|
Name |
Accession |
Description |
Interval |
E-value |
| 5aminolev_synth |
TIGR01821 |
5-aminolevulinic acid synthase; This model represents 5-aminolevulinic acid synthase, an ... |
199-604 |
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: 654.88 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 628601867 199 FQYDHFFEKKIDEKKNDHTYRVFKTVNRRAQIFPMADDYTDSliTKKQVSVWCSNDYLGMSRHPRVCGAVMETVKQHGAG 278
Cdd:TIGR01821 1 MDYDQFFNKEIDKLHLEGRYRVFADLERQAGEFPFAQWHRPD--GAKDVTVWCSNDYLGMGQHPEVLQAMHETLDKYGAG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 628601867 279 AGGTRNISGTSKFHVELEQALADLHGKDAALLFSSCFVANDSTLFTLAKMMPGCEIYSDSGNHASMIQGIRNSRVPKYIF 358
Cdd:TIGR01821 79 AGGTRNISGTNIPHVELEAELADLHGKESALVFTSGYVANDATLATLAKIIPGCVIFSDELNHASMIEGIRHSGAEKFIF 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 628601867 359 RHNDVNHLRELLQRSDPSVPKIVAFETVHSMDGAVCPLEELCDVAHEFGAITFVDEVHAVGLYGARGGGIGDRDGVMPKM 438
Cdd:TIGR01821 159 RHNDVAHLEKLLQSVDPNRPKIIAFESVYSMDGDIAPIEEICDLADKYGALTYLDEVHAVGLYGPRGGGIAERDGLMHRI 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 628601867 439 DIISGTLGKAFGCVGGYIASTSLLIDTVRSYAAGFIFTTSLPPMLLAGALESVRILKSSEgrALRRQHQRNVKLLRQMLM 518
Cdd:TIGR01821 239 DIIEGTLAKAFGVVGGYIAASRKLIDAIRSYAPGFIFTTSLPPAIAAGATASIRHLKESQ--DLRRAHQENVKRLKNLLE 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 628601867 519 DAGLPVIHCPSHIIPVRVADAAKNTEICDELMTRHNIYVQAINYPTVPRGEELLRIAPTPHHTPQMMNFFVEKLLVTWKR 598
Cdd:TIGR01821 317 ALGIPVIPNPSHIVPVIIGDAALCKKVSDLLLNKHGIYVQPINYPTVPRGTERLRITPTPAHTDKMIDDLVEALLLVWDR 396
|
....*.
gi 628601867 599 VGLELK 604
Cdd:TIGR01821 397 LGLPLS 402
|
|
| KBL_like |
cd06454 |
KBL_like; this family belongs to the pyridoxal phosphate (PLP)-dependent aspartate ... |
245-592 |
1.17e-177 |
|
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: 507.87 E-value: 1.17e-177
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 628601867 245 KQVSVWCSNDYLGMSRHPRVCGAVMETVKQHGAGAGGTRNISGTSKFHVELEQALADLHGKDAALLFSSCFVANDSTLFT 324
Cdd:cd06454 1 KKVLNFCSNDYLGLANHPEVIEAAKEALDKYGVGAGGSRLISGTSDLHEELEEELAEFHGKEAALVFSSGYAANDGVLST 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 628601867 325 LakMMPGCEIYSDSGNHASMIQGIRNSRVPKYIFRHNDVNHLRELLQRSD-PSVPKIVAFETVHSMDGAVCPLEELCDVA 403
Cdd:cd06454 81 L--AGKGDLIISDSLNHASIIDGIRLSGAKKRIFKHNDMEDLEKLLREARrPYGKKLIVTEGVYSMDGDIAPLPELVDLA 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 628601867 404 HEFGAITFVDEVHAVGLYGARGGGIGDRDGVMPKMDIISGTLGKAFGCVGGYIASTSLLIDTVRSYAAGFIFTTSLPPML 483
Cdd:cd06454 159 KKYGAILFVDEAHSVGVYGPHGRGVEEFGGLTDDVDIIMGTLGKAFGAVGGYIAGSKELIDYLRSYARGFIFSTSLPPAV 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 628601867 484 LAGALESVRILKSseGRALRRQHQRNVKLLRQMLMDAGLPVIHCPSHIIPVRVAD-AAKNTEICDELMtRHNIYVQAINY 562
Cdd:cd06454 239 AAAALAALEVLQG--GPERRERLQENVRYLRRGLKELGFPVGGSPSHIIPPLIGDdPAKAVAFSDALL-ERGIYVQAIRY 315
|
330 340 350
....*....|....*....|....*....|
gi 628601867 563 PTVPRGEELLRIAPTPHHTPQMMNFFVEKL 592
Cdd:cd06454 316 PTVPRGTARLRISLSAAHTKEDIDRLLEAL 345
|
|
| PRK13392 |
PRK13392 |
5-aminolevulinate synthase; Provisional |
199-610 |
1.32e-169 |
|
5-aminolevulinate synthase; Provisional
Pssm-ID: 184023 [Multi-domain] Cd Length: 410 Bit Score: 489.75 E-value: 1.32e-169
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 628601867 199 FQYDHFFEKKIDEKKNDHTYRVFKTVNRRAQIFPMADDYTDSliTKKQVSVWCSNDYLGMSRHPRVCGAVMETVKQHGAG 278
Cdd:PRK13392 2 MNYDSYFDAALAQLHQEGRYRVFADLEREAGRFPRARDHGPD--GPRRVTIWCSNDYLGMGQHPDVIGAMVDALDRYGAG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 628601867 279 AGGTRNISGTSKFHVELEQALADLHGKDAALLFSSCFVANDSTLFTLAKMMPGCEIYSDSGNHASMIQGIRNSRVPKYIF 358
Cdd:PRK13392 80 AGGTRNISGTSHPHVLLERELADLHGKESALLFTSGYVSNDAALSTLGKLLPGCVILSDALNHASMIEGIRRSGAEKQVF 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 628601867 359 RHNDVNHLRELLQRSDPSVPKIVAFETVHSMDGAVCPLEELCDVAHEFGAITFVDEVHAVGLYGARGGGIGDRDGVMPKM 438
Cdd:PRK13392 160 RHNDLADLEEQLASVDPDRPKLIAFESVYSMDGDIAPIEAICDLADRYNALTYVDEVHAVGLYGARGGGIAERDGLMDRI 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 628601867 439 DIISGTLGKAFGCVGGYIASTSLLIDTVRSYAAGFIFTTSLPPMLLAGALESVRILKSSEgrALRRQHQRNVKLLRQMLM 518
Cdd:PRK13392 240 DMIQGTLAKAFGCLGGYIAASADLIDFVRSFAPGFIFTTALPPAVAAGATAAIRHLKTSQ--TERDAHQDRVAALKAKLN 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 628601867 519 DAGLPVIHCPSHIIPVRVADAAKNTEICDELMTRHNIYVQAINYPTVPRGEELLRIAPTPHHTPQMMNFFVEKLLVTWKR 598
Cdd:PRK13392 318 ANGIPVMPSPSHIVPVMVGDPTLCKAISDRLMSEHGIYIQPINYPTVPRGTERLRITPTPLHDDEDIDALVAALVAIWDR 397
|
410
....*....|..
