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Comparing WP_015927965.1 NCBI__GCF_000022085.1:WP_015927965.1 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)
2r0nA The effect of a glu370asp mutation in glutaryl-coa dehydrogenase on proton transfer to the dienolate intermediate (see paper)
67% identity, 94% coverage: 25:412/413 of query aligns to 2:388/390 of 2r0nA
- active site: L133 (= L157), T134 (= T158), A247 (= A271), E368 (= E392), R380 (= R404)
- binding flavin-adenine dinucleotide: F131 (= F155), L133 (= L157), T134 (= T158), G139 (= G163), S140 (= S164), W166 (= W188), I167 (= I189), T168 (≠ S190), Y367 (= Y391), T370 (= T394), D372 (= D396)
- binding 3-thiaglutaryl-CoA: R92 (= R116), S93 (= S117), V97 (= V121), P142 (= P166), G238 (≠ K262), F241 (= F265), L244 (= L268), N245 (= N269), P318 (= P342), Y367 (= Y391), E368 (= E392), I377 (= I401)
1sirA The crystal structure and mechanism of human glutaryl-coa dehydrogenase (see paper)
67% identity, 94% coverage: 25:412/413 of query aligns to 2:388/390 of 1sirA
- active site: L133 (= L157), T134 (= T158), A247 (= A271), E368 (= E392), R380 (= R404)
- binding flavin-adenine dinucleotide: F131 (= F155), L133 (= L157), T134 (= T158), G139 (= G163), S140 (= S164), W166 (= W188), I167 (= I189), T168 (≠ S190), Y367 (= Y391), T370 (= T394)
- binding s-4-nitrobutyryl-coa: S93 (= S117), S140 (= S164), F241 (= F265), G242 (= G266), L244 (= L268), N245 (= N269), R248 (= R272), P318 (= P342), Y367 (= Y391), E368 (= E392), R380 (= R404)
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)
67% identity, 94% coverage: 25:412/413 of query aligns to 3:385/385 of 3gqtC
- active site: L135 (= L157), T136 (= T158), A250 (= A271), E365 (= E392), R377 (= R404)
- binding 1-(1,4-dimethyl-1,2,3,4-tetrahydroquinoxalin-6-yl)methanamine: W166 (= W188), K210 (= K231), L213 (= L234), T218 (= T239), Y364 (= Y391)
2r0mA The effect of a glu370asp mutation in glutaryl-coa dehydrogenase on proton transfer to the dienolate intermediate (see paper)
67% identity, 94% coverage: 25:412/413 of query aligns to 2:388/390 of 2r0mA
- active site: L133 (= L157), T134 (= T158), A247 (= A271), D368 (≠ E392), R380 (= R404)
- binding 4-nitrobutanoic acid: L101 (= L125), Y367 (= Y391), D368 (≠ E392)
- binding flavin-adenine dinucleotide: F131 (= F155), L133 (= L157), T134 (= T158), G139 (= G163), S140 (= S164), W166 (= W188), I167 (= I189), T168 (≠ S190), L210 (= L234), Y367 (= Y391), T370 (= T394)
3gncA Crystal structure of glutaryl-coa dehydrogenase from burkholderia pseudomallei with fragment 6421 (see paper)
66% identity, 94% coverage: 25:411/413 of query aligns to 4:380/380 of 3gncA
3eonC 2.55a crystal structure of native glutaryl-coa dehydrogenase from burkholderia pseudomallei in complex with a small molecule (see paper)
66% identity, 94% coverage: 25:411/413 of query aligns to 3:382/382 of 3eonC
3d6bC 2.2 a crystal structure of glutaryl-coa dehydrogenase from burkholderia pseudomallei (see paper)
65% identity, 94% coverage: 25:411/413 of query aligns to 3:377/377 of 3d6bC
2ebaA Crystal structure of the putative glutaryl-coa dehydrogenase from thermus thermophilus
