SitesBLAST
Comparing WP_028322395.1 NCBI__GCF_000422285.1:WP_028322395.1 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)
5ol2F The electron transferring flavoprotein/butyryl-coa dehydrogenase complex from clostridium difficile (see paper)
51% identity, 97% coverage: 11:385/385 of query aligns to 10:376/378 of 5ol2F
- active site: L124 (= L124), T125 (= T125), G241 (≠ T242), G374 (≠ S383)
- binding calcium ion: E29 (≠ K30), E33 (= E34), R35 (≠ Q36)
- binding coenzyme a persulfide: L238 (= L239), R242 (= R243), E362 (= E371), G363 (= G372)
- binding flavin-adenine dinucleotide: F122 (= F122), L124 (= L124), T125 (= T125), P127 (= P127), T131 (≠ S131), F155 (= F155), I156 (= I156), T157 (≠ S157), E198 (= E199), R267 (= R268), F270 (= F271), L274 (= L275), F277 (= F278), Q335 (= Q344), L336 (= L345), G338 (= G347), G339 (= G348), Y361 (= Y370), T364 (= T373), E366 (≠ Q375)
8i4rA Crystal structure of acyl-coa dehydrogenase complexed with acetyl-coa from thermobifida fusca
48% identity, 99% coverage: 3:385/385 of query aligns to 4:379/381 of 8i4rA
- binding acetyl coenzyme *a: S132 (= S131), T134 (≠ V133), R180 (≠ K179), R234 (≠ P233), L237 (≠ M236), R238 (≠ K237), L240 (= L239), D241 (= D240), R244 (= R243), E365 (= E371), G366 (= G372), R377 (≠ S383)
- binding flavin-adenine dinucleotide: Y123 (≠ F122), L125 (= L124), S126 (≠ T125), G131 (= G130), S132 (= S131), W156 (≠ F155), I157 (= I156), T158 (≠ S157), I360 (= I366), T367 (= T373), Q369 (= Q375)
8i4pA Crystal structure of acyl-coa dehydrogenase from thermobifida fusca
48% identity, 99% coverage: 3:385/385 of query aligns to 4:379/381 of 8i4pA
- binding flavin-adenine dinucleotide: Y123 (≠ F122), L125 (= L124), S126 (≠ T125), G131 (= G130), S132 (= S131), W156 (≠ F155), I157 (= I156), T158 (≠ S157), I360 (= I366), Y364 (= Y370), T367 (= T373), Q369 (= Q375)
7w0jE Acyl-coa dehydrogenase, tfu_1647
48% identity, 99% coverage: 3:385/385 of query aligns to 5:380/382 of 7w0jE
- binding [[(2R,3S,4R,5R)-5-(6-aminopurin-9-yl)-3,4-bis(oxidanyl)oxolan-2-yl]methoxy-oxidanyl-phosphoryl] [(2R,3S,4S)-5-azanyl-2,3,4-tris(oxidanyl)pentyl] hydrogen phosphate: S127 (≠ T125), W157 (≠ F155), R270 (= R268), Q272 (= Q270), F273 (= F271), I277 (≠ L275), F280 (= F278), I283 (≠ L281), Q339 (= Q344), L340 (= L345), G343 (= G348), Y365 (= Y370), E366 (= E371), T368 (= T373), Q370 (= Q375), I371 (= I376)
5lnxD Crystal structure of mmgc, an acyl-coa dehydrogenase from bacillus subtilis.
