|
Name |
Accession |
Description |
Interval |
E-value |
| 5aminolev_synth |
TIGR01821 |
5-aminolevulinic acid synthase; This model represents 5-aminolevulinic acid synthase, an ... |
106-511 |
0e+00 |
|
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: 760.42 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83977440 106 FSYDQFFRDKIMEKKQDHTYRVFKTVNRWADAYPFAQHFSEASvaSKDVSVWCSNDYLGMSRHPQVLQATQETLQRHGAG 185
Cdd:TIGR01821 1 MDYDQFFNKEIDKLHLEGRYRVFADLERQAGEFPFAQWHRPDG--AKDVTVWCSNDYLGMGQHPEVLQAMHETLDKYGAG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83977440 186 AGGTRNISGTSKFHVELEQELAELHQKDSALLFSSCFVANDSTLFTLAKILPGCEIYSDAGNHASMIQGIRNSGAAKFVF 265
Cdd:TIGR01821 79 AGGTRNISGTNIPHVELEAELADLHGKESALVFTSGYVANDATLATLAKIIPGCVIFSDELNHASMIEGIRHSGAEKFIF 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83977440 266 RHNDPDHLKKLLEKSNPKIPKIVAFETVHSMDGAICPLEELCDVSHQYGALTFVDEVHAVGLYGSRGAGIGERDGIMHKI 345
Cdd:TIGR01821 159 RHNDVAHLEKLLQSVDPNRPKIIAFESVYSMDGDIAPIEEICDLADKYGALTYLDEVHAVGLYGPRGGGIAERDGLMHRI 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83977440 346 DIISGTLGKAFGCVGGYIASTRDLVDMVRSYAAGFIFTTSLPPMVLSGALESVRLLKGEegQALRRAHQRNVKHMRQLLM 425
Cdd:TIGR01821 239 DIIEGTLAKAFGVVGGYIAASRKLIDAIRSYAPGFIFTTSLPPAIAAGATASIRHLKES--QDLRRAHQENVKRLKNLLE 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83977440 426 DRGLPVIPCPSHIIPIRVGNAALNSKLCDLLLSKHGIYVQAINYPTVPRGEELLRLAPSPHHSPQMMEDFVEKLLLAWTA 505
Cdd:TIGR01821 317 ALGIPVIPNPSHIVPVIIGDAALCKKVSDLLLNKHGIYVQPINYPTVPRGTERLRITPTPAHTDKMIDDLVEALLLVWDR 396
|
....*.
gi 83977440 506 VGLPLQ 511
Cdd:TIGR01821 397 LGLPLS 402
|
|
| KBL_like |
cd06454 |
KBL_like; this family belongs to the pyridoxal phosphate (PLP)-dependent aspartate ... |
152-503 |
0e+00 |
|
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: 529.05 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83977440 152 KDVSVWCSNDYLGMSRHPQVLQATQETLQRHGAGAGGTRNISGTSKFHVELEQELAELHQKDSALLFSSCFVANDSTLFT 231
Cdd:cd06454 1 KKVLNFCSNDYLGLANHPEVIEAAKEALDKYGVGAGGSRLISGTSDLHEELEEELAEFHGKEAALVFSSGYAANDGVLST 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83977440 232 LAkiLPGCEIYSDAGNHASMIQGIRNSGAAKFVFRHNDPDHLKKLLEKS-NPKIPKIVAFETVHSMDGAICPLEELCDVS 310
Cdd:cd06454 81 LA--GKGDLIISDSLNHASIIDGIRLSGAKKRIFKHNDMEDLEKLLREArRPYGKKLIVTEGVYSMDGDIAPLPELVDLA 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83977440 311 HQYGALTFVDEVHAVGLYGSRGAGIGERDGIMHKIDIISGTLGKAFGCVGGYIASTRDLVDMVRSYAAGFIFTTSLPPMV 390
Cdd:cd06454 159 KKYGAILFVDEAHSVGVYGPHGRGVEEFGGLTDDVDIIMGTLGKAFGAVGGYIAGSKELIDYLRSYARGFIFSTSLPPAV 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83977440 391 LSGALESVRLLKGeeGQALRRAHQRNVKHMRQLLMDRGLPVIPCPSHIIPIRVG-NAALNSKLCDLLLsKHGIYVQAINY 469
Cdd:cd06454 239 AAAALAALEVLQG--GPERRERLQENVRYLRRGLKELGFPVGGSPSHIIPPLIGdDPAKAVAFSDALL-ERGIYVQAIRY 315
|
330 340 350
....*....|....*....|....*....|....
gi 83977440 470 PTVPRGEELLRLAPSPHHSPQMMEDFVEKLLLAW 503
Cdd:cd06454 316 PTVPRGTARLRISLSAAHTKEDIDRLLEALKEVG 349
|
|
| PRK13392 |
PRK13392 |
5-aminolevulinate synthase; Provisional |
105-509 |
0e+00 |
|
5-aminolevulinate synthase; Provisional
Pssm-ID: 184023 [Multi-domain] Cd Length: 410 Bit Score: 520.95 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83977440 105 VFSYDQFFRDKIMEKKQDHTYRVFKTVNRWADAYPFAqhFSEASVASKDVSVWCSNDYLGMSRHPQVLQATQETLQRHGA 184
Cdd:PRK13392 1 MMNYDSYFDAALAQLHQEGRYRVFADLEREAGRFPRA--RDHGPDGPRRVTIWCSNDYLGMGQHPDVIGAMVDALDRYGA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83977440 185 GAGGTRNISGTSKFHVELEQELAELHQKDSALLFSSCFVANDSTLFTLAKILPGCEIYSDAGNHASMIQGIRNSGAAKFV 264
Cdd:PRK13392 79 GAGGTRNISGTSHPHVLLERELADLHGKESALLFTSGYVSNDAALSTLGKLLPGCVILSDALNHASMIEGIRRSGAEKQV 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83977440 265 FRHNDPDHLKKLLEKSNPKIPKIVAFETVHSMDGAICPLEELCDVSHQYGALTFVDEVHAVGLYGSRGAGIGERDGIMHK 344
Cdd:PRK13392 159 FRHNDLADLEEQLASVDPDRPKLIAFESVYSMDGDIAPIEAICDLADRYNALTYVDEVHAVGLYGARGGGIAERDGLMDR 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83977440 345 IDIISGTLGKAFGCVGGYIASTRDLVDMVRSYAAGFIFTTSLPPMVLSGALESVRLLKgeEGQALRRAHQRNVKHMRQLL 424
Cdd:PRK13392 239 IDMIQGTLAKAFGCLGGYIAASADLIDFVRSFAPGFIFTTALPPAVAAGATAAIRHLK--TSQTERDAHQDRVAALKAKL 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83977440 425 MDRGLPVIPCPSHIIPIRVGNAALNSKLCDLLLSKHGIYVQAINYPTVPRGEELLRLAPSPHHSPQMMEDFVEKLLLAWT 504
