SitesBLAST
Comparing WP_057509244.1 NCBI__GCF_001431535.1:WP_057509244.1 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)
2ebaA Crystal structure of the putative glutaryl-coa dehydrogenase from thermus thermophilus
55% identity, 98% coverage: 7:387/387 of query aligns to 3:380/380 of 2ebaA
- active site: L131 (= L135), T132 (= T136), A239 (= A246), E360 (= E367), R372 (= R379)
- binding flavin-adenine dinucleotide: L131 (= L135), T132 (= T136), G136 (= G140), G137 (= G141), S138 (= S142), W161 (= W166), T163 (= T168), R265 (= R272), L272 (= L279), K275 (≠ T282), D333 (= D340), I334 (≠ L341), G337 (≠ A344), T355 (≠ S362), T358 (= T365), Y359 (= Y366), T362 (= T369)
3sf6A Crystal structure of glutaryl-coa dehydrogenase from mycobacterium smegmatis (see paper)
54% identity, 98% coverage: 7:387/387 of query aligns to 6:386/387 of 3sf6A
- active site: L134 (= L135), T135 (= T136), A245 (= A246), E366 (= E367), Q378 (≠ R379)
- binding dihydroflavine-adenine dinucleotide: F132 (= F133), L134 (= L135), T135 (= T136), G140 (= G141), S141 (= S142), W165 (= W166), I166 (= I167), T167 (= T168), S361 (= S362), T364 (= T365), Y365 (= Y366), T368 (= T369), E370 (≠ T371), M371 (≠ V372)
3swoA Crystal structure of a glutaryl-coa dehydrogenase from mycobacterium smegmatis in complex with fadh2 (see paper)
52% identity, 99% coverage: 5:387/387 of query aligns to 6:387/388 of 3swoA
- active site: L135 (= L135), T136 (= T136), A246 (= A246), E367 (= E367), K379 (≠ R379)
- binding dihydroflavine-adenine dinucleotide: F133 (= F133), L135 (= L135), T136 (= T136), G141 (= G141), S142 (= S142), W166 (= W166), I167 (= I167), T168 (= T168), R272 (= R272), V274 (≠ L274), F275 (= F275), L279 (= L279), Y282 (≠ T282), T340 (≠ D340), L341 (= L341), G344 (≠ A344), I347 (= I347), T365 (= T365), Y366 (= Y366), T369 (= T369), E371 (≠ T371), M372 (≠ V372)
2r0nA The effect of a glu370asp mutation in glutaryl-coa dehydrogenase on proton transfer to the dienolate intermediate (see paper)
51% identity, 96% coverage: 15:387/387 of query aligns to 14:388/390 of 2r0nA
- active site: L133 (= L135), T134 (= T136), A247 (= A246), E368 (= E367), R380 (= R379)
- binding flavin-adenine dinucleotide: F131 (= F133), L133 (= L135), T134 (= T136), G139 (= G141), S140 (= S142), W166 (= W166), I167 (= I167), T168 (= T168), Y367 (= Y366), T370 (= T369), D372 (≠ T371)
- binding 3-thiaglutaryl-CoA: R92 (= R94), S93 (= S95), V97 (= V99), P142 (= P144), G238 (≠ K237), F241 (≠ L240), L244 (= L243), N245 (= N244), P318 (= P317), Y367 (= Y366), E368 (= E367), I377 (≠ V376)
1sirA The crystal structure and mechanism of human glutaryl-coa dehydrogenase (see paper)
51% identity, 96% coverage: 15:387/387 of query aligns to 14:388/390 of 1sirA
- active site: L133 (= L135), T134 (= T136), A247 (= A246), E368 (= E367), R380 (= R379)
- binding flavin-adenine dinucleotide: F131 (= F133), L133 (= L135), T134 (= T136), G139 (= G141), S140 (= S142), W166 (= W166), I167 (= I167), T168 (= T168), Y367 (= Y366), T370 (= T369)
- binding s-4-nitrobutyryl-coa: S93 (= S95), S140 (= S142), F241 (≠ L240), G242 (= G241), L244 (= L243), N245 (= N244), R248 (= R247), P318 (= P317), Y367 (= Y366), E368 (= E367), R380 (= R379)
