|
Name |
Accession |
Description |
Interval |
E-value |
| AAT_I super family |
cl18945 |
Aspartate aminotransferase (AAT) superfamily (fold type I) of pyridoxal phosphate (PLP) ... |
214-564 |
0e+00 |
|
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). The actual alignment was detected with superfamily member TIGR01821:
Pssm-ID: 450240 [Multi-domain] Cd Length: 402 Bit Score: 548.95 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767922627 214 FQYDRFFEKKIDEKKNDHTYRVFKTVNRRAHIFPMADDYSDSliTKKQVSVWCSNDYLGMSRHPRVCGAVMDTLKQHGAG 293
Cdd:TIGR01821 1 MDYDQFFNKEIDKLHLEGRYRVFADLERQAGEFPFAQWHRPD--GAKDVTVWCSNDYLGMGQHPEVLQAMHETLDKYGAG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767922627 294 AGGTRNISGTSKFHVDLERELADLHGKDAALLFSSCFVANDSTLFTLAKMMPGCEIYSDSGNHASMIQGIRNSRVPKYIF 373
Cdd:TIGR01821 79 AGGTRNISGTNIPHVELEAELADLHGKESALVFTSGYVANDATLATLAKIIPGCVIFSDELNHASMIEGIRHSGAEKFIF 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767922627 374 RHNDVSHLRELLQRSDPSVPKIVAFETVHSMDG----------------------------------------------- 406
Cdd:TIGR01821 159 RHNDVAHLEKLLQSVDPNRPKIIAFESVYSMDGdiapieeicdladkygaltyldevhavglygprgggiaerdglmhri 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767922627 407 --------KAFGCVGGYIASTSSLIDTVRSYAAGFIFTTSLPPMLLAGALESVRILKSAEgrVLRRQHQRNVKLMRQMLM 478
Cdd:TIGR01821 239 diiegtlaKAFGVVGGYIAASRKLIDAIRSYAPGFIFTTSLPPAIAAGATASIRHLKESQ--DLRRAHQENVKRLKNLLE 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767922627 479 DAGLPVVHCPSHIIPVRVADAAKNTEVCDELMSRHNIYVQAINYPTVPRGEELLRIAPTPHHTPQMMNYFLENLLVTWKQ 558
Cdd:TIGR01821 317 ALGIPVIPNPSHIVPVIIGDAALCKKVSDLLLNKHGIYVQPINYPTVPRGTERLRITPTPAHTDKMIDDLVEALLLVWDR 396
|
....*.
gi 767922627 559 VGLELK 564
Cdd:TIGR01821 397 LGLPLS 402
|
|
| Preseq_ALAS |
pfam09029 |
5-aminolevulinate synthase presequence; The N terminal presequence domain found in ... |
19-154 |
1.16e-54 |
|
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: 181.15 E-value: 1.16e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767922627 19 ESVVRRCPFLSRVPQAFLQKAGKSLLFYAQNCPKMMevgakpaPRALSTAAVHYQQIKE-TPPASEKDKTAKAkvqqtpd 97
Cdd:pfam09029 1 ASVLRRCPFLSRVPQAFLQKARKSLLSYAQRCPVMM-------TRALSTSSANLQGEKEeTPVAGPTAKQAKA------- 66
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 767922627 98 gsqqspdgtqLPSGHPLPATSQGTASKCPFLAAQMNQRGSSVFCKASLELQEDVQEM 154
Cdd:pfam09029 67 ----------LPLGHPSPQAGQSVASKCPFLAAEMGQKNSNVVRKASPEVQEDVQEV 113
|
|
|
|
Name |
Accession |
Description |
Interval |
E-value |
| 5aminolev_synth |
TIGR01821 |
5-aminolevulinic acid synthase; This model represents 5-aminolevulinic acid synthase, an ... |
214-564 |
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: 548.95 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767922627 214 FQYDRFFEKKIDEKKNDHTYRVFKTVNRRAHIFPMADDYSDSliTKKQVSVWCSNDYLGMSRHPRVCGAVMDTLKQHGAG 293
Cdd:TIGR01821 1 MDYDQFFNKEIDKLHLEGRYRVFADLERQAGEFPFAQWHRPD--GAKDVTVWCSNDYLGMGQHPEVLQAMHETLDKYGAG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767922627 294 AGGTRNISGTSKFHVDLERELADLHGKDAALLFSSCFVANDSTLFTLAKMMPGCEIYSDSGNHASMIQGIRNSRVPKYIF 373
Cdd:TIGR01821 79 AGGTRNISGTNIPHVELEAELADLHGKESALVFTSGYVANDATLATLAKIIPGCVIFSDELNHASMIEGIRHSGAEKFIF 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767922627 374 RHNDVSHLRELLQRSDPSVPKIVAFETVHSMDG----------------------------------------------- 406
Cdd:TIGR01821 159 RHNDVAHLEKLLQSVDPNRPKIIAFESVYSMDGdiapieeicdladkygaltyldevhavglygprgggiaerdglmhri 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767922627 407 --------KAFGCVGGYIASTSSLIDTVRSYAAGFIFTTSLPPMLLAGALESVRILKSAEgrVLRRQHQRNVKLMRQMLM 478
Cdd:TIGR01821 239 diiegtlaKAFGVVGGYIAASRKLIDAIRSYAPGFIFTTSLPPAIAAGATASIRHLKESQ--DLRRAHQENVKRLKNLLE 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767922627 479 DAGLPVVHCPSHIIPVRVADAAKNTEVCDELMSRHNIYVQAINYPTVPRGEELLRIAPTPHHTPQMMNYFLENLLVTWKQ 558
Cdd:TIGR01821 317 ALGIPVIPNPSHIVPVIIGDAALCKKVSDLLLNKHGIYVQPINYPTVPRGTERLRITPTPAHTDKMIDDLVEALLLVWDR 396
|
....*.
