SitesBLAST
Comparing WP_086511948.1 NCBI__GCF_002151265.1:WP_086511948.1 to proteins with known functional sites using BLASTp with E ≤ 0.001.
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Found 20 (the maximum) hits to proteins with known functional sites (download)
I6YCA3 Acyl-CoA dehydrogenase FadE26; ACAD; 3-oxocholest-4-en-26-oyl-CoA dehydrogenase alpha subunit; EC 1.3.99.- from Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv) (see paper)
35% identity, 100% coverage: 1:398/398 of query aligns to 1:395/400 of I6YCA3
- IGYS 127:130 (≠ QGYS 126:129) binding
- T136 (≠ S135) binding
- S162 (≠ T161) binding
- E247 (= E244) mutation to A: Loss of dehydrogenase activity.
- TNE 380:382 (≠ SNE 383:385) binding
4x28A Crystal structure of the chse4-chse5 complex from mycobacterium tuberculosis (see paper)
34% identity, 100% coverage: 1:398/398 of query aligns to 1:382/386 of 4x28A
- active site: Y122 (= Y128), S123 (= S129), E240 (= E244), G365 (= G381), M377 (≠ K393)
- binding dihydroflavine-adenine dinucleotide: I120 (≠ Q126), Y122 (= Y128), S123 (= S129), G128 (= G134), T129 (≠ S135), W153 (= W159), S155 (≠ T161), F363 (≠ I379), T367 (≠ S383), E369 (= E385), V370 (≠ I386)
P96855 Acyl-CoA dehydrogenase FadE34; ACAD; 3-oxochol-4-en-24-oyl-CoA dehydrogenase; EC 1.3.99.- from Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv) (see paper)
36% identity, 89% coverage: 43:398/398 of query aligns to 381:709/711 of P96855
- E581 (= E244) mutation to Q: Displays less than 1% activity with cholyl-CoA as substrate. Still binds FAD.
Sites not aligning to the query:
- 236 R→A: Displays less than 2% activity with cholyl-CoA as substrate. Cannot bind FAD.
6wy9A Tcur3481-tcur3483 steroid acad g363a variant (see paper)
32% identity, 97% coverage: 12:398/398 of query aligns to 8:377/380 of 6wy9A
- active site: Y122 (= Y128), T123 (≠ S129), E237 (= E244), T372 (≠ K393)
- binding dihydroflavine-adenine dinucleotide: I120 (≠ Q126), Y122 (= Y128), T123 (≠ S129), G128 (= G134), T129 (≠ S135), F153 (≠ W159), S155 (≠ T161), F358 (≠ I379), V362 (≠ S383), E364 (= E385)
6wy8B Tcur3481-tcur3483 steroid acad (see paper)
32% identity, 97% coverage: 12:398/398 of query aligns to 12:381/384 of 6wy8B
- active site: Y126 (= Y128), T127 (≠ S129), E241 (= E244), T376 (≠ K393)
- binding flavin-adenine dinucleotide: I124 (≠ Q126), Y126 (= Y128), T127 (≠ S129), G132 (= G134), T133 (≠ S135), F157 (≠ W159), S159 (≠ T161), V359 (≠ L372), F362 (≠ I379), G363 (≠ Y380), V366 (≠ S383), E368 (= E385)
P71858 Acyl-CoA dehydrogenase FadE29; ACAD; 3-oxo-23,24-bisnorchol-4-en-22-oyl-CoA dehydrogenase beta subunit; 3-oxo-4-pregnene-20-carboxyl-CoA dehydrogenase beta subunit; EC 1.3.99.- from Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv) (see paper)
31% identity, 99% coverage: 1:396/398 of query aligns to 1:380/387 of P71858
- E241 (= E244) mutation to Q: Unable to dehydrogenate pregnene-carboxyl-CoA ester.