2r0mA The effect of a glu370asp mutation in glutaryl-coa dehydrogenase on proton transfer to the dienolate intermediate (see paper)
51% identity, 96% coverage: 15:387/387 of query aligns to 14:388/390 of 2r0mA
- active site: L133 (= L135), T134 (= T136), A247 (= A246), D368 (≠ E367), R380 (= R379)
- binding 4-nitrobutanoic acid: L101 (= L103), Y367 (= Y366), D368 (≠ E367)
- binding flavin-adenine dinucleotide: F131 (= F133), L133 (= L135), T134 (= T136), G139 (= G141), S140 (= S142), W166 (= W166), I167 (= I167), T168 (= T168), L210 (= L209), Y367 (= Y366), T370 (= T369)
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)
49% identity, 96% coverage: 15:387/387 of query aligns to 15:385/385 of 3gqtC
- active site: L135 (= L135), T136 (= T136), A250 (= A246), E365 (= E367), R377 (= R379)
- binding 1-(1,4-dimethyl-1,2,3,4-tetrahydroquinoxalin-6-yl)methanamine: W166 (= W166), K210 (= K206), L213 (= L209), T218 (= T214), Y364 (= Y366)
3eonC 2.55a crystal structure of native glutaryl-coa dehydrogenase from burkholderia pseudomallei in complex with a small molecule (see paper)
48% identity, 96% coverage: 15:386/387 of query aligns to 15:382/382 of 3eonC
3gncA Crystal structure of glutaryl-coa dehydrogenase from burkholderia pseudomallei with fragment 6421 (see paper)
47% identity, 96% coverage: 15:386/387 of query aligns to 16:380/380 of 3gncA
3d6bC 2.2 a crystal structure of glutaryl-coa dehydrogenase from burkholderia pseudomallei (see paper)
47% identity, 96% coverage: 15:386/387 of query aligns to 15:377/377 of 3d6bC
2ix5A Short chain specific acyl-coa oxidase from arabidopsis thaliana, acx4 in complex with acetoacetyl-coa (see paper)
34% identity, 99% coverage: 5:387/387 of query aligns to 27:412/415 of 2ix5A
- active site: L158 (= L135), T159 (= T136), S271 (≠ A246), E392 (= E367), R404 (= R379)
- binding acetoacetyl-coenzyme a: S165 (= S142), A167 (≠ P144), S168 (= S145), F261 (≠ M236), L268 (= L243), R272 (= R247), E392 (= E367), G393 (= G368), R404 (= R379)
- binding flavin-adenine dinucleotide: L158 (= L135), T159 (= T136), G164 (= G141), S165 (= S142), W189 (= W166), N239 (≠ T214), R297 (= R272), F300 (= F275), L304 (= L279), F307 (≠ T282), L309 (≠ S284), N310 (≠ A285), E365 (≠ D340), L366 (= L341), G368 (= G343), G369 (≠ A344), Y391 (= Y366), T394 (= T369), D396 (≠ T371), I397 (≠ V372)
2ix6A Short chain specific acyl-coa oxidase from arabidopsis thaliana, acx4 (see paper)
34% identity, 99% coverage: 5:387/387 of query aligns to 27:412/416 of 2ix6A
- active site: L158 (= L135), T159 (= T136), S271 (≠ A246), E392 (= E367), R404 (= R379)
- binding flavin-adenine dinucleotide: T159 (= T136), G164 (= G141), S165 (= S142), W189 (= W166), N239 (≠ T214), R297 (= R272), F300 (= F275), L304 (= L279), F307 (≠ T282), N310 (≠ A285), E365 (≠ D340), L366 (= L341), G369 (≠ A344), I372 (= I347), Y391 (= Y366), T394 (= T369), D396 (≠ T371)
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, 99% coverage: 5:387/387 of query aligns to 43:428/436 of Q96329
4l1fA Electron transferring flavoprotein of acidaminococcus fermentans: towards a mechanism of flavin-based electron bifurcation (see paper)