gi 767922627 559 VGLELK 564
Cdd:TIGR01821 397 LGLPLS 402
|
|
| PRK13392 |
PRK13392 |
5-aminolevulinate synthase; Provisional |
214-570 |
1.35e-140 |
|
5-aminolevulinate synthase; Provisional
Pssm-ID: 184023 [Multi-domain] Cd Length: 410 Bit Score: 414.25 E-value: 1.35e-140
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767922627 214 FQYDRFFEKKIDEKKNDHTYRVFKTVNRRAHIFPMADDYSDSliTKKQVSVWCSNDYLGMSRHPRVCGAVMDTLKQHGAG 293
Cdd:PRK13392 2 MNYDSYFDAALAQLHQEGRYRVFADLEREAGRFPRARDHGPD--GPRRVTIWCSNDYLGMGQHPDVIGAMVDALDRYGAG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767922627 294 AGGTRNISGTSKFHVDLERELADLHGKDAALLFSSCFVANDSTLFTLAKMMPGCEIYSDSGNHASMIQGIRNSRVPKYIF 373
Cdd:PRK13392 80 AGGTRNISGTSHPHVLLERELADLHGKESALLFTSGYVSNDAALSTLGKLLPGCVILSDALNHASMIEGIRRSGAEKQVF 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767922627 374 RHNDVSHLRELLQRSDPSVPKIVAFETVHSMDG----------------------------------------------- 406
Cdd:PRK13392 160 RHNDLADLEEQLASVDPDRPKLIAFESVYSMDGdiapieaicdladrynaltyvdevhavglygargggiaerdglmdri 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767922627 407 --------KAFGCVGGYIASTSSLIDTVRSYAAGFIFTTSLPPMLLAGALESVRILKSAEGRvlRRQHQRNVKLMRQMLM 478
Cdd:PRK13392 240 dmiqgtlaKAFGCLGGYIAASADLIDFVRSFAPGFIFTTALPPAVAAGATAAIRHLKTSQTE--RDAHQDRVAALKAKLN 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767922627 479 DAGLPVVHCPSHIIPVRVADAAKNTEVCDELMSRHNIYVQAINYPTVPRGEELLRIAPTPHHTPQMMNYFLENLLVTWKQ 558
Cdd:PRK13392 318 ANGIPVMPSPSHIVPVMVGDPTLCKAISDRLMSEHGIYIQPINYPTVPRGTERLRITPTPLHDDEDIDALVAALVAIWDR 397
|
410
....*....|..
gi 767922627 559 VGLELKPHSSAE 570
Cdd:PRK13392 398 LELPRWREAAQA 409
|
|
| KBL_like |
cd06454 |
KBL_like; this family belongs to the pyridoxal phosphate (PLP)-dependent aspartate ... |
260-560 |
5.66e-138 |
|
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: 405.41 E-value: 5.66e-138
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767922627 260 KQVSVWCSNDYLGMSRHPRVCGAVMDTLKQHGAGAGGTRNISGTSKFHVDLERELADLHGKDAALLFSSCFVANDSTLFT 339
Cdd:cd06454 1 KKVLNFCSNDYLGLANHPEVIEAAKEALDKYGVGAGGSRLISGTSDLHEELEEELAEFHGKEAALVFSSGYAANDGVLST 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767922627 340 LakMMPGCEIYSDSGNHASMIQGIRNSRVPKYIFRHNDVSHLRELLQRSD-PSVPKIVAFETVHSMDG------------ 406
Cdd:cd06454 81 L--AGKGDLIISDSLNHASIIDGIRLSGAKKRIFKHNDMEDLEKLLREARrPYGKKLIVTEGVYSMDGdiaplpelvdla 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767922627 407 -------------------------------------------KAFGCVGGYIASTSSLIDTVRSYAAGFIFTTSLPPML 443
Cdd:cd06454 159 kkygailfvdeahsvgvygphgrgveefggltddvdiimgtlgKAFGAVGGYIAGSKELIDYLRSYARGFIFSTSLPPAV 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767922627 444 LAGALESVRILKSAEGRvlRRQHQRNVKLMRQMLMDAGLPVVHCPSHIIPVRVAD-AAKNTEVCDELMSRhNIYVQAINY 522
Cdd:cd06454 239 AAAALAALEVLQGGPER--RERLQENVRYLRRGLKELGFPVGGSPSHIIPPLIGDdPAKAVAFSDALLER-GIYVQAIRY 315
|
330 340 350
....*....|....*....|....*....|....*...