46% identity, 98% coverage: 7:385/385 of query aligns to 4:372/374 of 5lnxD
- active site: L122 (= L124), T123 (= T125), G239 (≠ T242), E358 (= E371), K370 (≠ S383)
- binding flavin-adenine dinucleotide: L122 (= L124), T123 (= T125), G128 (= G130), S129 (= S131), F153 (= F155), T155 (≠ S157), R265 (= R268), Q267 (= Q270), F268 (= F271), I272 (≠ L275), N275 (≠ F278), I278 (≠ L281), Q331 (= Q344), I332 (≠ L345), G335 (= G348), Y357 (= Y370), T360 (= T373), E362 (≠ Q375)
7p9xA Structure of cyclohex-1-ene-1-carboxyl-coa dehydrogenase complexed with cyclohex-1-ene-1-carboxyl-coa (see paper)
48% identity, 99% coverage: 5:385/385 of query aligns to 2:375/378 of 7p9xA
- binding 1-monoenoyl-CoA: L82 (≠ V85), D89 (≠ L92), S129 (= S131), L131 (≠ V133), K176 (= K179), F229 (= F232), M233 (= M236), L236 (= L239), R240 (= R243), Y360 (= Y370), T361 (≠ E371), G362 (= G372), R373 (≠ S383)
- binding flavin-adenine dinucleotide: A122 (≠ L124), T123 (= T125), G128 (= G130), S129 (= S131), F153 (= F155), I154 (= I156), T155 (≠ S157), N206 (≠ T209), L356 (≠ I366), Y360 (= Y370), T363 (= T373), Q365 (= Q375), I366 (= I376)
7p9aA Structure of cyclohex-1-ene-1-carboxyl-coa dehydrogenase complexed with cyclohex-1,5-diene-1-carboxyl-coa (see paper)
48% identity, 99% coverage: 5:385/385 of query aligns to 4:377/380 of 7p9aA
- binding 1,5 Dienoyl-CoA: S131 (= S131), L133 (≠ V133), K178 (= K179), F231 (= F232), M235 (= M236), L238 (= L239), N241 (≠ T242), R242 (= R243), Y362 (= Y370), T363 (≠ E371), G364 (= G372), R375 (≠ S383)
- binding flavin-adenine dinucleotide: L122 (≠ F122), A124 (≠ L124), T125 (= T125), G130 (= G130), S131 (= S131), F155 (= F155), I156 (= I156), T157 (≠ S157), K200 (= K201), N208 (≠ T209), L358 (≠ I366), T365 (= T373), Q367 (= Q375), I368 (= I376)
4l1fA Electron transferring flavoprotein of acidaminococcus fermentans: towards a mechanism of flavin-based electron bifurcation (see paper)
48% identity, 100% coverage: 1:385/385 of query aligns to 1:377/380 of 4l1fA
- active site: L125 (= L124), T126 (= T125), G242 (≠ T242), E363 (= E371), R375 (≠ S383)
- binding coenzyme a persulfide: T132 (≠ S131), H179 (≠ K179), F232 (= F232), M236 (= M236), E237 (≠ K237), L239 (= L239), D240 (= D240), R243 (= R243), Y362 (= Y370), E363 (= E371), G364 (= G372), R375 (≠ S383)
- binding flavin-adenine dinucleotide: F123 (= F122), L125 (= L124), T126 (= T125), G131 (= G130), T132 (≠ S131), F156 (= F155), I157 (= I156), T158 (≠ S157), R268 (= R268), Q270 (= Q270), F271 (= F271), I275 (≠ L275), F278 (= F278), L281 (= L281), Q336 (= Q344), I337 (≠ L345), G340 (= G348), I358 (= I366), Y362 (= Y370), T365 (= T373), Q367 (= Q375)
- binding 1,3-propandiol: L5 (= L5), Q10 (≠ L10)
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)
46% identity, 98% coverage: 9:385/385 of query aligns to 1:367/369 of 3pfdC
- active site: L116 (= L124), S117 (≠ T125), T233 (= T242), E353 (= E371), R365 (≠ S383)
- binding dihydroflavine-adenine dinucleotide: Y114 (≠ F122), L116 (= L124), S117 (≠ T125), G122 (= G130), S123 (= S131), W147 (≠ F155), I148 (= I156), T149 (≠ S157), R259 (= R268), F262 (= F271), V266 (≠ L275), N269 (≠ F278), Q326 (= Q344), L327 (= L345), G330 (= G348), I348 (= I366), Y352 (= Y370), T355 (= T373), Q357 (= Q375)
1ukwB Crystal structure of medium-chain acyl-coa dehydrogenase from thermus thermophilus hb8
44% identity, 100% coverage: 1:385/385 of query aligns to 1:376/379 of 1ukwB
- active site: L124 (= L124), S125 (≠ T125), T241 (= T242), E362 (= E371), R374 (≠ S383)
- binding cobalt (ii) ion: D145 (= D145), H146 (≠ G146)
- binding flavin-adenine dinucleotide: F122 (= F122), L124 (= L124), S125 (≠ T125), G130 (= G130), S131 (= S131), W155 (≠ F155), S157 (= S157), K200 (= K201), L357 (≠ I366), Y361 (= Y370), E362 (= E371), T364 (= T373), E366 (≠ Q375), L370 (≠ V379)
1ukwA Crystal structure of medium-chain acyl-coa dehydrogenase from thermus thermophilus hb8
44% identity, 100% coverage: 1:385/385 of query aligns to 1:376/379 of 1ukwA
- active site: L124 (= L124), S125 (≠ T125), T241 (= T242), E362 (= E371), R374 (≠ S383)
- binding flavin-adenine dinucleotide: F122 (= F122), L124 (= L124), S125 (≠ T125), G130 (= G130), S131 (= S131), W155 (≠ F155), S157 (= S157), L357 (≠ I366), Y361 (= Y370), E362 (= E371), T364 (= T373), E366 (≠ Q375), L370 (≠ V379)
Q9VSA3 Medium-chain specific acyl-CoA dehydrogenase, mitochondrial; EC 1.3.8.7 from Drosophila melanogaster (Fruit fly) (see paper)
43% identity, 99% coverage: 3:385/385 of query aligns to 35:411/419 of Q9VSA3
- S347 (≠ L320) modified: Phosphoserine; by Pink1; mutation to A: Prevents phosphorylation by Pink1. Does not rescue climbing and flight defects in Pink1 mutants.; mutation to D: Phosphomimetic mutant that fully rescues climbing defects and significantly improves flight defects, and thorax and wing posture phenotypes in Pink1 mutants. No effect on acyl-CoA dehydrogenase activity.; mutation to DD: Phosphomimetic mutant that fully rescues climbing defects and significantly improves flight defects, and thorax and wing posture phenotypes in Pink1 mutants. No effect on acyl-CoA dehydrogenase activity.
