SitesBLAST
Comparing Ac3H11_2514 FitnessBrowser__acidovorax_3H11:Ac3H11_2514 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)
5ez3B Crystal structure acyl-coa dehydrogenase from brucella melitensis in complex with fad
47% identity, 99% coverage: 9:553/553 of query aligns to 2:540/541 of 5ez3B
- active site: M181 (= M187), T182 (= T188), T295 (= T305), E423 (= E436), R435 (= R448)
- binding flavin-adenine dinucleotide: M181 (= M187), T182 (= T188), G186 (= G192), G187 (= G193), T188 (≠ S194), F213 (= F223), S215 (= S225), R321 (= R331), F324 (= F334), L328 (= L338), Q331 (= Q341), M334 (= M344), E396 (= E406), C397 (= C407), G399 (= G409), G400 (= G410), W422 (= W435), E423 (= E436), S425 (≠ A438), N427 (= N440), L431 (= L444)
3u33A Crystal structure of the e. Coli adaptive response protein aidb in the space group p3(2) (see paper)
45% identity, 97% coverage: 9:547/553 of query aligns to 5:533/540 of 3u33A
- active site: M184 (= M187), T185 (= T188), T298 (= T305), E425 (= E436), R437 (= R448)
- binding flavin-adenine dinucleotide: M182 (= M185), M184 (= M187), T185 (= T188), G190 (= G193), S191 (= S194), F216 (= F223), S218 (= S225), R324 (= R331), F327 (= F334), L331 (= L338), Q334 (= Q341), M337 (= M344), E398 (= E406), V399 (≠ C407), G401 (= G409), G402 (= G410), W424 (= W435), G426 (= G437), S427 (≠ A438), N429 (= N440), L433 (= L444)
P33224 Putative acyl-CoA dehydrogenase AidB; EC 1.3.99.- from Escherichia coli (strain K12) (see paper)
45% identity, 97% coverage: 9:547/553 of query aligns to 5:533/541 of P33224
- 182:191 (vs. 185:194, 100% identical) binding
- T185 (= T188) binding
- S191 (= S194) binding
- FFS 216:218 (= FFS 223:225) binding
- S218 (= S225) binding
- 423:433 (vs. 434:444, 82% identical) binding
- N429 (= N440) binding
- R437 (= R448) mutation to Q: Does not affect DNA binding affinity.
- R518 (≠ D529) mutation to Q: Reduces DNA binding affinity.
6sdaB Bd2924 c10 acyl-coenzymea bound form (see paper)
31% identity, 89% coverage: 13:504/553 of query aligns to 2:493/503 of 6sdaB
- active site: M171 (= M187), T172 (= T188), T296 (= T305), R439 (= R448)
- binding flavin-adenine dinucleotide: Q169 (≠ M185), M171 (= M187), T172 (= T188), G177 (= G193), S178 (= S194), F208 (= F223), T209 (≠ F224), R322 (= R331), F325 (= F334), L329 (= L338), H332 (≠ Q341), E400 (= E406), M401 (≠ C407), G404 (= G410), Y407 (= Y413), W426 (= W435), T429 (≠ A438), N431 (= N440), L435 (= L444)
- binding decanoyl-CoA: C128 (= C137), G177 (= G193), S178 (= S194), S230 (vs. gap), V286 (= V295), A290 (≠ L299), L293 (≠ G302), N294 (≠ T303), R297 (= R306), R377 (= R383), W426 (= W435), E427 (= E436)
6sd8X Bd2924 apo-form (see paper)
31% identity, 89% coverage: 13:504/553 of query aligns to 2:493/503 of 6sd8X
- active site: M171 (= M187), T172 (= T188), T296 (= T305), R439 (= R448)
- binding flavin-adenine dinucleotide: Q169 (≠ M185), M171 (= M187), T172 (= T188), G176 (= G192), G177 (= G193), S178 (= S194), F208 (= F223), T209 (≠ F224), R322 (= R331), F325 (= F334), L329 (= L338), H332 (≠ Q341), M401 (≠ C407), G404 (= G410), W426 (= W435), T429 (≠ A438), V432 (≠ I441), L435 (= L444)
