SitesBLAST
Comparing WP_058929536.1 NCBI__GCF_001484605.1:WP_058929536.1 to proteins with known functional sites using BLASTp with E ≤ 0.001.
Or try Sites on a Tree, PaperBLAST, Conserved Domains, or compare to all protein structures
Found 20 (the maximum) hits to proteins with known functional sites (download)
Q96329 Acyl-coenzyme A oxidase 4, peroxisomal; AOX 4; G6p; Short-chain acyl-CoA oxidase; AtCX4; AtG6; SAOX; EC 1.3.3.6 from Arabidopsis thaliana (Mouse-ear cress) (see paper)
44% identity, 97% coverage: 9:394/396 of query aligns to 39:427/436 of Q96329
Sites not aligning to the query:
2ix6A Short chain specific acyl-coa oxidase from arabidopsis thaliana, acx4 (see paper)
44% identity, 97% coverage: 9:394/396 of query aligns to 23:411/416 of 2ix6A
- active site: L158 (= L140), T159 (= T141), S271 (≠ T254), E392 (= E375), R404 (= R387)
- binding flavin-adenine dinucleotide: T159 (= T141), G164 (= G146), S165 (= S147), W189 (= W172), N239 (= N222), R297 (= R280), F300 (= F283), L304 (= L287), F307 (= F290), N310 (≠ V293), E365 (≠ S348), L366 (= L349), G369 (= G352), I372 (= I355), Y391 (= Y374), T394 (= T377), D396 (≠ E379)
2ix5A Short chain specific acyl-coa oxidase from arabidopsis thaliana, acx4 in complex with acetoacetyl-coa (see paper)
44% identity, 97% coverage: 9:394/396 of query aligns to 23:411/415 of 2ix5A
- active site: L158 (= L140), T159 (= T141), S271 (≠ T254), E392 (= E375), R404 (= R387)
- binding acetoacetyl-coenzyme a: S165 (= S147), A167 (= A150), S168 (≠ G151), F261 (= F244), L268 (= L251), R272 (= R255), E392 (= E375), G393 (= G376), R404 (= R387)
- binding flavin-adenine dinucleotide: L158 (= L140), T159 (= T141), G164 (= G146), S165 (= S147), W189 (= W172), N239 (= N222), R297 (= R280), F300 (= F283), L304 (= L287), F307 (= F290), L309 (= L292), N310 (≠ V293), E365 (≠ S348), L366 (= L349), G368 (= G351), G369 (= G352), Y391 (= Y374), T394 (= T377), D396 (≠ E379), I397 (= I380)
2ebaA Crystal structure of the putative glutaryl-coa dehydrogenase from thermus thermophilus
37% identity, 96% coverage: 17:395/396 of query aligns to 3:380/380 of 2ebaA
- active site: L131 (= L140), T132 (= T141), A239 (≠ T254), E360 (= E375), R372 (= R387)
- binding flavin-adenine dinucleotide: L131 (= L140), T132 (= T141), G136 (= G145), G137 (= G146), S138 (= S147), W161 (= W172), T163 (≠ G174), R265 (= R280), L272 (= L287), K275 (≠ F290), D333 (≠ S348), I334 (≠ L349), G337 (= G352), T355 (≠ A370), T358 (≠ S373), Y359 (= Y374), T362 (= T377)
3sf6A Crystal structure of glutaryl-coa dehydrogenase from mycobacterium smegmatis (see paper)
35% identity, 95% coverage: 17:394/396 of query aligns to 6:385/387 of 3sf6A
- active site: L134 (= L140), T135 (= T141), A245 (≠ T254), E366 (= E375), Q378 (≠ R387)
- binding dihydroflavine-adenine dinucleotide: F132 (= F138), L134 (= L140), T135 (= T141), G140 (= G146), S141 (= S147), W165 (= W172), I166 (= I173), T167 (≠ G174), S361 (≠ A370), T364 (≠ S373), Y365 (= Y374), T368 (= T377), E370 (= E379), M371 (≠ I380)
2r0nA The effect of a glu370asp mutation in glutaryl-coa dehydrogenase on proton transfer to the dienolate intermediate (see paper)
33% identity, 95% coverage: 17:394/396 of query aligns to 6:387/390 of 2r0nA