gi 628601867 599 VGLELKPHSSAE 610
Cdd:PRK13392 398 LELPRWREAAQA 409
|
|
| BioF |
COG0156 |
7-keto-8-aminopelargonate synthetase or related enzyme [Coenzyme transport and metabolism]; |
199-600 |
1.22e-136 |
|
7-keto-8-aminopelargonate synthetase or related enzyme [Coenzyme transport and metabolism];
Pssm-ID: 223234 [Multi-domain] Cd Length: 388 Bit Score: 404.71 E-value: 1.22e-136
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 628601867 199 FQYDHFFEKKIDEKKNDHTYRVFKTVNRRAQIFPMADdytdslitKKQVSVWCSNDYLGMSRHPRVCGAVMETVKQHGAG 278
Cdd:COG0156 1 MDFLSFLRQALQALKAEGLYRGLRALDRRQGLAIRAD--------GRKVLNFCSNDYLGLASHPELIEAAKAAIRRYGVG 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 628601867 279 AGGTRNISGTSKFHVELEQALADLHGKDAALLFSSCFVANDSTLFTLAKmmPGCEIYSDSGNHASMIQGIRNSRVPKYIF 358
Cdd:COG0156 73 AGGSRLISGTSDLHVELEEELADFLGAEAALLFSSGFVANLGLLSALLK--KGDLIFSDELNHASIIDGIRLSRAEVRRF 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 628601867 359 RHNDVNHLRELLQ--RSDPSVPKIVAFETVHSMDGAVCPLEELCDVAHEFGAITFVDEVHAVGLYGARGGGIGDRDGVMP 436
Cdd:COG0156 151 KHNDLDHLEALLEeaRENGARRKLIVTEGVFSMDGDIAPLPELVELAEKYGALLYVDEAHAVGVLGPNGRGLAEHFGLEP 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 628601867 437 K-MDIISGTLGKAFGCVGGYIASTSLLIDTVRSYAAGFIFTTSLPPMLLAGALESVRILKssEGRALRRQHQRNVKLLRQ 515
Cdd:COG0156 231 EeVDIIVGTLGKALGSSGGYIAGSAALIDYLRNRARPFIFSTALPPAVAAAALAALRILE--EGPERRERLQELAAFFRS 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 628601867 516 MLMDAGLPVIHCPSHIIPVRVADAAKNTEICDELMTRhNIYVQAINYPTVPRGEELLRIAPTPHHTPQMmnffVEKLLVT 595
Cdd:COG0156 309 LLKALGLVLLPSESPIIPVILGDEERALEASRALLEE-GIYVSAIRPPTVPKGTARLRITLTAAHTEED----IDRLAEA 383
|
....*
gi 628601867 596 WKRVG 600
Cdd:COG0156 384 LSEVG 388
|
|
| Aminotran_1_2 |
pfam00155 |
Aminotransferase class I and II; |
250-592 |
5.41e-71 |
|
Aminotransferase class I and II;
Pssm-ID: 395103 [Multi-domain] Cd Length: 351 Bit Score: 233.35 E-value: 5.41e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 628601867 250 WCSNDYLGMsrhprVCGAVMETVKQhgAGAGGTRNISGTSKFHVELEQALADLHG--------KDAALLFSSCFVANDST 321
Cdd:pfam00155 6 LGSNEYLGD-----TLPAVAKAEKD--ALAGGTRNLYGPTDGHPELREALAKFLGrspvlkldREAAVVFGSGAGANIEA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 628601867 322 LFTLAKMmPGCEIYSDSGNHASMIQGIRNSRVPKYIFR-------HNDVNHLRELLQRSdpsvPKIVAFETVHSMDGAVC 394
Cdd:pfam00155 79 LIFLLAN-PGDAILVPAPTYASYIRIARLAGGEVVRYPlydsndfHLDFDALEAALKEK----PKVVLHTSPHNPTGTVA 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 628601867 395 PLEELCDVA---HEFGAITFVDEVHAVGLYGARGGGIGDRDgVMPKMD-IISGTLGKAFGCVG---GYIASTSLLIDTVR 467
Cdd:pfam00155 154 TLEELEKLLdlaKEHNILLLVDEAYAGFVFGSPDAVATRAL-LAEGPNlLVVGSFSKAFGLAGwrvGYILGNAAVISQLR 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 628601867 468 SYAAGFIFTTSLPPMLLAGALESvrILKSSEGRALRRQHQRNVKLLRQMLMDAGLPVIHCPSHIIPVRVADAAKNTEICD 547
Cdd:pfam00155 233 KLARPFYSSTHLQAAAAAALSDP--LLVASELEEMRQRIKERRDYLRDGLQAAGLSVLPSQAGFFLLTGLDPETAKELAQ 310
|
330 340 350 360
....*....|....*....|....*....|....*....|....*
gi 628601867 548 ELMTRHNIYVQAINYPTVPrgeELLRIAPTpHHTPQMMNFFVEKL 592
Cdd:pfam00155 311 VLLEEVGVYVTPGSSPGVP---GWLRITVA-GGTEEELEELLEAI 351
|
|
| Preseq_ALAS |
pfam09029 |
5-aminolevulinate synthase presequence; The N terminal presequence domain found in ... |
2-140 |
2.92e-53 |
|
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: 401101 Cd Length: 114 Bit Score: 178.06 E-value: 2.92e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 628601867 2 ETVVRRCPFLSRVPQAFLQKAGKSLLFYAQNCPKMMevgakpaPRTLSTSAVHCQQVKE-TPPANEKEKTAKAavqqapd 80
Cdd:pfam09029 1 ASVLRRCPFLSRVPQAFLQKARKSLLSYAQRCPVMM-------TRALSTSSANLQGEKEeTPVAGPTAKQAKA------- 66
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 628601867 81 esqmaqtpdgtqLPSGHPSPATSQGSGSKCPFLAAQLSQTGSSVFRKASLELQEDVQEMH 140
Cdd:pfam09029 67 ------------LPLGHPSPQAGQSVASKCPFLAAEMGQKNSNVVRKASPEVQEDVQEVR 114
|
|
|
|
Name |
Accession |
Description |
Interval |
E-value |
| 5aminolev_synth |
TIGR01821 |
5-aminolevulinic acid synthase; This model represents 5-aminolevulinic acid synthase, an ... |
199-604 |
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: 654.88 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 628601867 199 FQYDHFFEKKIDEKKNDHTYRVFKTVNRRAQIFPMADDYTDSliTKKQVSVWCSNDYLGMSRHPRVCGAVMETVKQHGAG 278
Cdd:TIGR01821 1 MDYDQFFNKEIDKLHLEGRYRVFADLERQAGEFPFAQWHRPD--GAKDVTVWCSNDYLGMGQHPEVLQAMHETLDKYGAG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 628601867 279 AGGTRNISGTSKFHVELEQALADLHGKDAALLFSSCFVANDSTLFTLAKMMPGCEIYSDSGNHASMIQGIRNSRVPKYIF 358
Cdd:TIGR01821 79 AGGTRNISGTNIPHVELEAELADLHGKESALVFTSGYVANDATLATLAKIIPGCVIFSDELNHASMIEGIRHSGAEKFIF 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 628601867 359 RHNDVNHLRELLQRSDPSVPKIVAFETVHSMDGAVCPLEELCDVAHEFGAITFVDEVHAVGLYGARGGGIGDRDGVMPKM 438
Cdd:TIGR01821 159 RHNDVAHLEKLLQSVDPNRPKIIAFESVYSMDGDIAPIEEICDLADKYGALTYLDEVHAVGLYGPRGGGIAERDGLMHRI 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 628601867 439 DIISGTLGKAFGCVGGYIASTSLLIDTVRSYAAGFIFTTSLPPMLLAGALESVRILKSSEgrALRRQHQRNVKLLRQMLM 518
Cdd:TIGR01821 239 DIIEGTLAKAFGVVGGYIAASRKLIDAIRSYAPGFIFTTSLPPAIAAGATASIRHLKESQ--DLRRAHQENVKRLKNLLE 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 628601867 519 DAGLPVIHCPSHIIPVRVADAAKNTEICDELMTRHNIYVQAINYPTVPRGEELLRIAPTPHHTPQMMNFFVEKLLVTWKR 598
Cdd:TIGR01821 317 ALGIPVIPNPSHIVPVIIGDAALCKKVSDLLLNKHGIYVQPINYPTVPRGTERLRITPTPAHTDKMIDDLVEALLLVWDR 396
|
....*.