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)
45% identity, 97% coverage: 5:377/385 of query aligns to 57:420/432 of P45954
- V137 (= V85) mutation to L: Decreased acyl-CoA dehydrogenase activity.
- F138 (≠ I86) mutation to L: Increased acyl-CoA dehydrogenase activity. No effect on substrate specificity.
- 174:183 (vs. 122:131, 60% identical) binding in other chain
- S183 (= S131) binding substrate
- WIS 207:209 (≠ FIS 155:157) binding in other chain
- S210 (≠ H158) mutation to N: Increased acyl-CoA dehydrogenase activity. Changed substrate specificity.
- Y229 (≠ H178) binding substrate
- L255 (= L204) to F: in SBCADD; loss of protein expression; loss of 2-methylbutyryl-CoA dehydrogenase activity; dbSNP:rs137852649
- Y283 (≠ F232) binding substrate
- NEGR 291:294 (≠ DITR 240:243) binding substrate
- I316 (≠ T265) to V: in dbSNP:rs1131430
- R319 (= R268) binding FAD
- Q330 (= Q279) binding FAD
- EWMGG 387:391 (≠ QLLGG 344:348) binding FAD
- A416 (≠ T373) mutation to T: Increased acyl-CoA dehydrogenase activity. No effect on substrate specificity.
- ASN 416:418 (≠ TSQ 373:375) 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)
44% identity, 99% coverage: 5:385/385 of query aligns to 6:377/381 of 2jifA
- active site: L125 (= L124), S126 (≠ T125), G242 (≠ T242), E363 (= E371), K375 (≠ S383)
- binding coenzyme a persulfide: S132 (= S131), S134 (≠ V133), Y178 (≠ H178), Y232 (≠ F232), I236 (≠ M236), L239 (= L239), N240 (≠ D240), R243 (= R243), Y362 (= Y370), E363 (= E371), G364 (= G372), I368 (= I376)
- binding flavin-adenine dinucleotide: F123 (= F122), L125 (= L124), S126 (≠ T125), G131 (= G130), S132 (= S131), W156 (≠ F155), I157 (= I156), S158 (= S157), K201 (= K201), T209 (= T209), R268 (= R268), F271 (= F271), L275 (= L275), F278 (= F278), L281 (= L281), E336 (≠ Q344), W337 (≠ L345), G340 (= G348), N367 (≠ Q375), I368 (= I376)
3mdeA Crystal structures of medium chain acyl-coa dehydrogenase from pig liver mitochondria with and without substrate (see paper)
42% identity, 99% coverage: 1:382/385 of query aligns to 2:377/385 of 3mdeA
- active site: V125 (≠ L124), T126 (= T125), T245 (= T242), E366 (= E371)
- binding octanoyl-coenzyme a: T86 (≠ V85), E89 (≠ L88), L93 (= L92), S132 (= S131), V134 (= V133), S181 (≠ H178), F235 (= F232), M239 (= M236), F242 (≠ L239), R314 (≠ E319), Y365 (= Y370), E366 (= E371), G367 (= G372)
- binding flavin-adenine dinucleotide: Y123 (≠ F122), V125 (≠ L124), T126 (= T125), G131 (= G130), S132 (= S131), W156 (≠ F155), I157 (= I156), T158 (≠ S157), R271 (= R268), T273 (≠ Q270), F274 (= F271), L278 (= L275), H281 (≠ F278), Q339 (= Q344), V340 (≠ L345), G343 (= G348), I361 (= I366), T368 (= T373), Q370 (= Q375)
Sites not aligning to the query:
3mddA Crystal structures of medium chain acyl-coa dehydrogenase from pig liver mitochondria with and without substrate (see paper)
42% identity, 99% coverage: 1:382/385 of query aligns to 2:377/385 of 3mddA
- active site: V125 (≠ L124), T126 (= T125), T245 (= T242), E366 (= E371)
- binding flavin-adenine dinucleotide: Y123 (≠ F122), T126 (= T125), G131 (= G130), S132 (= S131), W156 (≠ F155), T158 (≠ S157), R271 (= R268), T273 (≠ Q270), F274 (= F271), H281 (≠ F278), Q339 (= Q344), V340 (≠ L345), G343 (= G348), I361 (= I366), T368 (= T373), Q370 (= Q375)
