SitesBLAST
Comparing WP_028321302.1 NCBI__GCF_000422285.1:WP_028321302.1 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)
1ukwB Crystal structure of medium-chain acyl-coa dehydrogenase from thermus thermophilus hb8
39% identity, 99% coverage: 1:380/382 of query aligns to 1:378/379 of 1ukwB
- active site: L124 (≠ V123), S125 (≠ T124), T241 (≠ N243), E362 (= E364), R374 (= R376)
- binding cobalt (ii) ion: D145 (≠ E144), H146 (≠ D145)
- binding flavin-adenine dinucleotide: F122 (≠ T121), L124 (≠ V123), S125 (≠ T124), G130 (= G129), S131 (= S130), W155 (≠ F154), S157 (≠ T156), K200 (= K201), L357 (≠ I359), Y361 (= Y363), E362 (= E364), T364 (= T366), E366 (= E368), L370 (≠ N372)
1ukwA Crystal structure of medium-chain acyl-coa dehydrogenase from thermus thermophilus hb8
39% identity, 99% coverage: 1:380/382 of query aligns to 1:378/379 of 1ukwA
- active site: L124 (≠ V123), S125 (≠ T124), T241 (≠ N243), E362 (= E364), R374 (= R376)
- binding flavin-adenine dinucleotide: F122 (≠ T121), L124 (≠ V123), S125 (≠ T124), G130 (= G129), S131 (= S130), W155 (≠ F154), S157 (≠ T156), L357 (≠ I359), Y361 (= Y363), E362 (= E364), T364 (= T366), E366 (= E368), L370 (≠ N372)
4l1fA Electron transferring flavoprotein of acidaminococcus fermentans: towards a mechanism of flavin-based electron bifurcation (see paper)
43% identity, 99% coverage: 1:379/382 of query aligns to 1:378/380 of 4l1fA
- active site: L125 (≠ V123), T126 (= T124), G242 (≠ N243), E363 (= E364), R375 (= R376)
- binding coenzyme a persulfide: T132 (≠ S130), H179 (≠ Y178), F232 (= F233), M236 (= M237), E237 (= E238), L239 (≠ F240), D240 (≠ N241), R243 (= R244), Y362 (= Y363), E363 (= E364), G364 (≠ A365), R375 (= R376)
- binding flavin-adenine dinucleotide: F123 (≠ T121), L125 (≠ V123), T126 (= T124), G131 (= G129), T132 (≠ S130), F156 (= F154), I157 (= I155), T158 (= T156), R268 (= R269), Q270 (≠ A271), F271 (= F272), I275 (= I276), F278 (= F279), L281 (≠ V282), Q336 (= Q337), I337 (≠ L338), G340 (= G341), I358 (= I359), Y362 (= Y363), T365 (= T366), Q367 (≠ E368)
- binding 1,3-propandiol: L5 (= L5), Q10 (≠ K10)
5ol2F The electron transferring flavoprotein/butyryl-coa dehydrogenase complex from clostridium difficile (see paper)
42% identity, 98% coverage: 6:379/382 of query aligns to 5:377/378 of 5ol2F
- active site: L124 (≠ V123), T125 (= T124), G241 (≠ N243), G374 (≠ R376)
- binding calcium ion: E29 (= E30), E33 (≠ R34), R35 (≠ E36)
- binding coenzyme a persulfide: L238 (≠ F240), R242 (= R244), E362 (= E364), G363 (≠ A365)
- binding flavin-adenine dinucleotide: F122 (≠ T121), L124 (≠ V123), T125 (= T124), P127 (= P126), T131 (≠ S130), F155 (= F154), I156 (= I155), T157 (= T156), E198 (≠ K199), R267 (= R269), F270 (= F272), L274 (≠ I276), F277 (= F279), Q335 (= Q337), L336 (= L338), G338 (= G340), G339 (= G341), Y361 (= Y363), T364 (= T366), E366 (= E368)
2pg0A Crystal structure of acyl-coa dehydrogenase from geobacillus kaustophilus
40% identity, 98% coverage: 5:378/382 of query aligns to 5:378/380 of 2pg0A
- active site: M124 (≠ V123), T125 (= T124), E243 (≠ N243), A364 (≠ E364), R376 (= R376)
- binding flavin-adenine dinucleotide: I122 (≠ T121), M124 (≠ V123), T125 (= T124), G130 (= G129), S131 (= S130), F155 (= F154), I156 (= I155), T157 (= T156), R269 (= R269), F272 (= F272), F279 (= F279), Q337 (= Q337), L338 (= L338), G340 (= G340), G341 (= G341), V359 (≠ I359), I362 (= I362), Y363 (= Y363), T366 (= T366), E368 (= E368), M369 (= M369)
5lnxD Crystal structure of mmgc, an acyl-coa dehydrogenase from bacillus subtilis.