4y9jB Crystal structure of caenorhabditis elegans acdh-11 in complex with c11-coa (see paper)
31% identity, 79% coverage: 13:449/553 of query aligns to 17:459/593 of 4y9jB
- active site: M190 (= M187), T191 (= T188), T315 (= T305), E446 (= E436), R458 (= R448)
- binding flavin-adenine dinucleotide: Q188 (≠ M185), M190 (= M187), T191 (= T188), G196 (= G193), S197 (= S194), F223 (= F223), S224 (≠ F224), S225 (= S225), R341 (= R331), V343 (≠ A333), F344 (= F334), Q348 (≠ L338), E419 (= E406), C420 (= C407), G422 (= G409), G423 (= G410), Y426 (= Y413), W445 (= W435), T448 (≠ A438), V451 (≠ I441), L454 (= L444)
- binding S-{(3S,5R,9R)-1-[(2R,3S,4R,5R)-5-(6-amino-9H-purin-9-yl)-4-hydroxy-3-(phosphonooxy)tetrahydrofuran-2-yl]-3,5,9-trihydroxy-8,8-dimethyl-3,5-dioxido-10,14-dioxo-2,4,6-trioxa-11,15-diaza-3lambda~5~,5lambda~5~-diphosphaheptadecan-17-yl} undecanethioate: S143 (≠ L136), A147 (≠ S140), Q188 (≠ M185), S197 (= S194), S249 (≠ P239), R303 (= R293), V305 (= V295), S309 (≠ L299), L312 (≠ G302), N313 (≠ T303), R316 (= R306), A322 (≠ G312), R396 (= R383), W445 (= W435), E446 (= E436), V451 (≠ I441), R458 (= R448)
Q9XWZ2 Acyl-CoA dehydrogenase family member 11; EC 1.3.99.- from Caenorhabditis elegans (see paper)
31% identity, 79% coverage: 13:449/553 of query aligns to 35:477/617 of Q9XWZ2
- E91 (≠ N67) mutation to K: In n5655; suppresses the defects in egg-laying and response to reoxygenation of paqr-2 mutants.
- S156 (≠ A131) mutation to F: In n5657; suppresses the defects in egg-laying and response to reoxygenation of paqr-2 mutants.
- G158 (≠ P133) mutation to R: In n5661; suppresses the defects in egg-laying and response to reoxygenation of paqr-2 mutants.
- G214 (= G193) mutation to E: In n5879; suppresses the defects in egg-laying and response to reoxygenation of paqr-2 mutants.
- G443 (= G412) mutation to R: In n5877; suppresses the defects in egg-laying and response to reoxygenation of paqr-2 mutants.
- R455 (= R424) mutation to H: In n5876; suppresses the defects in egg-laying and response to reoxygenation of paqr-2 mutants.
A3SI50 3-methylmercaptopropionyl-CoA dehydrogenase; MMPA-CoA dehydrogenase; EC 1.3.99.41 from Roseovarius nubinhibens (strain ATCC BAA-591 / DSM 15170 / ISM) (see paper)
29% identity, 48% coverage: 185:447/553 of query aligns to 161:446/591 of A3SI50
- M161 (= M185) mutation to A: Retains 37% of wild-type activity.
- T170 (≠ S194) mutation to A: Retains 8.8% of wild-type activity.
- F195 (= F223) mutation to A: Almost completely abolishes the activity.
- S197 (= S225) mutation to A: Retains 3.6% of wild-type activity.
- K223 (vs. gap) mutation to A: Retains 9.4% of wild-type activity.
- H280 (≠ G292) mutation to A: Retains 18% of wild-type activity.
- K281 (≠ R293) mutation to A: Retains 54% of wild-type activity.
- R284 (≠ A296) mutation to A: Retains 97% of wild-type activity.
- F287 (≠ L299) mutation to A: Retains 76% of wild-type activity.
- Y434 (≠ W435) mutation to A: Retains 51% of wild-type activity.
- E435 (= E436) mutation to A: Loss of activity.
Sites not aligning to the query:
- 448 R→A: Retains 44% of wild-type activity.
