SitesBLAST
Comparing Ga0059261_0740 FitnessBrowser__Korea:Ga0059261_0740 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
48% identity, 98% coverage: 12:540/540 of query aligns to 2:541/541 of 5ez3B
- active site: M181 (= M188), T182 (= T189), T295 (= T304), E423 (= E426), R435 (= R438)
- binding flavin-adenine dinucleotide: M181 (= M188), T182 (= T189), G186 (= G193), G187 (= G194), T188 (≠ S195), F213 (= F221), S215 (= S223), R321 (= R330), F324 (= F333), L328 (= L337), Q331 (= Q340), M334 (= M343), E396 (= E399), C397 (= C400), G399 (= G402), G400 (= G403), W422 (= W425), E423 (= E426), S425 (= S428), N427 (= N430), L431 (= L434)
3u33A Crystal structure of the e. Coli adaptive response protein aidb in the space group p3(2) (see paper)
44% identity, 94% coverage: 12:517/540 of query aligns to 5:519/540 of 3u33A
- active site: M184 (= M188), T185 (= T189), T298 (= T304), E425 (= E426), R437 (= R438)
- binding flavin-adenine dinucleotide: M182 (= M186), M184 (= M188), T185 (= T189), G190 (= G194), S191 (= S195), F216 (= F221), S218 (= S223), R324 (= R330), F327 (= F333), L331 (= L337), Q334 (= Q340), M337 (= M343), E398 (= E399), V399 (≠ C400), G401 (= G402), G402 (= G403), W424 (= W425), G426 (= G427), S427 (= S428), N429 (= N430), L433 (= L434)
P33224 Putative acyl-CoA dehydrogenase AidB; EC 1.3.99.- from Escherichia coli (strain K12) (see paper)
44% identity, 94% coverage: 12:517/540 of query aligns to 5:519/541 of P33224
- 182:191 (vs. 186:195, 90% identical) binding FAD
- T185 (= T189) binding FAD
- S191 (= S195) binding FAD
- FFS 216:218 (≠ FCS 221:223) binding FAD
- S218 (= S223) binding FAD
- 423:433 (vs. 424:434, 73% identical) binding FAD
- N429 (= N430) binding FAD
- R437 (= R438) mutation to Q: Does not affect DNA binding affinity.
- R518 (= R516) mutation to Q: Reduces DNA binding affinity.
4y9jB Crystal structure of caenorhabditis elegans acdh-11 in complex with c11-coa (see paper)
32% identity, 76% coverage: 31:443/540 of query aligns to 35:464/593 of 4y9jB
- active site: M190 (= M188), T191 (= T189), T315 (= T304), E446 (= E426), R458 (= R438)
- binding flavin-adenine dinucleotide: Q188 (≠ M186), M190 (= M188), T191 (= T189), G196 (= G194), S197 (= S195), F223 (= F221), S224 (≠ C222), S225 (= S223), R341 (= R330), V343 (≠ A332), F344 (= F333), Q348 (≠ L337), E419 (= E399), C420 (= C400), G422 (= G402), G423 (= G403), Y426 (= Y406), W445 (= W425), T448 (≠ S428), V451 (= V431), L454 (= L434)
- 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 (= S137), A147 (≠ T141), Q188 (≠ M186), S197 (= S195), S249 (≠ Q237), R303 (= R292), V305 (= V294), S309 (≠ I298), L312 (≠ V301), N313 (≠ Q302), R316 (= R305), A322 (≠ G311), R396 (= R376), W445 (= W425), E446 (= E426), V451 (= V431), R458 (= R438)
Q9XWZ2 Acyl-CoA dehydrogenase family member 11; EC 1.3.99.- from Caenorhabditis elegans (see paper)
32% identity, 76% coverage: 31:443/540 of query aligns to 53:482/617 of Q9XWZ2
- E91 (≠ N70) mutation to K: In n5655; suppresses the defects in egg-laying and response to reoxygenation of paqr-2 mutants.
- S156 (≠ A132) mutation to F: In n5657; suppresses the defects in egg-laying and response to reoxygenation of paqr-2 mutants.
- G158 (≠ S134) mutation to R: In n5661; suppresses the defects in egg-laying and response to reoxygenation of paqr-2 mutants.