2pg0A Crystal structure of acyl-coa dehydrogenase from geobacillus kaustophilus
32% identity, 84% coverage: 63:398/398 of query aligns to 58:380/380 of 2pg0A
- active site: M124 (≠ Y128), T125 (≠ S129), E243 (= E244), A364 (≠ G381), R376 (≠ K393)
- binding flavin-adenine dinucleotide: I122 (≠ Q126), M124 (≠ Y128), T125 (≠ S129), G130 (= G134), S131 (= S135), F155 (≠ W159), I156 (≠ T160), T157 (= T161), R269 (≠ E268), F272 (≠ D271), F279 (≠ D278), Q337 (= Q351), L338 (= L352), G340 (≠ D355), G341 (= G356), V359 (≠ K376), I362 (= I379), Y363 (= Y380), T366 (≠ S383), E368 (= E385), M369 (≠ I386)
1egcA Structure of t255e, e376g mutant of human medium chain acyl-coa dehydrogenase complexed with octanoyl-coa (see paper)
26% identity, 99% coverage: 1:396/398 of query aligns to 3:382/387 of 1egcA
- active site: V126 (≠ Y128), T127 (≠ S129), E246 (= E244), G367 (= G381), R379 (≠ K393)
- binding octanoyl-coenzyme a: E90 (≠ S91), L94 (≠ N95), Y124 (≠ Q126), S133 (= S135), V135 (≠ L137), N182 (≠ G184), F236 (≠ W234), M240 (≠ K238), F243 (≠ L241), D244 (≠ T242), R247 (= R245), Y366 (= Y380), G367 (= G381), G368 (= G382)
- binding flavin-adenine dinucleotide: Y124 (≠ Q126), V126 (≠ Y128), T127 (≠ S129), G132 (= G134), S133 (= S135), W157 (= W159), T159 (= T161), R272 (≠ E268), T274 (≠ I270), F275 (≠ D271), L279 (≠ A275), H282 (≠ D278), I285 (≠ L281), Q340 (≠ R336), I341 (≠ V337), G344 (≠ P340), I362 (≠ V365), I365 (= I379), Y366 (= Y380), T369 (≠ S383), Q371 (≠ E385)
3r7kA Crystal structure of a probable acyl coa dehydrogenase from mycobacterium abscessus atcc 19977 / dsm 44196 (see paper)
31% identity, 85% coverage: 54:393/398 of query aligns to 49:375/378 of 3r7kA
- active site: V126 (≠ Y128), T127 (≠ S129), E242 (= E244), G363 (= G381), K375 (= K393)
- binding dihydroflavine-adenine dinucleotide: V126 (≠ Y128), T127 (≠ S129), G132 (= G134), S133 (= S135), F157 (≠ W159), I158 (≠ T160), T159 (= T161), R268 (≠ E268), T270 (≠ I270), F271 (≠ D271), L275 (≠ A275), R278 (≠ D278), I281 (≠ L281), Q336 (≠ R336), I337 (≠ V337), G340 (≠ A342), I358 (≠ K376), T365 (≠ S383), E367 (= E385)
2jifA Structure of human short-branched chain acyl-coa dehydrogenase (acadsb)
28% identity, 98% coverage: 5:393/398 of query aligns to 6:375/381 of 2jifA
- active site: L125 (≠ Y128), S126 (= S129), G242 (≠ E244), E363 (≠ G381), K375 (= K393)
- binding coenzyme a persulfide: S132 (= S135), S134 (≠ L137), Y178 (≠ P181), Y232 (≠ W234), I236 (≠ K238), L239 (= L241), N240 (≠ T242), R243 (= R245), Y362 (= Y380), E363 (≠ G381), G364 (= G382), I368 (= I386)
- binding flavin-adenine dinucleotide: F123 (≠ W124), L125 (≠ Y128), S126 (= S129), G131 (= G134), S132 (= S135), W156 (= W159), I157 (≠ T160), S158 (≠ T161), K201 (≠ T204), T209 (≠ V211), R268 (≠ E268), F271 (≠ D271), L275 (≠ A275), F278 (≠ D278), L281 (= L281), E336 (≠ R336), W337 (≠ V337), G340 (= G356), N367 (≠ E385), I368 (= I386)
1ukwB Crystal structure of medium-chain acyl-coa dehydrogenase from thermus thermophilus hb8
29% identity, 86% coverage: 50:393/398 of query aligns to 45:374/379 of 1ukwB
- active site: L124 (≠ Y128), S125 (= S129), T241 (≠ E244), E362 (≠ G381), R374 (≠ K393)