gi 767922627 523 PTVPRGEELLRIAPTPHHTPQMMNYFLENLlvtwKQVG 560
Cdd:cd06454 316 PTVPRGTARLRISLSAAHTKEDIDRLLEAL----KEVG 349
|
|
| BioF |
COG0156 |
7-keto-8-aminopelargonate synthetase or related enzyme [Coenzyme transport and metabolism]; ... |
216-558 |
1.13e-125 |
|
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: 375.16 E-value: 1.13e-125
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767922627 216 YDRFFEKKIDEKKNDHTYRVFKTVNRRAHIFPMADDysdslitkKQVSVWCSNDYLGMSRHPRVCGAVMDTLKQHGAGAG 295
Cdd:COG0156 1 LLDRLEAELAALKAAGLYRYLRVLESPQGPRVTIDG--------REVLNFSSNDYLGLANHPRVIEAAAEALDRYGTGSG 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767922627 296 GTRNISGTSKFHVDLERELADLHGKDAALLFSSCFVANDSTLFTLAKmmPGCEIYSDSGNHASMIQGIRNSRVPKYIFRH 375
Cdd:COG0156 73 GSRLVSGTTPLHEELEEELAEFLGKEAALLFSSGYAANLGVISALAG--RGDLIFSDELNHASIIDGARLSGAKVVRFRH 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767922627 376 NDVSHLRELLQRSDPSVPKIVAFETVHSMDG------------------------------------------------- 406
Cdd:COG0156 151 NDMDDLERLLKKARAARRKLIVTDGVFSMDGdiaplpeivelaekygallyvddahgtgvlgetgrglvehfgledrvdi 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767922627 407 ------KAFGCVGGYIASTSSLIDTVRSYAAGFIFTTSLPPMLLAGALESVRILKSAEGRvlRRQHQRNVKLMRQMLMDA 480
Cdd:COG0156 231 imgtlsKALGSSGGFVAGSKELIDYLRNRARPFIFSTALPPAVAAAALAALEILREEPEL--RERLWENIAYFREGLKEL 308
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 767922627 481 GLPVVHCPSHIIPVRVADAAKNTEVCDELMSRhNIYVQAINYPTVPRGEELLRIAPTPHHTPQMMNYFLENLLVTWKQ 558
Cdd:COG0156 309 GFDLGPSESPIVPVIVGDAERALALADALLER-GIYVSAIRPPTVPKGTARLRITLSAAHTEEDIDRLLEALAEVGKE 385
|
|
| Preseq_ALAS |
pfam09029 |
5-aminolevulinate synthase presequence; The N terminal presequence domain found in ... |
19-154 |
1.16e-54 |
|
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: 181.15 E-value: 1.16e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767922627 19 ESVVRRCPFLSRVPQAFLQKAGKSLLFYAQNCPKMMevgakpaPRALSTAAVHYQQIKE-TPPASEKDKTAKAkvqqtpd 97
Cdd:pfam09029 1 ASVLRRCPFLSRVPQAFLQKARKSLLSYAQRCPVMM-------TRALSTSSANLQGEKEeTPVAGPTAKQAKA------- 66
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 767922627 98 gsqqspdgtqLPSGHPLPATSQGTASKCPFLAAQMNQRGSSVFCKASLELQEDVQEM 154
Cdd:pfam09029 67 ----------LPLGHPSPQAGQSVASKCPFLAAEMGQKNSNVVRKASPEVQEDVQEV 113
|
|
| Aminotran_1_2 |
pfam00155 |
Aminotransferase class I and II; |
265-550 |
6.75e-45 |
|
Aminotransferase class I and II;
Pssm-ID: 395103 [Multi-domain] Cd Length: 351 Bit Score: 162.86 E-value: 6.75e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767922627 265 WCSNDYLGMsrhprVCGAVMDTLKQhgAGAGGTRNISGTSKFHVDLERELADLHG--------KDAALLFSSCFVANDST 336
Cdd:pfam00155 6 LGSNEYLGD-----TLPAVAKAEKD--ALAGGTRNLYGPTDGHPELREALAKFLGrspvlkldREAAVVFGSGAGANIEA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767922627 337 LFTLAKMmPGCEIYSDSGNHASMIQGIRNSRVPKYIFR-------HNDVSHLRELLQRSdpsvPKIVAFETVHSMDG--- 406
Cdd:pfam00155 79 LIFLLAN-PGDAILVPAPTYASYIRIARLAGGEVVRYPlydsndfHLDFDALEAALKEK----PKVVLHTSPHNPTGtva 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767922627 407 -------------------------------------------------------KAFGCVG---GYIASTSSLIDTVRS 428
Cdd:pfam00155 154 tleeleklldlakehnilllvdeayagfvfgspdavatrallaegpnllvvgsfsKAFGLAGwrvGYILGNAAVISQLRK 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767922627 429 YAAGFIFTTSLPPMLLAGALESvrILKSAEGRVLRRQHQRNVKLMRQMLMDAGLPVVHCPSHIIPVRVADAAKNTEVCDE 508
Cdd:pfam00155 234 LARPFYSSTHLQAAAAAALSDP--LLVASELEEMRQRIKERRDYLRDGLQAAGLSVLPSQAGFFLLTGLDPETAKELAQV 311
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 767922627 509 LMSRHNIYVQAINYPTVPrgeELLRIAPTpHHTPQMMNYFLE 550
Cdd:pfam00155 312 LLEEVGVYVTPGSSPGVP---GWLRITVA-GGTEEELEELLE 349
|
|
|
|
Name |
Accession |
Description |
Interval |
E-value |
| 5aminolev_synth |
TIGR01821 |
5-aminolevulinic acid synthase; This model represents 5-aminolevulinic acid synthase, an ... |
214-564 |
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: 548.95 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767922627 214 FQYDRFFEKKIDEKKNDHTYRVFKTVNRRAHIFPMADDYSDSliTKKQVSVWCSNDYLGMSRHPRVCGAVMDTLKQHGAG 293
Cdd:TIGR01821 1 MDYDQFFNKEIDKLHLEGRYRVFADLERQAGEFPFAQWHRPD--GAKDVTVWCSNDYLGMGQHPEVLQAMHETLDKYGAG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767922627 294 AGGTRNISGTSKFHVDLERELADLHGKDAALLFSSCFVANDSTLFTLAKMMPGCEIYSDSGNHASMIQGIRNSRVPKYIF 373
Cdd:TIGR01821 79 AGGTRNISGTNIPHVELEAELADLHGKESALVFTSGYVANDATLATLAKIIPGCVIFSDELNHASMIEGIRHSGAEKFIF 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767922627 374 RHNDVSHLRELLQRSDPSVPKIVAFETVHSMDG----------------------------------------------- 406
Cdd:TIGR01821 159 RHNDVAHLEKLLQSVDPNRPKIIAFESVYSMDGdiapieeicdladkygaltyldevhavglygprgggiaerdglmhri 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767922627 407 --------KAFGCVGGYIASTSSLIDTVRSYAAGFIFTTSLPPMLLAGALESVRILKSAEgrVLRRQHQRNVKLMRQMLM 478
Cdd:TIGR01821 239 diiegtlaKAFGVVGGYIAASRKLIDAIRSYAPGFIFTTSLPPAIAAGATASIRHLKESQ--DLRRAHQENVKRLKNLLE 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767922627 479 DAGLPVVHCPSHIIPVRVADAAKNTEVCDELMSRHNIYVQAINYPTVPRGEELLRIAPTPHHTPQMMNYFLENLLVTWKQ 558
Cdd:TIGR01821 317 ALGIPVIPNPSHIVPVIIGDAALCKKVSDLLLNKHGIYVQPINYPTVPRGTERLRITPTPAHTDKMIDDLVEALLLVWDR 396
|
....*.