- G214 (= G194) mutation to E: In n5879; suppresses the defects in egg-laying and response to reoxygenation of paqr-2 mutants.
- G443 (= G405) mutation to R: In n5877; suppresses the defects in egg-laying and response to reoxygenation of paqr-2 mutants.
- R455 (= R417) mutation to H: In n5876; suppresses the defects in egg-laying and response to reoxygenation of paqr-2 mutants.
6sdaB Bd2924 c10 acyl-coenzymea bound form (see paper)
31% identity, 79% coverage: 26:454/540 of query aligns to 11:454/503 of 6sdaB
- active site: M171 (= M188), T172 (= T189), T296 (= T304), R439 (= R438)
- binding flavin-adenine dinucleotide: Q169 (≠ M186), M171 (= M188), T172 (= T189), G177 (= G194), S178 (= S195), F208 (= F221), T209 (≠ C222), R322 (= R330), F325 (= F333), L329 (= L337), H332 (≠ Q340), E400 (= E399), M401 (≠ C400), G404 (= G403), Y407 (= Y406), W426 (= W425), T429 (≠ S428), N431 (= N430), L435 (= L434)
- binding decanoyl-CoA: C128 (= C138), G177 (= G194), S178 (= S195), S230 (vs. gap), V286 (= V294), A290 (≠ I298), L293 (≠ V301), N294 (≠ Q302), R297 (= R305), R377 (= R376), W426 (= W425), E427 (= E426)
6sd8X Bd2924 apo-form (see paper)
31% identity, 79% coverage: 26:454/540 of query aligns to 11:454/503 of 6sd8X
- active site: M171 (= M188), T172 (= T189), T296 (= T304), R439 (= R438)
- binding flavin-adenine dinucleotide: Q169 (≠ M186), M171 (= M188), T172 (= T189), G176 (= G193), G177 (= G194), S178 (= S195), F208 (= F221), T209 (≠ C222), R322 (= R330), F325 (= F333), L329 (= L337), H332 (≠ Q340), M401 (≠ C400), G404 (= G403), W426 (= W425), T429 (≠ S428), V432 (= V431), L435 (= L434)
7p9xA Structure of cyclohex-1-ene-1-carboxyl-coa dehydrogenase complexed with cyclohex-1-ene-1-carboxyl-coa (see paper)
26% identity, 66% coverage: 86:440/540 of query aligns to 28:375/378 of 7p9xA
- binding 1-monoenoyl-CoA: L82 (≠ V147), D89 (≠ E154), S129 (= S195), L131 (≠ V197), K176 (≠ G238), F229 (≠ V294), M233 (≠ I298), L236 (≠ V301), R240 (= R305), Y360 (≠ W425), T361 (≠ E426), G362 (= G427), R373 (= R438)
- binding flavin-adenine dinucleotide: A122 (≠ M188), T123 (= T189), G128 (= G194), S129 (= S195), F153 (= F221), I154 (≠ C222), T155 (≠ S223), N206 (≠ S274), L356 (= L421), Y360 (≠ W425), T363 (≠ S428), Q365 (≠ N430), I366 (≠ V431)
7p9aA Structure of cyclohex-1-ene-1-carboxyl-coa dehydrogenase complexed with cyclohex-1,5-diene-1-carboxyl-coa (see paper)
26% identity, 66% coverage: 86:440/540 of query aligns to 30:377/380 of 7p9aA
- binding 1,5 Dienoyl-CoA: S131 (= S195), L133 (≠ V197), K178 (≠ G238), F231 (≠ V294), M235 (≠ I298), L238 (≠ V301), N241 (≠ T304), R242 (= R305), Y362 (≠ W425), T363 (≠ E426), G364 (= G427), R375 (= R438)
- binding flavin-adenine dinucleotide: L122 (≠ M186), A124 (≠ M188), T125 (= T189), G130 (= G194), S131 (= S195), F155 (= F221), I156 (≠ C222), T157 (≠ S223), K200 (= K266), N208 (≠ S274), L358 (= L421), T365 (≠ S428), Q367 (≠ N430), I368 (≠ V431)
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)
26% identity, 66% coverage: 86:440/540 of query aligns to 30:377/380 of Q39QF5
- D91 (≠ E154) 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 (≠ M186) binding FAD
- A124 (≠ M188) binding FAD
- T125 (= T189) binding FAD
- S131 (= S195) binding cyclohex-1-ene-1-carbonyl-CoA; binding cyclohexa-1,5-diene-1-carbonyl-CoA; binding FAD
- T157 (≠ S223) binding FAD
- K178 (≠ G238) binding cyclohex-1-ene-1-carbonyl-CoA; binding cyclohexa-1,5-diene-1-carbonyl-CoA