- binding cobalt (ii) ion: D145 (= D149), H146 (= H150)
- binding flavin-adenine dinucleotide: F122 (≠ Q126), L124 (≠ Y128), S125 (= S129), G130 (= G134), S131 (= S135), W155 (= W159), S157 (≠ T161), K200 (≠ L205), L357 (= L374), Y361 (= Y380), E362 (≠ G381), T364 (≠ S383), E366 (= E385), L370 (≠ N389)
1ukwA Crystal structure of medium-chain acyl-coa dehydrogenase from thermus thermophilus hb8
29% identity, 86% coverage: 50:393/398 of query aligns to 45:374/379 of 1ukwA
- active site: L124 (≠ Y128), S125 (= S129), T241 (≠ E244), E362 (≠ G381), R374 (≠ K393)
- binding flavin-adenine dinucleotide: F122 (≠ Q126), L124 (≠ Y128), S125 (= S129), G130 (= G134), S131 (= S135), W155 (= W159), S157 (≠ T161), L357 (= L374), Y361 (= Y380), E362 (≠ G381), T364 (≠ S383), E366 (= E385), L370 (≠ N389)
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)
28% identity, 98% coverage: 5:393/398 of query aligns to 57:426/432 of P45954
- V137 (≠ I90) mutation to L: Decreased acyl-CoA dehydrogenase activity.
- F138 (≠ S91) mutation to L: Increased acyl-CoA dehydrogenase activity. No effect on substrate specificity.
- 174:183 (vs. 124:135, 58% identical) binding in other chain
- S183 (= S135) binding
- WIS 207:209 (≠ WTT 159:161) binding in other chain
- S210 (≠ L162) mutation to N: Increased acyl-CoA dehydrogenase activity. Changed substrate specificity.
- Y229 (≠ P181) binding
- L255 (vs. gap) to F: in SBCADD; loss of protein expression; loss of 2-methylbutyryl-CoA dehydrogenase activity; dbSNP:rs137852649
- Y283 (≠ W234) binding
- NEGR 291:294 (≠ THER 242:245) binding
- I316 (≠ A265) to V: in dbSNP:rs1131430
- R319 (≠ E268) binding
- Q330 (≠ P279) binding
- EWMG----------------G 387:391 (≠ RVLGPHALPFLAEEMQLEHDG 336:356) binding
- A416 (≠ S383) mutation to T: Increased acyl-CoA dehydrogenase activity. No effect on substrate specificity.
- ASN 416:418 (≠ SNE 383:385) binding in other chain
Sites not aligning to the query:
- 1:33 modified: transit peptide, Mitochondrion
- 13 R → K: in dbSNP:rs12263012
3pfdC Crystal structure of an acyl-coa dehydrogenase from mycobacterium thermoresistibile bound to reduced flavin adenine dinucleotide solved by combined iodide ion sad mr (see paper)
28% identity, 97% coverage: 10:396/398 of query aligns to 2:368/369 of 3pfdC
- active site: L116 (≠ Y128), S117 (= S129), T233 (≠ E244), E353 (≠ G381), R365 (≠ K393)
- binding dihydroflavine-adenine dinucleotide: Y114 (≠ Q126), L116 (≠ Y128), S117 (= S129), G122 (= G134), S123 (= S135), W147 (= W159), I148 (≠ T160), T149 (= T161), R259 (= R266), F262 (≠ V269), V266 (≠ A275), N269 (≠ D278), Q326 (≠ R336), L327 (≠ V337), G330 (= G356), I348 (≠ L377), Y352 (= Y380), T355 (≠ S383), Q357 (≠ E385)
P11310 Medium-chain specific acyl-CoA dehydrogenase, mitochondrial; MCAD; Medium chain acyl-CoA dehydrogenase; MCADH; EC 1.3.8.7 from Homo sapiens (Human) (see 16 papers)
26% identity, 99% coverage: 1:396/398 of query aligns to 37:416/421 of P11310
- Y67 (≠ K31) to H: in ACADMD; mild; dbSNP:rs121434280
- L86 (vs. gap) mutation to M: Strongly reduced rate of electron transfer to ETF.