gi 628601867 599 VGLELK 604
Cdd:TIGR01821 397 LGLPLS 402
|
|
| KBL_like |
cd06454 |
KBL_like; this family belongs to the pyridoxal phosphate (PLP)-dependent aspartate ... |
245-592 |
1.17e-177 |
|
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: 507.87 E-value: 1.17e-177
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 628601867 245 KQVSVWCSNDYLGMSRHPRVCGAVMETVKQHGAGAGGTRNISGTSKFHVELEQALADLHGKDAALLFSSCFVANDSTLFT 324
Cdd:cd06454 1 KKVLNFCSNDYLGLANHPEVIEAAKEALDKYGVGAGGSRLISGTSDLHEELEEELAEFHGKEAALVFSSGYAANDGVLST 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 628601867 325 LakMMPGCEIYSDSGNHASMIQGIRNSRVPKYIFRHNDVNHLRELLQRSD-PSVPKIVAFETVHSMDGAVCPLEELCDVA 403
Cdd:cd06454 81 L--AGKGDLIISDSLNHASIIDGIRLSGAKKRIFKHNDMEDLEKLLREARrPYGKKLIVTEGVYSMDGDIAPLPELVDLA 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 628601867 404 HEFGAITFVDEVHAVGLYGARGGGIGDRDGVMPKMDIISGTLGKAFGCVGGYIASTSLLIDTVRSYAAGFIFTTSLPPML 483
Cdd:cd06454 159 KKYGAILFVDEAHSVGVYGPHGRGVEEFGGLTDDVDIIMGTLGKAFGAVGGYIAGSKELIDYLRSYARGFIFSTSLPPAV 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 628601867 484 LAGALESVRILKSseGRALRRQHQRNVKLLRQMLMDAGLPVIHCPSHIIPVRVAD-AAKNTEICDELMtRHNIYVQAINY 562
Cdd:cd06454 239 AAAALAALEVLQG--GPERRERLQENVRYLRRGLKELGFPVGGSPSHIIPPLIGDdPAKAVAFSDALL-ERGIYVQAIRY 315
|
330 340 350
....*....|....*....|....*....|
gi 628601867 563 PTVPRGEELLRIAPTPHHTPQMMNFFVEKL 592
Cdd:cd06454 316 PTVPRGTARLRISLSAAHTKEDIDRLLEAL 345
|
|
| PRK13392 |
PRK13392 |
5-aminolevulinate synthase; Provisional |
199-610 |
1.32e-169 |
|
5-aminolevulinate synthase; Provisional
Pssm-ID: 184023 [Multi-domain] Cd Length: 410 Bit Score: 489.75 E-value: 1.32e-169
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 628601867 199 FQYDHFFEKKIDEKKNDHTYRVFKTVNRRAQIFPMADDYTDSliTKKQVSVWCSNDYLGMSRHPRVCGAVMETVKQHGAG 278
Cdd:PRK13392 2 MNYDSYFDAALAQLHQEGRYRVFADLEREAGRFPRARDHGPD--GPRRVTIWCSNDYLGMGQHPDVIGAMVDALDRYGAG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 628601867 279 AGGTRNISGTSKFHVELEQALADLHGKDAALLFSSCFVANDSTLFTLAKMMPGCEIYSDSGNHASMIQGIRNSRVPKYIF 358
Cdd:PRK13392 80 AGGTRNISGTSHPHVLLERELADLHGKESALLFTSGYVSNDAALSTLGKLLPGCVILSDALNHASMIEGIRRSGAEKQVF 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 628601867 359 RHNDVNHLRELLQRSDPSVPKIVAFETVHSMDGAVCPLEELCDVAHEFGAITFVDEVHAVGLYGARGGGIGDRDGVMPKM 438
Cdd:PRK13392 160 RHNDLADLEEQLASVDPDRPKLIAFESVYSMDGDIAPIEAICDLADRYNALTYVDEVHAVGLYGARGGGIAERDGLMDRI 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 628601867 439 DIISGTLGKAFGCVGGYIASTSLLIDTVRSYAAGFIFTTSLPPMLLAGALESVRILKSSEgrALRRQHQRNVKLLRQMLM 518
Cdd:PRK13392 240 DMIQGTLAKAFGCLGGYIAASADLIDFVRSFAPGFIFTTALPPAVAAGATAAIRHLKTSQ--TERDAHQDRVAALKAKLN 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 628601867 519 DAGLPVIHCPSHIIPVRVADAAKNTEICDELMTRHNIYVQAINYPTVPRGEELLRIAPTPHHTPQMMNFFVEKLLVTWKR 598
Cdd:PRK13392 318 ANGIPVMPSPSHIVPVMVGDPTLCKAISDRLMSEHGIYIQPINYPTVPRGTERLRITPTPLHDDEDIDALVAALVAIWDR 397
|
410
....*....|..