- N241 (≠ T304) 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 (= R305) binding cyclohex-1-ene-1-carbonyl-CoA; binding cyclohexa-1,5-diene-1-carbonyl-CoA
- T363 (≠ E426) 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 (≠ S428) binding FAD
- Q367 (≠ N430) binding FAD
- R375 (= R438) binding cyclohex-1-ene-1-carbonyl-CoA; binding cyclohexa-1,5-diene-1-carbonyl-CoA
1ukwB Crystal structure of medium-chain acyl-coa dehydrogenase from thermus thermophilus hb8
29% identity, 49% coverage: 174:440/540 of query aligns to 111:376/379 of 1ukwB
- active site: L124 (≠ M188), S125 (≠ T189), T241 (= T304), E362 (= E426), R374 (= R438)
- binding cobalt (ii) ion: D145 (≠ E209), H146 (≠ W212)
- binding flavin-adenine dinucleotide: F122 (≠ M186), L124 (≠ M188), S125 (≠ T189), G130 (= G194), S131 (= S195), W155 (= W220), S157 (≠ C222), K200 (= K266), L357 (= L421), Y361 (≠ W425), E362 (= E426), T364 (≠ S428), E366 (≠ N430), L370 (= L434)
1ukwA Crystal structure of medium-chain acyl-coa dehydrogenase from thermus thermophilus hb8
29% identity, 49% coverage: 174:440/540 of query aligns to 111:376/379 of 1ukwA
- active site: L124 (≠ M188), S125 (≠ T189), T241 (= T304), E362 (= E426), R374 (= R438)
- binding flavin-adenine dinucleotide: F122 (≠ M186), L124 (≠ M188), S125 (≠ T189), G130 (= G194), S131 (= S195), W155 (= W220), S157 (≠ C222), L357 (= L421), Y361 (≠ W425), E362 (= E426), T364 (≠ S428), E366 (≠ N430), L370 (= L434)
1ivhA Structure of human isovaleryl-coa dehydrogenase at 2.6 angstroms resolution: structural basis for substrate specificity (see paper)
26% identity, 64% coverage: 95:440/540 of query aligns to 47:384/387 of 1ivhA
- active site: M130 (= M188), S131 (≠ T189), E249 (≠ T304), A370 (≠ E426), R382 (= R438)
- binding coenzyme a persulfide: S137 (= S195), S185 (≠ Q237), R186 (≠ G238), V239 (= V294), Y240 (≠ A295), M243 (≠ I298), E249 (≠ T304), R250 (= R305), G369 (≠ W425), A370 (≠ E426), G371 (= G427), V375 (= V431)
- binding flavin-adenine dinucleotide: L128 (≠ M186), M130 (= M188), S131 (≠ T189), G136 (= G194), S137 (= S195), W161 (= W220), T163 (≠ C222), R275 (= R330), F278 (= F333), F285 (≠ Q340), M288 (= M343), Q343 (≠ E399), C344 (= C400), G347 (= G403), T372 (≠ S428), E374 (≠ N430)
8sgrA Human liver mitochondrial isovaleryl-coa dehydrogenase (see paper)
26% identity, 64% coverage: 95:440/540 of query aligns to 51:388/393 of 8sgrA
- binding flavin-adenine dinucleotide: S135 (≠ T189), G140 (= G194), S141 (= S195), W165 (= W220), T167 (≠ C222), R279 (= R330), F282 (= F333), I286 (≠ L337), F289 (≠ Q340), Q347 (≠ E399), C348 (= C400), G351 (= G403), L369 (= L421), G375 (= G427), T376 (≠ S428), L382 (= L434)
P26440 Isovaleryl-CoA dehydrogenase, mitochondrial; IVD; Butyryl-CoA dehydrogenase; EC 1.3.8.4; EC 1.3.8.1 from Homo sapiens (Human) (see 5 papers)
26% identity, 64% coverage: 95:440/540 of query aligns to 84:421/426 of P26440
- 165:174 (vs. 186:195, 50% identical) binding FAD
- S174 (= S195) binding substrate
- WIT 198:200 (≠ WFC 220:222) binding FAD
- SR 222:223 (≠ QG 237:238) binding substrate
- G250 (≠ S271) to A: in IVA; uncertain significance
- Y277 (≠ A295) binding substrate
- DLER 284:287 (≠ QHTR 302:305) binding substrate
- E286 (≠ T304) active site, Proton acceptor; mutation to D: Residual isovaleryl-CoA dehydrogenase activity.; mutation to G: Loss of isovaleryl-CoA dehydrogenase activity. Does not affect isovaleryl-CoA dehydrogenase activity; when associated with 407-E.; mutation to Q: Loss of isovaleryl-CoA dehydrogenase activity.