- active site: L133 (= L140), T134 (= T141), A247 (≠ T254), E368 (= E375), R380 (= R387)
- binding flavin-adenine dinucleotide: F131 (= F138), L133 (= L140), T134 (= T141), G139 (= G146), S140 (= S147), W166 (= W172), I167 (= I173), T168 (≠ G174), Y367 (= Y374), T370 (= T377), D372 (≠ E379)
- binding 3-thiaglutaryl-CoA: R92 (≠ A99), S93 (≠ T100), V97 (= V104), P142 (≠ V149), G238 (≠ R245), F241 (≠ N248), L244 (= L251), N245 (≠ K252), P318 (≠ D325), Y367 (= Y374), E368 (= E375), I377 (≠ V384)
1sirA The crystal structure and mechanism of human glutaryl-coa dehydrogenase (see paper)
33% identity, 95% coverage: 17:394/396 of query aligns to 6:387/390 of 1sirA
- active site: L133 (= L140), T134 (= T141), A247 (≠ T254), E368 (= E375), R380 (= R387)
- binding flavin-adenine dinucleotide: F131 (= F138), L133 (= L140), T134 (= T141), G139 (= G146), S140 (= S147), W166 (= W172), I167 (= I173), T168 (≠ G174), Y367 (= Y374), T370 (= T377)
- binding s-4-nitrobutyryl-coa: S93 (≠ T100), S140 (= S147), F241 (≠ N248), G242 (≠ K249), L244 (= L251), N245 (≠ K252), R248 (= R255), P318 (≠ D325), Y367 (= Y374), E368 (= E375), R380 (= R387)
2r0mA The effect of a glu370asp mutation in glutaryl-coa dehydrogenase on proton transfer to the dienolate intermediate (see paper)
33% identity, 95% coverage: 17:394/396 of query aligns to 6:387/390 of 2r0mA
- active site: L133 (= L140), T134 (= T141), A247 (≠ T254), D368 (≠ E375), R380 (= R387)
- binding 4-nitrobutanoic acid: L101 (= L108), Y367 (= Y374), D368 (≠ E375)
- binding flavin-adenine dinucleotide: F131 (= F138), L133 (= L140), T134 (= T141), G139 (= G146), S140 (= S147), W166 (= W172), I167 (= I173), T168 (≠ G174), L210 (= L217), Y367 (= Y374), T370 (= T377)
3swoA Crystal structure of a glutaryl-coa dehydrogenase from mycobacterium smegmatis in complex with fadh2 (see paper)
32% identity, 97% coverage: 13:395/396 of query aligns to 4:387/388 of 3swoA
- active site: L135 (= L140), T136 (= T141), A246 (≠ T254), E367 (= E375), K379 (≠ R387)
- binding dihydroflavine-adenine dinucleotide: F133 (= F138), L135 (= L140), T136 (= T141), G141 (= G146), S142 (= S147), W166 (= W172), I167 (= I173), T168 (≠ G174), R272 (= R280), V274 (≠ Q282), F275 (= F283), L279 (= L287), Y282 (≠ F290), T340 (≠ S348), L341 (= L349), G344 (= G352), I347 (= I355), T365 (≠ S373), Y366 (= Y374), T369 (= T377), E371 (= E379), M372 (≠ I380)
3eonC 2.55a crystal structure of native glutaryl-coa dehydrogenase from burkholderia pseudomallei in complex with a small molecule (see paper)
31% identity, 84% coverage: 64:394/396 of query aligns to 54:382/382 of 3eonC
3gncA Crystal structure of glutaryl-coa dehydrogenase from burkholderia pseudomallei with fragment 6421 (see paper)
31% identity, 84% coverage: 64:394/396 of query aligns to 55:380/380 of 3gncA
3gqtC Crystal structure of glutaryl-coa dehydrogenase from burkholderia pseudomallei with fragment (1,4-dimethyl-1,2,3,4- tetrahydroquinoxalin-6-yl)methylamine (see paper)
31% identity, 84% coverage: 64:394/396 of query aligns to 54:384/385 of 3gqtC
- active site: L135 (= L140), T136 (= T141), A250 (≠ T254), E365 (= E375), R377 (= R387)
- binding 1-(1,4-dimethyl-1,2,3,4-tetrahydroquinoxalin-6-yl)methanamine: W166 (= W172), K210 (= K214), L213 (= L217), T218 (≠ N222), Y364 (= Y374)