Cdd:PRK13392 317 NANGIPVMPSPSHIVPVMVGDPTLCKAISDRLMSEHGIYIQPINYPTVPRGTERLRITPTPLHDDEDIDALVAALVAIWD 396
|
....*
gi 83977440 505 AVGLP 509
Cdd:PRK13392 397 RLELP 401
|
|
| BioF |
COG0156 |
7-keto-8-aminopelargonate synthetase or related enzyme [Coenzyme transport and metabolism]; ... |
108-499 |
3.70e-171 |
|
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: 489.18 E-value: 3.70e-171
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83977440 108 YDQFFRDKIMEKKQDHTYRVFKTVNRWADAypfaqhfsEASVASKDVSVWCSNDYLGMSRHPQVLQATQETLQRHGAGAG 187
Cdd:COG0156 1 LLDRLEAELAALKAAGLYRYLRVLESPQGP--------RVTIDGREVLNFSSNDYLGLANHPRVIEAAAEALDRYGTGSG 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83977440 188 GTRNISGTSKFHVELEQELAELHQKDSALLFSSCFVANDSTLFTLAKilPGCEIYSDAGNHASMIQGIRNSGAAKFVFRH 267
Cdd:COG0156 73 GSRLVSGTTPLHEELEEELAEFLGKEAALLFSSGYAANLGVISALAG--RGDLIFSDELNHASIIDGARLSGAKVVRFRH 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83977440 268 NDPDHLKKLLEKSNPKIPKIVAFETVHSMDGAICPLEELCDVSHQYGALTFVDEVHAVGLYGSRGAGIGERDGIMHKIDI 347
Cdd:COG0156 151 NDMDDLERLLKKARAARRKLIVTDGVFSMDGDIAPLPEIVELAEKYGALLYVDDAHGTGVLGETGRGLVEHFGLEDRVDI 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83977440 348 ISGTLGKAFGCVGGYIASTRDLVDMVRSYAAGFIFTTSLPPMVLSGALESVRLLKGEEgqALRRAHQRNVKHMRQLLMDR 427
Cdd:COG0156 231 IMGTLSKALGSSGGFVAGSKELIDYLRNRARPFIFSTALPPAVAAAALAALEILREEP--ELRERLWENIAYFREGLKEL 308
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 83977440 428 GLPVIPCPSHIIPIRVGNAALNSKLCDLLLsKHGIYVQAINYPTVPRGEELLRLAPSPHHSPQMMEDFVEKL 499
Cdd:COG0156 309 GFDLGPSESPIVPVIVGDAERALALADALL-ERGIYVSAIRPPTVPKGTARLRITLSAAHTEEDIDRLLEAL 379
|
|
| Aminotran_1_2 |
pfam00155 |
Aminotransferase class I and II; |
152-499 |
2.35e-73 |
|
Aminotransferase class I and II;
Pssm-ID: 395103 [Multi-domain] Cd Length: 351 Bit Score: 237.20 E-value: 2.35e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83977440 152 KDVSVWCSNDYLGMSRhPQVLQATQEtlqrhgAGAGGTRNISGTSKFHVELEQELAELH--------QKDSALLFSSCFV 223
Cdd:pfam00155 1 TDKINLGSNEYLGDTL-PAVAKAEKD------ALAGGTRNLYGPTDGHPELREALAKFLgrspvlklDREAAVVFGSGAG 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83977440 224 ANDSTLFTLAKiLPGCEIYSDAGNHASMIQGIRNSGAAKFVFR-------HNDPDHLKKLLEKSnpkiPKIVAFETVHSM 296
Cdd:pfam00155 74 ANIEALIFLLA-NPGDAILVPAPTYASYIRIARLAGGEVVRYPlydsndfHLDFDALEAALKEK----PKVVLHTSPHNP 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83977440 297 DGAICPLEELC---DVSHQYGALTFVDEVHAVGLYGSRGAgIGERDGIMHKID-IISGTLGKAFGCVG---GYIASTRDL 369
Cdd:pfam00155 149 TGTVATLEELEkllDLAKEHNILLLVDEAYAGFVFGSPDA-VATRALLAEGPNlLVVGSFSKAFGLAGwrvGYILGNAAV 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83977440 370 VDMVRSYAAGFIFTTSLPPMVLSGALESvrLLKGEEGQALRRAHQRNVKHMRQLLMDRGLPVIPCPSHIIPIRVGNAALN 449
Cdd:pfam00155 228 ISQLRKLARPFYSSTHLQAAAAAALSDP--LLVASELEEMRQRIKERRDYLRDGLQAAGLSVLPSQAGFFLLTGLDPETA 305
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|
gi 83977440 450 SKLCDLLLSKHGIYVQAINYPTVPrgeELLRLAPSpHHSPQMMEDFVEKL 499
Cdd:pfam00155 306 KELAQVLLEEVGVYVTPGSSPGVP---GWLRITVA-GGTEEELEELLEAI 351
|
|
| Preseq_ALAS |
pfam09029 |
5-aminolevulinate synthase presequence; The N terminal presequence domain found in ... |
5-100 |
3.94e-14 |
|
5-aminolevulinate synthase presequence; The N terminal presequence domain found in 5-aminolevulinate synthase exists as an amphipathic helix, with a positively charged surface provided by lysine residues and no stable helix at the N-terminus. The domain is essential for the import process by which ALAS is transported into the mitochondria: translocase of the outer membrane (Tom) and translocase of the inner membrane protein complexes appear responsible for recognition and import through the mitochondrial membrane. The protein Tom20 is anchored to the mitochondrial outer membrane, and its interaction with presequences is thought to be the recognition step which allows subsequent import.
Pssm-ID: 462658 Cd Length: 114 Bit Score: 68.67 E-value: 3.94e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83977440 5 AMLLQCCPVLARGPTSLLGKVVKThqFLFGIGRCPILATQGPNCSQIHL----KATKAGGDSPSWAK----GH------- 69
Cdd:pfam09029 1 ASVLRRCPFLSRVPQAFLQKARKS--LLSYAQRCPVMMTRALSTSSANLqgekEETPVAGPTAKQAKalplGHpspqagq 78
|
90 100 110
....*....|....*....|....*....|....*.