gi 628601867 599 VGLELKPHSSAE 610
Cdd:PRK13392 398 LELPRWREAAQA 409
|
|
| BioF |
COG0156 |
7-keto-8-aminopelargonate synthetase or related enzyme [Coenzyme transport and metabolism]; |
199-600 |
1.22e-136 |
|
7-keto-8-aminopelargonate synthetase or related enzyme [Coenzyme transport and metabolism];
Pssm-ID: 223234 [Multi-domain] Cd Length: 388 Bit Score: 404.71 E-value: 1.22e-136
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 628601867 199 FQYDHFFEKKIDEKKNDHTYRVFKTVNRRAQIFPMADdytdslitKKQVSVWCSNDYLGMSRHPRVCGAVMETVKQHGAG 278
Cdd:COG0156 1 MDFLSFLRQALQALKAEGLYRGLRALDRRQGLAIRAD--------GRKVLNFCSNDYLGLASHPELIEAAKAAIRRYGVG 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 628601867 279 AGGTRNISGTSKFHVELEQALADLHGKDAALLFSSCFVANDSTLFTLAKmmPGCEIYSDSGNHASMIQGIRNSRVPKYIF 358
Cdd:COG0156 73 AGGSRLISGTSDLHVELEEELADFLGAEAALLFSSGFVANLGLLSALLK--KGDLIFSDELNHASIIDGIRLSRAEVRRF 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 628601867 359 RHNDVNHLRELLQ--RSDPSVPKIVAFETVHSMDGAVCPLEELCDVAHEFGAITFVDEVHAVGLYGARGGGIGDRDGVMP 436
Cdd:COG0156 151 KHNDLDHLEALLEeaRENGARRKLIVTEGVFSMDGDIAPLPELVELAEKYGALLYVDEAHAVGVLGPNGRGLAEHFGLEP 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 628601867 437 K-MDIISGTLGKAFGCVGGYIASTSLLIDTVRSYAAGFIFTTSLPPMLLAGALESVRILKssEGRALRRQHQRNVKLLRQ 515
Cdd:COG0156 231 EeVDIIVGTLGKALGSSGGYIAGSAALIDYLRNRARPFIFSTALPPAVAAAALAALRILE--EGPERRERLQELAAFFRS 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 628601867 516 MLMDAGLPVIHCPSHIIPVRVADAAKNTEICDELMTRhNIYVQAINYPTVPRGEELLRIAPTPHHTPQMmnffVEKLLVT 595
Cdd:COG0156 309 LLKALGLVLLPSESPIIPVILGDEERALEASRALLEE-GIYVSAIRPPTVPKGTARLRITLTAAHTEED----IDRLAEA 383
|
....*
gi 628601867 596 WKRVG 600
Cdd:COG0156 384 LSEVG 388
|
|
| PRK05958 |
PRK05958 |
8-amino-7-oxononanoate synthase; Reviewed |
205-592 |
1.02e-95 |
|
8-amino-7-oxononanoate synthase; Reviewed
Pssm-ID: 235655 [Multi-domain] Cd Length: 385 Bit Score: 299.38 E-value: 1.02e-95
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 628601867 205 FEKKIDEKKNDHTYRVFKTVNRRAQIFPMADDytdslitkKQVSVWCSNDYLGMSRHPRVCGAVMETVKQHGAGAGGTRN 284
Cdd:PRK05958 7 LEAALAQRRAAGLYRSLRPREGGAGRWLVVDG--------RRMLNFASNDYLGLARHPRLIAAAQQAARRYGAGSGGSRL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 628601867 285 ISGTSKFHVELEQALADLHGKDAALLFSSCFVANDSTLFTLakMMPGCEIYSDSGNHASMIQGIRNSRVPKYIFRHNDVN 364
Cdd:PRK05958 79 VTGNSPAHEALEEELAEWFGAERALLFSSGYAANLAVLTAL--AGKGDLIVSDKLNHASLIDGARLSRARVRRYPHNDVD 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 628601867 365 HLRELLQRSDPSvPKIVAFETVHSMDGAVCPLEELCDVAHEFGAITFVDEVHAVGLYGARGG-GIGDRDGVMPKMDIISG 443
Cdd:PRK05958 157 ALEALLAKWRAG-RALIVTESVFSMDGDLAPLAELVALARRHGAWLLVDEAHGTGVLGPQGRgLAAEAGLAGEPDVILVG 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 628601867 444 TLGKAFGCVGGYIASTSLLIDTVRSYAAGFIFTTSLPPMLLAGALESVRILKSSEGralRRQH-QRNVKLLRQMLMDAGL 522
Cdd:PRK05958 236 TLGKALGSSGAAVLGSETLIDYLINRARPFIFTTALPPAQAAAARAALRILRREPE---RRERlAALIARLRAGLRALGF 312
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 628601867 523 PVIHCPSHIIPVRVADAAKNTEICDELMTRhNIYVQAINYPTVPRGEELLRIAPTPHHTPQMMNFFVEKL 592
Cdd:PRK05958 313 QLMDSQSAIQPLIVGDNERALALAAALQEQ-GFWVGAIRPPTVPAGTSRLRITLTAAHTEADIDRLLEAL 381
|
|
| bioF |
TIGR00858 |
8-amino-7-oxononanoate synthase; 7-keto-8-aminopelargonic acid synthetase is an alternate name. ... |
245-592 |
1.02e-95 |
|
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: 298.41 E-value: 1.02e-95
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 628601867 245 KQVSVWCSNDYLGMSRHPRVCGAVMETVKQHGAGAGGTRNISGTSKFHVELEQALADLHGKDAALLFSSCFVANDSTLFT 324
Cdd:TIGR00858 16 RRLLNFSSNDYLGLASHPEVIQAAQQGAEQYGAGSTASRLVSGNSPLHEELEEELAEWKGTEAALLFSSGYLANVGVISA 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 628601867 325 LAKmmPGCEIYSDSGNHASMIQGIRNSRVPKYIFRHNDVNHLRELLQRSDPSVPKIVAFETVHSMDGAVCPLEELCDVAH 404
Cdd:TIGR00858 96 LVG--KGDLILSDALNHASLIDGCRLSGARVRRYRHNDVEHLERLLEKNRGERRKLIVTDGVFSMDGDIAPLPQLVALAE 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 628601867 405 EFGAITFVDEVHAVGLYGARGGGIGDRDGVMPKMDIIS-GTLGKAFGCVGGYIASTSLLIDTVRSYAAGFIFTTSLPPML 483
Cdd:TIGR00858 174 RYGAWLMVDDAHGTGVLGEDGRGTLEHFGLKPEPVDIQvGTLSKALGSYGAYVAGSQALIDYLINRARTLIFSTALPPAV 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 628601867 484 LAGALESVRILKssEGRALRRQHQRNVKLLRQMLMDAGLPVIHCPSHIIPVRVADAAKNTEICDELMtRHNIYVQAINYP 563
Cdd:TIGR00858 254 AAAALAALELIQ--EEPWRREKLLALIARLRAGLEALGFTLMPSCTPIVPVIIGDNASALALAEELQ-QQGIFVGAIRPP 330
|
330 340
....*....|....*....|....*....
