SitesBLAST
Comparing WP_058930113.1 NCBI__GCF_001484605.1:WP_058930113.1 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)
2ix6A Short chain specific acyl-coa oxidase from arabidopsis thaliana, acx4 (see paper)
43% identity, 97% coverage: 10:414/416 of query aligns to 17:411/416 of 2ix6A
- active site: L158 (= L145), T159 (= T146), S271 (= S274), E392 (= E395), R404 (= R407)
- binding flavin-adenine dinucleotide: T159 (= T146), G164 (= G151), S165 (= S152), W189 (= W187), N239 (= N242), R297 (= R300), F300 (= F303), L304 (= L307), F307 (= F310), N310 (≠ I313), E365 (≠ S368), L366 (= L369), G369 (= G372), I372 (= I375), Y391 (= Y394), T394 (≠ S397), D396 (≠ E399)
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)
43% identity, 97% coverage: 10:414/416 of query aligns to 33:427/436 of Q96329
Sites not aligning to the query:
2ix5A Short chain specific acyl-coa oxidase from arabidopsis thaliana, acx4 in complex with acetoacetyl-coa (see paper)
43% identity, 97% coverage: 10:414/416 of query aligns to 17:411/415 of 2ix5A
- active site: L158 (= L145), T159 (= T146), S271 (= S274), E392 (= E395), R404 (= R407)
- binding acetoacetyl-coenzyme a: S165 (= S152), A167 (= A155), S168 (≠ G156), F261 (= F264), L268 (= L271), R272 (= R275), E392 (= E395), G393 (= G396), R404 (= R407)
- binding flavin-adenine dinucleotide: L158 (= L145), T159 (= T146), G164 (= G151), S165 (= S152), W189 (= W187), N239 (= N242), R297 (= R300), F300 (= F303), L304 (= L307), F307 (= F310), L309 (= L312), N310 (≠ I313), E365 (≠ S368), L366 (= L369), G368 (= G371), G369 (= G372), Y391 (= Y394), T394 (≠ S397), D396 (≠ E399), I397 (= I400)
2ebaA Crystal structure of the putative glutaryl-coa dehydrogenase from thermus thermophilus
34% identity, 94% coverage: 23:415/416 of query aligns to 3:380/380 of 2ebaA
- active site: L131 (= L145), T132 (= T146), A239 (≠ S274), E360 (= E395), R372 (= R407)
- binding flavin-adenine dinucleotide: L131 (= L145), T132 (= T146), G136 (≠ H150), G137 (= G151), S138 (= S152), W161 (= W187), T163 (≠ G189), R265 (= R300), L272 (= L307), K275 (≠ F310), D333 (≠ S368), I334 (≠ L369), G337 (= G372), T355 (≠ A390), T358 (= T393), Y359 (= Y394), T362 (≠ S397)
3sf6A Crystal structure of glutaryl-coa dehydrogenase from mycobacterium smegmatis (see paper)
31% identity, 94% coverage: 23:414/416 of query aligns to 6:385/387 of 3sf6A
- active site: L134 (= L145), T135 (= T146), A245 (≠ S274), E366 (= E395), Q378 (≠ R407)
- binding dihydroflavine-adenine dinucleotide: F132 (= F143), L134 (= L145), T135 (= T146), G140 (= G151), S141 (= S152), W165 (= W187), I166 (= I188), T167 (≠ G189), S361 (≠ A390), T364 (= T393), Y365 (= Y394), T368 (≠ S397), E370 (= E399), M371 (≠ I400)
2r0nA The effect of a glu370asp mutation in glutaryl-coa dehydrogenase on proton transfer to the dienolate intermediate (see paper)
31% identity, 94% coverage: 23:414/416 of query aligns to 6:387/390 of 2r0nA
- active site: L133 (= L145), T134 (= T146), A247 (≠ S274), E368 (= E395), R380 (= R407)