- A291 (≠ V309) to V: in IVA; uncertain significance; dbSNP:rs886042098
- R312 (= R330) binding FAD
- Q323 (≠ P341) binding FAD
- I379 (≠ M398) to T: in IVA; uncertain significance
- QCFGG 380:384 (≠ ECHGG 399:403) binding FAD
- R398 (= R417) to Q: in IVA; uncertain significance; dbSNP:rs1477527791
- Y403 (≠ N422) to N: in IVA; uncertain significance
- A407 (≠ E426) mutation to E: Does not affect isovaleryl-CoA dehydrogenase activity; when associated with 286-D.
- AG 407:408 (≠ EG 426:427) binding substrate
- TSE 409:411 (≠ SGN 428:430) binding FAD
Sites not aligning to the query:
- 1:32 modified: transit peptide, Mitochondrion
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)
27% identity, 48% coverage: 186:445/540 of query aligns to 161:455/591 of A3SI50
- M161 (= M186) mutation to A: Retains 37% of wild-type activity.
- T170 (≠ S195) mutation to A: Retains 8.8% of wild-type activity.
- F195 (= F221) mutation to A: Almost completely abolishes the activity.
- S197 (= S223) mutation to A: Retains 3.6% of wild-type activity.
- K223 (≠ G238) mutation to A: Retains 9.4% of wild-type activity.
- H280 (≠ G291) mutation to A: Retains 18% of wild-type activity.
- K281 (≠ R292) mutation to A: Retains 54% of wild-type activity.
- R284 (≠ A295) mutation to A: Retains 97% of wild-type activity.
- F287 (≠ I298) mutation to A: Retains 76% of wild-type activity.
- Y434 (≠ W425) mutation to A: Retains 51% of wild-type activity.
- E435 (= E426) mutation to A: Loss of activity.
- R448 (= R438) mutation to A: Retains 44% of wild-type activity.