gi 767922627 559 VGLELK 564
Cdd:TIGR01821 397 LGLPLS 402
|
|
| PRK13392 |
PRK13392 |
5-aminolevulinate synthase; Provisional |
214-570 |
1.35e-140 |
|
5-aminolevulinate synthase; Provisional
Pssm-ID: 184023 [Multi-domain] Cd Length: 410 Bit Score: 414.25 E-value: 1.35e-140
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767922627 214 FQYDRFFEKKIDEKKNDHTYRVFKTVNRRAHIFPMADDYSDSliTKKQVSVWCSNDYLGMSRHPRVCGAVMDTLKQHGAG 293
Cdd:PRK13392 2 MNYDSYFDAALAQLHQEGRYRVFADLEREAGRFPRARDHGPD--GPRRVTIWCSNDYLGMGQHPDVIGAMVDALDRYGAG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767922627 294 AGGTRNISGTSKFHVDLERELADLHGKDAALLFSSCFVANDSTLFTLAKMMPGCEIYSDSGNHASMIQGIRNSRVPKYIF 373
Cdd:PRK13392 80 AGGTRNISGTSHPHVLLERELADLHGKESALLFTSGYVSNDAALSTLGKLLPGCVILSDALNHASMIEGIRRSGAEKQVF 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767922627 374 RHNDVSHLRELLQRSDPSVPKIVAFETVHSMDG----------------------------------------------- 406
Cdd:PRK13392 160 RHNDLADLEEQLASVDPDRPKLIAFESVYSMDGdiapieaicdladrynaltyvdevhavglygargggiaerdglmdri 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767922627 407 --------KAFGCVGGYIASTSSLIDTVRSYAAGFIFTTSLPPMLLAGALESVRILKSAEGRvlRRQHQRNVKLMRQMLM 478
Cdd:PRK13392 240 dmiqgtlaKAFGCLGGYIAASADLIDFVRSFAPGFIFTTALPPAVAAGATAAIRHLKTSQTE--RDAHQDRVAALKAKLN 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767922627 479 DAGLPVVHCPSHIIPVRVADAAKNTEVCDELMSRHNIYVQAINYPTVPRGEELLRIAPTPHHTPQMMNYFLENLLVTWKQ 558
Cdd:PRK13392 318 ANGIPVMPSPSHIVPVMVGDPTLCKAISDRLMSEHGIYIQPINYPTVPRGTERLRITPTPLHDDEDIDALVAALVAIWDR 397
|
410
....*....|..
gi 767922627 559 VGLELKPHSSAE 570
Cdd:PRK13392 398 LELPRWREAAQA 409
|
|
| KBL_like |
cd06454 |
KBL_like; this family belongs to the pyridoxal phosphate (PLP)-dependent aspartate ... |
260-560 |
5.66e-138 |
|
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: 405.41 E-value: 5.66e-138
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767922627 260 KQVSVWCSNDYLGMSRHPRVCGAVMDTLKQHGAGAGGTRNISGTSKFHVDLERELADLHGKDAALLFSSCFVANDSTLFT 339
Cdd:cd06454 1 KKVLNFCSNDYLGLANHPEVIEAAKEALDKYGVGAGGSRLISGTSDLHEELEEELAEFHGKEAALVFSSGYAANDGVLST 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767922627 340 LakMMPGCEIYSDSGNHASMIQGIRNSRVPKYIFRHNDVSHLRELLQRSD-PSVPKIVAFETVHSMDG------------ 406
Cdd:cd06454 81 L--AGKGDLIISDSLNHASIIDGIRLSGAKKRIFKHNDMEDLEKLLREARrPYGKKLIVTEGVYSMDGdiaplpelvdla 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767922627 407 -------------------------------------------KAFGCVGGYIASTSSLIDTVRSYAAGFIFTTSLPPML 443
Cdd:cd06454 159 kkygailfvdeahsvgvygphgrgveefggltddvdiimgtlgKAFGAVGGYIAGSKELIDYLRSYARGFIFSTSLPPAV 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767922627 444 LAGALESVRILKSAEGRvlRRQHQRNVKLMRQMLMDAGLPVVHCPSHIIPVRVAD-AAKNTEVCDELMSRhNIYVQAINY 522
Cdd:cd06454 239 AAAALAALEVLQGGPER--RERLQENVRYLRRGLKELGFPVGGSPSHIIPPLIGDdPAKAVAFSDALLER-GIYVQAIRY 315
|
330 340 350
....*....|....*....|....*....|....*...
