALGFQLMDSQ 318
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446041004 318 SAIQPLIVGDNARALHLAEKLRQQGCWVTAIRPPTVPAGTARLRLTLTAAHETQDIDLLLEVLHG 382
Cdd:PRK05958 319 SAIQPLIVGDNERALALAAALQEQGFWVGAIRPPTVPAGTSRLRITLTAAHTEADIDRLLEALAE 383
|
|
| BioF |
COG0156 |
7-keto-8-aminopelargonate synthetase or related enzyme [Coenzyme transport and metabolism]; ... |
3-381 |
5.25e-174 |
|
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: 489.95 E-value: 5.25e-174
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446041004 3 WQEKINAALDARRTADALRRRYPVAQGAGRWLVADECQYLNFSSNDYLGLSHHPDIIRAWKQGAEQFGVGSGGSGHVSGY 82
Cdd:COG0156 1 LLDRLEAELAALKAAGLYRYLRVLESPQGPRVTIDGREVLNFSSNDYLGLANHPRVIEAAAEALDRYGTGSGGSRLVSGT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446041004 83 SVAHQALEEELAEWLGYSRALLFISGFAANQAVITAMMAKEDRIVADRLSHASLLEAASLSPAQLRRFTHNDVAHLARLL 162
Cdd:COG0156 81 TPLHEELEEELAEFLGKEAALLFSSGYAANLGVISALAGRGDLIFSDELNHASIIDGARLSGAKVVRFRHNDMDDLERLL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446041004 163 A-SPCPGQQLVVTEGVFSMDGDRAPLAEIQQVTQQHNGWLVVDDAHGTGVIGEQGRGSCWQQQVKPE--LLVVTFGKGFG 239
Cdd:COG0156 161 KkARAARRKLIVTDGVFSMDGDIAPLPEIVELAEKYGALLYVDDAHGTGVLGETGRGLVEHFGLEDRvdIIMGTLSKALG 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446041004 240 VSGAAVLCSNTVADYLLQFARHLIYSTSMPPAQAQALRASLAVIRGEegDARREKLAVLITRFRAGLQGLPFTLADSRSA 319
Cdd:COG0156 241 SSGGFVAGSKELIDYLRNRARPFIFSTALPPAVAAAALAALEILREE--PELRERLWENIAYFREGLKELGFDLGPSESP 318
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446041004 320 IQPLIVGDNARALHLAEKLRQQGCWVTAIRPPTVPAGTARLRLTLTAAHETQDIDLLLEVLH 381
Cdd:COG0156 319 IVPVIVGDAERALALADALLERGIYVSAIRPPTVPKGTARLRITLSAAHTEEDIDRLLEALA 380
|
|
| bioF |
TIGR00858 |
8-amino-7-oxononanoate synthase; 7-keto-8-aminopelargonic acid synthetase is an alternate name. ... |
24-381 |
1.78e-172 |
|
8-amino-7-oxononanoate synthase; 7-keto-8-aminopelargonic acid synthetase is an alternate name. This model represents 8-amino-7-oxononanoate synthase, the BioF protein of biotin biosynthesis. This model is based on a careful phylogenetic analysis to separate members of this family from 2-amino-3-ketobutyrate and other related pyridoxal phosphate-dependent enzymes. In several species, including Staphylococcus and Coxiella, a candidate 8-amino-7-oxononanoate synthase is confirmed by location in the midst of a biotin biosynthesis operon but scores below the trusted cutoff of this model. [Biosynthesis of cofactors, prosthetic groups, and carriers, Biotin]
Pssm-ID: 273303 [Multi-domain] Cd Length: 360 Bit Score: 484.85 E-value: 1.78e-172
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446041004 24 YPVAQGAGRWLVADECQYLNFSSNDYLGLSHHPDIIRAWKQGAEQFGVGSGGSGHVSGYSVAHQALEEELAEWLGYSRAL 103
Cdd:TIGR00858 1 RPLDRGPGPEVVRDGRRLLNFSSNDYLGLASHPEVIQAAQQGAEQYGAGSTASRLVSGNSPLHEELEEELAEWKGTEAAL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446041004 104 LFISGFAANQAVITAMMAKEDRIVADRLSHASLLEAASLSPAQLRRFTHNDVAHLARLLASPC-PGQQLVVTEGVFSMDG 182
Cdd:TIGR00858 81 LFSSGYLANVGVISALVGKGDLILSDALNHASLIDGCRLSGARVRRYRHNDVEHLERLLEKNRgERRKLIVTDGVFSMDG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446041004 183 DRAPLAEIQQVTQQHNGWLVVDDAHGTGVIGEQGRGSCWQQQVKPE---LLVVTFGKGFGVSGAAVLCSNTVADYLLQFA 259
Cdd:TIGR00858 161 DIAPLPQLVALAERYGAWLMVDDAHGTGVLGEDGRGTLEHFGLKPEpvdIQVGTLSKALGSYGAYVAGSQALIDYLINRA 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446041004 260 RHLIYSTSMPPAQAQALRASLAVIrgEEGDARREKLAVLITRFRAGLQGLPFTLADSRSAIQPLIVGDNARALHLAEKLR 339
Cdd:TIGR00858 241 RTLIFSTALPPAVAAAALAALELI--QEEPWRREKLLALIARLRAGLEALGFTLMPSCTPIVPVIIGDNASALALAEELQ 318
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 446041004 340 QQGCWVTAIRPPTVPAGTARLRLTLTAAHETQDIDLLLEVLH 381