gi 628601867 564 TVPRGEELLRIAPTPHHTPQMMNFFVEKL 592
Cdd:TIGR00858 331 TVPAGTSRLRLTLSAAHTPGDIDRLAEAL 359
|
|
| PRK06939 |
PRK06939 |
2-amino-3-ketobutyrate coenzyme A ligase; Provisional |
204-604 |
3.44e-90 |
|
2-amino-3-ketobutyrate coenzyme A ligase; Provisional
Pssm-ID: 235893 [Multi-domain] Cd Length: 397 Bit Score: 285.17 E-value: 3.44e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 628601867 204 FFEKKIDEKKNDHTY---RVFKTVNRrAQIfpmaddytdSLITKKQVSVWCSNDYLGMSRHPRVCGAVMETVKQHGAGAG 280
Cdd:PRK06939 8 QLREELEEIKAEGLYkeeRVITSPQG-ADI---------TVADGKEVINFCANNYLGLANHPELIAAAKAALDSHGFGMA 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 628601867 281 GTRNISGTSKFHVELEQALADLHGKDAALLFSSCFVANDSTLFTLakMMPGCEIYSDSGNHASMIQGIRNSRVPKYIFRH 360
Cdd:PRK06939 78 SVRFICGTQDLHKELEEKLAKFLGTEDAILYSSCFDANGGLFETL--LGKEDAIISDALNHASIIDGVRLCKAKRYRYAN 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 628601867 361 NDVNHLRELLQRSDPSVP--KIVAFETVHSMDGAVCPLEELCDVAHEFGAITFVDEVHAVGLYGARGGGIGDRDGVMPKM 438
Cdd:PRK06939 156 NDMADLEAQLKEAKEAGArhKLIATDGVFSMDGDIAPLPEICDLADKYDALVMVDDSHAVGFVGENGRGTVEHFGVMDRV 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 628601867 439 DIISGTLGKAF-GCVGGYIASTSLLIDTVRSYAAGFIFTTSLPPMLLAGALESVRILKssEGRALRRQHQRNVKLLRQML 517
Cdd:PRK06939 236 DIITGTLGKALgGASGGYTAGRKEVIDWLRQRSRPYLFSNSLAPAIVAASIKVLELLE--ESDELRDRLWENARYFREGM 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 628601867 518 MDAGLPVIHCPSHIIPVRVADAAKNTEICDELMTRhNIYVQAINYPTVPRGEELLRIAPTPHHTPQMmnffVEKLLVTWK 597
Cdd:PRK06939 314 TAAGFTLGPGEHPIIPVMLGDAKLAQEFADRLLEE-GVYVIGFSFPVVPKGQARIRTQMSAAHTKEQ----LDRAIDAFE 388
|
....*..
gi 628601867 598 RVGLELK 604
Cdd:PRK06939 389 KVGKELG 395
|
|
| Aminotran_1_2 |
pfam00155 |
Aminotransferase class I and II; |
250-592 |
5.41e-71 |
|
Aminotransferase class I and II;
Pssm-ID: 395103 [Multi-domain] Cd Length: 351 Bit Score: 233.35 E-value: 5.41e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 628601867 250 WCSNDYLGMsrhprVCGAVMETVKQhgAGAGGTRNISGTSKFHVELEQALADLHG--------KDAALLFSSCFVANDST 321
Cdd:pfam00155 6 LGSNEYLGD-----TLPAVAKAEKD--ALAGGTRNLYGPTDGHPELREALAKFLGrspvlkldREAAVVFGSGAGANIEA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 628601867 322 LFTLAKMmPGCEIYSDSGNHASMIQGIRNSRVPKYIFR-------HNDVNHLRELLQRSdpsvPKIVAFETVHSMDGAVC 394
Cdd:pfam00155 79 LIFLLAN-PGDAILVPAPTYASYIRIARLAGGEVVRYPlydsndfHLDFDALEAALKEK----PKVVLHTSPHNPTGTVA 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 628601867 395 PLEELCDVA---HEFGAITFVDEVHAVGLYGARGGGIGDRDgVMPKMD-IISGTLGKAFGCVG---GYIASTSLLIDTVR 467
Cdd:pfam00155 154 TLEELEKLLdlaKEHNILLLVDEAYAGFVFGSPDAVATRAL-LAEGPNlLVVGSFSKAFGLAGwrvGYILGNAAVISQLR 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 628601867 468 SYAAGFIFTTSLPPMLLAGALESvrILKSSEGRALRRQHQRNVKLLRQMLMDAGLPVIHCPSHIIPVRVADAAKNTEICD 547
Cdd:pfam00155 233 KLARPFYSSTHLQAAAAAALSDP--LLVASELEEMRQRIKERRDYLRDGLQAAGLSVLPSQAGFFLLTGLDPETAKELAQ 310
|
330 340 350 360
....*....|....*....|....*....|....*....|....*
gi 628601867 548 ELMTRHNIYVQAINYPTVPrgeELLRIAPTpHHTPQMMNFFVEKL 592
Cdd:pfam00155 311 VLLEEVGVYVTPGSSPGVP---GWLRITVA-GGTEEELEELLEAI 351
|
|
| Preseq_ALAS |
pfam09029 |
5-aminolevulinate synthase presequence; The N terminal presequence domain found in ... |
2-140 |
2.92e-53 |
|
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: 401101 Cd Length: 114 Bit Score: 178.06 E-value: 2.92e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 628601867 2 ETVVRRCPFLSRVPQAFLQKAGKSLLFYAQNCPKMMevgakpaPRTLSTSAVHCQQVKE-TPPANEKEKTAKAavqqapd 80
Cdd:pfam09029 1 ASVLRRCPFLSRVPQAFLQKARKSLLSYAQRCPVMM-------TRALSTSSANLQGEKEeTPVAGPTAKQAKA------- 66
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 628601867 81 esqmaqtpdgtqLPSGHPSPATSQGSGSKCPFLAAQLSQTGSSVFRKASLELQEDVQEMH 140
Cdd:pfam09029 67 ------------LPLGHPSPQAGQSVASKCPFLAAEMGQKNSNVVRKASPEVQEDVQEVR 114
|
|
| PLN02483 |
PLN02483 |
serine palmitoyltransferase |
252-566 |
2.04e-46 |
|
serine palmitoyltransferase
Pssm-ID: 178101 [Multi-domain] Cd Length: 489 Bit Score: 171.10 E-value: 2.04e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 628601867 252 SNDYLGMSRHPRVCGA-VMETVKQHGAGAGGTRNISGTSKFHVELEQALADLHGKDAALLFSSCFVANDSTLFTLakMMP 330
Cdd:PLN02483 107 SYNYLGFAAADEYCTPrVIESLKKYSASTCSSRVDGGTTKLHRELEELVARFVGKPAAIVFGMGYATNSTIIPAL--IGK 184
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 628601867 331 GCEIYSDSGNHASMIQGIRNSRVPKYIFRHNDVNHLRELLQ--------RSDPSVPKI-VAFETVHSMDGAVCPLEELCD 401
Cdd:PLN02483 185 GGLIISDSLNHNSIVNGARGSGATIRVFQHNTPSHLEEVLReqiaegqpRTHRPWKKIiVIVEGIYSMEGELCKLPEIVA 264
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 628601867 402 VAHEFGAITFVDEVHAVGLYGARGGGIGDRDGVMPK-MDIISGTLGKAFGCVGGYIASTSLLIDTVRSYAAGFIFTTSLP 480
Cdd:PLN02483 265 VCKKYKAYVYLDEAHSIGAVGKTGRGVCELLGVDPAdVDIMMGTFTKSFGSCGGYIAGSKELIQYLKRTCPAHLYATSMS 344
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 628601867 481 PMLLAGALESVRIL----KSSEGRALRRQHQRNVKLLRQMLMDAGLPVI-HCPSHIIPVRVADAAKNTEICDELMTRhNI 555
Cdd:PLN02483 345 PPAVQQVISAIKVIlgedGTNRGAQKLAQIRENSNFFRSELQKMGFEVLgDNDSPVMPIMLYNPAKIPAFSRECLKQ-NV 423
|
330
....*....|.