gi 767922627 523 PTVPRGEELLRIAPTPHHTPQMMNYFLENLlvtwKQVG 560
Cdd:cd06454 316 PTVPRGTARLRISLSAAHTKEDIDRLLEAL----KEVG 349
|
|
| BioF |
COG0156 |
7-keto-8-aminopelargonate synthetase or related enzyme [Coenzyme transport and metabolism]; ... |
216-558 |
1.13e-125 |
|
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: 375.16 E-value: 1.13e-125
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767922627 216 YDRFFEKKIDEKKNDHTYRVFKTVNRRAHIFPMADDysdslitkKQVSVWCSNDYLGMSRHPRVCGAVMDTLKQHGAGAG 295
Cdd:COG0156 1 LLDRLEAELAALKAAGLYRYLRVLESPQGPRVTIDG--------REVLNFSSNDYLGLANHPRVIEAAAEALDRYGTGSG 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767922627 296 GTRNISGTSKFHVDLERELADLHGKDAALLFSSCFVANDSTLFTLAKmmPGCEIYSDSGNHASMIQGIRNSRVPKYIFRH 375
Cdd:COG0156 73 GSRLVSGTTPLHEELEEELAEFLGKEAALLFSSGYAANLGVISALAG--RGDLIFSDELNHASIIDGARLSGAKVVRFRH 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767922627 376 NDVSHLRELLQRSDPSVPKIVAFETVHSMDG------------------------------------------------- 406
Cdd:COG0156 151 NDMDDLERLLKKARAARRKLIVTDGVFSMDGdiaplpeivelaekygallyvddahgtgvlgetgrglvehfgledrvdi 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767922627 407 ------KAFGCVGGYIASTSSLIDTVRSYAAGFIFTTSLPPMLLAGALESVRILKSAEGRvlRRQHQRNVKLMRQMLMDA 480
Cdd:COG0156 231 imgtlsKALGSSGGFVAGSKELIDYLRNRARPFIFSTALPPAVAAAALAALEILREEPEL--RERLWENIAYFREGLKEL 308
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 767922627 481 GLPVVHCPSHIIPVRVADAAKNTEVCDELMSRhNIYVQAINYPTVPRGEELLRIAPTPHHTPQMMNYFLENLLVTWKQ 558
Cdd:COG0156 309 GFDLGPSESPIVPVIVGDAERALALADALLER-GIYVSAIRPPTVPKGTARLRITLSAAHTEEDIDRLLEALAEVGKE 385
|
|
| PRK05958 |
PRK05958 |
8-amino-7-oxononanoate synthase; Reviewed |
220-552 |
3.62e-73 |
|
8-amino-7-oxononanoate synthase; Reviewed
Pssm-ID: 235655 [Multi-domain] Cd Length: 385 Bit Score: 239.29 E-value: 3.62e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767922627 220 FEKKIDEKKNDHTYRVFKTVNRRAHIFPMADDysdslitkKQVSVWCSNDYLGMSRHPRVCGAVMDTLKQHGAGAGGTRN 299
Cdd:PRK05958 7 LEAALAQRRAAGLYRSLRPREGGAGRWLVVDG--------RRMLNFASNDYLGLARHPRLIAAAQQAARRYGAGSGGSRL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767922627 300 ISGTSKFHVDLERELADLHGKDAALLFSSCFVANDSTLFTLakMMPGCEIYSDSGNHASMIQGIRNSRVPKYIFRHNDVS 379
Cdd:PRK05958 79 VTGNSPAHEALEEELAEWFGAERALLFSSGYAANLAVLTAL--AGKGDLIVSDKLNHASLIDGARLSRARVRRYPHNDVD 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767922627 380 HLRELLQRSDPSvPKIVAFETVHSMDG----------------------------------------------------- 406
Cdd:PRK05958 157 ALEALLAKWRAG-RALIVTESVFSMDGdlaplaelvalarrhgawllvdeahgtgvlgpqgrglaaeaglagepdvilvg 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767922627 407 ---KAFGCVGGYIASTSSLIDTVRSYAAGFIFTTSLPPMLLAGALESVRILKSAEGrvlRRQH-QRNVKLMRQMLMDAGL 482
Cdd:PRK05958 236 tlgKALGSSGAAVLGSETLIDYLINRARPFIFTTALPPAQAAAARAALRILRREPE---RRERlAALIARLRAGLRALGF 312
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767922627 483 PVVHCPSHIIPVRVADAAKNTEVCDELmSRHNIYVQAINYPTVPRGEELLRIAPTPHHTPQMMNYFLENL 552
Cdd:PRK05958 313 QLMDSQSAIQPLIVGDNERALALAAAL-QEQGFWVGAIRPPTVPAGTSRLRITLTAAHTEADIDRLLEAL 381
|
|
| bioF |
TIGR00858 |
8-amino-7-oxononanoate synthase; 7-keto-8-aminopelargonic acid synthetase is an alternate name. ... |
260-552 |
1.91e-71 |
|
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: 234.08 E-value: 1.91e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767922627 260 KQVSVWCSNDYLGMSRHPRVCGAVMDTLKQHGAGAGGTRNISGTSKFHVDLERELADLHGKDAALLFSSCFVANDSTLFT 339
Cdd:TIGR00858 16 RRLLNFSSNDYLGLASHPEVIQAAQQGAEQYGAGSTASRLVSGNSPLHEELEEELAEWKGTEAALLFSSGYLANVGVISA 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767922627 340 LAKmmPGCEIYSDSGNHASMIQGIRNSRVPKYIFRHNDVSHLRELLQRSDPSVPKIVAFETVHSMDG------------- 406
Cdd:TIGR00858 96 LVG--KGDLILSDALNHASLIDGCRLSGARVRRYRHNDVEHLERLLEKNRGERRKLIVTDGVFSMDGdiaplpqlvalae 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767922627 407 -------------------------------------------KAFGCVGGYIASTSSLIDTVRSYAAGFIFTTSLPPML 443
Cdd:TIGR00858 174 rygawlmvddahgtgvlgedgrgtlehfglkpepvdiqvgtlsKALGSYGAYVAGSQALIDYLINRARTLIFSTALPPAV 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767922627 444 LAGALESVRILksAEGRVLRRQHQRNVKLMRQMLMDAGLPVVHCPSHIIPVRVADAAKNTEVCDELMSRhNIYVQAINYP 523
Cdd:TIGR00858 254 AAAALAALELI--QEEPWRREKLLALIARLRAGLEALGFTLMPSCTPIVPVIIGDNASALALAEELQQQ-GIFVGAIRPP 330
|
330 340
....*....|....*....|....*....