Cdd:TIGR00858 319 QQGIFVGAIRPPTVPAGTSRLRLTLSAAHTPGDIDRLAEALK 360
|
|
| KBL_like |
cd06454 |
KBL_like; this family belongs to the pyridoxal phosphate (PLP)-dependent aspartate ... |
40-384 |
6.87e-148 |
|
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: 422.35 E-value: 6.87e-148
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446041004 40 QYLNFSSNDYLGLSHHPDIIRAWKQGAEQFGVGSGGSGHVSGYSVAHQALEEELAEWLGYSRALLFISGFAANQAVITAM 119
Cdd:cd06454 2 KVLNFCSNDYLGLANHPEVIEAAKEALDKYGVGAGGSRLISGTSDLHEELEEELAEFHGKEAALVFSSGYAANDGVLSTL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446041004 120 MAKEDRIVADRLSHASLLEAASLSPAQLRRFTHNDVAHLARLLASP--CPGQQLVVTEGVFSMDGDRAPLAEIQQVTQQH 197
Cdd:cd06454 82 AGKGDLIISDSLNHASIIDGIRLSGAKKRIFKHNDMEDLEKLLREArrPYGKKLIVTEGVYSMDGDIAPLPELVDLAKKY 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446041004 198 NGWLVVDDAHGTGVIGEQGRGSC--WQQQVKPELLVVTFGKGFGVSGAAVLCSNTVADYLLQFARHLIYSTSMPPAQAQA 275
Cdd:cd06454 162 GAILFVDEAHSVGVYGPHGRGVEefGGLTDDVDIIMGTLGKAFGAVGGYIAGSKELIDYLRSYARGFIFSTSLPPAVAAA 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446041004 276 LRASLAVIRGeeGDARREKLAVLITRFRAGLQGLPFTLADSRS-AIQPLIVGDNARALHLAEKLRQQGCWVTAIRPPTVP 354
Cdd:cd06454 242 ALAALEVLQG--GPERRERLQENVRYLRRGLKELGFPVGGSPShIIPPLIGDDPAKAVAFSDALLERGIYVQAIRYPTVP 319
|
330 340 350
....*....|....*....|....*....|
gi 446041004 355 AGTARLRLTLTAAHETQDIDLLLEVLHGNG 384
Cdd:cd06454 320 RGTARLRISLSAAHTKEDIDRLLEALKEVG 349
|
|
| PRK06939 |
PRK06939 |
2-amino-3-ketobutyrate coenzyme A ligase; Provisional |
27-374 |
9.72e-82 |
|
2-amino-3-ketobutyrate coenzyme A ligase; Provisional
Pssm-ID: 235893 [Multi-domain] Cd Length: 397 Bit Score: 255.12 E-value: 9.72e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446041004 27 AQGAgRWLVADECQYLNFSSNDYLGLSHHPDIIRAWKQGAEQFGVGSGGSGHVSGYSVAHQALEEELAEWLGYSRALLFI 106
Cdd:PRK06939 31 PQGA-DITVADGKEVINFCANNYLGLANHPELIAAAKAALDSHGFGMASVRFICGTQDLHKELEEKLAKFLGTEDAILYS 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446041004 107 SGFAANQAVITAMMAKEDRIVADRLSHASLLEAASLSPAQLRRFTHNDVAHL-ARLLASPCPGQQ--LVVTEGVFSMDGD 183
Cdd:PRK06939 110 SCFDANGGLFETLLGKEDAIISDALNHASIIDGVRLCKAKRYRYANNDMADLeAQLKEAKEAGARhkLIATDGVFSMDGD 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446041004 184 RAPLAEIQQVTQQHNGWLVVDDAHGTGVIGEQGRGSCWQQQV--KPELLVVTFGKGF-GVSGAAVLCSNTVADYLLQFAR 260
Cdd:PRK06939 190 IAPLPEICDLADKYDALVMVDDSHAVGFVGENGRGTVEHFGVmdRVDIITGTLGKALgGASGGYTAGRKEVIDWLRQRSR 269
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446041004 261 HLIYSTSMPPAQAqalRASLAVIRG-EEGDARREKLAVLITRFRAGLQGLPFTLADSRSAIQPLIVGDNARALHLAEKLR 339
Cdd:PRK06939 270 PYLFSNSLAPAIV---AASIKVLELlEESDELRDRLWENARYFREGMTAAGFTLGPGEHPIIPVMLGDAKLAQEFADRLL 346
|
330 340 350
....*....|....*....|....*....|....*
gi 446041004 340 QQGCWVTAIRPPTVPAGTARLRLTLTAAHETQDID 374
Cdd:PRK06939 347 EEGVYVIGFSFPVVPKGQARIRTQMSAAHTKEQLD 381
|
|
| gly_Cac_T_rel |
TIGR01825 |
pyridoxal phosphate-dependent acyltransferase, putative; This model represents an enzyme ... |
27-379 |
1.59e-80 |
|
pyridoxal phosphate-dependent acyltransferase, putative; This model represents an enzyme subfamily related to three known enzymes; it appears closest to glycine C-acteyltransferase, shows no overlap with it in species distribution, and may share that function. The three closely related enzymes are glycine C-acetyltransferase (2-amino-3-ketobutyrate coenzyme A ligase), 5-aminolevulinic acid synthase, and 8-amino-7-oxononanoate synthase. All transfer the R-group (acetyl, succinyl, or 6-carboxyhexanoyl) from coenzyme A to an amino acid (Gly, Gly, Ala, respectively), with release of CO2 for the latter two reactions.