Sites not aligning to the query:
1udyA Medium-chain acyl-coa dehydrogenase with 3-thiaoctanoyl-coa (see paper)
42% identity, 99% coverage: 1:382/385 of query aligns to 2:377/385 of 1udyA
- active site: V125 (≠ L124), T126 (= T125), T245 (= T242), E366 (= E371)
- binding 3-thiaoctanoyl-coenzyme a: L93 (= L92), Y123 (≠ F122), S132 (= S131), S181 (≠ H178), F235 (= F232), M239 (= M236), F242 (≠ L239), V249 (= V246), R314 (≠ E319), Y365 (= Y370), E366 (= E371), G367 (= G372), I371 (= I376), I375 (≠ V380)
- binding flavin-adenine dinucleotide: Y123 (≠ F122), T126 (= T125), G131 (= G130), S132 (= S131), W156 (≠ F155), T158 (≠ S157), T273 (≠ Q270), F274 (= F271), Q339 (= Q344), V340 (≠ L345), G343 (= G348), T368 (= T373), Q370 (= Q375)
Sites not aligning to the query:
P41367 Medium-chain specific acyl-CoA dehydrogenase, mitochondrial; MCAD; EC 1.3.8.7 from Sus scrofa (Pig) (see 2 papers)
42% identity, 99% coverage: 1:382/385 of query aligns to 37:412/421 of P41367
- 158:167 (vs. 122:131, 60% identical) binding in other chain
- S167 (= S131) binding octanoyl-CoA
- WIT 191:193 (≠ FIS 155:157) binding in other chain
- S216 (≠ H178) binding octanoyl-CoA
- D278 (= D240) binding octanoyl-CoA
- R281 (= R243) binding octanoyl-CoA
- RKT 306:308 (≠ RQQ 268:270) binding FAD
- HQ 316:317 (≠ FQ 278:279) binding in other chain
- R349 (= R318) binding octanoyl-CoA
- T351 (≠ L320) binding octanoyl-CoA
- QVFGG 374:378 (≠ QLLGG 344:348) binding FAD
- E401 (= E371) active site, Proton acceptor; binding octanoyl-CoA
- GTAQ 402:405 (≠ GTSQ 372:375) binding in other chain
1bucA Three-dimensional structure of butyryl-coa dehydrogenase from megasphaera elsdenii (see paper)
45% identity, 100% coverage: 1:385/385 of query aligns to 1:381/383 of 1bucA
- active site: L128 (= L124), T129 (= T125), G246 (≠ T242), E367 (= E371), G379 (≠ S383)
- binding acetoacetyl-coenzyme a: L96 (= L92), F126 (= F122), G134 (= G130), T135 (≠ S131), T162 (≠ S157), N182 (≠ H178), H183 (≠ K179), F236 (= F232), M240 (= M236), M241 (≠ K237), L243 (= L239), D244 (= D240), T317 (≠ N312), Y366 (= Y370), E367 (= E371), G368 (= G372)
- binding flavin-adenine dinucleotide: F126 (= F122), L128 (= L124), T129 (= T125), G134 (= G130), T135 (≠ S131), F160 (= F155), T162 (≠ S157), Y366 (= Y370), T369 (= T373), E371 (≠ Q375), M375 (≠ V379)
Q06319 Acyl-CoA dehydrogenase, short-chain specific; Butyryl-CoA dehydrogenase; BCAD; SCAD; EC 1.3.8.1 from Megasphaera elsdenii (see paper)
45% identity, 100% coverage: 1:385/385 of query aligns to 1:381/383 of Q06319
- E367 (= E371) active site, Proton acceptor; mutation to Q: Loss of activity.
Query Sequence
>WP_028322395.1 NCBI__GCF_000422285.1:WP_028322395.1
MQYDLTEEQLMLKETVARIAREQVAPGAEKRDEEAQFPWDMVEILKENALFGADFPEVYG
GSEMGLLALCVMIEELAKACASTAVILLVHELGTMPIFLAGNSEQKSRYLPRLAAGDALI
AFGLTEPNAGSDVSSLRTRAVKEGDGYLLNGSKIFISHADVAEVICVAARTDTTVPGHKG
TGVFIVDKGTSGLSIGKREKKMGLRASSTVEVVLEDVRVPAANLLAEENSGFPIIMKTLD
ITRIPVAAQAVGIAQGALDYAIQYTKERQQFGKPLFSFQGLQWMMADMATRVEASRQLTY
KAAALFEAVPKNLDRVSRELIRHSAMAKVFAADTAMQVTTDAVQLLGGYGYVKEYPVERM
MRDAKITQIYEGTSQIQKVVISSTL
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