7p9xA Structure of cyclohex-1-ene-1-carboxyl-coa dehydrogenase complexed with cyclohex-1-ene-1-carboxyl-coa (see paper)
28% identity, 48% coverage: 175:441/553 of query aligns to 110:366/378 of 7p9xA
- binding 1-monoenoyl-CoA: S129 (= S194), L131 (≠ V196), K176 (≠ G240), F229 (≠ V295), M233 (≠ L299), L236 (≠ G302), R240 (= R306), Y360 (≠ W435), T361 (≠ E436), G362 (= G437)
- binding flavin-adenine dinucleotide: A122 (≠ M187), T123 (= T188), G128 (= G193), S129 (= S194), F153 (= F223), I154 (≠ F224), T155 (≠ S225), N206 (≠ S275), L356 (= L431), Y360 (≠ W435), T363 (≠ A438), Q365 (≠ N440), I366 (= I441)
Sites not aligning to the query:
7p9aA Structure of cyclohex-1-ene-1-carboxyl-coa dehydrogenase complexed with cyclohex-1,5-diene-1-carboxyl-coa (see paper)
28% identity, 48% coverage: 175:441/553 of query aligns to 112:368/380 of 7p9aA
- binding 1,5 Dienoyl-CoA: S131 (= S194), L133 (≠ V196), K178 (≠ G240), F231 (≠ V295), M235 (≠ L299), L238 (≠ G302), N241 (≠ T305), R242 (= R306), Y362 (≠ W435), T363 (≠ E436), G364 (= G437)
- binding flavin-adenine dinucleotide: L122 (≠ M185), A124 (≠ M187), T125 (= T188), G130 (= G193), S131 (= S194), F155 (= F223), I156 (≠ F224), T157 (≠ S225), K200 (= K267), N208 (≠ S275), L358 (= L431), T365 (≠ A438), Q367 (≠ N440), I368 (= I441)
Sites not aligning to the query:
2pg0A Crystal structure of acyl-coa dehydrogenase from geobacillus kaustophilus
30% identity, 48% coverage: 181:448/553 of query aligns to 118:376/380 of 2pg0A
- active site: M124 (= M187), T125 (= T188), E243 (≠ T305), A364 (≠ E436), R376 (= R448)
- binding flavin-adenine dinucleotide: I122 (≠ M185), M124 (= M187), T125 (= T188), G130 (= G193), S131 (= S194), F155 (= F223), I156 (≠ F224), T157 (≠ S225), R269 (= R331), F272 (= F334), F279 (≠ Q341), Q337 (≠ E406), L338 (≠ C407), G340 (= G409), G341 (= G410), V359 (≠ L431), I362 (= I434), Y363 (≠ W435), T366 (≠ A438), E368 (≠ N440), M369 (≠ I441)
4iv6B X-ray crystal structure of an isovaleryl-coa dehydrogenase from mycobacterium smegmatis (see paper)
30% identity, 50% coverage: 167:441/553 of query aligns to 105:366/383 of 4iv6B
- active site: L121 (≠ M187), T122 (= T188), G240 (≠ T305), E361 (= E436)
- binding dihydroflavine-adenine dinucleotide: L121 (≠ M187), T122 (= T188), G126 (= G192), G127 (= G193), S128 (= S194), W152 (= W222), I153 (≠ F223), S154 (≠ F224), R266 (= R331), S268 (≠ A333), F269 (= F334), I273 (≠ L338), H276 (≠ Q341), V279 (≠ M344), R334 (≠ E406), V335 (≠ C407), G338 (= G410), L356 (= L431), G360 (≠ W435), T363 (≠ A438), E365 (≠ N440), I366 (= I441)
Sites not aligning to the query:
6fahD Molecular basis of the flavin-based electron-bifurcating caffeyl-coa reductase reaction (see paper)
26% identity, 47% coverage: 187:444/553 of query aligns to 124:370/379 of 6fahD
- active site: L124 (≠ M187), T125 (= T188), G241 (≠ T305)