Pssm-ID: 130884 [Multi-domain] Cd Length: 385 Bit Score: 251.66 E-value: 1.59e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446041004 27 AQGAgrWLVADECQYLNFSSNDYLGLSHHPDIIRAWKQGAEQFGVGSGGSGHVSGYSVAHQALEEELAEWLGYSRALLFI 106
Cdd:TIGR01825 23 AQGP--RVRVNGKEVINLSSNNYLGFADHPRLKEAAAQAIQQYGVGAGAVRTIAGTLRLHEELEEKLAKFKKTEAALVFQ 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446041004 107 SGFAANQAVITAMMAKEDRIVADRLSHASLLEAASLSPAQLRRFTHNDVAHLARLL-ASPCPGQQLVVTEGVFSMDGDRA 185
Cdd:TIGR01825 101 SGFNTNQGVLSALLRKGDIVLSDELNHASIIDGLRLTKATKKIYKHADMDDLDRVLrENPSYGKKLIVTDGVFSMDGDVA 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446041004 186 PLAEIQQVTQQHNGWLVVDDAHGTGVIGEQGRGSC--WQQQVKPELLVVTFGKGFGVSGAAVLCSNTVADYLLQFARHLI 263
Cdd:TIGR01825 181 PLPEIVELAERYGAVTYVDDAHGSGVMGEAGRGTVhhFGLEDKVDIQVGTLSKAIGVVGGYAAGHKELIEYLKNRARPFL 260
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446041004 264 YSTSMPPAQAQALRASLAVIrgEEGDARREKLAVLITRFRAGLQGLPFTLADSRSAIQPLIVGDNARALHLAEKLRQQGC 343
Cdd:TIGR01825 261 FSTAQPPAVVAALAAAVDEL--QRSPELMERLWDNTRFFKAGLGKLGYDTGGSETPITPVVIGDEKAAQEFSRRLFDEGI 338
|
330 340 350
....*....|....*....|....*....|....*.
gi 446041004 344 WVTAIRPPTVPAGTARLRLTLTAAHETQDIDLLLEV 379
Cdd:TIGR01825 339 FAQSIVFPTVPRGTARIRNIPTAEHTKDDLDQALDA 374
|
|
| PLN02955 |
PLN02955 |
8-amino-7-oxononanoate synthase |
42-380 |
6.40e-62 |
|
8-amino-7-oxononanoate synthase
Pssm-ID: 178541 [Multi-domain] Cd Length: 476 Bit Score: 206.45 E-value: 6.40e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446041004 42 LNFSSNDYLGLSHHPDIIRAWKQGAEQFGVGSGGSGHVSGYSVAHQALEEELAEWLGYSRALLFISGFAANQAVITAMMA 121
Cdd:PLN02955 105 LLFSGNDYLGLSSHPTISNAAANAAKEYGMGPKGSALICGYTTYHRLLESSLADLKKKEDCLVCPTGFAANMAAMVAIGS 184
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446041004 122 ------------KEDR--IVADRLSHASLLEAASLSP----AQLRRFTHNDVAHLARLLASPCPGQQLVVTEGVFSMDGD 183
Cdd:PLN02955 185 vasllaasgkplKNEKvaIFSDALNHASIIDGVRLAErqgnVEVFVYRHCDMYHLNSLLSSCKMKRKVVVTDSLFSMDGD 264
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446041004 184 RAPLAEIQQVTQQHNGWLVVDDAHGTGVIGEQGRGSC--WQQQVKPELLVVTFGKGFGVSGAAVLCSNTVADYLLQFARH 261
Cdd:PLN02955 265 FAPMEELSQLRKKYGFLLVIDDAHGTFVCGENGGGVAeeFNCEADVDLCVGTLSKAAGCHGGFIACSKKWKQLIQSRGRS 344
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446041004 262 LIYSTSMPPAQAQALRASLAVIRGEEGdaRREKLAVLITRFRAgLQGLPFTladsrSAIQPLIVGDNARALHLAEKLRQQ 341
Cdd:PLN02955 345 FIFSTAIPVPMAAAAYAAVVVARKEKW--RRKAIWERVKEFKA-LSGVDIS-----SPIISLVVGNQEKALKASRYLLKS 416
|
330 340 350
....*....|....*....|....*....|....*....