gi 83977440 70 -----CPFMLSELQDGKSKIVQKAAPEVQEDVKAFK 100
Cdd:pfam09029 79 svaskCPFLAAEMGQKNSNVVRKASPEVQEDVQEVK 114
|
|
|
|
Name |
Accession |
Description |
Interval |
E-value |
| 5aminolev_synth |
TIGR01821 |
5-aminolevulinic acid synthase; This model represents 5-aminolevulinic acid synthase, an ... |
106-511 |
0e+00 |
|
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: 760.42 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83977440 106 FSYDQFFRDKIMEKKQDHTYRVFKTVNRWADAYPFAQHFSEASvaSKDVSVWCSNDYLGMSRHPQVLQATQETLQRHGAG 185
Cdd:TIGR01821 1 MDYDQFFNKEIDKLHLEGRYRVFADLERQAGEFPFAQWHRPDG--AKDVTVWCSNDYLGMGQHPEVLQAMHETLDKYGAG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83977440 186 AGGTRNISGTSKFHVELEQELAELHQKDSALLFSSCFVANDSTLFTLAKILPGCEIYSDAGNHASMIQGIRNSGAAKFVF 265
Cdd:TIGR01821 79 AGGTRNISGTNIPHVELEAELADLHGKESALVFTSGYVANDATLATLAKIIPGCVIFSDELNHASMIEGIRHSGAEKFIF 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83977440 266 RHNDPDHLKKLLEKSNPKIPKIVAFETVHSMDGAICPLEELCDVSHQYGALTFVDEVHAVGLYGSRGAGIGERDGIMHKI 345
Cdd:TIGR01821 159 RHNDVAHLEKLLQSVDPNRPKIIAFESVYSMDGDIAPIEEICDLADKYGALTYLDEVHAVGLYGPRGGGIAERDGLMHRI 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83977440 346 DIISGTLGKAFGCVGGYIASTRDLVDMVRSYAAGFIFTTSLPPMVLSGALESVRLLKGEegQALRRAHQRNVKHMRQLLM 425
Cdd:TIGR01821 239 DIIEGTLAKAFGVVGGYIAASRKLIDAIRSYAPGFIFTTSLPPAIAAGATASIRHLKES--QDLRRAHQENVKRLKNLLE 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83977440 426 DRGLPVIPCPSHIIPIRVGNAALNSKLCDLLLSKHGIYVQAINYPTVPRGEELLRLAPSPHHSPQMMEDFVEKLLLAWTA 505
Cdd:TIGR01821 317 ALGIPVIPNPSHIVPVIIGDAALCKKVSDLLLNKHGIYVQPINYPTVPRGTERLRITPTPAHTDKMIDDLVEALLLVWDR 396
|
....*.
gi 83977440 506 VGLPLQ 511
Cdd:TIGR01821 397 LGLPLS 402
|
|
| KBL_like |
cd06454 |
KBL_like; this family belongs to the pyridoxal phosphate (PLP)-dependent aspartate ... |
152-503 |
0e+00 |
|
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: 529.05 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83977440 152 KDVSVWCSNDYLGMSRHPQVLQATQETLQRHGAGAGGTRNISGTSKFHVELEQELAELHQKDSALLFSSCFVANDSTLFT 231
Cdd:cd06454 1 KKVLNFCSNDYLGLANHPEVIEAAKEALDKYGVGAGGSRLISGTSDLHEELEEELAEFHGKEAALVFSSGYAANDGVLST 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83977440 232 LAkiLPGCEIYSDAGNHASMIQGIRNSGAAKFVFRHNDPDHLKKLLEKS-NPKIPKIVAFETVHSMDGAICPLEELCDVS 310
Cdd:cd06454 81 LA--GKGDLIISDSLNHASIIDGIRLSGAKKRIFKHNDMEDLEKLLREArRPYGKKLIVTEGVYSMDGDIAPLPELVDLA 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83977440 311 HQYGALTFVDEVHAVGLYGSRGAGIGERDGIMHKIDIISGTLGKAFGCVGGYIASTRDLVDMVRSYAAGFIFTTSLPPMV 390
Cdd:cd06454 159 KKYGAILFVDEAHSVGVYGPHGRGVEEFGGLTDDVDIIMGTLGKAFGAVGGYIAGSKELIDYLRSYARGFIFSTSLPPAV 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83977440 391 LSGALESVRLLKGeeGQALRRAHQRNVKHMRQLLMDRGLPVIPCPSHIIPIRVG-NAALNSKLCDLLLsKHGIYVQAINY 469
Cdd:cd06454 239 AAAALAALEVLQG--GPERRERLQENVRYLRRGLKELGFPVGGSPSHIIPPLIGdDPAKAVAFSDALL-ERGIYVQAIRY 315
|
330 340 350
....*....|....*....|....*....|....
gi 83977440 470 PTVPRGEELLRLAPSPHHSPQMMEDFVEKLLLAW 503
Cdd:cd06454 316 PTVPRGTARLRISLSAAHTKEDIDRLLEALKEVG 349
|
|
| PRK13392 |
PRK13392 |
5-aminolevulinate synthase; Provisional |
105-509 |
0e+00 |
|
5-aminolevulinate synthase; Provisional
Pssm-ID: 184023 [Multi-domain] Cd Length: 410 Bit Score: 520.95 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83977440 105 VFSYDQFFRDKIMEKKQDHTYRVFKTVNRWADAYPFAqhFSEASVASKDVSVWCSNDYLGMSRHPQVLQATQETLQRHGA 184
Cdd:PRK13392 1 MMNYDSYFDAALAQLHQEGRYRVFADLEREAGRFPRA--RDHGPDGPRRVTIWCSNDYLGMGQHPDVIGAMVDALDRYGA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83977440 185 GAGGTRNISGTSKFHVELEQELAELHQKDSALLFSSCFVANDSTLFTLAKILPGCEIYSDAGNHASMIQGIRNSGAAKFV 264
Cdd:PRK13392 79 GAGGTRNISGTSHPHVLLERELADLHGKESALLFTSGYVSNDAALSTLGKLLPGCVILSDALNHASMIEGIRRSGAEKQV 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83977440 265 FRHNDPDHLKKLLEKSNPKIPKIVAFETVHSMDGAICPLEELCDVSHQYGALTFVDEVHAVGLYGSRGAGIGERDGIMHK 344
Cdd:PRK13392 159 FRHNDLADLEEQLASVDPDRPKLIAFESVYSMDGDIAPIEAICDLADRYNALTYVDEVHAVGLYGARGGGIAERDGLMDR 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83977440 345 IDIISGTLGKAFGCVGGYIASTRDLVDMVRSYAAGFIFTTSLPPMVLSGALESVRLLKgeEGQALRRAHQRNVKHMRQLL 424
Cdd:PRK13392 239 IDMIQGTLAKAFGCLGGYIAASADLIDFVRSFAPGFIFTTALPPAVAAGATAAIRHLK--TSQTERDAHQDRVAALKAKL 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83977440 425 MDRGLPVIPCPSHIIPIRVGNAALNSKLCDLLLSKHGIYVQAINYPTVPRGEELLRLAPSPHHSPQMMEDFVEKLLLAWT 504