32% identity, 95% coverage: 15:381/387 of query aligns to 5:377/380 of 4l1fA
- active site: L125 (= L135), T126 (= T136), G242 (≠ A246), E363 (= E367), R375 (= R379)
- binding coenzyme a persulfide: T132 (≠ S142), H179 (vs. gap), F232 (≠ M236), M236 (≠ L240), E237 (≠ G241), L239 (= L243), D240 (≠ N244), R243 (= R247), Y362 (= Y366), E363 (= E367), G364 (= G368), R375 (= R379)
- binding flavin-adenine dinucleotide: F123 (= F133), L125 (= L135), T126 (= T136), G131 (= G141), T132 (≠ S142), F156 (≠ W166), I157 (= I167), T158 (= T168), R268 (= R272), Q270 (≠ L274), F271 (= F275), I275 (≠ L279), F278 (≠ T282), L281 (≠ A285), Q336 (≠ D340), I337 (≠ L341), G340 (≠ A344), I358 (≠ S362), Y362 (= Y366), T365 (= T369), Q367 (≠ T371)
- binding 1,3-propandiol: L5 (= L15), Q10 (≠ R20)
5ol2F The electron transferring flavoprotein/butyryl-coa dehydrogenase complex from clostridium difficile (see paper)
34% identity, 95% coverage: 14:381/387 of query aligns to 3:376/378 of 5ol2F
- active site: L124 (= L135), T125 (= T136), G241 (≠ A246), G374 (≠ R379)
- binding calcium ion: E29 (≠ D40), E33 (≠ Q44), R35 (= R46)
- binding coenzyme a persulfide: L238 (= L243), R242 (= R247), E362 (= E367), G363 (= G368)
- binding flavin-adenine dinucleotide: F122 (= F133), L124 (= L135), T125 (= T136), P127 (≠ A138), T131 (≠ S142), F155 (≠ W166), I156 (= I167), T157 (= T168), E198 (≠ G204), R267 (= R272), F270 (= F275), L274 (= L279), F277 (≠ T282), Q335 (≠ D340), L336 (= L341), G338 (= G343), G339 (≠ A344), Y361 (= Y366), T364 (= T369), E366 (≠ T371)
5lnxD Crystal structure of mmgc, an acyl-coa dehydrogenase from bacillus subtilis.
34% identity, 95% coverage: 18:383/387 of query aligns to 5:374/374 of 5lnxD
- active site: L122 (= L135), T123 (= T136), G239 (≠ A246), E358 (= E367), K370 (≠ R379)
- binding flavin-adenine dinucleotide: L122 (= L135), T123 (= T136), G128 (= G141), S129 (= S142), F153 (≠ W166), T155 (= T168), R265 (= R272), Q267 (≠ L274), F268 (= F275), I272 (≠ L279), N275 (≠ T282), I278 (≠ A285), Q331 (≠ D340), I332 (≠ L341), G335 (≠ A344), Y357 (= Y366), T360 (= T369), E362 (≠ T371)
4n5fA Crystal structure of a putative acyl-coa dehydrogenase with bound fadh2 from burkholderia cenocepacia j2315
35% identity, 95% coverage: 14:381/387 of query aligns to 5:378/378 of 4n5fA
- active site: L126 (= L135), T127 (= T136), G243 (≠ A246), E364 (= E367), R376 (= R379)
- binding dihydroflavine-adenine dinucleotide: L126 (= L135), T127 (= T136), G132 (= G141), S133 (= S142), F157 (≠ W166), T159 (= T168), T210 (= T214), Y363 (= Y366), T366 (= T369), E368 (≠ T371), M372 (≠ L375)
P45954 Short/branched chain specific acyl-CoA dehydrogenase, mitochondrial; SBCAD; 2-methyl branched chain acyl-CoA dehydrogenase; 2-MEBCAD; 2-methylbutyryl-coenzyme A dehydrogenase; 2-methylbutyryl-CoA dehydrogenase; EC 1.3.8.5 from Homo sapiens (Human) (see 6 papers)
31% identity, 95% coverage: 15:381/387 of query aligns to 57:428/432 of P45954
- V137 (≠ S95) mutation to L: Decreased acyl-CoA dehydrogenase activity.
- F138 (= F96) mutation to L: Increased acyl-CoA dehydrogenase activity. No effect on substrate specificity.