gi 446041004 342 GCWVTAIRPPTVPAGTARLRLTLTAAHETQDIDLLLEVL 380
Cdd:PLN02955 417 GFHVMAIRPPTVPPNSCRLRVTLSAAHTTEDVKKLITAL 455
|
|
| 5aminolev_synth |
TIGR01821 |
5-aminolevulinic acid synthase; This model represents 5-aminolevulinic acid synthase, an ... |
1-381 |
4.31e-61 |
|
5-aminolevulinic acid synthase; This model represents 5-aminolevulinic acid synthase, an enzyme for one of two routes to the heme precursor 5-aminolevulinate. The protein is a pyridoxal phosphate-dependent enzyme related to 2-amino-3-ketobutyrate CoA tranferase and 8-amino-7-oxononanoate synthase. This enzyme appears restricted to the alpha Proteobacteria and mitochondrial derivatives. [Biosynthesis of cofactors, prosthetic groups, and carriers, Heme, porphyrin, and cobalamin]
Pssm-ID: 273820 [Multi-domain] Cd Length: 402 Bit Score: 201.88 E-value: 4.31e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446041004 1 MSWQEKINAALDAR------RTADALRR---RYPVAQgagrWLVADECQYLN-FSSNDYLGLSHHPDIIRAWKQGAEQFG 70
Cdd:TIGR01821 1 MDYDQFFNKEIDKLhlegryRVFADLERqagEFPFAQ----WHRPDGAKDVTvWCSNDYLGMGQHPEVLQAMHETLDKYG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446041004 71 VGSGGSGHVSGYSVAHQALEEELAEWLGYSRALLFISGFAANQAVIT--AMMAKEDRIVADRLSHASLLEAASLSPAQLR 148
Cdd:TIGR01821 77 AGAGGTRNISGTNIPHVELEAELADLHGKESALVFTSGYVANDATLAtlAKIIPGCVIFSDELNHASMIEGIRHSGAEKF 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446041004 149 RFTHNDVAHLARLLASPCPGQ-QLVVTEGVFSMDGDRAPLAEIQQVTQQHNGWLVVDDAHGTGVIGEQGRGSCWQQQVKP 227
Cdd:TIGR01821 157 IFRHNDVAHLEKLLQSVDPNRpKIIAFESVYSMDGDIAPIEEICDLADKYGALTYLDEVHAVGLYGPRGGGIAERDGLMH 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446041004 228 ELLVV--TFGKGFGVSGAAVLCSNTVADYLLQFARHLIYSTSMPPAQAQALRASLAVIRGEEgdARREKLAVLITRFRAG 305
Cdd:TIGR01821 237 RIDIIegTLAKAFGVVGGYIAASRKLIDAIRSYAPGFIFTTSLPPAIAAGATASIRHLKESQ--DLRRAHQENVKRLKNL 314
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446041004 306 LQGLPFTLADSRSAIQPLIVGDNARALHLAEKL-RQQGCWVTAIRPPTVPAGTARLRLTLTAAHETQDIDLLLEVLH 381
Cdd:TIGR01821 315 LEALGIPVIPNPSHIVPVIIGDAALCKKVSDLLlNKHGIYVQPINYPTVPRGTERLRITPTPAHTDKMIDDLVEALL 391
|
|
| PRK13392 |
PRK13392 |
5-aminolevulinate synthase; Provisional |
46-380 |
6.86e-61 |
|
5-aminolevulinate synthase; Provisional
Pssm-ID: 184023 [Multi-domain] Cd Length: 410 Bit Score: 201.62 E-value: 6.86e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446041004 46 SNDYLGLSHHPDIIRAWKQGAEQFGVGSGGSGHVSGYSVAHQALEEELAEWLGYSRALLFISGFAANQAVITAMMAKEDR 125
Cdd:PRK13392 53 SNDYLGMGQHPDVIGAMVDALDRYGAGAGGTRNISGTSHPHVLLERELADLHGKESALLFTSGYVSNDAALSTLGKLLPG 132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446041004 126 --IVADRLSHASLLEAASLSPAQLRRFTHNDVAHLARLLASPCPGQ-QLVVTEGVFSMDGDRAPLAEIQQVTQQHNGWLV 202
Cdd:PRK13392 133 cvILSDALNHASMIEGIRRSGAEKQVFRHNDLADLEEQLASVDPDRpKLIAFESVYSMDGDIAPIEAICDLADRYNALTY 212
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446041004 203 VDDAHGTGVIGEQGRGSCWQQQVKPELLVV--TFGKGFGVSGAAVLCSNTVADYLLQFARHLIYSTSMPPAQAQALRASL 280
Cdd:PRK13392 213 VDEVHAVGLYGARGGGIAERDGLMDRIDMIqgTLAKAFGCLGGYIAASADLIDFVRSFAPGFIFTTALPPAVAAGATAAI 292
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446041004 281 AVIRgeEGDARREKLAVLITRFRAGLQGLPFTLADSRSAIQPLIVGDNARALHLAEKL-RQQGCWVTAIRPPTVPAGTAR 359
Cdd:PRK13392 293 RHLK--TSQTERDAHQDRVAALKAKLNANGIPVMPSPSHIVPVMVGDPTLCKAISDRLmSEHGIYIQPINYPTVPRGTER 370
|
330 340
....*....|....*....|.