1jqiA Crystal structure of rat short chain acyl-coa dehydrogenase complexed with acetoacetyl-coa (see paper)
32% identity, 88% coverage: 36:384/396 of query aligns to 18:374/384 of 1jqiA
- binding acetoacetyl-coenzyme a: L95 (= L108), F125 (= F138), S134 (= S147), F234 (= F244), M238 (≠ N248), Q239 (≠ K249), L241 (= L251), D242 (≠ K252), R245 (= R255), Y364 (= Y374), E365 (= E375), G366 (= G376)
- binding flavin-adenine dinucleotide: F125 (= F138), L127 (= L140), S128 (≠ T141), G133 (= G146), S134 (= S147), W158 (= W172), T160 (≠ G174), R270 (= R280), F273 (= F283), L280 (≠ F290), Q338 (≠ S348), I339 (≠ L349), G342 (= G352), I360 (≠ A370), T367 (= T377), E369 (= E379), I370 (= I380)
Sites not aligning to the query:
P15651 Short-chain specific acyl-CoA dehydrogenase, mitochondrial; SCAD; Butyryl-CoA dehydrogenase; EC 1.3.8.1 from Rattus norvegicus (Rat) (see 2 papers)
32% identity, 88% coverage: 36:384/396 of query aligns to 45:401/412 of P15651
- 152:161 (vs. 138:147, 60% identical) binding FAD
- S161 (= S147) binding substrate
- WIT 185:187 (≠ WIG 172:174) binding FAD
- DMGR 269:272 (≠ KVTR 252:255) binding substrate
- R297 (= R280) binding FAD
- QILGG 365:369 (≠ SLLGG 348:352) binding FAD
- E392 (= E375) active site, Proton acceptor
- TSE 394:396 (≠ THE 377:379) binding FAD
Sites not aligning to the query:
- 1:24 modified: transit peptide, Mitochondrion
8sgsA Human liver mitochondrial short-chain specific acyl-coa dehydrogenase (see paper)
32% identity, 91% coverage: 25:384/396 of query aligns to 4:371/381 of 8sgsA
- binding coenzyme a: S131 (= S147), A133 (= A150), N177 (≠ D191), F231 (= F244), M235 (≠ N248), L238 (= L251), I312 (≠ D325), E362 (= E375), G363 (= G376)
- binding flavin-adenine dinucleotide: F122 (= F138), L124 (= L140), S125 (≠ T141), G130 (= G146), S131 (= S147), W155 (= W172), T157 (≠ G174), R267 (= R280), F270 (= F283), L274 (= L287), L277 (≠ F290), Q335 (≠ S348), I336 (≠ L349), G338 (= G351), G339 (= G352), I357 (≠ A370), I360 (≠ S373), Y361 (= Y374), T364 (= T377), E366 (= E379)
7y0bA Crystal structure of human short-chain acyl-coa dehydrogenase
32% identity, 91% coverage: 25:384/396 of query aligns to 7:374/385 of 7y0bA
- binding (2S,3R,4R,5S,6R)-2-[4-chloranyl-3-[[4-[(3S)-oxolan-3-yl]oxyphenyl]methyl]phenyl]-6-(hydroxymethyl)oxane-3,4,5-triol: M343 (≠ N353), T347 (= T357), E348 (≠ D358)
- binding flavin-adenine dinucleotide: F125 (= F138), L127 (= L140), S128 (≠ T141), G133 (= G146), S134 (= S147), W158 (= W172), T160 (≠ G174), R270 (= R280), F273 (= F283), L280 (≠ F290), V282 (≠ L292), Q338 (≠ S348), I339 (≠ L349), G342 (= G352), I360 (≠ A370), Y364 (= Y374), T367 (= T377), E369 (= E379), I370 (= I380), L373 (= L383)
P16219 Short-chain specific acyl-CoA dehydrogenase, mitochondrial; SCAD; Butyryl-CoA dehydrogenase; EC 1.3.8.1 from Homo sapiens (Human) (see 3 papers)
32% identity, 91% coverage: 25:384/396 of query aligns to 34:401/412 of P16219
- G90 (≠ R76) to S: in ACADSD; loss of acyl-CoA dehydrogenase activity; dbSNP:rs121908005
- E104 (= E90) natural variant: Missing (in ACADSD; loss of acyl-CoA dehydrogenase activity; dbSNP:rs387906308)
- 152:161 (vs. 138:147, 60% identical) binding in other chain