6fahD Molecular basis of the flavin-based electron-bifurcating caffeyl-coa reductase reaction (see paper)
27% identity, 46% coverage: 184:431/540 of query aligns to 120:367/379 of 6fahD
- active site: L124 (≠ M188), T125 (= T189), G241 (≠ T304)
- binding flavin-adenine dinucleotide: F122 (≠ M186), L124 (≠ M188), T125 (= T189), R152 (≠ H218), F155 (= F221), T157 (≠ S223), E198 (≠ K264), R267 (= R330), Q269 (≠ A332), F270 (= F333), I274 (≠ L337), F277 (≠ Q340), Q335 (≠ E399), I336 (≠ C400), G339 (= G403), Y361 (≠ W425), T364 (≠ S428), Q366 (≠ N430)
Sites not aligning to the query:
4l1fA Electron transferring flavoprotein of acidaminococcus fermentans: towards a mechanism of flavin-based electron bifurcation (see paper)
27% identity, 50% coverage: 175:443/540 of query aligns to 113:380/380 of 4l1fA
- active site: L125 (≠ M188), T126 (= T189), G242 (≠ T304), E363 (= E426), R375 (= R438)
- binding coenzyme a persulfide: T132 (≠ S195), H179 (vs. gap), F232 (≠ V294), M236 (≠ I298), E237 (≠ Q299), L239 (≠ V301), D240 (≠ Q302), R243 (= R305), Y362 (≠ W425), E363 (= E426), G364 (= G427), R375 (= R438)
- binding flavin-adenine dinucleotide: F123 (≠ M186), L125 (≠ M188), T126 (= T189), G131 (= G194), T132 (≠ S195), F156 (= F221), I157 (≠ C222), T158 (≠ S223), R268 (= R330), Q270 (≠ A332), F271 (= F333), I275 (≠ L337), F278 (≠ Q340), L281 (≠ M343), Q336 (≠ E399), I337 (≠ C400), G340 (= G403), I358 (≠ L421), Y362 (≠ W425), T365 (≠ S428), Q367 (≠ N430)
Sites not aligning to the query:
2jifA Structure of human short-branched chain acyl-coa dehydrogenase (acadsb)
29% identity, 47% coverage: 176:431/540 of query aligns to 116:368/381 of 2jifA
- active site: L125 (≠ M188), S126 (≠ T189), G242 (≠ T304), E363 (= E426)
- binding coenzyme a persulfide: S132 (= S195), S134 (≠ V197), Y178 (vs. gap), Y232 (≠ V294), I236 (= I298), L239 (≠ V301), N240 (≠ Q302), R243 (= R305), Y362 (≠ W425), E363 (= E426), G364 (= G427), I368 (≠ V431)
- binding flavin-adenine dinucleotide: F123 (≠ M186), L125 (≠ M188), S126 (≠ T189), G131 (= G194), S132 (= S195), W156 (= W220), I157 (≠ F221), S158 (≠ C222), K201 (= K266), T209 (≠ S274), R268 (= R330), F271 (= F333), L275 (= L337), F278 (≠ Q340), L281 (≠ M343), E336 (= E399), W337 (≠ C400), G340 (= G403), N367 (= N430), I368 (≠ V431)
Sites not aligning to the query:
7xp7B Crystal structure of the flavoprotein colb1 catalyzing assembly line- tethered cysteine dehydrogenation (see paper)
33% identity, 49% coverage: 186:448/540 of query aligns to 115:376/376 of 7xp7B
- binding flavin-adenine dinucleotide: F115 (≠ M186), L117 (≠ M188), S118 (≠ T189), G123 (= G194), S124 (= S195), W148 (= W220), S150 (≠ C222), R255 (= R330), F258 (= F333), I262 (≠ L337), H265 (≠ Q340), V268 (≠ M343), E326 (= E399), T327 (≠ C400), G330 (= G403), I351 (= I424), Y352 (≠ W425), T355 (≠ S428), N357 (= N430)
Query Sequence
>Ga0059261_0740 FitnessBrowser__Korea:Ga0059261_0740
MSSIRPIVQLDTHEVLNQPPPFEEVNLFTGDRALADAVARAGGARHRERLTSLGARCGSA
EVIDWGVEANRNIPVLESYDRFGQRIDEVRFHPAYHQLMRLGLDSGLASVAWDGTPAGHV
AHAAILFLTGQADSGTSCPMTMTYAAVPALRADEGVAGEWVPRITAGLYDPASRPAAEKA
GVTIGMAMTEKQGGSDVRANTTRAEPAGEAGWYSLTGHKWFCSAPMCDAFLTLAYAQGGL
TCFLVPRWLPDGTRNAGFRVMRLKDKLGDRSNASSEIEYHGALAQRLGEEGRGVATIIQM
VQHTRLDCVIGSAQQMRGALAQALWHTAHRSAFQRRLIDQPAMAAVLADLAVESEAATVL
GLRLAQAFDEADPVARLLTPIAKYWVCKRAPGLVYEAMECHGGGGYIEAGPMPRLFRQSP
LNAIWEGSGNVIALDLLRAIGREPGGVEALNGFLAAQRGRDAAYDAWIGVIDLKSAHEGN
ARLCVEQLALAAQAAVLLGWDSPGADAFCRLRLSPRGSAYGAFDAVVDTRALIERAMPVA
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