53% identity, 93% coverage: 29:412/413 of query aligns to 3:380/380 of 2ebaA
- active site: L131 (= L157), T132 (= T158), A239 (= A271), E360 (= E392), R372 (= R404)
- binding flavin-adenine dinucleotide: L131 (= L157), T132 (= T158), G136 (≠ A162), G137 (= G163), S138 (= S164), W161 (= W188), T163 (≠ S190), R265 (= R297), L272 (= L304), K275 (≠ T307), D333 (= D365), I334 (≠ M366), G337 (= G369), T355 (= T387), T358 (= T390), Y359 (= Y391), T362 (= T394)
3sf6A Crystal structure of glutaryl-coa dehydrogenase from mycobacterium smegmatis (see paper)
52% identity, 95% coverage: 22:412/413 of query aligns to 2:386/387 of 3sf6A
- active site: L134 (= L157), T135 (= T158), A245 (= A271), E366 (= E392), Q378 (≠ R404)
- binding dihydroflavine-adenine dinucleotide: F132 (= F155), L134 (= L157), T135 (= T158), G140 (= G163), S141 (= S164), W165 (= W188), I166 (= I189), T167 (≠ S190), S361 (≠ T387), T364 (= T390), Y365 (= Y391), T368 (= T394), E370 (≠ D396), M371 (≠ V397)
3swoA Crystal structure of a glutaryl-coa dehydrogenase from mycobacterium smegmatis in complex with fadh2 (see paper)
48% identity, 92% coverage: 35:412/413 of query aligns to 13:387/388 of 3swoA
- active site: L135 (= L157), T136 (= T158), A246 (= A271), E367 (= E392), K379 (≠ R404)
- binding dihydroflavine-adenine dinucleotide: F133 (= F155), L135 (= L157), T136 (= T158), G141 (= G163), S142 (= S164), W166 (= W188), I167 (= I189), T168 (≠ S190), R272 (= R297), V274 (≠ Q299), F275 (= F300), L279 (= L304), Y282 (≠ T307), T340 (≠ D365), L341 (≠ M366), G344 (= G369), I347 (= I372), T365 (= T390), Y366 (= Y391), T369 (= T394), E371 (≠ D396), M372 (≠ V397)
2ix5A Short chain specific acyl-coa oxidase from arabidopsis thaliana, acx4 in complex with acetoacetyl-coa (see paper)
34% identity, 100% coverage: 1:412/413 of query aligns to 10:412/415 of 2ix5A
- active site: L158 (= L157), T159 (= T158), S271 (≠ A271), E392 (= E392), R404 (= R404)
- binding acetoacetyl-coenzyme a: S165 (= S164), A167 (≠ P166), S168 (≠ G167), F261 (≠ L261), L268 (= L268), R272 (= R272), E392 (= E392), G393 (= G393), R404 (= R404)
- binding flavin-adenine dinucleotide: L158 (= L157), T159 (= T158), G164 (= G163), S165 (= S164), W189 (= W188), N239 (≠ T239), R297 (= R297), F300 (= F300), L304 (= L304), F307 (≠ T307), L309 (= L309), N310 (≠ V310), E365 (≠ D365), L366 (≠ M366), G368 (= G368), G369 (= G369), Y391 (= Y391), T394 (= T394), D396 (= D396), I397 (≠ V397)
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)
34% identity, 100% coverage: 1:412/413 of query aligns to 26:428/436 of Q96329
2ix6A Short chain specific acyl-coa oxidase from arabidopsis thaliana, acx4 (see paper)
34% identity, 100% coverage: 1:412/413 of query aligns to 10:412/416 of 2ix6A
- active site: L158 (= L157), T159 (= T158), S271 (≠ A271), E392 (= E392), R404 (= R404)
- binding flavin-adenine dinucleotide: T159 (= T158), G164 (= G163), S165 (= S164), W189 (= W188), N239 (≠ T239), R297 (= R297), F300 (= F300), L304 (= L304), F307 (≠ T307), N310 (≠ V310), E365 (≠ D365), L366 (≠ M366), G369 (= G369), I372 (= I372), Y391 (= Y391), T394 (= T394), D396 (= D396)
5lnxD Crystal structure of mmgc, an acyl-coa dehydrogenase from bacillus subtilis.