- 174:183 (vs. 133:142, 60% identical) binding in other chain
- S183 (= S142) binding
- WIS 207:209 (≠ WIT 166:168) binding in other chain
- S210 (≠ N169) mutation to N: Increased acyl-CoA dehydrogenase activity. Changed substrate specificity.
- Y229 (vs. gap) binding
- L255 (= L209) to F: in SBCADD; loss of protein expression; loss of 2-methylbutyryl-CoA dehydrogenase activity; dbSNP:rs137852649
- Y283 (≠ M236) binding
- NEGR 291:294 (≠ NQAR 244:247) binding
- I316 (≠ A269) to V: in dbSNP:rs1131430
- R319 (= R272) binding
- Q330 (= Q283) binding
- EWMGG 387:391 (≠ DLLGA 340:344) binding
- A416 (≠ T369) mutation to T: Increased acyl-CoA dehydrogenase activity. No effect on substrate specificity.
- ASN 416:418 (≠ TET 369:371) binding in other chain
Sites not aligning to the query:
- 1:33 modified: transit peptide, Mitochondrion
- 13 R → K: in dbSNP:rs12263012
2jifA Structure of human short-branched chain acyl-coa dehydrogenase (acadsb)
31% identity, 95% coverage: 15:381/387 of query aligns to 6:377/381 of 2jifA
- active site: L125 (= L135), S126 (≠ T136), G242 (≠ A246), E363 (= E367), K375 (≠ R379)
- binding coenzyme a persulfide: S132 (= S142), S134 (≠ P144), Y178 (vs. gap), Y232 (≠ M236), I236 (≠ L240), L239 (= L243), N240 (= N244), R243 (= R247), Y362 (= Y366), E363 (= E367), G364 (= G368), I368 (≠ V372)
- binding flavin-adenine dinucleotide: F123 (= F133), L125 (= L135), S126 (≠ T136), G131 (= G141), S132 (= S142), W156 (= W166), I157 (= I167), S158 (≠ T168), K201 (= K206), T209 (= T214), R268 (= R272), F271 (= F275), L275 (= L279), F278 (≠ T282), L281 (≠ A285), E336 (≠ D340), W337 (≠ L341), G340 (≠ A344), N367 (≠ T371), I368 (≠ V372)
1jqiA Crystal structure of rat short chain acyl-coa dehydrogenase complexed with acetoacetyl-coa (see paper)
32% identity, 95% coverage: 15:381/387 of query aligns to 7:379/384 of 1jqiA
- active site: G377 (≠ R379)
- binding acetoacetyl-coenzyme a: L95 (= L103), F125 (= F133), S134 (= S142), F234 (≠ M236), M238 (≠ L240), Q239 (≠ G241), L241 (= L243), D242 (≠ N244), R245 (= R247), Y364 (= Y366), E365 (= E367), G366 (= G368)
- binding flavin-adenine dinucleotide: F125 (= F133), L127 (= L135), S128 (≠ T136), G133 (= G141), S134 (= S142), W158 (= W166), T160 (= T168), R270 (= R272), F273 (= F275), L280 (≠ T282), Q338 (≠ D340), I339 (≠ L341), G342 (≠ A344), I360 (≠ S362), T367 (= T369), E369 (≠ T371), I370 (≠ V372)
Query Sequence
>WP_057509244.1 NCBI__GCF_001431535.1:WP_057509244.1
MRLDPCDLFDVRSLLSDEERAVQDSVARFVDQRVLPVIGDCFDQARFPAELVPEIAALGL
LGATLPPAYGGGGMDAVAYGLICQELERGDSGLRSFVSVQSSLCMHPIFAYGSEAQRLRW
LPAMARGERIGCFGLTEAHGGSDPSSMKTRAVREGDQWRLDGSKMWITNAPIADLAIVWA
QTEDGVQGFILERGMAGFSVQEIGRKMSLRASSTGALFFDQVQVPEANRLAGVVGMKGPL
GCLNQARFGISWGPIGAAIACLREVLAYAGQRELFGRPLAATQSAQIKLADMARRITGAQ
LLALQLGRLKEAGRLQPQQVSLAKWNNCRMAIDIARECRDLLGAAGITTEHAAIRHALNL
ESVITYEGTETVHQLVIGRELTGLTAF
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