40% identity, 98% coverage: 7:380/382 of query aligns to 4:374/374 of 5lnxD
- active site: L122 (≠ V123), T123 (= T124), G239 (≠ N243), E358 (= E364), K370 (≠ R376)
- binding flavin-adenine dinucleotide: L122 (≠ V123), T123 (= T124), G128 (= G129), S129 (= S130), F153 (= F154), T155 (= T156), R265 (= R269), Q267 (≠ A271), F268 (= F272), I272 (= I276), N275 (≠ F279), I278 (≠ V282), Q331 (= Q337), I332 (≠ L338), G335 (= G341), Y357 (= Y363), T360 (= T366), E362 (= E368)
P41367 Medium-chain specific acyl-CoA dehydrogenase, mitochondrial; MCAD; EC 1.3.8.7 from Sus scrofa (Pig) (see 2 papers)
38% identity, 100% coverage: 1:382/382 of query aligns to 37:419/421 of P41367
- 158:167 (vs. 121:130, 70% identical) binding in other chain
- S167 (= S130) binding octanoyl-CoA
- WIT 191:193 (≠ FIT 154:156) binding in other chain
- S216 (≠ G179) binding octanoyl-CoA
- D278 (≠ N241) binding octanoyl-CoA
- R281 (= R244) binding octanoyl-CoA
- RKT 306:308 (≠ RQA 269:271) binding FAD
- HQ 316:317 (≠ FQ 279:280) binding in other chain
- R349 (≠ T312) binding octanoyl-CoA
- T351 (≠ P314) binding octanoyl-CoA
- QVFGG 374:378 (≠ QLHGG 337:341) binding FAD
- E401 (= E364) active site, Proton acceptor; binding octanoyl-CoA
- GTAQ 402:405 (≠ ATKE 365:368) binding in other chain
3mdeA Crystal structures of medium chain acyl-coa dehydrogenase from pig liver mitochondria with and without substrate (see paper)
38% identity, 100% coverage: 1:382/382 of query aligns to 2:384/385 of 3mdeA
- active site: V125 (= V123), T126 (= T124), T245 (≠ N243), E366 (= E364), R378 (= R376)
- binding octanoyl-coenzyme a: T86 (≠ L88), E89 (vs. gap), L93 (≠ F91), S132 (= S130), V134 (≠ I132), S181 (≠ G179), F235 (= F233), M239 (= M237), F242 (= F240), R314 (≠ T312), Y365 (= Y363), E366 (= E364), G367 (≠ A365)
- binding flavin-adenine dinucleotide: Y123 (≠ T121), V125 (= V123), T126 (= T124), G131 (= G129), S132 (= S130), W156 (≠ F154), I157 (= I155), T158 (= T156), R271 (= R269), T273 (≠ A271), F274 (= F272), L278 (≠ I276), H281 (≠ F279), Q339 (= Q337), V340 (≠ L338), G343 (= G341), I361 (= I359), T368 (= T366), Q370 (≠ E368)
3mddA Crystal structures of medium chain acyl-coa dehydrogenase from pig liver mitochondria with and without substrate (see paper)
38% identity, 100% coverage: 1:382/382 of query aligns to 2:384/385 of 3mddA
- active site: V125 (= V123), T126 (= T124), T245 (≠ N243), E366 (= E364), R378 (= R376)
- binding flavin-adenine dinucleotide: Y123 (≠ T121), T126 (= T124), G131 (= G129), S132 (= S130), W156 (≠ F154), T158 (= T156), R271 (= R269), T273 (≠ A271), F274 (= F272), H281 (≠ F279), Q339 (= Q337), V340 (≠ L338), G343 (= G341), I361 (= I359), T368 (= T366), Q370 (≠ E368)
1udyA Medium-chain acyl-coa dehydrogenase with 3-thiaoctanoyl-coa (see paper)