- binding flavin-adenine dinucleotide: F131 (= F143), L133 (= L145), T134 (= T146), G139 (= G151), S140 (= S152), W166 (= W187), I167 (= I188), T168 (≠ G189), Y367 (= Y394), T370 (≠ S397), D372 (≠ E399)
- binding 3-thiaglutaryl-CoA: R92 (≠ A104), S93 (≠ T105), V97 (= V109), P142 (≠ V154), G238 (≠ E265), F241 (≠ N268), L244 (= L271), N245 (≠ R272), P318 (≠ M345), Y367 (= Y394), E368 (= E395), I377 (= I404)
1sirA The crystal structure and mechanism of human glutaryl-coa dehydrogenase (see paper)
31% identity, 94% coverage: 23:414/416 of query aligns to 6:387/390 of 1sirA
- active site: L133 (= L145), T134 (= T146), A247 (≠ S274), E368 (= E395), R380 (= R407)
- binding flavin-adenine dinucleotide: F131 (= F143), L133 (= L145), T134 (= T146), G139 (= G151), S140 (= S152), W166 (= W187), I167 (= I188), T168 (≠ G189), Y367 (= Y394), T370 (≠ S397)
- binding s-4-nitrobutyryl-coa: S93 (≠ T105), S140 (= S152), F241 (≠ N268), G242 (≠ Q269), L244 (= L271), N245 (≠ R272), R248 (= R275), P318 (≠ M345), Y367 (= Y394), E368 (= E395), R380 (= R407)
2r0mA The effect of a glu370asp mutation in glutaryl-coa dehydrogenase on proton transfer to the dienolate intermediate (see paper)
31% identity, 94% coverage: 23:414/416 of query aligns to 6:387/390 of 2r0mA
- active site: L133 (= L145), T134 (= T146), A247 (≠ S274), D368 (≠ E395), R380 (= R407)
- binding 4-nitrobutanoic acid: L101 (= L113), Y367 (= Y394), D368 (≠ E395)
- binding flavin-adenine dinucleotide: F131 (= F143), L133 (= L145), T134 (= T146), G139 (= G151), S140 (= S152), W166 (= W187), I167 (= I188), T168 (≠ G189), L210 (= L237), Y367 (= Y394), T370 (≠ S397)
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)
30% identity, 94% coverage: 23:414/416 of query aligns to 7:384/385 of 3gqtC
- active site: L135 (= L145), T136 (= T146), A250 (≠ S274), E365 (= E395), R377 (= R407)
- binding 1-(1,4-dimethyl-1,2,3,4-tetrahydroquinoxalin-6-yl)methanamine: W166 (= W187), K210 (= K234), L213 (= L237), T218 (≠ N242), Y364 (= Y394)
3eonC 2.55a crystal structure of native glutaryl-coa dehydrogenase from burkholderia pseudomallei in complex with a small molecule (see paper)
30% identity, 94% coverage: 23:414/416 of query aligns to 7:382/382 of 3eonC
3gncA Crystal structure of glutaryl-coa dehydrogenase from burkholderia pseudomallei with fragment 6421 (see paper)
29% identity, 94% coverage: 23:414/416 of query aligns to 8:380/380 of 3gncA
3swoA Crystal structure of a glutaryl-coa dehydrogenase from mycobacterium smegmatis in complex with fadh2 (see paper)
29% identity, 94% coverage: 23:415/416 of query aligns to 8:387/388 of 3swoA
- active site: L135 (= L145), T136 (= T146), A246 (≠ S274), E367 (= E395), K379 (≠ R407)
- binding dihydroflavine-adenine dinucleotide: F133 (= F143), L135 (= L145), T136 (= T146), G141 (= G151), S142 (= S152), W166 (= W187), I167 (= I188), T168 (≠ G189), R272 (= R300), V274 (≠ Q302), F275 (= F303), L279 (= L307), Y282 (≠ F310), T340 (≠ S368), L341 (= L369), G344 (= G372), I347 (= I375), T365 (= T393), Y366 (= Y394), T369 (≠ S397), E371 (= E399), M372 (≠ I400)