- L98 (≠ T67) mutation to W: Strongly reduced rate of electron transfer to ETF.
- L100 (≠ W69) mutation to Y: Strongly reduced rate of electron transfer to ETF.
- I108 (≠ F77) mutation to M: Strongly reduced rate of electron transfer to ETF.
- P132 (= P99) to R: in a breast cancer sample; somatic mutation; dbSNP:rs875989854
- 158:167 (vs. 126:135, 60% identical) binding in other chain
- S167 (= S135) binding
- W191 (= W159) mutation to A: Loss of electron transfer to ETF.; mutation to F: Reduces rate of electron transfer to ETF about six-fold.
- WIT 191:193 (≠ WTT 159:161) binding in other chain
- T193 (= T161) to A: in ACADMD; the thermostability is markedly decreased; dbSNP:rs121434279
- E237 (≠ P201) mutation to A: Strongly reduced rate of electron transfer to ETF.
- D278 (≠ T242) binding
- T280 (≠ E244) mutation to E: Narrower substrate specificity. Changed substrate specificity towards longer acyl chains; when associated with G-401. Loss of acyl-CoA dehydrogenase activity; when associated with T-410.
- R281 (= R245) binding ; to T: in ACADMD; mild clinical phenotype; dbSNP:rs121434282
- RKT 306:308 (≠ EVI 268:270) binding
- HQ 316:317 (≠ DP 278:279) binding in other chain
- K329 (≠ R291) to E: in ACADMD; may alter splicing; decreased fatty acid beta-oxidation; dbSNP:rs77931234
- QILGG 374:378 (≠ RVLGP 336:340) binding
- E384 (= E353) mutation to A: Reduces rate of electron transfer to ETF three-fold.; mutation to Q: Reduces rate of electron transfer to ETF two-fold.
- E401 (≠ G381) active site, Proton acceptor; binding ; mutation to G: Changed substrate specificity towards longer acyl chains; when associated with E-280.; mutation to Q: Loss of acyl-CoA dehydrogenase activity.; mutation to T: Loss of acyl-CoA dehydrogenase activity; when associated with E-280.
- EGTSQ 401:405 (≠ GGSNE 381:385) binding in other chain
2a1tC Structure of the human mcad:etf e165betaa complex (see paper)
26% identity, 99% coverage: 1:396/398 of query aligns to 4:383/388 of 2a1tC
- active site: V127 (≠ Y128), T128 (≠ S129), T247 (≠ E244), E368 (≠ G381), R380 (≠ K393)
- binding flavin-adenine dinucleotide: Y125 (≠ Q126), V127 (≠ Y128), T128 (≠ S129), G133 (= G134), S134 (= S135), Q155 (= Q156), W158 (= W159), W158 (= W159), I159 (≠ T160), T160 (= T161), R273 (≠ E268), T275 (≠ I270), F276 (≠ D271), L280 (≠ A275), H283 (≠ D278), I286 (≠ L281), Q341 (≠ R336), I342 (≠ V337), G345 (≠ P340), I363 (≠ V365), T370 (≠ S383), Q372 (≠ E385)
P41367 Medium-chain specific acyl-CoA dehydrogenase, mitochondrial; MCAD; EC 1.3.8.7 from Sus scrofa (Pig) (see 2 papers)
25% identity, 100% coverage: 1:397/398 of query aligns to 37:417/421 of P41367
- 158:167 (vs. 126:135, 60% identical) binding in other chain
- S167 (= S135) binding
- WIT 191:193 (≠ WTT 159:161) binding in other chain
- S216 (≠ G184) binding
- D278 (≠ T242) binding
- R281 (= R245) binding
- RKT 306:308 (≠ EVI 268:270) binding