gi 628601867 556 YVQAINYPTVP 566
Cdd:PLN02483 424 AVVVVGFPATP 434
|
|
| PLN02955 |
PLN02955 |
8-amino-7-oxononanoate synthase |
245-594 |
4.75e-44 |
|
8-amino-7-oxononanoate synthase
Pssm-ID: 178541 [Multi-domain] Cd Length: 476 Bit Score: 164.46 E-value: 4.75e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 628601867 245 KQVSVWCSNDYLGMSRHPRVCGAVMETVKQHGAGAGGTRNISGTSKFHVELEQALADLHGKDAALLFSSCFVANDSTLFT 324
Cdd:PLN02955 102 KKLLLFSGNDYLGLSSHPTISNAAANAAKEYGMGPKGSALICGYTTYHRLLESSLADLKKKEDCLVCPTGFAANMAAMVA 181
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 628601867 325 L--------AKMMP----GCEIYSDSGNHASMIQGIR----NSRVPKYIFRHNDVNHLRELLQRSDPSvPKIVAFETVHS 388
Cdd:PLN02955 182 IgsvasllaASGKPlkneKVAIFSDALNHASIIDGVRlaerQGNVEVFVYRHCDMYHLNSLLSSCKMK-RKVVVTDSLFS 260
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 628601867 389 MDGAVCPLEELCDVAHEFGAITFVDEVHAVGLYGARGGGIGDRDGVMPKMDIISGTLGKAFGCVGGYIASTSLLIDTVRS 468
Cdd:PLN02955 261 MDGDFAPMEELSQLRKKYGFLLVIDDAHGTFVCGENGGGVAEEFNCEADVDLCVGTLSKAAGCHGGFIACSKKWKQLIQS 340
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 628601867 469 YAAGFIFTTSLPPMLLAGALESVRILKSSEGRalRRQHQRNVKLLRQMlmdAGLPVihcPSHIIPVRVADAAKNTEICDE 548
Cdd:PLN02955 341 RGRSFIFSTAIPVPMAAAAYAAVVVARKEKWR--RKAIWERVKEFKAL---SGVDI---SSPIISLVVGNQEKALKASRY 412
|
330 340 350 360
....*....|....*....|....*....|....*....|....*.
gi 628601867 549 LMtRHNIYVQAINYPTVPRGEELLRIAPTPHHTPQMmnffVEKLLV 594
Cdd:PLN02955 413 LL-KSGFHVMAIRPPTVPPNSCRLRVTLSAAHTTED----VKKLIT 453
|
|
| PRK07179 |
PRK07179 |
quorum-sensing autoinducer synthase; |
252-605 |
3.93e-43 |
|
quorum-sensing autoinducer synthase;
Pssm-ID: 180866 [Multi-domain] Cd Length: 407 Bit Score: 160.17 E-value: 3.93e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 628601867 252 SNDYLGMSRHPRVCGAVMETVKQHGAG----AGGTRNISGTSKFhvelEQALADLHGKDAALLFSSCFVANDSTLFTLAK 327
Cdd:PRK07179 61 SNDYLNLSGHPDIIKAQIAALQEEGDSlvmsAVFLHDDSPKPQF----EKKLAAFTGFESCLLCQSGWAANVGLLQTIAD 136
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 628601867 328 mmPGCEIYSDSGNHASMIQGIRNSRVPKYIFRHNDVNHLRELLQRSDPSvpkIVAFETVHSMDGAVCPLEELCDVAHEFG 407
Cdd:PRK07179 137 --PNTPVYIDFFAHMSLWEGVRAAGAQAHPFRHNDVDHLRRQIERHGPG---IIVVDSVYSTTGTIAPLADIVDIAEEFG 211
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 628601867 408 AITFVDEVHAVGLYGARGGGIGDRDGVMPKMDIISGTLGKAFGCVGGYIASTSLLIDTVR--SYAAgfIFTTSLPPMLLA 485
Cdd:PRK07179 212 CVLVVDESHSLGTHGPQGAGLVAELGLTSRVHFITASLAKAFAGRAGIITCPRELAEYVPfvSYPA--IFSSTLLPHEIA 289
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 628601867 486 GALESVRILKSSEGRalRRQHQRNVKLLRQMLMDAGLPvIHCPSHIIPVrVADAAKNTEIC-DELMTRhNIYVQAINYPT 564
Cdd:PRK07179 290 GLEATLEVIESADDR--RARLHANARFLREGLSELGYN-IRSESQIIAL-ETGSERNTEVLrDALEER-NVFGAVFCAPA 364
|
330 340 350 360
....*....|....*....|....*....|....*....|.
gi 628601867 565 VPRGEELLRIAPTPHHTPQMMNFFVEKLLVTWKRVGLELKP 605
Cdd:PRK07179 365 TPKNRNLIRLSLNADLTASDLDRVLEVCREARDEVDLWFWK 405
|
|
| PLN03227 |
PLN03227 |
serine palmitoyltransferase-like protein; Provisional |
249-555 |
4.33e-31 |
|
serine palmitoyltransferase-like protein; Provisional
Pssm-ID: 178766 [Multi-domain] Cd Length: 392 Bit Score: 125.40 E-value: 4.33e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 628601867 249 VWCSNDYLGMSRHPRVCGAVMETVKQHGAGAGGTRNISGTSKFHVELEQALADLHGKDAALLFSSCFVANDSTLFTLAKM 328
Cdd:PLN03227 2 NFATHDFLSTSSSPTLRQTALESLSHYGCGSCGPRGFYGTIDAHLELEQCMAEFLGTESAILYSDGASTTSSTVAAFAKR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 628601867 329 mpGCEIYSDSGNHASMIQGIRNSRVPKYIFRHNDVNHLRELL----------QRSDPSVPKIVAFETVHSMDGAVCPLEE 398
Cdd:PLN03227 82 --GDLLVVDRGVNEALLVGVSLSRANVRWFRHNDMKDLRRVLeqvraqdvalKRKPTDQRRFLVVEGLYKNTGTLAPLKE 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 628601867 399 LCDVAHEFGAITFVDEVHAVGLYGARGGGIGDRDGVMP--KMDIISGTLGKAFGCVGGYIASTSLLIDTVRSYAAGFIFT 476
Cdd:PLN03227 160 LVALKEEFHYRLILDESFSFGTLGKSGRGSLEHAGLKPmvHAEIVTFSLENAFGSVGGMTVGSEEVVDHQRLSGSGYCFS 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 628601867 477 TSLPPMLLAGALESVRILKSSEgRALRRQHQrNVKLLRQMLMDAGLPVIHCP-----------SHIIPVRVADAAKnTEI 545
Cdd:PLN03227 240 ASAPPFLAKADATATAGELAGP-QLLNRLHD-SIANLYSTLTNSSHPYALKLrnrlvitsdpiSPIIYLRLSDQEA-TRR 316
|
330
....*....|
gi 628601867 546 CDELMTRHNI 555
Cdd:PLN03227 317 TDETLILDQI 326
|
|
| PLN02822 |
PLN02822 |
serine palmitoyltransferase |
242-519 |
1.06e-27 |
|
serine palmitoyltransferase
Pssm-ID: 178417 [Multi-domain] Cd Length: 481 Bit Score: 116.76 E-value: 1.06e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 628601867 242 ITKKQVSVWCSNDYLGMSRHPRVCGAVMETVKQHGAGAGGTRNISGTSKFHVELEQALADLHGKDAALLFSSCFVANDST 321
Cdd:PLN02822 106 INGKDVVNFASANYLGLIGNEKIKESCTSALEKYGVGSCGPRGFYGTIDVHLDCETKIAKFLGTPDSILYSYGLSTIFSV 185
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 628601867 322 LFTLAKMmpGCEIYSDSGNHASMIQGIRNSRVPKYIFRHNDVNHLRELLQ-------RSDPSVPKIVAfETVHSMDGAVC 394