Cdd:PRK13392 317 NANGIPVMPSPSHIVPVMVGDPTLCKAISDRLMSEHGIYIQPINYPTVPRGTERLRITPTPLHDDEDIDALVAALVAIWD 396
|
....*
gi 83977440 505 AVGLP 509
Cdd:PRK13392 397 RLELP 401
|
|
| BioF |
COG0156 |
7-keto-8-aminopelargonate synthetase or related enzyme [Coenzyme transport and metabolism]; ... |
108-499 |
3.70e-171 |
|
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: 489.18 E-value: 3.70e-171
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83977440 108 YDQFFRDKIMEKKQDHTYRVFKTVNRWADAypfaqhfsEASVASKDVSVWCSNDYLGMSRHPQVLQATQETLQRHGAGAG 187
Cdd:COG0156 1 LLDRLEAELAALKAAGLYRYLRVLESPQGP--------RVTIDGREVLNFSSNDYLGLANHPRVIEAAAEALDRYGTGSG 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83977440 188 GTRNISGTSKFHVELEQELAELHQKDSALLFSSCFVANDSTLFTLAKilPGCEIYSDAGNHASMIQGIRNSGAAKFVFRH 267
Cdd:COG0156 73 GSRLVSGTTPLHEELEEELAEFLGKEAALLFSSGYAANLGVISALAG--RGDLIFSDELNHASIIDGARLSGAKVVRFRH 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83977440 268 NDPDHLKKLLEKSNPKIPKIVAFETVHSMDGAICPLEELCDVSHQYGALTFVDEVHAVGLYGSRGAGIGERDGIMHKIDI 347
Cdd:COG0156 151 NDMDDLERLLKKARAARRKLIVTDGVFSMDGDIAPLPEIVELAEKYGALLYVDDAHGTGVLGETGRGLVEHFGLEDRVDI 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83977440 348 ISGTLGKAFGCVGGYIASTRDLVDMVRSYAAGFIFTTSLPPMVLSGALESVRLLKGEEgqALRRAHQRNVKHMRQLLMDR 427
Cdd:COG0156 231 IMGTLSKALGSSGGFVAGSKELIDYLRNRARPFIFSTALPPAVAAAALAALEILREEP--ELRERLWENIAYFREGLKEL 308
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 83977440 428 GLPVIPCPSHIIPIRVGNAALNSKLCDLLLsKHGIYVQAINYPTVPRGEELLRLAPSPHHSPQMMEDFVEKL 499
Cdd:COG0156 309 GFDLGPSESPIVPVIVGDAERALALADALL-ERGIYVSAIRPPTVPKGTARLRITLSAAHTEEDIDRLLEAL 379
|
|
| PRK05958 |
PRK05958 |
8-amino-7-oxononanoate synthase; Reviewed |
158-499 |
2.58e-107 |
|
8-amino-7-oxononanoate synthase; Reviewed
Pssm-ID: 235655 [Multi-domain] Cd Length: 385 Bit Score: 326.34 E-value: 2.58e-107
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83977440 158 CSNDYLGMSRHPQVLQATQETLQRHGAGAGGTRNISGTSKFHVELEQELAELHQKDSALLFSSCFVANDSTLFTLAKilP 237
Cdd:PRK05958 45 ASNDYLGLARHPRLIAAAQQAARRYGAGSGGSRLVTGNSPAHEALEEELAEWFGAERALLFSSGYAANLAVLTALAG--K 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83977440 238 GCEIYSDAGNHASMIQGIRNSGAAKFVFRHNDPDHLKKLLEKSNPKiPKIVAFETVHSMDGAICPLEELCDVSHQYGALT 317
Cdd:PRK05958 123 GDLIVSDKLNHASLIDGARLSRARVRRYPHNDVDALEALLAKWRAG-RALIVTESVFSMDGDLAPLAELVALARRHGAWL 201
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83977440 318 FVDEVHAVGLYGSRGAGIGERDGIMHKIDIIS-GTLGKAFGCVGGYIASTRDLVDMVRSYAAGFIFTTSLPPMVLSGALE 396
Cdd:PRK05958 202 LVDEAHGTGVLGPQGRGLAAEAGLAGEPDVILvGTLGKALGSSGAAVLGSETLIDYLINRARPFIFTTALPPAQAAAARA 281
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83977440 397 SVRLLKGEEGqalRRAH-QRNVKHMRQLLMDRGLPVIPCPSHIIPIRVGN--AALN-SKLCDlllsKHGIYVQAINYPTV 472
Cdd:PRK05958 282 ALRILRREPE---RRERlAALIARLRAGLRALGFQLMDSQSAIQPLIVGDneRALAlAAALQ----EQGFWVGAIRPPTV 354
|
330 340
....*....|....*....|....*..
gi 83977440 473 PRGEELLRLAPSPHHSPQMMEDFVEKL 499
Cdd:PRK05958 355 PAGTSRLRITLTAAHTEADIDRLLEAL 381
|
|
| bioF |
TIGR00858 |
8-amino-7-oxononanoate synthase; 7-keto-8-aminopelargonic acid synthetase is an alternate name. ... |
157-499 |
5.59e-102 |
|
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: 311.89 E-value: 5.59e-102
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83977440 157 WCSNDYLGMSRHPQVLQATQETLQRHGAGAGGTRNISGTSKFHVELEQELAELHQKDSALLFSSCFVANDSTLFTLAKil 236
Cdd:TIGR00858 21 FSSNDYLGLASHPEVIQAAQQGAEQYGAGSTASRLVSGNSPLHEELEEELAEWKGTEAALLFSSGYLANVGVISALVG-- 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83977440 237 PGCEIYSDAGNHASMIQGIRNSGAAKFVFRHNDPDHLKKLLEKSNPKIPKIVAFETVHSMDGAICPLEELCDVSHQYGAL 316
Cdd:TIGR00858 99 KGDLILSDALNHASLIDGCRLSGARVRRYRHNDVEHLERLLEKNRGERRKLIVTDGVFSMDGDIAPLPQLVALAERYGAW 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83977440 317 TFVDEVHAVGLYGSRGAGIGERDGIMHKIDIIS-GTLGKAFGCVGGYIASTRDLVDMVRSYAAGFIFTTSLPPMVLSGAL 395
Cdd:TIGR00858 179 LMVDDAHGTGVLGEDGRGTLEHFGLKPEPVDIQvGTLSKALGSYGAYVAGSQALIDYLINRARTLIFSTALPPAVAAAAL 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83977440 396 ESVRLLkgEEGQALRRAHQRNVKHMRQLLMDRGLPVIPCPSHIIPIRVGNAALNsklcdLLLSKH----GIYVQAINYPT 471
Cdd:TIGR00858 259 AALELI--QEEPWRREKLLALIARLRAGLEALGFTLMPSCTPIVPVIIGDNASA-----LALAEElqqqGIFVGAIRPPT 331
|
330 340
....*....|....*....|....*...