gi 446041004 360 LRLTLTAAHETQDIDLLLEVL 380
Cdd:PRK13392 371 LRITPTPLHDDEDIDALVAAL 391
|
|
| Aminotran_1_2 |
pfam00155 |
Aminotransferase class I and II; |
42-380 |
1.28e-59 |
|
Aminotransferase class I and II;
Pssm-ID: 395103 [Multi-domain] Cd Length: 351 Bit Score: 196.76 E-value: 1.28e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446041004 42 LNFSSNDYLGlshhpDIIRAWKQgAEQFGVGSGGSGHVSGYSVaHQALEEELAEWLGYS--------RALLFISGFAANQ 113
Cdd:pfam00155 4 INLGSNEYLG-----DTLPAVAK-AEKDALAGGTRNLYGPTDG-HPELREALAKFLGRSpvlkldreAAVVFGSGAGANI 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446041004 114 AVITAMMA-KEDRIVADRLSHASLLEAASLSPAQLRRFT-------HNDVAHLARLLASPCpgqQLVVTEGVFSMDGDRA 185
Cdd:pfam00155 77 EALIFLLAnPGDAILVPAPTYASYIRIARLAGGEVVRYPlydsndfHLDFDALEAALKEKP---KVVLHTSPHNPTGTVA 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446041004 186 PLAEIQQV---TQQHNGWLVVDDAHGTGVIGEQGRGSCWQQ-QVKPELLVV-TFGKGFGVSG---AAVLCSNTVADYLLQ 257
Cdd:pfam00155 154 TLEELEKLldlAKEHNILLLVDEAYAGFVFGSPDAVATRALlAEGPNLLVVgSFSKAFGLAGwrvGYILGNAAVISQLRK 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446041004 258 FARHLIYSTSMPPAQAQALRASLAVIrgEEGDARREKLAVLITRFRAGLQGLPFTLADSRSAIQPLIVGDNARALHLAEK 337
Cdd:pfam00155 234 LARPFYSSTHLQAAAAAALSDPLLVA--SELEEMRQRIKERRDYLRDGLQAAGLSVLPSQAGFFLLTGLDPETAKELAQV 311
|
330 340 350 360
....*....|....*....|....*....|....*....|....
gi 446041004 338 LRQQ-GCWVTAIRPPTVPagtARLRLTLtAAHETQDIDLLLEVL 380
Cdd:pfam00155 312 LLEEvGVYVTPGSSPGVP---GWLRITV-AGGTEEELEELLEAI 351
|
|
| PLN02483 |
PLN02483 |
serine palmitoyltransferase |
42-380 |
3.68e-53 |
|
serine palmitoyltransferase
Pssm-ID: 178101 [Multi-domain] Cd Length: 489 Bit Score: 183.42 E-value: 3.68e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446041004 42 LNFSSNDYLGLSHH-----PDIIRAWKQgaeqFGVGSGGSGHVSGYSVAHQALEEELAEWLGYSRALLFISGFAANQAVI 116
Cdd:PLN02483 103 LNLGSYNYLGFAAAdeyctPRVIESLKK----YSASTCSSRVDGGTTKLHRELEELVARFVGKPAAIVFGMGYATNSTII 178
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446041004 117 TAMMAKEDRIVADRLSHASLLEAASLSPAQLRRFTHNDVAHLARLLASPCPGQQ----------LVVTEGVFSMDGDRAP 186
Cdd:PLN02483 179 PALIGKGGLIISDSLNHNSIVNGARGSGATIRVFQHNTPSHLEEVLREQIAEGQprthrpwkkiIVIVEGIYSMEGELCK 258
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446041004 187 LAEIQQVTQQHNGWLVVDDAHGTGVIGEQGRGSCWQQQVKP---ELLVVTFGKGFGVSGAAVLCSNTVADYLLQFARHLI 263
Cdd:PLN02483 259 LPEIVAVCKKYKAYVYLDEAHSIGAVGKTGRGVCELLGVDPadvDIMMGTFTKSFGSCGGYIAGSKELIQYLKRTCPAHL 338
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446041004 264 YSTSMPPAQAQALRASLAVIRGEEGDAR-REKLAVLITR---FRAGLQGLPF-TLADSRSAIQPLIVGDNARALHLAEKL 338
Cdd:PLN02483 339 YATSMSPPAVQQVISAIKVILGEDGTNRgAQKLAQIRENsnfFRSELQKMGFeVLGDNDSPVMPIMLYNPAKIPAFSREC 418
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 446041004 339 RQQGCWVTAIRPPTVPAGTARLRLTLTAAHETQDIDLLLEVL 380
Cdd:PLN02483 419 LKQNVAVVVVGFPATPLLLARARICISASHSREDLIKALEVI 460
|
|
| PRK07179 |
PRK07179 |
quorum-sensing autoinducer synthase; |
42-381 |
2.86e-49 |
|
quorum-sensing autoinducer synthase;
Pssm-ID: 180866 [Multi-domain] Cd Length: 407 Bit Score: 170.96 E-value: 2.86e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446041004 42 LNFSSNDYLGLSHHPDIIRAWKQGAEQFGVGSGGSGHVSGYSVAHQALEEELAEWLGYSRALLFISGFAANQAVITAMMA 121
Cdd:PRK07179 57 IILQSNDYLNLSGHPDIIKAQIAALQEEGDSLVMSAVFLHDDSPKPQFEKKLAAFTGFESCLLCQSGWAANVGLLQTIAD 136
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446041004 122 KEDRIVADRLSHASLLEAASLSPAQLRRFTHNDVAHLARLLASPCPGqqLVVTEGVFSMDGDRAPLAEIQQVTQQHNGWL 201
Cdd:PRK07179 137 PNTPVYIDFFAHMSLWEGVRAAGAQAHPFRHNDVDHLRRQIERHGPG--IIVVDSVYSTTGTIAPLADIVDIAEEFGCVL 214
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446041004 202 VVDDAHGTGVIGEQGRGSC----WQQQVkpELLVVTFGKGFGVSGAAVLCSNTVADYLLQFARHLIYSTSMPPAQAQALR 277
Cdd:PRK07179 215 VVDESHSLGTHGPQGAGLVaelgLTSRV--HFITASLAKAFAGRAGIITCPRELAEYVPFVSYPAIFSSTLLPHEIAGLE 292
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446041004 278 ASLAVIRgeEGDARREKLAVLITRFRAGLQGLPFTLAdSRSAIQPLIVGDNARALHLAEKLRQQGCWVTAIRPPTVPAGT 357
Cdd:PRK07179 293 ATLEVIE--SADDRRARLHANARFLREGLSELGYNIR-SESQIIALETGSERNTEVLRDALEERNVFGAVFCAPATPKNR 369
|
330 340
....*....|....*....|....