- binding flavin-adenine dinucleotide: L124 (≠ M187), T125 (= T188), R152 (≠ H220), F155 (= F223), T157 (≠ S225), E198 (≠ K265), R267 (= R331), Q269 (≠ A333), F270 (= F334), I274 (≠ L338), F277 (≠ Q341), Q335 (≠ E406), I336 (≠ C407), G339 (= G410), Y361 (≠ W435), T364 (≠ A438), Q366 (≠ N440)
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)
29% identity, 48% coverage: 187:451/553 of query aligns to 154:411/412 of P16219
- R171 (≠ V204) to W: 69% of wild-type acyl-CoA dehydrogenase activity; confers susceptibility to ethylmalonicaciduria; dbSNP:rs1800556
- WIT 185:187 (≠ IIG 217:219) binding in other chain
- A192 (≠ F224) to V: in ACADSD; loss of acyl-CoA dehydrogenase activity; dbSNP:rs28940874
- G209 (= G241) to S: 86% of wild-type acyl-CoA dehydrogenase activity; confers susceptibility to ethylmalonicaciduria; dbSNP:rs1799958
- R297 (= R331) binding
- Q308 (≠ P342) binding in other chain
- R325 (≠ T359) to W: in ACADSD; loss of acyl-CoA dehydrogenase activity; dbSNP:rs121908006
- S353 (≠ P387) to L: in ACADSD; loss of acyl-CoA dehydrogenase activity; dbSNP:rs28941773
- QILGG 365:369 (≠ ECLGG 406:410) binding
- R380 (= R424) to W: in ACADSD; loss of acyl-CoA dehydrogenase activity; dbSNP:rs28940875
- TSE 394:396 (≠ AGN 438:440) binding in other chain
Sites not aligning to the query:
- 1:24 modified: transit peptide, Mitochondrion
- 90 G → S: in ACADSD; loss of acyl-CoA dehydrogenase activity; dbSNP:rs121908005
- 104 natural variant: Missing (in ACADSD; loss of acyl-CoA dehydrogenase activity; dbSNP:rs387906308)
- 152:161 binding in other chain
7y0bA Crystal structure of human short-chain acyl-coa dehydrogenase
29% identity, 48% coverage: 187:451/553 of query aligns to 127:384/385 of 7y0bA
- binding (2S,3R,4R,5S,6R)-2-[4-chloranyl-3-[[4-[(3S)-oxolan-3-yl]oxyphenyl]methyl]phenyl]-6-(hydroxymethyl)oxane-3,4,5-triol: M343 (≠ N411), T347 (≠ E415), E348 (= E419)
- binding flavin-adenine dinucleotide: L127 (≠ M187), S128 (≠ T188), G133 (= G193), S134 (= S194), W158 (≠ I217), T160 (≠ G219), R270 (= R331), F273 (= F334), L280 (≠ Q341), V282 (≠ L343), Q338 (≠ E406), I339 (≠ C407), G342 (= G410), I360 (≠ L431), Y364 (≠ W435), T367 (≠ A438), E369 (≠ N440), I370 (= I441), L373 (= L444)
Sites not aligning to the query:
7y0aC Crystal structure of human short-chain acyl-coa dehydrogenase
29% identity, 48% coverage: 187:451/553 of query aligns to 130:387/387 of 7y0aC
- binding flavin-adenine dinucleotide: L130 (≠ M187), S131 (≠ T188), G136 (= G193), S137 (= S194), W161 (≠ I217), T163 (≠ G219), T214 (≠ S275), R273 (= R331), F276 (= F334), L280 (= L338), L283 (≠ Q341), V285 (≠ L343), Q341 (≠ E406), I342 (≠ C407), G345 (= G410), I363 (≠ L431), Y367 (≠ W435), T370 (≠ A438), E372 (≠ N440), L376 (= L444)
Sites not aligning to the query:
8sgsA Short-chain specific acyl-CoA dehydrogenase, mitochondrial (see paper)
29% identity, 48% coverage: 187:451/553 of query aligns to 124:381/381 of 8sgsA
- binding coenzyme a: S131 (= S194), A133 (≠ V196), N177 (≠ P239), F231 (≠ V295), M235 (≠ L299), L238 (≠ G302), I312 (≠ E376), E362 (= E436), G363 (= G437)