35% identity, 88% coverage: 40:404/413 of query aligns to 5:370/374 of 5lnxD
- active site: L122 (= L157), T123 (= T158), G239 (≠ A271), E358 (= E392), K370 (≠ R404)
- binding flavin-adenine dinucleotide: L122 (= L157), T123 (= T158), G128 (= G163), S129 (= S164), F153 (≠ W188), T155 (≠ S190), R265 (= R297), Q267 (= Q299), F268 (= F300), I272 (≠ L304), N275 (≠ T307), I278 (≠ V310), Q331 (≠ D365), I332 (≠ M366), G335 (= G369), Y357 (= Y391), T360 (= T394), E362 (≠ D396)
4l1fA Electron transferring flavoprotein of acidaminococcus fermentans: towards a mechanism of flavin-based electron bifurcation (see paper)
35% identity, 90% coverage: 33:405/413 of query aligns to 1:376/380 of 4l1fA
- active site: L125 (= L157), T126 (= T158), G242 (≠ A271), E363 (= E392), R375 (= R404)
- binding coenzyme a persulfide: T132 (≠ S164), H179 (≠ N209), F232 (≠ L261), M236 (≠ F265), E237 (≠ G266), L239 (= L268), D240 (≠ N269), R243 (= R272), Y362 (= Y391), E363 (= E392), G364 (= G393), R375 (= R404)
- binding flavin-adenine dinucleotide: F123 (= F155), L125 (= L157), T126 (= T158), G131 (= G163), T132 (≠ S164), F156 (≠ W188), I157 (= I189), T158 (≠ S190), R268 (= R297), Q270 (= Q299), F271 (= F300), I275 (≠ L304), F278 (≠ T307), L281 (≠ V310), Q336 (≠ D365), I337 (≠ M366), G340 (= G369), I358 (≠ T387), Y362 (= Y391), T365 (= T394), Q367 (≠ D396)
- binding 1,3-propandiol: L5 (= L37), Q10 (≠ R42)
4n5fA Crystal structure of a putative acyl-coa dehydrogenase with bound fadh2 from burkholderia cenocepacia j2315
34% identity, 90% coverage: 33:404/413 of query aligns to 2:376/378 of 4n5fA
- active site: L126 (= L157), T127 (= T158), G243 (≠ A271), E364 (= E392), R376 (= R404)
- binding dihydroflavine-adenine dinucleotide: L126 (= L157), T127 (= T158), G132 (= G163), S133 (= S164), F157 (≠ W188), T159 (≠ S190), T210 (= T239), Y363 (= Y391), T366 (= T394), E368 (≠ D396), M372 (≠ L400)
2dvlA Crystal structure of project tt0160 from thermus thermophilus hb8
35% identity, 89% coverage: 37:404/413 of query aligns to 1:366/370 of 2dvlA
- active site: L121 (= L157), T122 (= T158), G233 (≠ A271), E354 (= E392), R366 (= R404)
- binding flavin-adenine dinucleotide: L121 (= L157), T122 (= T158), G127 (= G163), S128 (= S164), W152 (= W188), I153 (= I189), T154 (≠ S190), T356 (= T394), E358 (≠ D396)
5ol2F The electron transferring flavoprotein/butyryl-coa dehydrogenase complex from clostridium difficile (see paper)
32% identity, 87% coverage: 42:402/413 of query aligns to 9:372/378 of 5ol2F
- active site: L124 (= L157), T125 (= T158), G241 (≠ A271)
- binding calcium ion: E29 (= E62), E33 (= E66), R35 (≠ K68)
- binding coenzyme a persulfide: L238 (= L268), R242 (= R272), E362 (= E392), G363 (= G393)