38% identity, 100% coverage: 1:382/382 of query aligns to 2:384/385 of 1udyA
- active site: V125 (= V123), T126 (= T124), T245 (≠ N243), E366 (= E364), R378 (= R376)
- binding 3-thiaoctanoyl-coenzyme a: L93 (≠ F91), Y123 (≠ T121), S132 (= S130), S181 (≠ G179), F235 (= F233), M239 (= M237), F242 (= F240), V249 (≠ A247), R314 (≠ T312), Y365 (= Y363), E366 (= E364), G367 (≠ A365), I371 (≠ M369), I375 (≠ T373)
- binding flavin-adenine dinucleotide: Y123 (≠ T121), T126 (= T124), G131 (= G129), S132 (= S130), W156 (≠ F154), T158 (= T156), T273 (≠ A271), F274 (= F272), Q339 (= Q337), V340 (≠ L338), G343 (= G341), T368 (= T366), Q370 (≠ E368)
7p9aA Structure of cyclohex-1-ene-1-carboxyl-coa dehydrogenase complexed with cyclohex-1,5-diene-1-carboxyl-coa (see paper)
40% identity, 98% coverage: 4:379/382 of query aligns to 3:378/380 of 7p9aA
- binding 1,5 Dienoyl-CoA: S131 (= S130), L133 (≠ I132), K178 (≠ R177), F231 (= F233), M235 (= M237), L238 (≠ F240), N241 (= N243), R242 (= R244), Y362 (= Y363), T363 (≠ E364), G364 (≠ A365), R375 (= R376)
- binding flavin-adenine dinucleotide: L122 (≠ V123), A124 (vs. gap), T125 (= T124), G130 (= G129), S131 (= S130), F155 (= F154), I156 (= I155), T157 (= T156), K200 (= K201), N208 (≠ T209), L358 (≠ I359), T365 (= T366), Q367 (≠ E368), I368 (≠ M369)
Q39QF5 Cyclohex-1-ene-1-carbonyl-CoA dehydrogenase; CHeneCoA dehydrogenase; EC 1.3.8.10 from Geobacter metallireducens (strain ATCC 53774 / DSM 7210 / GS-15) (see paper)
40% identity, 98% coverage: 4:379/382 of query aligns to 3:378/380 of Q39QF5
- D91 (vs. gap) mutation to E: Retains minor activity.; mutation to N: Loss of activity. Gains a low but significant C1,C2-dehydrogenation activity, but the C3,C6- and C3,C4-dehydrogenating activities are largely diminished; when associated with D-241.
- L122 (≠ V123) binding FAD
- A124 (vs. gap) binding FAD
- T125 (= T124) binding FAD
- S131 (= S130) binding cyclohex-1-ene-1-carbonyl-CoA; binding cyclohexa-1,5-diene-1-carbonyl-CoA; binding FAD
- T157 (= T156) binding FAD
- K178 (≠ R177) binding cyclohex-1-ene-1-carbonyl-CoA; binding cyclohexa-1,5-diene-1-carbonyl-CoA
- N241 (= N243) mutation to D: Shows decreased activity, with a shift towards C3,C4- versus C3,C6-dehydrogenation. Gains a low but significant C1,C2-dehydrogenation activity, but the C3,C6- and C3,C4-dehydrogenating activities are largely diminished; when associated with N-91.
- R242 (= R244) binding cyclohex-1-ene-1-carbonyl-CoA; binding cyclohexa-1,5-diene-1-carbonyl-CoA
- T363 (≠ E364) binding cyclohex-1-ene-1-carbonyl-CoA; binding cyclohexa-1,5-diene-1-carbonyl-CoA; mutation to V: Shows decreased activity, with a shift towards C3,C4- versus C3,C6-dehydrogenation.