- R171 (≠ Q158) to W: 69% of wild-type acyl-CoA dehydrogenase activity; confers susceptibility to ethylmalonicaciduria; dbSNP:rs1800556
- WIT 185:187 (≠ WIG 172:174) binding in other chain
- A192 (≠ S179) to V: in ACADSD; loss of acyl-CoA dehydrogenase activity; dbSNP:rs28940874
- G209 (≠ Q193) to S: 86% of wild-type acyl-CoA dehydrogenase activity; confers susceptibility to ethylmalonicaciduria; dbSNP:rs1799958
- R297 (= R280) binding FAD
- Q308 (= Q291) binding in other chain
- R325 (≠ M308) to W: in ACADSD; loss of acyl-CoA dehydrogenase activity; dbSNP:rs121908006
- S353 (≠ M339) to L: in ACADSD; loss of acyl-CoA dehydrogenase activity; dbSNP:rs28941773
- QILGG 365:369 (≠ SLLGG 348:352) binding FAD
- R380 (≠ K363) to W: in ACADSD; loss of acyl-CoA dehydrogenase activity; dbSNP:rs28940875
- TSE 394:396 (≠ THE 377:379) binding in other chain
Sites not aligning to the query:
- 1:24 modified: transit peptide, Mitochondrion
7y0aC Crystal structure of human short-chain acyl-coa dehydrogenase
32% identity, 91% coverage: 25:384/396 of query aligns to 10:377/387 of 7y0aC
- binding flavin-adenine dinucleotide: F128 (= F138), L130 (= L140), S131 (≠ T141), G136 (= G146), S137 (= S147), W161 (= W172), T163 (≠ G174), T214 (≠ N222), R273 (= R280), F276 (= F283), L280 (= L287), L283 (≠ F290), V285 (≠ L292), Q341 (≠ S348), I342 (≠ L349), G345 (= G352), I363 (≠ A370), Y367 (= Y374), T370 (= T377), E372 (= E379), L376 (= L383)
1ukwB Crystal structure of medium-chain acyl-coa dehydrogenase from thermus thermophilus hb8
32% identity, 92% coverage: 25:389/396 of query aligns to 5:376/379 of 1ukwB
- active site: L124 (= L140), S125 (≠ T141), T241 (= T254), E362 (= E375), R374 (= R387)
- binding cobalt (ii) ion: D145 (= D162), H146 (≠ T163)
- binding flavin-adenine dinucleotide: F122 (= F138), L124 (= L140), S125 (≠ T141), G130 (= G146), S131 (= S147), W155 (= W172), S157 (≠ G174), K200 (= K214), L357 (≠ A370), Y361 (= Y374), E362 (= E375), T364 (= T377), E366 (= E379), L370 (= L383)
1ukwA Crystal structure of medium-chain acyl-coa dehydrogenase from thermus thermophilus hb8
32% identity, 92% coverage: 25:389/396 of query aligns to 5:376/379 of 1ukwA
- active site: L124 (= L140), S125 (≠ T141), T241 (= T254), E362 (= E375), R374 (= R387)
- binding flavin-adenine dinucleotide: F122 (= F138), L124 (= L140), S125 (≠ T141), G130 (= G146), S131 (= S147), W155 (= W172), S157 (≠ G174), L357 (≠ A370), Y361 (= Y374), E362 (= E375), T364 (= T377), E366 (= E379), L370 (= L383)
Query Sequence
>WP_058929536.1 NCBI__GCF_001484605.1:WP_058929536.1
MSKASVDINNLPYADGDFFAFEQLLTAKEQDRLAEIRGFLAREVRPIAVDCWNRGEFPME
LIPKLAEIDLVSPVRRQGYSNLFAGLVHAEATRADTSIATFMGVHDGLFAGSIEALASQE
QQDAWLPDIYSLKKIGAFGLTEPLGGSDVAGGTRTTAQRNGDTWILNGAKRWIGNATFSD
WVVVYARDLADNQVKGFLVDTALPGFSATKIENKISLRTVQNADIVLENVVVPDFFKLAG
ANSFRDTNKVLKVTRLSVGWQAVGQQLAAFDVARRYAVERHQFGRPLASFQLVQSQLVQI
LGNAVSSMGMMVRLSQLEDAGQAKDEQSALAKAFTTARMRESVAIGRSLLGGNGIVTDFE
MAKIFADAEAIYSYEGTHEINTLVTGRAITGISAIV
Or try a new SitesBLAST search
SitesBLAST's Database
SitesBLAST's database includes
(1) SwissProt
entries with experimentally-supported functional features;
and (2) protein structures with bound ligands, from the
BioLip database.
by Morgan Price,
Arkin group
Lawrence Berkeley National Laboratory