Cdd:PLN02822 186 IPAFCKK--GDIIVADEGVHWGIQNGLYLSRSTIVYFKHNDMESLRNTLEkltaenkRKKKLRRYIVV-EAIYQNSGQIA 262
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 628601867 395 PLEELCDVAHEFGAITFVDEVHAVGLYGARGGGIGDRDGVMP-KMDIISGTLGKAFGCVGGYIASTSLLIDTVRSYAAGF 473
Cdd:PLN02822 263 PLDEIVRLKEKYRFRVLLDESNSFGVLGKSGRGLSEHFGVPIeKIDIITAAMGHALATEGGFCTGSARVVDHQRLSSSGY 342
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 628601867 474 IFTTSLPPMLLAGALESVRILKssEGRALRRQHQRNVKLLRQMLMD 519
Cdd:PLN02822 343 VFSASLPPYLASAAITAIDVLE--DNPSVLAKLKENIALLHKGLSD 386
|
|
| PRK07505 |
PRK07505 |
hypothetical protein; Provisional |
251-583 |
5.08e-27 |
|
hypothetical protein; Provisional
Pssm-ID: 181006 [Multi-domain] Cd Length: 402 Bit Score: 113.54 E-value: 5.08e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 628601867 251 CSNDYLGMSRHPRVCGAVMETVKqhgagAGGTRNISgTSKFHV------ELEQALADLHGKDAaLLFSSCFVANDSTLFT 324
Cdd:PRK07505 52 VSCSYLGLDTHPAIIEGAVDALK-----RTGSLHLS-SSRTRVrsqilkDLEEALSELFGASV-LTFTSCSAAHLGILPL 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 628601867 325 LAK--MMPGCEIYS--DSGNHASM--IQGIRNSRVPKYIFRHNDVNHLRELLQRSdpsvpKIVAF--ETVHSMdGAVCPL 396
Cdd:PRK07505 125 LASghLTGGVPPHMvfDKNAHASLniLKGICADETEVETIDHNDLDALEDICKTN-----KTVAYvaDGVYSM-GGIAPV 198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 628601867 397 EELCDVAHEFGAITFVDEVHAVGLYGargggIGDRDGVMPKMD-------IISGTLGKAFGCVGGYIA-STSLLIDTVRS 468
Cdd:PRK07505 199 KELLRLQEKYGLFLYIDDAHGLSIYG-----KNGEGYVRSELDyrlnertIIAASLGKAFGASGGVIMlGDAEQIELILR 273
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 628601867 469 YAAGFIFTTSLPPMLLAGALESVRILKSSEGRALRRQHQRNVKLLRQMLMD--AGLPVihcpshiiPVRVA---DAAKNT 543
Cdd:PRK07505 274 YAGPLAFSQSLNVAALGAILASAEIHLSEELDQLQQKLQNNIALFDSLIPTeqSGSFL--------PIRLIyigDEDTAI 345
|
330 340 350 360
....*....|....*....|....*....|....*....|
gi 628601867 544 EICDELMTRhNIYVQAINYPTVPRGEELLRIAPTPHHTPQ 583
Cdd:PRK07505 346 KAAKQLLDR-GFYTSPVFFPVVAKGRAGLRIMFRASHTND 384
|
|
| PRK05937 |
PRK05937 |
8-amino-7-oxononanoate synthase; Provisional |
252-544 |
1.24e-21 |
|
8-amino-7-oxononanoate synthase; Provisional
Pssm-ID: 102071 [Multi-domain] Cd Length: 370 Bit Score: 97.16 E-value: 1.24e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 628601867 252 SNDYLGMSRHPRVCGAVMETVKQH-------GAGAGGTRNISGTSKFHVELEQALADLHGKDAALLFSSCFVANDSTLFT 324
Cdd:PRK05937 11 TNDFLGFSRSDTLVHEVEKRYRLYcrqfphaQLGYGGSRAILGPSSLLDDLEHKIAHFHGAPEAFIVPSGYMANLGLCAH 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 628601867 325 LAKMMPgcEIYSDSGNHASMIQGIRNSRVPKYIFRHNDVNHLRELLQ--RSDPSVPKIVAFETVHSMDGAVCPLEELCDV 402
Cdd:PRK05937 91 LSSVTD--YVLWDEQVHISVVYSLSVISGWHQSFRHNDLDHLESLLEscRQRSFGRIFIFVCSVYSFKGTLAPLEQIIAL 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 628601867 403 AHEFGAITFVDEVHAVGLYGARGGGIGDRDGVMPKMDIISgTLGKAFGCVGGYIASTSLLIDTVRSYAAGFIFTTSLPPM 482
Cdd:PRK05937 169 SKKYHAHLIVDEAHAMGIFGDDGKGFCHSLGYENFYAVLV-TYSKALGSMGAALLSSSEVKQDLMLNSPPLRYSTGLPPH 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 628601867 483 LLAGALESVRILkSSEGRALRRQ--------HQR-----------------NVKLLRQMLMDAGLPV-IHCPSHIIPVRV 536
Cdd:PRK05937 248 LLISIQVAYDFL-SQEGELARKQlfrlkeyfAQKfssaapgcvqpiflpgiSEQELYSKLVETGIRVgVVCFPTGPFLRV 326
|
....*...
gi 628601867 537 ADAAKNTE 544
Cdd:PRK05937 327 NLHAFNTE 334
|
|
| AAT_I |
cd01494 |
Aspartate aminotransferase (AAT) superfamily (fold type I) of pyridoxal phosphate (PLP) ... |
291-454 |
1.64e-12 |
|
Aspartate aminotransferase (AAT) superfamily (fold type I) of pyridoxal phosphate (PLP)-dependent enzymes. PLP combines with an alpha-amino acid to form a compound called a Schiff base or aldimine intermediate, which depending on the reaction, is the substrate in four kinds of reactions (1) transamination (movement of amino groups), (2) racemization (redistribution of enantiomers), (3) decarboxylation (removing COOH groups), and (4) various side-chain reactions depending on the enzyme involved. Pyridoxal phosphate (PLP) dependent enzymes were previously classified into alpha, beta and gamma classes, based on the chemical characteristics (carbon atom involved) of the reaction they catalyzed. The availability of several structures allowed a comprehensive analysis of the evolutionary classification of PLP dependent enzymes, and it was found that the functional classification did not always agree with the evolutionary history of these enzymes. Structure and sequence analysis has revealed that the PLP dependent enzymes can be classified into four major groups of different evolutionary origin: aspartate aminotransferase superfamily (fold type I), tryptophan synthase beta superfamily (fold type II), alanine racemase superfamily (fold type III), and D-amino acid superfamily (fold type IV) and Glycogen phophorylase family (fold type V).