gi 446041004 358 ARLRLTLTAAHETQDIDLLLEVLH 381
Cdd:PRK07179 370 NLIRLSLNADLTASDLDRVLEVCR 393
|
|
| PRK07505 |
PRK07505 |
hypothetical protein; Provisional |
25-381 |
3.13e-42 |
|
hypothetical protein; Provisional
Pssm-ID: 181006 [Multi-domain] Cd Length: 402 Bit Score: 152.44 E-value: 3.13e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446041004 25 PVAQGAGRWLVADECQYLNFSSNDYLGLSHHPDIIRAWKQGAEQFGVGSGGSGHVSGYSVAHQALEEELAEWLGySRALL 104
Cdd:PRK07505 32 VGEREGILITLADGHTFVNFVSCSYLGLDTHPAIIEGAVDALKRTGSLHLSSSRTRVRSQILKDLEEALSELFG-ASVLT 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446041004 105 FISGFAANQAVI----TAMMAKEDRI--VADRLSHASL--LEAASLSPAQLRRFTHNDVAHLARLlaspCPGQQLV--VT 174
Cdd:PRK07505 111 FTSCSAAHLGILpllaSGHLTGGVPPhmVFDKNAHASLniLKGICADETEVETIDHNDLDALEDI----CKTNKTVayVA 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446041004 175 EGVFSMdGDRAPLAEIQQVTQQHNGWLVVDDAHGTGVIGEQGRG---SCWQQQVKPELLVVT-FGKGFGVSGAAVLC-SN 249
Cdd:PRK07505 187 DGVYSM-GGIAPVKELLRLQEKYGLFLYIDDAHGLSIYGKNGEGyvrSELDYRLNERTIIAAsLGKAFGASGGVIMLgDA 265
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446041004 250 TVADYLLQFARHLIYSTSMPPAQAQALRASLAVIRGEEGDARREKLAVLITRFRaglQGLPFTLADSRSAIQPLIVGDNA 329
Cdd:PRK07505 266 EQIELILRYAGPLAFSQSLNVAALGAILASAEIHLSEELDQLQQKLQNNIALFD---SLIPTEQSGSFLPIRLIYIGDED 342
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|..
gi 446041004 330 RALHLAEKLRQQGCWVTAIRPPTVPAGTARLRLTLTAAHETQDIDLLLEVLH 381
Cdd:PRK07505 343 TAIKAAKQLLDRGFYTSPVFFPVVAKGRAGLRIMFRASHTNDEIKRLCSLLK 394
|
|
| PLN03227 |
PLN03227 |
serine palmitoyltransferase-like protein; Provisional |
42-380 |
5.41e-37 |
|
serine palmitoyltransferase-like protein; Provisional
Pssm-ID: 178766 [Multi-domain] Cd Length: 392 Bit Score: 138.11 E-value: 5.41e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446041004 42 LNFSSNDYLGLSHHPDIIRAWKQGAEQFGVGSGGSGHVSGYSVAHQALEEELAEWLGYSRALLFISGFAANQAVITAMMA 121
Cdd:PLN03227 1 LNFATHDFLSTSSSPTLRQTALESLSHYGCGSCGPRGFYGTIDAHLELEQCMAEFLGTESAILYSDGASTTSSTVAAFAK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446041004 122 KEDRIVADRLSHASLLEAASLSPAQLRRFTHNDVAHLARLLAS----------PCPGQ-QLVVTEGVFSMDGDRAPLAEI 190
Cdd:PLN03227 81 RGDLLVVDRGVNEALLVGVSLSRANVRWFRHNDMKDLRRVLEQvraqdvalkrKPTDQrRFLVVEGLYKNTGTLAPLKEL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446041004 191 QQVTQQHNGWLVVDDAHGTGVIGEQGRGSCWQQQVKP--ELLVVTFG--KGFGVSGAAVLCSNTVADYLLQFARHLIYST 266
Cdd:PLN03227 161 VALKEEFHYRLILDESFSFGTLGKSGRGSLEHAGLKPmvHAEIVTFSleNAFGSVGGMTVGSEEVVDHQRLSGSGYCFSA 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446041004 267 SMPPAQAQALRASLAVIRGEE------GDARR---EKLAVLITRFRAGLQGLPFTLADSRSAIQPLIVGDNARA------ 331
Cdd:PLN03227 241 SAPPFLAKADATATAGELAGPqllnrlHDSIAnlySTLTNSSHPYALKLRNRLVITSDPISPIIYLRLSDQEATrrtdet 320
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*.