gi 767922627 524 TVPRGEELLRIAPTPHHTPQMMNYFLENL 552
Cdd:TIGR00858 331 TVPAGTSRLRLTLSAAHTPGDIDRLAEAL 359
|
|
| PRK06939 |
PRK06939 |
2-amino-3-ketobutyrate coenzyme A ligase; Provisional |
219-564 |
8.00e-58 |
|
2-amino-3-ketobutyrate coenzyme A ligase; Provisional
Pssm-ID: 235893 [Multi-domain] Cd Length: 397 Bit Score: 199.27 E-value: 8.00e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767922627 219 FFEKKIDEKKNDHTY---RVFKTVNRrAHIfpmaddysdSLITKKQVSVWCSNDYLGMSRHPRVCGAVMDTLKQHGAGAG 295
Cdd:PRK06939 8 QLREELEEIKAEGLYkeeRVITSPQG-ADI---------TVADGKEVINFCANNYLGLANHPELIAAAKAALDSHGFGMA 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767922627 296 GTRNISGTSKFHVDLERELADLHGKDAALLFSSCFVANDSTLFTLakMMPGCEIYSDSGNHASMIQGIRNSRVPKYIFRH 375
Cdd:PRK06939 78 SVRFICGTQDLHKELEEKLAKFLGTEDAILYSSCFDANGGLFETL--LGKEDAIISDALNHASIIDGVRLCKAKRYRYAN 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767922627 376 NDVSHLRELLQRSDPSVP--KIVAFETVHSMDG----------------------------------------------- 406
Cdd:PRK06939 156 NDMADLEAQLKEAKEAGArhKLIATDGVFSMDGdiaplpeicdladkydalvmvddshavgfvgengrgtvehfgvmdrv 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767922627 407 --------KAF-GCVGGYIASTSSLIDTVRSYAAGFIFTTSLPPMLLAGALESVRILKsaEGRVLRRQHQRNVKLMRQML 477
Cdd:PRK06939 236 diitgtlgKALgGASGGYTAGRKEVIDWLRQRSRPYLFSNSLAPAIVAASIKVLELLE--ESDELRDRLWENARYFREGM 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767922627 478 MDAGLPVVHCPSHIIPVRVADAAKNTEVCDELMSRhNIYVQAINYPTVPRGEELLRIAPTPHHTPQMMNYFLEnllvTWK 557
Cdd:PRK06939 314 TAAGFTLGPGEHPIIPVMLGDAKLAQEFADRLLEE-GVYVIGFSFPVVPKGQARIRTQMSAAHTKEQLDRAID----AFE 388
|
....*..
gi 767922627 558 QVGLELK 564
Cdd:PRK06939 389 KVGKELG 395
|
|
| Preseq_ALAS |
pfam09029 |
5-aminolevulinate synthase presequence; The N terminal presequence domain found in ... |
19-154 |
1.16e-54 |
|
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: 181.15 E-value: 1.16e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767922627 19 ESVVRRCPFLSRVPQAFLQKAGKSLLFYAQNCPKMMevgakpaPRALSTAAVHYQQIKE-TPPASEKDKTAKAkvqqtpd 97
Cdd:pfam09029 1 ASVLRRCPFLSRVPQAFLQKARKSLLSYAQRCPVMM-------TRALSTSSANLQGEKEeTPVAGPTAKQAKA------- 66
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 767922627 98 gsqqspdgtqLPSGHPLPATSQGTASKCPFLAAQMNQRGSSVFCKASLELQEDVQEM 154
Cdd:pfam09029 67 ----------LPLGHPSPQAGQSVASKCPFLAAEMGQKNSNVVRKASPEVQEDVQEV 113
|
|
| Aminotran_1_2 |
pfam00155 |
Aminotransferase class I and II; |
265-550 |
6.75e-45 |
|
Aminotransferase class I and II;
Pssm-ID: 395103 [Multi-domain] Cd Length: 351 Bit Score: 162.86 E-value: 6.75e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767922627 265 WCSNDYLGMsrhprVCGAVMDTLKQhgAGAGGTRNISGTSKFHVDLERELADLHG--------KDAALLFSSCFVANDST 336
Cdd:pfam00155 6 LGSNEYLGD-----TLPAVAKAEKD--ALAGGTRNLYGPTDGHPELREALAKFLGrspvlkldREAAVVFGSGAGANIEA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767922627 337 LFTLAKMmPGCEIYSDSGNHASMIQGIRNSRVPKYIFR-------HNDVSHLRELLQRSdpsvPKIVAFETVHSMDG--- 406
Cdd:pfam00155 79 LIFLLAN-PGDAILVPAPTYASYIRIARLAGGEVVRYPlydsndfHLDFDALEAALKEK----PKVVLHTSPHNPTGtva 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767922627 407 -------------------------------------------------------KAFGCVG---GYIASTSSLIDTVRS 428
Cdd:pfam00155 154 tleeleklldlakehnilllvdeayagfvfgspdavatrallaegpnllvvgsfsKAFGLAGwrvGYILGNAAVISQLRK 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767922627 429 YAAGFIFTTSLPPMLLAGALESvrILKSAEGRVLRRQHQRNVKLMRQMLMDAGLPVVHCPSHIIPVRVADAAKNTEVCDE 508
Cdd:pfam00155 234 LARPFYSSTHLQAAAAAALSDP--LLVASELEEMRQRIKERRDYLRDGLQAAGLSVLPSQAGFFLLTGLDPETAKELAQV 311
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 767922627 509 LMSRHNIYVQAINYPTVPrgeELLRIAPTpHHTPQMMNYFLE 550
Cdd:pfam00155 312 LLEEVGVYVTPGSSPGVP---GWLRITVA-GGTEEELEELLE 349
|
|
| PLN02955 |
PLN02955 |
8-amino-7-oxononanoate synthase |
260-543 |
7.91e-29 |
|
8-amino-7-oxononanoate synthase