4n5fA Crystal structure of a putative acyl-coa dehydrogenase with bound fadh2 from burkholderia cenocepacia j2315
31% identity, 92% coverage: 27:407/416 of query aligns to 2:376/378 of 4n5fA
- active site: L126 (= L145), T127 (= T146), G243 (≠ S274), E364 (= E395), R376 (= R407)
- binding dihydroflavine-adenine dinucleotide: L126 (= L145), T127 (= T146), G132 (= G151), S133 (= S152), F157 (≠ W187), T159 (≠ G189), T210 (≠ N242), Y363 (= Y394), T366 (≠ S397), E368 (= E399), M372 (≠ L403)
3d6bC 2.2 a crystal structure of glutaryl-coa dehydrogenase from burkholderia pseudomallei (see paper)
29% identity, 94% coverage: 23:414/416 of query aligns to 7:377/377 of 3d6bC
1jqiA Crystal structure of rat short chain acyl-coa dehydrogenase complexed with acetoacetyl-coa (see paper)
29% identity, 88% coverage: 42:405/416 of query aligns to 18:375/384 of 1jqiA
- binding acetoacetyl-coenzyme a: L95 (= L113), F125 (= F143), S134 (= S152), F234 (= F264), M238 (≠ N268), Q239 (= Q269), L241 (= L271), D242 (≠ R272), R245 (= R275), Y364 (= Y394), E365 (= E395), G366 (= G396)
- binding flavin-adenine dinucleotide: F125 (= F143), L127 (= L145), S128 (≠ T146), G133 (= G151), S134 (= S152), W158 (= W187), T160 (≠ G189), R270 (= R300), F273 (= F303), L280 (≠ F310), Q338 (≠ S368), I339 (≠ L369), G342 (= G372), I360 (≠ A390), T367 (≠ S397), E369 (= E399), I370 (= I400)
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)
29% identity, 88% coverage: 42:405/416 of query aligns to 45:402/412 of P15651
- 152:161 (vs. 143:152, 80% identical) binding FAD
- S161 (= S152) binding substrate
- WIT 185:187 (≠ WIG 187:189) binding FAD
- DMGR 269:272 (≠ RGSR 272:275) binding substrate
- R297 (= R300) binding FAD
- QILGG 365:369 (≠ SLLGG 368:372) binding FAD
- E392 (= E395) active site, Proton acceptor
- TSE 394:396 (≠ SFE 397:399) binding FAD
Sites not aligning to the query:
- 1:24 modified: transit peptide, Mitochondrion
6fahD Molecular basis of the flavin-based electron-bifurcating caffeyl-coa reductase reaction (see paper)
30% identity, 88% coverage: 38:405/416 of query aligns to 12:372/379 of 6fahD
- active site: L124 (= L145), T125 (= T146), G241 (≠ S274)
- binding flavin-adenine dinucleotide: F122 (= F143), L124 (= L145), T125 (= T146), R152 (≠ A184), F155 (≠ W187), T157 (≠ G189), E198 (= E232), R267 (= R300), Q269 (= Q302), F270 (= F303), I274 (≠ L307), F277 (= F310), Q335 (≠ S368), I336 (≠ L369), G339 (= G372), Y361 (= Y394), T364 (≠ S397), Q366 (≠ E399)
Sites not aligning to the query:
5ol2F The electron transferring flavoprotein/butyryl-coa dehydrogenase complex from clostridium difficile (see paper)
28% identity, 90% coverage: 31:405/416 of query aligns to 3:372/378 of 5ol2F
- active site: L124 (= L145), T125 (= T146), G241 (≠ S274)
- binding calcium ion: E29 (≠ D56), E33 (≠ K60), R35 (≠ E62)
- binding coenzyme a persulfide: L238 (= L271), R242 (= R275), E362 (= E395), G363 (= G396)