- binding flavin-adenine dinucleotide: F122 (= F155), L124 (= L157), T125 (= T158), P127 (= P160), T131 (≠ S164), F155 (≠ W188), I156 (= I189), T157 (≠ S190), E198 (≠ K229), R267 (= R297), F270 (= F300), L274 (= L304), F277 (≠ T307), Q335 (≠ D365), L336 (≠ M366), G338 (= G368), G339 (= G369), Y361 (= Y391), T364 (= T394), E366 (≠ D396)
Sites not aligning to the query:
P26440 Isovaleryl-CoA dehydrogenase, mitochondrial; IVD; Butyryl-CoA dehydrogenase; EC 1.3.8.4; EC 1.3.8.1 from Homo sapiens (Human) (see 5 papers)
32% identity, 89% coverage: 37:405/413 of query aligns to 45:420/426 of P26440
- 165:174 (vs. 155:164, 50% identical) binding FAD
- S174 (= S164) binding substrate
- WIT 198:200 (≠ WIS 188:190) binding FAD
- SR 222:223 (≠ DN 208:209) binding substrate
- G250 (≠ A236) to A: in IVA; uncertain significance
- Y277 (≠ K262) binding substrate
- DLER 284:287 (≠ NRAR 269:272) binding substrate
- E286 (≠ A271) active site, Proton acceptor; mutation to D: Residual isovaleryl-CoA dehydrogenase activity.; mutation to G: Loss of isovaleryl-CoA dehydrogenase activity. Does not affect isovaleryl-CoA dehydrogenase activity; when associated with 407-E.; mutation to Q: Loss of isovaleryl-CoA dehydrogenase activity.
- A291 (≠ S276) to V: in IVA; uncertain significance; dbSNP:rs886042098
- R312 (= R297) binding FAD
- Q323 (= Q308) binding FAD
- I379 (≠ R364) to T: in IVA; uncertain significance
- QCFGG 380:384 (≠ DMHGG 365:369) binding FAD
- R398 (≠ Q383) to Q: in IVA; uncertain significance; dbSNP:rs1477527791
- Y403 (≠ V388) to N: in IVA; uncertain significance
- A407 (≠ E392) mutation to E: Does not affect isovaleryl-CoA dehydrogenase activity; when associated with 286-D.
- AG 407:408 (≠ EG 392:393) binding substrate
- TSE 409:411 (≠ THD 394:396) binding FAD
Sites not aligning to the query:
- 1:32 modified: transit peptide, Mitochondrion
8sgrA Human liver mitochondrial isovaleryl-coa dehydrogenase (see paper)
32% identity, 89% coverage: 37:405/413 of query aligns to 12:387/393 of 8sgrA
- binding flavin-adenine dinucleotide: S135 (≠ T158), G140 (= G163), S141 (= S164), W165 (= W188), T167 (≠ S190), R279 (= R297), F282 (= F300), I286 (≠ L304), F289 (≠ T307), Q347 (≠ D365), C348 (≠ M366), G351 (= G369), L369 (≠ T387), G375 (= G393), T376 (= T394), L382 (= L400)
Query Sequence
>WP_015927965.1 NCBI__GCF_000022085.1:WP_015927965.1
MTAASAAPQTSPSAARPQEGSRGAFRWDDPFLLEDQLTDEERLIRDTARSFAVERLLPGI
VEAYAEEKTDRNLFNAMGELGLLGVTLPEEYGCAGASYVAYGLVAREVERVDSGYRSMMS
VQSSLVMYPIYAYGDETQRKTYLPGLASGELVGCFGLTEPDAGSDPGGMKTRAKKIDGGY
LLSGVKTWISNAPIADVFVVWAKSAAHDNQIRGFILEKGMKGLSAPKIKGKLSLRASVTG
EIVMDGVEVPESALLPNVSGLKGPFGCLNRARYGISWGAMGAAEDCWHRARQYTLDRTQF
GRPLAQTQLVQRKLADMQTEIALGLQASLRVGRLFDEGRVAPEMISIVKRNNCGKALAIA
REARDMHGGNGIMGEYHVMRHAQNLETVNTYEGTHDVHALILGRAQTGLQAFF
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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