- HQ 316:317 (≠ DP 278:279) binding in other chain
- R349 (≠ V311) binding
- T351 (≠ G313) binding
- QVFGG 374:378 (≠ RVLGP 336:340) binding
- E401 (≠ G381) active site, Proton acceptor; binding
- GTAQ 402:405 (≠ GSNE 382:385) binding in other chain
3mdeA Crystal structures of medium chain acyl-coa dehydrogenase from pig liver mitochondria with and without substrate (see paper)
25% identity, 100% coverage: 1:397/398 of query aligns to 2:382/385 of 3mdeA
- active site: V125 (≠ Y128), T126 (≠ S129), T245 (≠ E244), E366 (≠ G381), R378 (≠ K393)
- binding octanoyl-coenzyme a: T86 (≠ I90), E89 (≠ G93), L93 (≠ V97), S132 (= S135), V134 (≠ L137), S181 (≠ G184), F235 (≠ W234), M239 (≠ K238), F242 (≠ L241), R314 (≠ V311), Y365 (= Y380), E366 (≠ G381), G367 (= G382)
- binding flavin-adenine dinucleotide: Y123 (≠ Q126), V125 (≠ Y128), T126 (≠ S129), G131 (= G134), S132 (= S135), W156 (= W159), I157 (≠ T160), T158 (= T161), R271 (≠ E268), T273 (≠ I270), F274 (≠ D271), L278 (≠ A275), H281 (≠ D278), Q339 (≠ R336), V340 (= V337), G343 (≠ P340), I361 (≠ V365), T368 (≠ S383), Q370 (≠ E385)
3mddA Crystal structures of medium chain acyl-coa dehydrogenase from pig liver mitochondria with and without substrate (see paper)
25% identity, 100% coverage: 1:397/398 of query aligns to 2:382/385 of 3mddA
- active site: V125 (≠ Y128), T126 (≠ S129), T245 (≠ E244), E366 (≠ G381), R378 (≠ K393)
- binding flavin-adenine dinucleotide: Y123 (≠ Q126), T126 (≠ S129), G131 (= G134), S132 (= S135), W156 (= W159), T158 (= T161), R271 (≠ E268), T273 (≠ I270), F274 (≠ D271), H281 (≠ D278), Q339 (≠ R336), V340 (= V337), G343 (≠ P340), I361 (≠ V365), T368 (≠ S383), Q370 (≠ E385)
1udyA Medium-chain acyl-coa dehydrogenase with 3-thiaoctanoyl-coa (see paper)
25% identity, 100% coverage: 1:397/398 of query aligns to 2:382/385 of 1udyA
- active site: V125 (≠ Y128), T126 (≠ S129), T245 (≠ E244), E366 (≠ G381), R378 (≠ K393)
- binding 3-thiaoctanoyl-coenzyme a: L93 (≠ V97), Y123 (≠ Q126), S132 (= S135), S181 (≠ G184), F235 (≠ W234), M239 (≠ K238), F242 (≠ L241), V249 (≠ T246), R314 (≠ V311), Y365 (= Y380), E366 (≠ G381), G367 (= G382), I371 (= I386), I375 (= I390)
- binding flavin-adenine dinucleotide: Y123 (≠ Q126), T126 (≠ S129), G131 (= G134), S132 (= S135), W156 (= W159), T158 (= T161), T273 (≠ I270), F274 (≠ D271), Q339 (≠ R336), V340 (= V337), G343 (≠ P340), T368 (≠ S383), Q370 (≠ E385)
Query Sequence
>WP_086511948.1 NCBI__GCF_002151265.1:WP_086511948.1
MNIHFSEQELAFRDEVRAFLAAELPADIAAKVRLGKKLTKQDHQRWQAILHRRGWYAANW
PVEHGGTGWSVVEKHIFEEECAAAGAPRLISFGVNMVAPVIIRFGTPEQKAHYLPRILDG
TDWWCQGYSEPGAGSDLAAVKTRAVREGDHYIVNGQKTWTTLGQHANWIFCLVRTDPEAK
PQAGISFLLIDMESPGISVRPIITLDGAHEVNEVFFDNVRVPVANLVGQENDGWTCAKYL
LTHERTGQAGIGISKAALAHLKEVARQEVIDGRPALEDPLLRQRIAEVEMRLMAVEMSTL
RILARAQAGGVPGAESSILKITGSEIRQAISDLARRVLGPHALPFLAEEMQLEHDGEPLH
ADYSVAPAAQYLNLRKLSIYGGSNEIQKNILAKAQLGL
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