gi 83977440 472 VPRGEELLRLAPSPHHSPQMMEDFVEKL 499
Cdd:TIGR00858 332 VPAGTSRLRLTLSAAHTPGDIDRLAEAL 359
|
|
| PRK06939 |
PRK06939 |
2-amino-3-ketobutyrate coenzyme A ligase; Provisional |
107-507 |
3.17e-101 |
|
2-amino-3-ketobutyrate coenzyme A ligase; Provisional
Pssm-ID: 235893 [Multi-domain] Cd Length: 397 Bit Score: 310.97 E-value: 3.17e-101
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83977440 107 SYDQFFRDKIMEKKQDHTY---RVFKTVNRwadaypfaqhfSEASVAS-KDVSVWCSNDYLGMSRHPQVLQATQETLQRH 182
Cdd:PRK06939 4 AFYAQLREELEEIKAEGLYkeeRVITSPQG-----------ADITVADgKEVINFCANNYLGLANHPELIAAAKAALDSH 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83977440 183 GAGAGGTRNISGTSKFHVELEQELAELHQKDSALLFSSCFVAND---STLFTlakilPGCEIYSDAGNHASMIQGIRNSG 259
Cdd:PRK06939 73 GFGMASVRFICGTQDLHKELEEKLAKFLGTEDAILYSSCFDANGglfETLLG-----KEDAIISDALNHASIIDGVRLCK 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83977440 260 AAKFVFRHNDPDHLKKLLEKSNPKIP--KIVAFETVHSMDGAICPLEELCDVSHQYGALTFVDEVHAVGLYGSRGAGIGE 337
Cdd:PRK06939 148 AKRYRYANNDMADLEAQLKEAKEAGArhKLIATDGVFSMDGDIAPLPEICDLADKYDALVMVDDSHAVGFVGENGRGTVE 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83977440 338 RDGIMHKIDIISGTLGKAF-GCVGGYIASTRDLVDMVRSYAAGFIFTTSLPPMVLSGALESVRLLkgEEGQALRRAHQRN 416
Cdd:PRK06939 228 HFGVMDRVDIITGTLGKALgGASGGYTAGRKEVIDWLRQRSRPYLFSNSLAPAIVAASIKVLELL--EESDELRDRLWEN 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83977440 417 VKHMRQLLMDRGLPVIPCPSHIIPIRVGNAALNSKLCDLLLsKHGIYVQAINYPTVPRGEELLRLAPSPHHSPQMmedfV 496
Cdd:PRK06939 306 ARYFREGMTAAGFTLGPGEHPIIPVMLGDAKLAQEFADRLL-EEGVYVIGFSFPVVPKGQARIRTQMSAAHTKEQ----L 380
|
410
....*....|.
gi 83977440 497 EKLLLAWTAVG 507
Cdd:PRK06939 381 DRAIDAFEKVG 391
|
|
| Aminotran_1_2 |
pfam00155 |
Aminotransferase class I and II; |
152-499 |
2.35e-73 |
|
Aminotransferase class I and II;
Pssm-ID: 395103 [Multi-domain] Cd Length: 351 Bit Score: 237.20 E-value: 2.35e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83977440 152 KDVSVWCSNDYLGMSRhPQVLQATQEtlqrhgAGAGGTRNISGTSKFHVELEQELAELH--------QKDSALLFSSCFV 223
Cdd:pfam00155 1 TDKINLGSNEYLGDTL-PAVAKAEKD------ALAGGTRNLYGPTDGHPELREALAKFLgrspvlklDREAAVVFGSGAG 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83977440 224 ANDSTLFTLAKiLPGCEIYSDAGNHASMIQGIRNSGAAKFVFR-------HNDPDHLKKLLEKSnpkiPKIVAFETVHSM 296
Cdd:pfam00155 74 ANIEALIFLLA-NPGDAILVPAPTYASYIRIARLAGGEVVRYPlydsndfHLDFDALEAALKEK----PKVVLHTSPHNP 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83977440 297 DGAICPLEELC---DVSHQYGALTFVDEVHAVGLYGSRGAgIGERDGIMHKID-IISGTLGKAFGCVG---GYIASTRDL 369
Cdd:pfam00155 149 TGTVATLEELEkllDLAKEHNILLLVDEAYAGFVFGSPDA-VATRALLAEGPNlLVVGSFSKAFGLAGwrvGYILGNAAV 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83977440 370 VDMVRSYAAGFIFTTSLPPMVLSGALESvrLLKGEEGQALRRAHQRNVKHMRQLLMDRGLPVIPCPSHIIPIRVGNAALN 449
Cdd:pfam00155 228 ISQLRKLARPFYSSTHLQAAAAAALSDP--LLVASELEEMRQRIKERRDYLRDGLQAAGLSVLPSQAGFFLLTGLDPETA 305
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|
gi 83977440 450 SKLCDLLLSKHGIYVQAINYPTVPrgeELLRLAPSpHHSPQMMEDFVEKL 499
Cdd:pfam00155 306 KELAQVLLEEVGVYVTPGSSPGVP---GWLRITVA-GGTEEELEELLEAI 351
|
|
| PLN02955 |
PLN02955 |
8-amino-7-oxononanoate synthase |
151-502 |
1.13e-56 |
|
8-amino-7-oxononanoate synthase
Pssm-ID: 178541 [Multi-domain] Cd Length: 476 Bit Score: 197.20 E-value: 1.13e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83977440 151 SKDVSVWCSNDYLGMSRHPQVLQATQETLQRHGAGAGGTRNISGTSKFHVELEQELAELHQKDSALLFSSCFVANDSTLF 230
Cdd:PLN02955 101 FKKLLLFSGNDYLGLSSHPTISNAAANAAKEYGMGPKGSALICGYTTYHRLLESSLADLKKKEDCLVCPTGFAANMAAMV 180
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83977440 231 TL---AKILPGCE---------IYSDAGNHASMIQGIR---NSGAAK-FVFRHNDPDHLKKLLekSNPKIP-KIVAFETV 293
Cdd:PLN02955 181 AIgsvASLLAASGkplknekvaIFSDALNHASIIDGVRlaeRQGNVEvFVYRHCDMYHLNSLL--SSCKMKrKVVVTDSL 258
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83977440 294 HSMDGAICPLEELCDVSHQYGALTFVDEVHAVGLYGSRGAGIGERDGIMHKIDIISGTLGKAFGCVGGYIASTRDLVDMV 373
Cdd:PLN02955 259 FSMDGDFAPMEELSQLRKKYGFLLVIDDAHGTFVCGENGGGVAEEFNCEADVDLCVGTLSKAAGCHGGFIACSKKWKQLI 338
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83977440 374 RSYAAGFIFTTSLPPMVLSGALESVRLLKGEEGQalRRAHQRNVKHMRQLlmdRGLPVipcPSHIIPIRVGNAALNSKLC 453
Cdd:PLN02955 339 QSRGRSFIFSTAIPVPMAAAAYAAVVVARKEKWR--RKAIWERVKEFKAL---SGVDI---SSPIISLVVGNQEKALKAS 410
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
gi 83977440 454 DLLLsKHGIYVQAINYPTVPRGEELLRLAPSPHHSpqmMEDfVEKLLLA 502
Cdd:PLN02955 411 RYLL-KSGFHVMAIRPPTVPPNSCRLRVTLSAAHT---TED-VKKLITA 454
|
|
| PLN02483 |
PLN02483 |
serine palmitoyltransferase |
159-493 |
2.45e-55 |
|
serine palmitoyltransferase
Pssm-ID: 178101 [Multi-domain] Cd Length: 489 Bit Score: 193.83 E-value: 2.45e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83977440 159 SNDYLGMSRH-----PQVLqatqETLQRHGAGAGGTRNISGTSKFHVELEQELAELHQKDSALLFSSCFVANDSTLFTLa 233
Cdd:PLN02483 107 SYNYLGFAAAdeyctPRVI----ESLKKYSASTCSSRVDGGTTKLHRELEELVARFVGKPAAIVFGMGYATNSTIIPAL- 181
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83977440 234 kILPGCEIYSDAGNHASMIQGIRNSGAAKFVFRHNDPDHLKKLLEKS----NPKIPK-----IVAFETVHSMDGAICPLE 304
Cdd:PLN02483 182 -IGKGGLIISDSLNHNSIVNGARGSGATIRVFQHNTPSHLEEVLREQiaegQPRTHRpwkkiIVIVEGIYSMEGELCKLP 260
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83977440 305 ELCDVSHQYGALTFVDEVHAVGLYGSRGAGIGERDGIMHK-IDIISGTLGKAFGCVGGYIASTRDLVDMVRSYAAGFIFT 383
Cdd:PLN02483 261 EIVAVCKKYKAYVYLDEAHSIGAVGKTGRGVCELLGVDPAdVDIMMGTFTKSFGSCGGYIAGSKELIQYLKRTCPAHLYA 340
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83977440 384 TSLPPMVLSGALESVRLLKGEEG-----QALRRAHQrNVKHMRQLLMDRGLPVI-PCPSHIIPIRVGNAALNSKLCDLLL 457
Cdd:PLN02483 341 TSMSPPAVQQVISAIKVILGEDGtnrgaQKLAQIRE-NSNFFRSELQKMGFEVLgDNDSPVMPIMLYNPAKIPAFSRECL 419
|
330 340 350
....*....|....*....|....*....|....*.