- T365 (= T366) binding FAD
- Q367 (≠ E368) binding FAD
- R375 (= R376) binding cyclohex-1-ene-1-carbonyl-CoA; binding cyclohexa-1,5-diene-1-carbonyl-CoA
7p9xA Structure of cyclohex-1-ene-1-carboxyl-coa dehydrogenase complexed with cyclohex-1-ene-1-carboxyl-coa (see paper)
40% identity, 98% coverage: 4:379/382 of query aligns to 1:376/378 of 7p9xA
- binding 1-monoenoyl-CoA: L82 (≠ C85), D89 (vs. gap), S129 (= S130), L131 (≠ I132), K176 (≠ R177), F229 (= F233), M233 (= M237), L236 (≠ F240), R240 (= R244), Y360 (= Y363), T361 (≠ E364), G362 (≠ A365), R373 (= R376)
- binding flavin-adenine dinucleotide: A122 (vs. gap), T123 (= T124), G128 (= G129), S129 (= S130), F153 (= F154), I154 (= I155), T155 (= T156), N206 (≠ T209), L356 (≠ I359), Y360 (= Y363), T363 (= T366), Q365 (≠ E368), I366 (≠ M369)
7w0jE Acyl-coa dehydrogenase, tfu_1647
37% identity, 99% coverage: 3:379/382 of query aligns to 5:381/382 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 (≠ T124), W157 (≠ F154), R270 (= R269), Q272 (≠ A271), F273 (= F272), I277 (= I276), F280 (= F279), I283 (≠ V282), Q339 (= Q337), L340 (= L338), G343 (= G341), Y365 (= Y363), E366 (= E364), T368 (= T366), Q370 (≠ E368), I371 (≠ M369)
8i4rA Crystal structure of acyl-coa dehydrogenase complexed with acetyl-coa from thermobifida fusca
37% identity, 99% coverage: 3:379/382 of query aligns to 4:380/381 of 8i4rA
- binding acetyl coenzyme *a: S132 (= S130), T134 (≠ I132), R180 (≠ G179), R234 (≠ E234), L237 (≠ M237), R238 (≠ E238), L240 (≠ F240), D241 (≠ N241), R244 (= R244), E365 (= E364), G366 (≠ A365), R377 (= R376)
- binding flavin-adenine dinucleotide: Y123 (≠ T121), L125 (≠ V123), S126 (≠ T124), G131 (= G129), S132 (= S130), W156 (≠ F154), I157 (= I155), T158 (= T156), I360 (= I359), T367 (= T366), Q369 (≠ E368)
8i4pA Crystal structure of acyl-coa dehydrogenase from thermobifida fusca
37% identity, 99% coverage: 3:379/382 of query aligns to 4:380/381 of 8i4pA
- binding flavin-adenine dinucleotide: Y123 (≠ T121), L125 (≠ V123), S126 (≠ T124), G131 (= G129), S132 (= S130), W156 (≠ F154), I157 (= I155), T158 (= T156), I360 (= I359), Y364 (= Y363), T367 (= T366), Q369 (≠ E368)
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)
37% identity, 100% coverage: 1:382/382 of query aligns to 37:419/421 of P11310
- Y67 (= Y31) to H: in ACADMD; mild; dbSNP:rs121434280
- L86 (≠ F50) mutation to M: Strongly reduced rate of electron transfer to ETF.
- L98 (≠ A62) mutation to W: Strongly reduced rate of electron transfer to ETF.
- L100 (= L64) mutation to Y: Strongly reduced rate of electron transfer to ETF.
- I108 (= I72) mutation to M: Strongly reduced rate of electron transfer to ETF.
- P132 (≠ T95) to R: in a breast cancer sample; somatic mutation; dbSNP:rs875989854
- 158:167 (vs. 121:130, 70% identical) binding in other chain
- S167 (= S130) binding octanoyl-CoA
- W191 (≠ F154) 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 (≠ FIT 154:156) binding in other chain
- T193 (= T156) to A: in ACADMD; the thermostability is markedly decreased; dbSNP:rs121434279
- E237 (≠ K199) mutation to A: Strongly reduced rate of electron transfer to ETF.