gi 446041004 332 --LH-LAEKLRQQGCWVTAIRPPTVPAGTAR----LRLTLTAAHETQDIDLLLEVL 380
Cdd:PLN03227 321 liLDqIAHHSLSEGVAVVSTGGHVKKFLQLVpppcLRVVANASHTREDIDKLLTVL 376
|
|
| PRK05937 |
PRK05937 |
8-amino-7-oxononanoate synthase; Provisional |
42-381 |
7.60e-32 |
|
8-amino-7-oxononanoate synthase; Provisional
Pssm-ID: 102071 [Multi-domain] Cd Length: 370 Bit Score: 123.74 E-value: 7.60e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446041004 42 LNFSSNDYLGLSHHPDIIRA----WKQGAEQFGVGSGGSGHVSGYSVAHQA---LEEELAEWLGYSRALLFISGFAANQA 114
Cdd:PRK05937 7 IDFVTNDFLGFSRSDTLVHEvekrYRLYCRQFPHAQLGYGGSRAILGPSSLlddLEHKIAHFHGAPEAFIVPSGYMANLG 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446041004 115 VITAMMAKEDRIVADRLSHASLLEAASLSPAQLRRFTHNDVAHLARLLAS---PCPGQQLVVTEGVFSMDGDRAPLAEIQ 191
Cdd:PRK05937 87 LCAHLSSVTDYVLWDEQVHISVVYSLSVISGWHQSFRHNDLDHLESLLEScrqRSFGRIFIFVCSVYSFKGTLAPLEQII 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446041004 192 QVTQQHNGWLVVDDAHGTGVIGEQGRGSCWQQQVKPELLV-VTFGKGFGVSGAAVLCSNTVADYLLQFARHLIYSTSMPP 270
Cdd:PRK05937 167 ALSKKYHAHLIVDEAHAMGIFGDDGKGFCHSLGYENFYAVlVTYSKALGSMGAALLSSSEVKQDLMLNSPPLRYSTGLPP 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446041004 271 AQAQALRASLAVIrGEEGDARREKLAVLITRFRAglqglPFTLAdSRSAIQPLIVGDNARALhLAEKLRQQGCWVTAIRP 350
Cdd:PRK05937 247 HLLISIQVAYDFL-SQEGELARKQLFRLKEYFAQ-----KFSSA-APGCVQPIFLPGISEQE-LYSKLVETGIRVGVVCF 318
|
330 340 350
....*....|....*....|....*....|.
gi 446041004 351 PTVPAgtarLRLTLTAAHETQDIDLLLEVLH 381
Cdd:PRK05937 319 PTGPF----LRVNLHAFNTEDEVDILVSVLA 345
|
|
| PLN02822 |
PLN02822 |
serine palmitoyltransferase |
17-380 |
1.28e-23 |
|
serine palmitoyltransferase
Pssm-ID: 178417 [Multi-domain] Cd Length: 481 Bit Score: 102.13 E-value: 1.28e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446041004 17 ADALRRRYPVAQGA-GRWLVADECQYLNFSSNDYLGLSHHPDIIRAWKQGAEQFGVGSGGSGHVSGYSVAHQALEEELAE 95
Cdd:PLN02822 86 TEEMRPEPPVLESAaGPHTIINGKDVVNFASANYLGLIGNEKIKESCTSALEKYGVGSCGPRGFYGTIDVHLDCETKIAK 165
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446041004 96 WLGYSRALLFISGFAANQAVITAMMAKEDRIVADRLSHASLLEAASLSPAQLRRFTHNDVAHLARLLASPCPG------- 168
Cdd:PLN02822 166 FLGTPDSILYSYGLSTIFSVIPAFCKKGDIIVADEGVHWGIQNGLYLSRSTIVYFKHNDMESLRNTLEKLTAEnkrkkkl 245
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446041004 169 QQLVVTEGVFSMDGDRAPLAEIQQVTQQHNGWLVVDDAHGTGVIGEQGRGSCWQQQVKPE---LLVVTFGKGFGVSGAAV 245
Cdd:PLN02822 246 RRYIVVEAIYQNSGQIAPLDEIVRLKEKYRFRVLLDESNSFGVLGKSGRGLSEHFGVPIEkidIITAAMGHALATEGGFC 325
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446041004 246 LCSNTVADYLLQFARHLIYSTSMPPAQAQALRASLAVIrgEEGDARREKLAVLITRFRAGL---QGLPFTlADSRSAIQP 322
Cdd:PLN02822 326 TGSARVVDHQRLSSSGYVFSASLPPYLASAAITAIDVL--EDNPSVLAKLKENIALLHKGLsdiPGLSIG-SNTLSPIVF 402
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446041004 323 L--------IVGDNARALHLAEK-LRQQGCWVTAIRPPTV-----PAGtarLRLTLTAAHETQDIDLLLEVL 380
Cdd:PLN02822 403 LhlekstgsAKEDLSLLEHIADRmLKEDSVLVVVSKRSTLdkcrlPVG---IRLFVSAGHTESDILKASESL 471
|
|
| AAT_I |
cd01494 |
Aspartate aminotransferase (AAT) superfamily (fold type I) of pyridoxal phosphate (PLP) ... |
89-247 |
1.72e-10 |
|