gi 83977440 458 sKHGIYVQAINYPTVPRGEELLRLAPSPHHSPQMME 493
Cdd:PLN02483 420 -KQNVAVVVVGFPATPLLLARARICISASHSREDLI 454
|
|
| PRK07179 |
PRK07179 |
quorum-sensing autoinducer synthase; |
159-510 |
5.92e-47 |
|
quorum-sensing autoinducer synthase;
Pssm-ID: 180866 [Multi-domain] Cd Length: 407 Bit Score: 169.03 E-value: 5.92e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83977440 159 SNDYLGMSRHPQVLQATQETLQRHGAG----AGGTRNISGTSKFhvelEQELAELHQKDSALLFSSCFVANDSTLFTLAK 234
Cdd:PRK07179 61 SNDYLNLSGHPDIIKAQIAALQEEGDSlvmsAVFLHDDSPKPQF----EKKLAAFTGFESCLLCQSGWAANVGLLQTIAD 136
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83977440 235 ilPGCEIYSDAGNHASMIQGIRNSGAAKFVFRHNDPDHLKKLLEKSNPKIpkiVAFETVHSMDGAICPLEELCDVSHQYG 314
Cdd:PRK07179 137 --PNTPVYIDFFAHMSLWEGVRAAGAQAHPFRHNDVDHLRRQIERHGPGI---IVVDSVYSTTGTIAPLADIVDIAEEFG 211
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83977440 315 ALTFVDEVHAVGLYGSRGAGIGERDGIMHKIDIISGTLGKAFGCVGGYIASTRDLVDMVR--SYAAgfIFTTSLPPMVLS 392
Cdd:PRK07179 212 CVLVVDESHSLGTHGPQGAGLVAELGLTSRVHFITASLAKAFAGRAGIITCPRELAEYVPfvSYPA--IFSSTLLPHEIA 289
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83977440 393 GALESVRLLKGEEGqalRRAH-QRNVKHMRQLLMDRGLPvIPCPSHIIPIRVGNAALNSKLCDLLLSKhGIYVQAINYPT 471
Cdd:PRK07179 290 GLEATLEVIESADD---RRARlHANARFLREGLSELGYN-IRSESQIIALETGSERNTEVLRDALEER-NVFGAVFCAPA 364
|
330 340 350
....*....|....*....|....*....|....*....
gi 83977440 472 VPRGEELLRLAPSPHHSPQMMEDFVEKLLLAWTAVGLPL 510
Cdd:PRK07179 365 TPKNRNLIRLSLNADLTASDLDRVLEVCREARDEVDLWF 403
|
|
| PLN03227 |
PLN03227 |
serine palmitoyltransferase-like protein; Provisional |
156-430 |
6.66e-38 |
|
serine palmitoyltransferase-like protein; Provisional
Pssm-ID: 178766 [Multi-domain] Cd Length: 392 Bit Score: 143.89 E-value: 6.66e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83977440 156 VWCSNDYLGMSRHPQVLQATQETLQRHGAGAGGTRNISGTSKFHVELEQELAELHQKDSALLFSSCFVANDSTLFTLAKi 235
Cdd:PLN03227 2 NFATHDFLSTSSSPTLRQTALESLSHYGCGSCGPRGFYGTIDAHLELEQCMAEFLGTESAILYSDGASTTSSTVAAFAK- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83977440 236 lPGCEIYSDAGNHASMIQGIRNSGAAKFVFRHNDPDHLKKLLEK----------SNPKIPKIVAFETVHSMDGAICPLEE 305
Cdd:PLN03227 81 -RGDLLVVDRGVNEALLVGVSLSRANVRWFRHNDMKDLRRVLEQvraqdvalkrKPTDQRRFLVVEGLYKNTGTLAPLKE 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83977440 306 LCDVSHQYGALTFVDEVHAVGLYGSRGAGIGERDGI--MHKIDIISGTLGKAFGCVGGYIASTRDLVDMVRSYAAGFIFT 383
Cdd:PLN03227 160 LVALKEEFHYRLILDESFSFGTLGKSGRGSLEHAGLkpMVHAEIVTFSLENAFGSVGGMTVGSEEVVDHQRLSGSGYCFS 239
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 83977440 384 TSLPPMVLSGALESVRLLKGEEgQALRRAHQrNVKHMRQLLMDRGLP 430
Cdd:PLN03227 240 ASAPPFLAKADATATAGELAGP-QLLNRLHD-SIANLYSTLTNSSHP 284
|
|
| PLN02822 |
PLN02822 |
serine palmitoyltransferase |
149-474 |
1.83e-36 |
|
serine palmitoyltransferase
Pssm-ID: 178417 [Multi-domain] Cd Length: 481 Bit Score: 141.80 E-value: 1.83e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83977440 149 VASKDVSVWCSNDYLGMSRHPQVLQATQETLQRHGAGAGGTRNISGTSKFHVELEQELAELHQKDSALLFSScfvandsT 228
Cdd:PLN02822 106 INGKDVVNFASANYLGLIGNEKIKESCTSALEKYGVGSCGPRGFYGTIDVHLDCETKIAKFLGTPDSILYSY-------G 178
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83977440 229 LFTLAKILPG-CE----IYSDAGNHASMIQGIRNSGAAKFVFRHNDPDHLKKLLE------KSNPKIPKIVAFETVHSMD 297
Cdd:PLN02822 179 LSTIFSVIPAfCKkgdiIVADEGVHWGIQNGLYLSRSTIVYFKHNDMESLRNTLEkltaenKRKKKLRRYIVVEAIYQNS 258
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83977440 298 GAICPLEELCDVSHQYGALTFVDEVHAVGLYGSRGAGIGERDGI-MHKIDIISGTLGKAFGCVGGYIASTRDLVDMVRSY 376
Cdd:PLN02822 259 GQIAPLDEIVRLKEKYRFRVLLDESNSFGVLGKSGRGLSEHFGVpIEKIDIITAAMGHALATEGGFCTGSARVVDHQRLS 338
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83977440 377 AAGFIFTTSLPPMVLSGALESVRLLKgEEGQALRRAHQrNVKHMRQLLMD-RGLPVIPCP-SHIIPIRV----GNAALNS 450
Cdd:PLN02822 339 SSGYVFSASLPPYLASAAITAIDVLE-DNPSVLAKLKE-NIALLHKGLSDiPGLSIGSNTlSPIVFLHLekstGSAKEDL 416
|
330 340
....*....|....*....|....*...