- binding flavin-adenine dinucleotide: L124 (≠ M187), S125 (≠ T188), G130 (= G193), S131 (= S194), W155 (≠ I217), T157 (≠ G219), R267 (= R331), F270 (= F334), L274 (= L338), L277 (≠ Q341), Q335 (≠ E406), I336 (≠ C407), G338 (= G409), G339 (= G410), I357 (≠ L431), I360 (= I434), Y361 (≠ W435), T364 (≠ A438), E366 (≠ N440)
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)
28% identity, 48% coverage: 187:451/553 of query aligns to 154:411/412 of P15651
Sites not aligning to the query:
- 1:24 modified: transit peptide, Mitochondrion
- 152:161 binding
4l1fA Electron transferring flavoprotein of acidaminococcus fermentans: towards a mechanism of flavin-based electron bifurcation (see paper)
26% identity, 48% coverage: 185:452/553 of query aligns to 123:379/380 of 4l1fA
- active site: L125 (≠ M187), T126 (= T188), G242 (≠ T305), E363 (= E436), R375 (= R448)
- binding coenzyme a persulfide: T132 (≠ S194), H179 (≠ G240), F232 (≠ V295), M236 (≠ L299), E237 (= E300), L239 (≠ G302), D240 (≠ T303), R243 (= R306), Y362 (≠ W435), E363 (= E436), G364 (= G437), R375 (= R448)
- binding flavin-adenine dinucleotide: F123 (≠ M185), L125 (≠ M187), T126 (= T188), G131 (= G193), T132 (≠ S194), F156 (= F223), I157 (≠ F224), T158 (≠ S225), R268 (= R331), Q270 (≠ A333), F271 (= F334), I275 (≠ L338), F278 (≠ Q341), L281 (≠ M344), Q336 (≠ E406), I337 (≠ C407), G340 (= G410), I358 (≠ L431), Y362 (≠ W435), T365 (≠ A438), Q367 (≠ N440)
Sites not aligning to the query:
1jqiA Crystal structure of rat short chain acyl-coa dehydrogenase complexed with acetoacetyl-coa (see paper)
28% identity, 48% coverage: 187:451/553 of query aligns to 127:384/384 of 1jqiA
- active site: G377 (vs. gap)
- binding acetoacetyl-coenzyme a: S134 (= S194), F234 (≠ V295), M238 (≠ L299), Q239 (≠ E300), L241 (≠ G302), D242 (≠ T303), R245 (= R306), Y364 (≠ W435), E365 (= E436), G366 (= G437)
- binding flavin-adenine dinucleotide: L127 (≠ M187), S128 (≠ T188), G133 (= G193), S134 (= S194), W158 (≠ I217), T160 (≠ G219), R270 (= R331), F273 (= F334), L280 (≠ Q341), Q338 (≠ E406), I339 (≠ C407), G342 (= G410), I360 (≠ L431), T367 (≠ A438), E369 (≠ N440), I370 (= I441)
Sites not aligning to the query:
Query Sequence
>Ac3H11_2514 FitnessBrowser__acidovorax_3H11:Ac3H11_2514
MTAASPAATHEVFNQSTPWADVNLFTTNQPLQDALRLHAPGLPLAGLAALGAEMGSAEMQ
AHARLANTYKPQLRTHDRFGHRTDVVEFHPSYHALIGAALRHGLHATPWSRQDTGHAHIE
RAAGFMLFTEAEPSVLCPVSMSYAVTPALRGNAAVWADWSKGLASTQYDPRLALFSQKSA
LTMGMGMTEKQGGSDVRANTTQAVPDGEDAWGARYRIIGHKWFFSAPMCDAFLILAQAPG
GLTCFFLPRVLPDDTVNAIRIQRLKDKLGNHANASSEVEFIGATAWRVGEEGRGVAQILE
MGTMTRLDCALGTSGLMRQALSIALHHTRQRSAFGKKLIDQPLMRNVLADLALESEAATA
LSIRLASAFDHKDKSEHEAVMARLLTPVAKFWVCKRGSVFAQEAMECLGGNGYVEEGGEG
TMARIYREMPLNSIWEGAGNIMALDLLRAVRRADTAAALADELAPARGAHPALDRMASAL
PLRVDAMTTEAEARRLAQDVALAVQAALLYRSAPSAVFSAFCDSRLGGDWGYSFGTLGAG
VEFDLLLNRALPA
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