Pssm-ID: 178541 [Multi-domain] Cd Length: 476 Bit Score: 120.16 E-value: 7.91e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767922627 260 KQVSVWCSNDYLGMSRHPRVCGAVMDTLKQHGAGAGGTRNISGTSKFHVDLERELADLHGKDAALLFSSCFVANDSTLFT 339
Cdd:PLN02955 102 KKLLLFSGNDYLGLSSHPTISNAAANAAKEYGMGPKGSALICGYTTYHRLLESSLADLKKKEDCLVCPTGFAANMAAMVA 181
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767922627 340 L--------AKMMP----GCEIYSDSGNHASMIQGI----RNSRVPKYIFRHNDVSHLRELLQRSDPSvPKIVAFETVHS 403
Cdd:PLN02955 182 IgsvasllaASGKPlkneKVAIFSDALNHASIIDGVrlaeRQGNVEVFVYRHCDMYHLNSLLSSCKMK-RKVVVTDSLFS 260
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767922627 404 MDG-------------------------------------------------------KAFGCVGGYIASTSSLIDTVRS 428
Cdd:PLN02955 261 MDGdfapmeelsqlrkkygfllviddahgtfvcgengggvaeefnceadvdlcvgtlsKAAGCHGGFIACSKKWKQLIQS 340
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767922627 429 YAAGFIFTTSLPPMLLAGALESVRILKSAEGRvlRRQHQRNVKLMRQMlmdAGLPVvhcPSHIIPVRVADAAKNTEVCDE 508
Cdd:PLN02955 341 RGRSFIFSTAIPVPMAAAAYAAVVVARKEKWR--RKAIWERVKEFKAL---SGVDI---SSPIISLVVGNQEKALKASRY 412
|
330 340 350
....*....|....*....|....*....|....*
gi 767922627 509 LMsRHNIYVQAINYPTVPRGEELLRIAPTPHHTPQ 543
Cdd:PLN02955 413 LL-KSGFHVMAIRPPTVPPNSCRLRVTLSAAHTTE 446
|
|
| PLN02483 |
PLN02483 |
serine palmitoyltransferase |
267-570 |
3.18e-28 |
|
serine palmitoyltransferase
Pssm-ID: 178101 [Multi-domain] Cd Length: 489 Bit Score: 118.33 E-value: 3.18e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767922627 267 SNDYLGMSRHPRVCGA-VMDTLKQHGAGAGGTRNISGTSKFHVDLERELADLHGKDAALLFSSCFVANDSTLFTLakMMP 345
Cdd:PLN02483 107 SYNYLGFAAADEYCTPrVIESLKKYSASTCSSRVDGGTTKLHRELEELVARFVGKPAAIVFGMGYATNSTIIPAL--IGK 184
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767922627 346 GCEIYSDSGNHASMIQGIRNSRVPKYIFRHNDVSHLRELLQ--------RSDPSVPKI-VAFETVHSMDG---------- 406
Cdd:PLN02483 185 GGLIISDSLNHNSIVNGARGSGATIRVFQHNTPSHLEEVLReqiaegqpRTHRPWKKIiVIVEGIYSMEGelcklpeiva 264
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767922627 407 ----------------------------------------------KAFGCVGGYIASTSSLIDTVRSYAAGFIFTTSLP 440
Cdd:PLN02483 265 vckkykayvyldeahsigavgktgrgvcellgvdpadvdimmgtftKSFGSCGGYIAGSKELIQYLKRTCPAHLYATSMS 344
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767922627 441 PMLLAGALESVRILKSAEG-----RVLRRQHQrNVKLMRQMLMDAGLPVV-HCPSHIIPVRVADAAKNTEVCDELMSRhN 514
Cdd:PLN02483 345 PPAVQQVISAIKVILGEDGtnrgaQKLAQIRE-NSNFFRSELQKMGFEVLgDNDSPVMPIMLYNPAKIPAFSRECLKQ-N 422
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*.
gi 767922627 515 IYVQAINYPTVPRGEELLRIAPTPHHTPQMMNYFLENLLVTWKQVGLELKPHSSAE 570
Cdd:PLN02483 423 VAVVVVGFPATPLLLARARICISASHSREDLIKALEVISEVGDLVGIKYFPAEPKK 478
|
|
| PRK07179 |
PRK07179 |
quorum-sensing autoinducer synthase; |
267-550 |
9.65e-27 |
|
quorum-sensing autoinducer synthase;
Pssm-ID: 180866 [Multi-domain] Cd Length: 407 Bit Score: 112.80 E-value: 9.65e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767922627 267 SNDYLGMSRHPRVCGAVMDTLKQHGagaggtRNISGTSKFHVD------LERELADLHGKDAALLFSSCFVANDSTLFTL 340
Cdd:PRK07179 61 SNDYLNLSGHPDIIKAQIAALQEEG------DSLVMSAVFLHDdspkpqFEKKLAAFTGFESCLLCQSGWAANVGLLQTI 134
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767922627 341 AKmmPGCEIYSDSGNHASMIQGIRNSRVPKYIFRHNDVSHLRELLQRSDPSvpkIVAFETVHSMDG------------KA 408
Cdd:PRK07179 135 AD--PNTPVYIDFFAHMSLWEGVRAAGAQAHPFRHNDVDHLRRQIERHGPG---IIVVDSVYSTTGtiapladivdiaEE 209
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767922627 409 FGCV-------------------------------------------GGYIASTSSLIDTVR--SYAAgfIFTTSLPPML 443
Cdd:PRK07179 210 FGCVlvvdeshslgthgpqgaglvaelgltsrvhfitaslakafagrAGIITCPRELAEYVPfvSYPA--IFSSTLLPHE 287
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767922627 444 LAGALESVRILKSAEGRvlRRQHQRNVKLMRQMLMDAGLPvVHCPSHIIPVrVADAAKNTEVC-DELMSRhNIYVQAINY 522
Cdd:PRK07179 288 IAGLEATLEVIESADDR--RARLHANARFLREGLSELGYN-IRSESQIIAL-ETGSERNTEVLrDALEER-NVFGAVFCA 362
|
330 340
....*....|....*....|....*...