gi 83977440 451 KL----CDLLLSKHGIYVQAINYPTVPR 474
Cdd:PLN02822 417 SLlehiADRMLKEDSVLVVVSKRSTLDK 444
|
|
| PRK07505 |
PRK07505 |
hypothetical protein; Provisional |
158-499 |
3.80e-35 |
|
hypothetical protein; Provisional
Pssm-ID: 181006 [Multi-domain] Cd Length: 402 Bit Score: 136.26 E-value: 3.80e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83977440 158 CSNDYLGMSRHPQVLQATQETLQRHGagaggTRNISgTSKFHV------ELEQELAELHQKDsALLFSSCFVANDSTLFT 231
Cdd:PRK07505 52 VSCSYLGLDTHPAIIEGAVDALKRTG-----SLHLS-SSRTRVrsqilkDLEEALSELFGAS-VLTFTSCSAAHLGILPL 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83977440 232 LAK-ILPGCE---IYSDAGNHASM--IQGIrnsgAAKF--VFR--HNDPDHLKKLleKSNPKIPKIVAfETVHSMDGAIc 301
Cdd:PRK07505 125 LASgHLTGGVpphMVFDKNAHASLniLKGI----CADEteVETidHNDLDALEDI--CKTNKTVAYVA-DGVYSMGGIA- 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83977440 302 PLEELCDVSHQYGALTFVDEVHAVGLYGSRGAG--IGERDGIMHKIDIISGTLGKAFGCVGGYIA-STRDLVDMVRSYAA 378
Cdd:PRK07505 197 PVKELLRLQEKYGLFLYIDDAHGLSIYGKNGEGyvRSELDYRLNERTIIAASLGKAFGASGGVIMlGDAEQIELILRYAG 276
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83977440 379 GFIFTTSLPPMVLSGALESVRLLKGEEGQALRRAHQRNVKHMRQLLMD--RGLPVipcpshiiPIR---VGNAALNSKLC 453
Cdd:PRK07505 277 PLAFSQSLNVAALGAILASAEIHLSEELDQLQQKLQNNIALFDSLIPTeqSGSFL--------PIRliyIGDEDTAIKAA 348
|
330 340 350 360
....*....|....*....|....*....|....*....|....*.
gi 83977440 454 DLLLsKHGIYVQAINYPTVPRGEELLRLAPSPHHSPQMMEDFVEKL 499
Cdd:PRK07505 349 KQLL-DRGFYTSPVFFPVVAKGRAGLRIMFRASHTNDEIKRLCSLL 393
|
|
| PRK05937 |
PRK05937 |
8-amino-7-oxononanoate synthase; Provisional |
159-391 |
4.14e-27 |
|
8-amino-7-oxononanoate synthase; Provisional
Pssm-ID: 102071 [Multi-domain] Cd Length: 370 Bit Score: 112.95 E-value: 4.14e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83977440 159 SNDYLGMSRHPQVLQATQETLQRH-------GAGAGGTRNISGTSKFHVELEQELAELHQKDSALLFSSCFVANDSTLFT 231
Cdd:PRK05937 11 TNDFLGFSRSDTLVHEVEKRYRLYcrqfphaQLGYGGSRAILGPSSLLDDLEHKIAHFHGAPEAFIVPSGYMANLGLCAH 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83977440 232 LAKILPgcEIYSDAGNHASMIQGIRNSGAAKFVFRHNDPDHLKKLLE----KSNPKIPKIVAfeTVHSMDGAICPLEELC 307
Cdd:PRK05937 91 LSSVTD--YVLWDEQVHISVVYSLSVISGWHQSFRHNDLDHLESLLEscrqRSFGRIFIFVC--SVYSFKGTLAPLEQII 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83977440 308 DVSHQYGALTFVDEVHAVGLYGSRGAGIGERDGIMHKIDIISgTLGKAFGCVGGYIASTRDLVDMVRSYAAGFIFTTSLP 387
Cdd:PRK05937 167 ALSKKYHAHLIVDEAHAMGIFGDDGKGFCHSLGYENFYAVLV-TYSKALGSMGAALLSSSEVKQDLMLNSPPLRYSTGLP 245
|
....
gi 83977440 388 PMVL 391
Cdd:PRK05937 246 PHLL 249
|
|
| AAT_I |
cd01494 |
Aspartate aminotransferase (AAT) superfamily (fold type I) of pyridoxal phosphate (PLP) ... |
198-361 |
6.76e-17 |
|
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: 78.58 E-value: 6.76e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83977440 198 FHVELEQELAELHQK--DSALLFSSCFVANDSTLFTLAKilPGCEIYSDAGNHASMIQGIRNSGAAKFVFRHNDPD---- 271
Cdd:cd01494 1 KLEELEEKLARLLQPgnDKAVFVPSGTGANEAALLALLG--PGDEVIVDANGHGSRYWVAAELAGAKPVPVPVDDAgygg 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83977440 272 -HLKKLLEKSNPKIPKIVAFETVHSMDGAICPLEELCDVSHQYGALTFVDEVHAVGlyGSRGAGIGERDGimhKIDIISG 350
Cdd:cd01494 79 lDVAILEELKAKPNVALIVITPNTTSGGVLVPLKEIRKIAKEYGILLLVDAASAGG--ASPAPGVLIPEG---GADVVTF 153
|
170
....*....|.
gi 83977440 351 TLGKAFGCVGG 361
Cdd:cd01494 154 SLHKNLGGEGG 164
|
|
| Preseq_ALAS |
pfam09029 |
5-aminolevulinate synthase presequence; The N terminal presequence domain found in ... |
5-100 |
3.94e-14 |
|
5-aminolevulinate synthase presequence; The N terminal presequence domain found in 5-aminolevulinate synthase exists as an amphipathic helix, with a positively charged surface provided by lysine residues and no stable helix at the N-terminus. The domain is essential for the import process by which ALAS is transported into the mitochondria: translocase of the outer membrane (Tom) and translocase of the inner membrane protein complexes appear responsible for recognition and import through the mitochondrial membrane. The protein Tom20 is anchored to the mitochondrial outer membrane, and its interaction with presequences is thought to be the recognition step which allows subsequent import.