- D278 (≠ N241) binding octanoyl-CoA
- T280 (≠ N243) 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 (= R244) binding octanoyl-CoA; to T: in ACADMD; mild clinical phenotype; dbSNP:rs121434282
- RKT 306:308 (≠ RQA 269:271) binding FAD
- HQ 316:317 (≠ FQ 279:280) binding in other chain
- K329 (≠ M292) to E: in ACADMD; may alter splicing; decreased fatty acid beta-oxidation; dbSNP:rs77931234
- QILGG 374:378 (≠ QLHGG 337:341) binding FAD
- E384 (= E347) 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 (= E364) active site, Proton acceptor; binding octanoyl-CoA; 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 (≠ EATKE 364:368) binding in other chain
2a1tC Structure of the human mcad:etf e165betaa complex (see paper)
37% identity, 100% coverage: 2:382/382 of query aligns to 5:386/388 of 2a1tC
- active site: V127 (= V123), T128 (= T124), T247 (≠ N243), E368 (= E364), R380 (= R376)
- binding flavin-adenine dinucleotide: Y125 (≠ T121), V127 (= V123), T128 (= T124), G133 (= G129), S134 (= S130), Q155 (≠ S151), W158 (≠ F154), W158 (≠ F154), I159 (= I155), T160 (= T156), R273 (= R269), T275 (≠ A271), F276 (= F272), L280 (≠ I276), H283 (≠ F279), I286 (≠ V282), Q341 (= Q337), I342 (≠ L338), G345 (= G341), I363 (= I359), T370 (= T366), Q372 (≠ E368)
4iv6B X-ray crystal structure of an isovaleryl-coa dehydrogenase from mycobacterium smegmatis (see paper)
36% identity, 99% coverage: 5:381/382 of query aligns to 2:378/383 of 4iv6B
- active site: L121 (≠ V123), T122 (= T124), G240 (≠ N243), E361 (= E364), K373 (≠ R376)
- binding dihydroflavine-adenine dinucleotide: L121 (≠ V123), T122 (= T124), G126 (≠ A128), G127 (= G129), S128 (= S130), W152 (≠ F154), I153 (= I155), S154 (≠ T156), R266 (= R269), S268 (≠ A271), F269 (= F272), I273 (= I276), H276 (≠ F279), V279 (= V282), R334 (≠ Q337), V335 (≠ L338), G338 (= G341), L356 (≠ I359), G360 (≠ Y363), T363 (= T366), E365 (= E368), I366 (≠ M369)
6fahD Molecular basis of the flavin-based electron-bifurcating caffeyl-coa reductase reaction (see paper)
39% identity, 99% coverage: 5:381/382 of query aligns to 3:379/379 of 6fahD
- active site: L124 (≠ V123), T125 (= T124), G241 (≠ N243), G374 (≠ R376)
- binding flavin-adenine dinucleotide: F122 (≠ T121), L124 (≠ V123), T125 (= T124), R152 (≠ S151), F155 (= F154), T157 (= T156), E198 (≠ K199), R267 (= R269), Q269 (≠ A271), F270 (= F272), I274 (= I276), F277 (= F279), Q335 (= Q337), I336 (≠ L338), G339 (= G341), Y361 (= Y363), T364 (= T366), Q366 (≠ E368)
Query Sequence
>WP_028321302.1 NCBI__GCF_000422285.1:WP_028321302.1
MNFELSKEQKDIKRAAREFAEGEIREVAKEYDRREEFPKDLWRKACELGFVGVYIKEEHG
GADLGLLECCLITEEFWRVDPGCGCVLLSSFGAETLQNHGTKEQKEKYLPPIPAGEAIMG
TAVTEPDAGSDIFGVRTTAFKDGEDYLINGSKIFITNGTIADYLAVFCLTDPDAKNRYGR
YSMIMMETDRAGFEASKIKGKLGIRASDTAELSFSDVRVPAGNLIGGKEGNGFEQIMELF
NMNRVVAASQGVGVGQGALDQTIAHVKKRQAFGSAIGKFQAVQFKLAEMATMVEAARVLT
YQAAWLLDNGKTDPKLIAMAKWLSGETGVRVTDDALQLHGGYGYINEYDIERFYRDAKIV
EIYEATKEMEKNTIARQLLGRF
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