Pssm-ID: 99742 [Multi-domain] Cd Length: 170 Bit Score: 65.87 E-value: 1.64e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 628601867 291 FHVELEQALADL--HGKDAALLFSSCFVANDSTLFTLAkmMPGCEIYSDSGNHAS--MIQGIRNSRVPKYIFRHNDVNHL 366
Cdd:cd01494 1 KLEELEEKLARLlqPGNDKAVFVPSGTGANEAALLALL--GPGDEVIVDANGHGSryWVAAELAGAKPVPVPVDDAGYGG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 628601867 367 RELLQRSD---PSVPKIVAFETVHSMDGAVCPLEELCDVAHEFGAITFVDEVHAVGLYGARGGGIGDRdgvmpKMDIISG 443
Cdd:cd01494 79 LDVAILEElkaKPNVALIVITPNTTSGGVLVPLKEIRKIAKEYGILLLVDAASAGGASPAPGVLIPEG-----GADVVTF 153
|
170
....*....|.
gi 628601867 444 TLGKAFGCVGG 454
Cdd:cd01494 154 SLHKNLGGEGG 164
|
|
| CsdA |
COG0520 |
Selenocysteine lyase/Cysteine desulfurase [Amino acid transport and metabolism]; |
254-419 |
4.01e-08 |
|
Selenocysteine lyase/Cysteine desulfurase [Amino acid transport and metabolism];
Pssm-ID: 223594 [Multi-domain] Cd Length: 405 Bit Score: 55.78 E-value: 4.01e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 628601867 254 DYLGMSRHPRVC-GAVMETVKQHGAGAGgtrniSGTSKFHVELEQALADLHGKDAALLFSS-----CFVANDST-LFTLA 326
Cdd:COG0520 27 DNAATSQKPQAVlDAVAEYYRRYNANVH-----RGAHTLAEEATDLYEAAREAVARFLNADssdeiVFTRGTTEaLNLVA 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 628601867 327 KMM-----PGCEIYSDSGNHASMI---------QGIRNSRVPkyiFRHNDVNHLRELLQRSDPSvPKIVAFETVHSMDGA 392
Cdd:COG0520 102 RGLgrslkPGDEIVVSDLEHHSNIvpwqelakrTGAKVRVIP---LDDDGLLDLDALEKLITPK-TKLVALSHVSNVTGT 177
|
170 180
....*....|....*....|....*..
gi 628601867 393 VCPLEELCDVAHEFGAITFVDEVHAVG 419
Cdd:COG0520 178 VNPVKEIAELAHEHGALVLVDAAQAAG 204
|
|
| CGS_like |
cd00614 |
CGS_like: Cystathionine gamma-synthase is a PLP dependent enzyme and catalyzes the committed ... |
292-413 |
2.73e-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: 2.73e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 628601867 292 HVELEQALADLHGKDAALLFSSCFVANDSTLFTLAK-----MMPGCeIYSDSGNHASMIQ---GIRNSRVPKyifrhNDV 363
Cdd:cd00614 42 VDALEKKLAALEGGEAALAFSSGMAAISTVLLALLKagdhvVASDD-LYGGTYRLFERLLpklGIEVTFVDP-----DDP 115
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 628601867 364 NHLRELLQRSdpsvPKIVAFETVHSMDGAVCPLEELCDVAHEFGAITFVD 413
Cdd:cd00614 116 EALEAAIKPE----TKLVYVESPTNPTLKVVDIEAIAELAHEHGALLVVD 161
|
|
| AAT_like |
cd00609 |
Aspartate aminotransferase family. This family belongs to pyridoxal phosphate (PLP)-dependent ... |
396-575 |
6.01e-07 |
|
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: 51.96 E-value: 6.01e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 628601867 396 LEELCDVAHEFGAITFVDEVHAvGLYGARGGGIGDRDGVMPKMDIISGTLGKAFGCVG---GY-IASTSLLIDTVRSYAa 471
Cdd:cd00609 154 LEELAELAKKHGILIISDEAYA-ELVYDGEPPPALALLDAYERVIVLRSFSKTFGLPGlriGYlIAPPEELLERLKKLL- 231
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 628601867 472 gfIFTTSLPPMLLAGALESVRILKSSEGRALRRQHQRNVKLLRQMLMDAGLPVIHCPS---HI-IPVRVADAAkntEICD 547
Cdd:cd00609 232 --PYTTSGPSTLSQAAAAAALDDGEEHLEELRERYRRRRDALLEALKELGPLVVVKPSggfFLwLDLPEGDDE---EFLE 306
|
170 180
....*....|....*....|....*...
gi 628601867 548 ELMTRHNIYVQAINYPtVPRGEELLRIA 575
Cdd:cd00609 307 RLLLEAGVVVRPGSAF-GEGGEGFVRLS 333
|
|
| HemL |
COG0001 |
Glutamate-1-semialdehyde aminotransferase [Coenzyme transport and metabolism]; |
357-524 |
2.66e-04 |
|
Glutamate-1-semialdehyde aminotransferase [Coenzyme transport and metabolism];
Pssm-ID: 223080 [Multi-domain] Cd Length: 432 Bit Score: 43.72 E-value: 2.66e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 628601867 357 IFRHNDVNHLRELLQRSDPSVPKIVaFETVHSMDGAVCP----LEELCDVAHEFGAITFVDEVH---------AVGLYGa 423
Cdd:COG0001 181 VLPYNDLEALEEAFEEYGDDIAAVI-VEPVAGNMGVVPPepgfLEGLRELTEEHGALLIFDEVItgfrvalggAQGYYG- 258
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 628601867 424 rgggigdrdgVMPkmDIIsgTLGKA------FGCVGGYIASTSLLIDTVRSYAAGfifTTSLPPMLLAGALESVRILKSS 497
Cdd:COG0001 259 ----------VEP--DLT--TLGKIiggglpIGAFGGRAEIMEQLAPLGPVYQAG---TLSGNPLAMAAGLATLEELMTE 321
|
170 180
....*....|....*....|....*....
gi 628601867 498 EG--RALRRQHQRNVKLLRQMLMDAGLPV 524
Cdd:COG0001 322 EGvyERLDALGERLAEGLRAAAERHGIPL 350
|
|
| Aminotran_5 |
pfam00266 |
Aminotransferase class-V; This domain is found in amino transferases, and other enzymes ... |
378-419 |
7.01e-03 |
|
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: 39.15 E-value: 7.01e-03
10 20 30 40
....*....|....*....|....*....|....*....|..
gi 628601867 378 PKIVAFETVHSMDGAVCPLEELCDVAHEFGAITFVDEVHAVG 419
Cdd:pfam00266 140 TKLVAITHVSNVTGTIQPVPEIGKLAHQYGALVLVDAAQAIG 181
|
|
|