Pssm-ID: 462658 Cd Length: 114 Bit Score: 68.67 E-value: 3.94e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83977440 5 AMLLQCCPVLARGPTSLLGKVVKThqFLFGIGRCPILATQGPNCSQIHL----KATKAGGDSPSWAK----GH------- 69
Cdd:pfam09029 1 ASVLRRCPFLSRVPQAFLQKARKS--LLSYAQRCPVMMTRALSTSSANLqgekEETPVAGPTAKQAKalplGHpspqagq 78
|
90 100 110
....*....|....*....|....*....|....*.
gi 83977440 70 -----CPFMLSELQDGKSKIVQKAAPEVQEDVKAFK 100
Cdd:pfam09029 79 svaskCPFLAAEMGQKNSNVVRKASPEVQEDVQEVK 114
|
|
| Aminotran_5 |
pfam00266 |
Aminotransferase class-V; This domain is found in amino transferases, and other enzymes ... |
169-326 |
1.12e-07 |
|
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: 54.18 E-value: 1.12e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83977440 169 PQVLQATQETLqRHGAGAGGtrniSGTSKFHVELEQELAELHQKDSALLFSScfvANDSTLFT--------------LAK 234
Cdd:pfam00266 13 QEVLDAIQEYY-TDYNGNVH----RGVHTLGKEATQAYEEAREKVAEFINAP---SNDEIIFTsgtteainlvalslGRS 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83977440 235 ILPGCEI-YSDAGNHASMI--QGIRNSGAAKFVF------RHNDPDHLKKLLeksNPKiPKIVAFETVHSMDGAICPLEE 305
Cdd:pfam00266 85 LKPGDEIvITEMEHHANLVpwQELAKRTGARVRVlpldedGLLDLDELEKLI---TPK-TKLVAITHVSNVTGTIQPVPE 160
|
170 180
....*....|....*....|.
gi 83977440 306 LCDVSHQYGALTFVDEVHAVG 326
Cdd:pfam00266 161 IGKLAHQYGALVLVDAAQAIG 181
|
|
| CGS_like |
cd00614 |
CGS_like: Cystathionine gamma-synthase is a PLP dependent enzyme and catalyzes the committed ... |
199-320 |
2.46e-07 |
|
CGS_like: Cystathionine gamma-synthase is a PLP dependent enzyme and catalyzes the committed step of methionine biosynthesis. This pathway is unique to microorganisms and plants, rendering the enzyme an attractive target for the development of antimicrobials and herbicides. This subgroup also includes cystathionine gamma-lyases (CGL), O-acetylhomoserine sulfhydrylases and O-acetylhomoserine thiol lyases. CGL's are very similar to CGS's. Members of this group are widely distributed among all three forms of life.
Pssm-ID: 99738 [Multi-domain] Cd Length: 369 Bit Score: 52.97 E-value: 2.46e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83977440 199 HVELEQELAELHQKDSALLFSSCFVANDSTLFTLAK----ILPGCEIYSDAGNHASMIqgIRNSG-AAKFVfrhnDPDHL 273
Cdd:cd00614 42 VDALEKKLAALEGGEAALAFSSGMAAISTVLLALLKagdhVVASDDLYGGTYRLFERL--LPKLGiEVTFV----DPDDP 115
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 83977440 274 KKLLEKSNPKiPKIVAFETVHSMDGAICPLEELCDVSHQYGALTFVD 320
Cdd:cd00614 116 EALEAAIKPE-TKLVYVESPTNPTLKVVDIEAIAELAHEHGALLVVD 161
|
|
| CsdA |
COG0520 |
Selenocysteine lyase/Cysteine desulfurase [Amino acid transport and metabolism]; |
269-335 |
6.25e-07 |
|
Selenocysteine lyase/Cysteine desulfurase [Amino acid transport and metabolism];
Pssm-ID: 440286 [Multi-domain] Cd Length: 396 Bit Score: 51.68 E-value: 6.25e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83977440 269 DPDHLKKLLeksNPKiPKIVAFETVHSMDGAICPLEELCDVSHQYGALTFVDEVHAVG--------------------LY 328
Cdd:COG0520 143 DLEALEALL---TPR-TKLVAVTHVSNVTGTVNPVKEIAALAHAHGALVLVDGAQSVPhlpvdvqalgcdfyafsghkLY 218
|
....*..
gi 83977440 329 GSRGAGI 335
Cdd:COG0520 219 GPTGIGV 225
|
|
| AAT_like |
cd00609 |
Aspartate aminotransferase family. This family belongs to pyridoxal phosphate (PLP)-dependent ... |
169-464 |
2.06e-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: 2.06e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83977440 169 PQVLQATQETLQRHGAGAGGTrnisgtSKFHVELEQELAELHQKDSALLF--SSCFVANDST--LFTLAKIL--PGCEIY 242
Cdd:cd00609 14 PEVLEALAAAALRAGLLGYYP------DPGLPELREAIAEWLGRRGGVDVppEEIVVTNGAQeaLSLLLRALlnPGDEVL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83977440 243 SDAGNHASMIQGIRNSGAaKFVF-----RHNDPDHLKKLLEKSNPKiPKIVAFETVHSMDGAICP---LEELCDVSHQYG 314
Cdd:cd00609 88 VPDPTYPGYEAAARLAGA-EVVPvpldeEGGFLLDLELLEAAKTPK-TKLLYLNNPNNPTGAVLSeeeLEELAELAKKHG 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83977440 315 ALTFVDEVHAvGLYGSRGAGIGERDGIMHKIDIISGTLGKAFGCVG---GY-IASTRDLVDMVRSYAagfIFTTSLPPMV 390
Cdd:cd00609 166 ILIISDEAYA-ELVYDGEPPPALALLDAYERVIVLRSFSKTFGLPGlriGYlIAPPEELLERLKKLL---PYTTSGPSTL 241
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 83977440 391 LSGALESVRLLKGEEGQALRRAHQRNVKHMRQLLMDRGLPVIPCPS---HI-IPIRVGNAAlnsKLCDLLLSKHGIYV 464
Cdd:cd00609 242 SQAAAAAALDDGEEHLEELRERYRRRRDALLEALKELGPLVVVKPSggfFLwLDLPEGDDE---EFLERLLLEAGVVV 316
|
|
| SufS_like |
cd06453 |
Cysteine desulfurase (SufS)-like. This family belongs to the pyridoxal phosphate (PLP) ... |
269-326 |
7.90e-04 |
|
Cysteine desulfurase (SufS)-like. This family belongs to the pyridoxal phosphate (PLP)-dependent aspartate aminotransferase superfamily (fold I). The major groups in this CD correspond to cysteine desulfurase (SufS) and selenocysteine lyase. SufS catalyzes the removal of elemental sulfur and selenium atoms from L-cysteine, L-cystine, L-selenocysteine, and L-selenocystine to produce L-alanine; and selenocysteine lyase catalyzes the decomposition of L-selenocysteine.
Pssm-ID: 99746 [Multi-domain] Cd Length: 373 Bit Score: 42.07 E-value: 7.90e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 83977440 269 DPDHLKKLLeksNPKIpKIVAFETVHSMDGAICPLEELCDVSHQYGALTFVDEVHAVG 326
Cdd:cd06453 128 DLEALEKLL---TERT-KLVAVTHVSNVLGTINPVKEIGEIAHEAGVPVLVDGAQSAG 181
|
|
|