- binding flavin-adenine dinucleotide: F122 (= F143), L124 (= L145), T125 (= T146), P127 (= P148), T131 (≠ S152), F155 (≠ W187), I156 (= I188), T157 (≠ G189), E198 (= E232), R267 (= R300), F270 (= F303), L274 (= L307), F277 (= F310), Q335 (≠ S368), L336 (= L369), G338 (= G371), G339 (= G372), Y361 (= Y394), T364 (≠ S397), E366 (= E399)
Sites not aligning to the query:
P16219 Short-chain specific acyl-CoA dehydrogenase, mitochondrial; SCAD; Butyryl-CoA dehydrogenase; EC 1.3.8.1 from Homo sapiens (Human) (see 3 papers)
31% identity, 88% coverage: 39:405/416 of query aligns to 42:402/412 of P16219
- G90 (≠ Y84) to S: in ACADSD; loss of acyl-CoA dehydrogenase activity; dbSNP:rs121908005
- E104 (= E95) natural variant: Missing (in ACADSD; loss of acyl-CoA dehydrogenase activity; dbSNP:rs387906308)
- 152:161 (vs. 143:152, 80% identical) binding in other chain
- R171 (= R163) to W: 69% of wild-type acyl-CoA dehydrogenase activity; confers susceptibility to ethylmalonicaciduria; dbSNP:rs1800556
- WIT 185:187 (≠ WIG 187:189) binding in other chain
- A192 (≠ C194) to V: in ACADSD; loss of acyl-CoA dehydrogenase activity; dbSNP:rs28940874
- G209 (= G210) to S: 86% of wild-type acyl-CoA dehydrogenase activity; confers susceptibility to ethylmalonicaciduria; dbSNP:rs1799958
- R297 (= R300) binding FAD
- Q308 (= Q311) binding in other chain
- R325 (≠ M328) to W: in ACADSD; loss of acyl-CoA dehydrogenase activity; dbSNP:rs121908006
- S353 (= S356) to L: in ACADSD; loss of acyl-CoA dehydrogenase activity; dbSNP:rs28941773
- QILGG 365:369 (≠ SLLGG 368:372) binding FAD
- R380 (≠ K383) to W: in ACADSD; loss of acyl-CoA dehydrogenase activity; dbSNP:rs28940875
- TSE 394:396 (≠ SFE 397:399) binding in other chain
Sites not aligning to the query:
- 1:24 modified: transit peptide, Mitochondrion
8sgsA Human liver mitochondrial short-chain specific acyl-coa dehydrogenase (see paper)
31% identity, 88% coverage: 39:405/416 of query aligns to 12:372/381 of 8sgsA
- binding coenzyme a: S131 (= S152), A133 (= A155), N177 (≠ A208), F231 (= F264), M235 (≠ N268), L238 (= L271), I312 (≠ M345), E362 (= E395), G363 (= G396)
- binding flavin-adenine dinucleotide: F122 (= F143), L124 (= L145), S125 (≠ T146), G130 (= G151), S131 (= S152), W155 (= W187), T157 (≠ G189), R267 (= R300), F270 (= F303), L274 (= L307), L277 (≠ F310), Q335 (≠ S368), I336 (≠ L369), G338 (= G371), G339 (= G372), I357 (≠ A390), I360 (≠ T393), Y361 (= Y394), T364 (≠ S397), E366 (= E399)
Query Sequence
>WP_058930113.1 NCBI__GCF_001484605.1:WP_058930113.1
MSLPGTSGPPSSEPAIDELPTADFFAFESLLSSKERAKLAELREFLATEIAPYASDWWNK
AEFPAHILPKLAALELSTPAQRGYSNLFAGLVIAEMTRVDTSIATFFLVHHDLFVESLYG
FGSAGQKERLLADASSLRITGAFALTEPGHGSDVAGGMETSARRISSATGEPDDDGDAWV
LNGAKRWIGNGTFCDYMLVWAKDEAVAANGQGAVRGFIVDASLPGVSRSRIENKIALRTV
QNADIVLKDVQVAEADRFAGISSFEDTNQLLRGSRIMVGWQAVGQQLAAFDVARQYAVER
HQFGRPLAKFQLIQQQLVTMLGNAVASMAMMARIAQLQDDGVADMPQVALAKSYTSARMR
ETVALGRSLLGGNGIVTDYRMAKIFADAEAIYTYEGSFEINTLIVGRAVTGVSAIV
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