gi 767922627 523 PTVPRGEELLRIAPTPHHTPQMMNYFLE 550
Cdd:PRK07179 363 PATPKNRNLIRLSLNADLTASDLDRVLE 390
|
|
| PLN03227 |
PLN03227 |
serine palmitoyltransferase-like protein; Provisional |
264-515 |
1.19e-17 |
|
serine palmitoyltransferase-like protein; Provisional
Pssm-ID: 178766 [Multi-domain] Cd Length: 392 Bit Score: 85.34 E-value: 1.19e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767922627 264 VWCSNDYLGMSRHPRVCGAVMDTLKQHGAGAGGTRNISGTSKFHVDLERELADLHGKDAALLFSSCFVANDSTLFTLAKM 343
Cdd:PLN03227 2 NFATHDFLSTSSSPTLRQTALESLSHYGCGSCGPRGFYGTIDAHLELEQCMAEFLGTESAILYSDGASTTSSTVAAFAKR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767922627 344 mpGCEIYSDSGNHASMIQGIRNSRVPKYIFRHNDVSHLRELLQR---SDPS------------------------VP--K 394
Cdd:PLN03227 82 --GDLLVVDRGVNEALLVGVSLSRANVRWFRHNDMKDLRRVLEQvraQDVAlkrkptdqrrflvveglykntgtlAPlkE 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767922627 395 IVAFETVHS----MD--------GK--------------------------AFGCVGGYIASTSSLIDTVRSYAAGFIFT 436
Cdd:PLN03227 160 LVALKEEFHyrliLDesfsfgtlGKsgrgslehaglkpmvhaeivtfslenAFGSVGGMTVGSEEVVDHQRLSGSGYCFS 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767922627 437 TSLPPMLLAGALESVRILKsAEGRVLRRQHQrNVKLMRQMLMDAGLPVVHCP-----------SHIIPVRVADAAKnTEV 505
Cdd:PLN03227 240 ASAPPFLAKADATATAGEL-AGPQLLNRLHD-SIANLYSTLTNSSHPYALKLrnrlvitsdpiSPIIYLRLSDQEA-TRR 316
|
330
....*....|
gi 767922627 506 CDELMSRHNI 515
Cdd:PLN03227 317 TDETLILDQI 326
|
|
| PLN02822 |
PLN02822 |
serine palmitoyltransferase |
257-479 |
1.01e-13 |
|
serine palmitoyltransferase
Pssm-ID: 178417 [Multi-domain] Cd Length: 481 Bit Score: 73.62 E-value: 1.01e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767922627 257 ITKKQVSVWCSNDYLGMSRHPRVCGAVMDTLKQHGAGAGGTRNISGTSKFHVDLERELADLHGKDAALLFSSCFVANDST 336
Cdd:PLN02822 106 INGKDVVNFASANYLGLIGNEKIKESCTSALEKYGVGSCGPRGFYGTIDVHLDCETKIAKFLGTPDSILYSYGLSTIFSV 185
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767922627 337 LFTLAKMmpGCEIYSDSGNHASMIQGIRNSRVPKYIFRHNDVSHLRELL-----------------------QRSDPSVP 393
Cdd:PLN02822 186 IPAFCKK--GDIIVADEGVHWGIQNGLYLSRSTIVYFKHNDMESLRNTLekltaenkrkkklrryivveaiyQNSGQIAP 263
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767922627 394 ---------------------------------------KIVAFETVHSMDGKAFGCVGGYIASTSSLIDTVRSYAAGFI 434
Cdd:PLN02822 264 ldeivrlkekyrfrvlldesnsfgvlgksgrglsehfgvPIEKIDIITAAMGHALATEGGFCTGSARVVDHQRLSSSGYV 343
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 767922627 435 FTTSLPPMLLAGALESVRILKSaEGRVLRRQHQrNVKLMRQMLMD 479
Cdd:PLN02822 344 FSASLPPYLASAAITAIDVLED-NPSVLAKLKE-NIALLHKGLSD 386
|
|
| PRK07505 |
PRK07505 |
hypothetical protein; Provisional |
266-543 |
1.71e-12 |
|
hypothetical protein; Provisional
Pssm-ID: 181006 [Multi-domain] Cd Length: 402 Bit Score: 69.62 E-value: 1.71e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767922627 266 CSNDYLGMSRHPRVCGAVMDTLKqhgagAGGTRNISgTSKFHV------DLERELADLHGKDAaLLFSSCFVANDSTLFT 339
Cdd:PRK07505 52 VSCSYLGLDTHPAIIEGAVDALK-----RTGSLHLS-SSRTRVrsqilkDLEEALSELFGASV-LTFTSCSAAHLGILPL 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767922627 340 LAK--MMPGCEIYS--DSGNHASM--IQGIRNSRVPKYIFRHNDVSHLRELLQRSdpsvpKIVAF--ETVHSMDG----- 406
Cdd:PRK07505 125 LASghLTGGVPPHMvfDKNAHASLniLKGICADETEVETIDHNDLDALEDICKTN-----KTVAYvaDGVYSMGGiapvk 199
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767922627 407 ---------------------------------------------------KAFGCVGGYIA-STSSLIDTVRSYAAGFI 434
Cdd:PRK07505 200 ellrlqekyglflyiddahglsiygkngegyvrseldyrlnertiiaaslgKAFGASGGVIMlGDAEQIELILRYAGPLA 279
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767922627 435 FTTSLPPMLLAGALESVRILKSAEGRVLRRQHQRNVKLMRQMLMD--AGLPVvhcpshiiPVRVA---DAAKNTEVCDEL 509
Cdd:PRK07505 280 FSQSLNVAALGAILASAEIHLSEELDQLQQKLQNNIALFDSLIPTeqSGSFL--------PIRLIyigDEDTAIKAAKQL 351
|
330 340 350
....*....|....*....|....*....|....
gi 767922627 510 MSRhNIYVQAINYPTVPRGEELLRIAPTPHHTPQ 543
Cdd:PRK07505 352 LDR-GFYTSPVFFPVVAKGRAGLRIMFRASHTND 384
|
|
| PRK05937 |
PRK05937 |
8-amino-7-oxononanoate synthase; Provisional |
267-386 |
2.20e-10 |
|
8-amino-7-oxononanoate synthase; Provisional
Pssm-ID: 102071 [Multi-domain] Cd Length: 370 Bit Score: 62.49 E-value: 2.20e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767922627 267 SNDYLGMSRHPRVCGAVMDTLKQH-------GAGAGGTRNISGTSKFHVDLERELADLHGKDAALLFSSCFVANDSTLFT 339
Cdd:PRK05937 11 TNDFLGFSRSDTLVHEVEKRYRLYcrqfphaQLGYGGSRAILGPSSLLDDLEHKIAHFHGAPEAFIVPSGYMANLGLCAH 90
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 767922627 340 LAKMMPgcEIYSDSGNHASMIQGIRNSRVPKYIFRHNDVSHLRELLQ 386
Cdd:PRK05937 91 LSSVTD--YVLWDEQVHISVVYSLSVISGWHQSFRHNDLDHLESLLE 135
|
|
|