Aspartate aminotransferase (AAT) superfamily (fold type I) of pyridoxal phosphate (PLP)-dependent enzymes. PLP combines with an alpha-amino acid to form a compound called a Schiff base or aldimine intermediate, which depending on the reaction, is the substrate in four kinds of reactions (1) transamination (movement of amino groups), (2) racemization (redistribution of enantiomers), (3) decarboxylation (removing COOH groups), and (4) various side-chain reactions depending on the enzyme involved. Pyridoxal phosphate (PLP) dependent enzymes were previously classified into alpha, beta and gamma classes, based on the chemical characteristics (carbon atom involved) of the reaction they catalyzed. The availability of several structures allowed a comprehensive analysis of the evolutionary classification of PLP dependent enzymes, and it was found that the functional classification did not always agree with the evolutionary history of these enzymes. Structure and sequence analysis has revealed that the PLP dependent enzymes can be classified into four major groups of different evolutionary origin: aspartate aminotransferase superfamily (fold type I), tryptophan synthase beta superfamily (fold type II), alanine racemase superfamily (fold type III), and D-amino acid superfamily (fold type IV) and Glycogen phophorylase family (fold type V).
Pssm-ID: 99742 [Multi-domain] Cd Length: 170 Bit Score: 59.32 E-value: 1.72e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446041004 89 LEEELAEWL------GYSRALLFISGFAANQAVITAMMAKEDRIVADRLSHASLLE-AASLSPAQLRRFT-------HND 154
Cdd:cd01494 1 KLEELEEKLarllqpGNDKAVFVPSGTGANEAALLALLGPGDEVIVDANGHGSRYWvAAELAGAKPVPVPvddagygGLD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446041004 155 VAHLARLLASPCPgqQLVVTEGVFSMDGDRAPLAEIQQVTQQHNGWLVVDDAHGTGVIGEQGRGSCWQqqvKPELLVVTF 234
Cdd:cd01494 81 VAILEELKAKPNV--ALIVITPNTTSGGVLVPLKEIRKIAKEYGILLLVDAASAGGASPAPGVLIPEG---GADVVTFSL 155
|
170
....*....|...
gi 446041004 235 GKGFGVSGAAVLC 247
Cdd:cd01494 156 HKNLGGEGGGVVI 168
|
|
| AAT_like |
cd00609 |
Aspartate aminotransferase family. This family belongs to pyridoxal phosphate (PLP)-dependent ... |
86-381 |
1.11e-05 |
|
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: 46.95 E-value: 1.11e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446041004 86 HQALEEELAEWLGYSRA--------LLFISGFAANQAVITAMMAKEDRIVADRLSHASLLEAASLSPAQLRR------FT 151
Cdd:cd00609 38 LPELREAIAEWLGRRGGvdvppeeiVVTNGAQEALSLLLRALLNPGDEVLVPDPTYPGYEAAARLAGAEVVPvpldeeGG 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446041004 152 HNDVAHLARLLASPCPGqqLVV-------TEGVFSMDgDRAPLAEIQqvtQQHNGWLVVDDAHGtGVIGEQGRGSCWQQQ 224
Cdd:cd00609 118 FLLDLELLEAAKTPKTK--LLYlnnpnnpTGAVLSEE-ELEELAELA---KKHGILIISDEAYA-ELVYDGEPPPALALL 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446041004 225 VKPELLVV--TFGKGFGVSG---AAVLCSNtvADYLLQFARHLIYSTSMPPAQAQAlrASLAVIRGEEG--DARREKLAV 297
Cdd:cd00609 191 DAYERVIVlrSFSKTFGLPGlriGYLIAPP--EELLERLKKLLPYTTSGPSTLSQA--AAAAALDDGEEhlEELRERYRR 266
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446041004 298 LITRFRAGLQGLPFTLADSRSA-----IQpliVGDNARALHLAEKLRQQGcwvTAIRPPTV--PAGTARLRLTLTAAHEt 370
Cdd:cd00609 267 RRDALLEALKELGPLVVVKPSGgfflwLD---LPEGDDEEFLERLLLEAG---VVVRPGSAfgEGGEGFVRLSFATPEE- 339
|
330
....*....|.
gi 446041004 371 qDIDLLLEVLH 381
Cdd:cd00609 340 -ELEEALERLA 349
|
|
| |
