SitesBLAST
Comparing H281DRAFT_01203 H281DRAFT_01203 acetyl-CoA synthetase 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)
8biqA Crystal structure of acyl-coa synthetase from metallosphaera sedula in complex with acetyl-amp
40% identity, 90% coverage: 33:540/567 of query aligns to 33:542/562 of 8biqA
8biqB Crystal structure of acyl-coa synthetase from metallosphaera sedula in complex with acetyl-amp
40% identity, 90% coverage: 33:540/567 of query aligns to 32:541/561 of 8biqB
- binding [[(2~{R},3~{S},4~{R},5~{R})-5-(6-aminopurin-9-yl)-3,4-bis(oxidanyl)oxolan-2-yl]methoxy-oxidanyl-phosphoryl] ethanoate: G319 (= G318), E320 (= E319), P321 (= P320), D340 (= D339), F341 (≠ G340), Y342 (≠ F341), G343 (= G342), Q344 (= Q343), T345 (= T344), D426 (= D426), F438 (≠ Y438), K447 (= K447), R452 (= R452)
8bitA Crystal structure of acyl-coa synthetase from metallosphaera sedula in complex with coenzyme a and acetyl-amp
40% identity, 90% coverage: 33:540/567 of query aligns to 34:543/562 of 8bitA
- binding [[(2~{R},3~{S},4~{R},5~{R})-5-(6-aminopurin-9-yl)-3,4-bis(oxidanyl)oxolan-2-yl]methoxy-oxidanyl-phosphoryl] ethanoate: W252 (= W251), G321 (= G318), E322 (= E319), P323 (= P320), D342 (= D339), F343 (≠ G340), Y344 (≠ F341), Q346 (= Q343), T347 (= T344), D428 (= D426), F440 (≠ Y438), K449 (= K447), R454 (= R452)
- binding coenzyme a: N128 (≠ Q125), W247 (= W246), K249 (= K248), K273 (≠ R271), L274 (≠ F272), Q300 (≠ M298), D452 (= D450), Y453 (= Y451), R483 (= R481), P517 (= P515)
3c5eA Crystal structure of human acyl-coa synthetase medium-chain family member 2a (l64p mutation) in complex with atp (see paper)
33% identity, 90% coverage: 35:544/567 of query aligns to 10:534/536 of 3c5eA
- active site: T188 (= T202), T331 (= T344), E332 (= E345), N434 (≠ K447), R439 (= R452), K524 (= K534)
- binding adenosine-5'-triphosphate: T188 (= T202), S189 (= S203), G190 (= G204), T191 (= T205), S192 (≠ T206), G305 (= G318), E306 (= E319), S307 (≠ P320), G329 (= G342), Q330 (= Q343), T331 (= T344), D413 (= D426), F425 (≠ Y438), R428 (= R441), K524 (= K534)
- binding magnesium ion: M450 (≠ I463), H452 (= H465), V455 (≠ I468)
3b7wA Crystal structure of human acyl-coa synthetase medium-chain family member 2a, with l64p mutation (see paper)
33% identity, 90% coverage: 35:544/567 of query aligns to 11:535/537 of 3b7wA
3eq6A Crystal structure of human acyl-coa synthetase medium-chain family member 2a (l64p mutation) in a ternary complex with products (see paper)
33% identity, 90% coverage: 35:544/567 of query aligns to 7:531/533 of 3eq6A
- active site: T185 (= T202), T328 (= T344), E329 (= E345), N431 (≠ K447), R436 (= R452), K521 (= K534)
- binding adenosine monophosphate: G302 (= G318), E303 (= E319), S304 (≠ P320), E323 (≠ D339), S324 (≠ G340), Y325 (≠ F341), G326 (= G342), Q327 (= Q343), T328 (= T344), D410 (= D426), F422 (≠ Y438), R425 (= R441), R436 (= R452)
- binding Butyryl Coenzyme A: W229 (= W246), F255 (= F272), I277 (≠ T294), V301 (≠ A317), S433 (= S449), G434 (≠ D450), Y435 (= Y451), P501 (= P515), Y502 (= Y516), Y504 (≠ R518), R506 (= R520)
2wd9A Crystal structure of human acyl-coa synthetase medium-chain family member 2a (l64p mutation) in complex with ibuprofen (see paper)
33% identity, 90% coverage: 35:544/567 of query aligns to 7:531/533 of 2wd9A
- active site: T185 (= T202), T328 (= T344), E329 (= E345), N431 (≠ K447), R436 (= R452), K521 (= K534)
- binding ibuprofen: I230 (≠ A247), L231 (≠ K248), G326 (= G342), Q327 (= Q343), T328 (= T344), R436 (= R452)
2vzeA Crystal structure of human acyl-coa synthetase medium-chain family member 2a (l64p mutation) in complex with amp (see paper)
33% identity, 90% coverage: 35:544/567 of query aligns to 7:531/533 of 2vzeA
- active site: T185 (= T202), T328 (= T344), E329 (= E345), N431 (≠ K447), R436 (= R452), K521 (= K534)
- binding adenosine monophosphate: W229 (= W246), G302 (= G318), E303 (= E319), S304 (≠ P320), E323 (≠ D339), Y325 (≠ F341), G326 (= G342), Q327 (= Q343), T328 (= T344), D410 (= D426), F422 (≠ Y438), R425 (= R441), R436 (= R452)
Q08AH3 Acyl-coenzyme A synthetase ACSM2A, mitochondrial; Acyl-CoA synthetase medium-chain family member 2A; Benzoate--CoA ligase; Butyrate--CoA ligase 2A; Butyryl-coenzyme A synthetase 2A; Middle-chain acyl-CoA synthetase 2A; EC 6.2.1.2; EC 6.2.1.25 from Homo sapiens (Human) (see 4 papers)
33% identity, 90% coverage: 35:544/567 of query aligns to 43:567/577 of Q08AH3
- Q139 (= Q125) binding
- 221:229 (vs. 202:210, 67% identical) binding
- ESYGQT 359:364 (≠ DGFGQT 339:344) binding
- T364 (= T344) binding
- D446 (= D426) binding
- R461 (= R441) binding
- SGY 469:471 (≠ SDY 449:451) binding
- R472 (= R452) binding
- R501 (= R481) binding
- S513 (≠ H493) to L: in dbSNP:rs1133607
- K532 (≠ R510) binding
- YPR 540:542 (≠ RIR 518:520) binding
- K557 (= K534) binding
3dayA Crystal structure of human acyl-coa synthetase medium-chain family member 2a (l64p mutation) in complex with amp-cpp (see paper)
33% identity, 90% coverage: 35:544/567 of query aligns to 11:533/535 of 3dayA
- active site: T189 (= T202), T332 (= T344), E333 (= E345), N435 (≠ K447), R440 (= R452), K523 (= K534)
- binding diphosphomethylphosphonic acid adenosyl ester: T189 (= T202), S190 (= S203), G191 (= G204), T192 (= T205), S193 (≠ T206), K197 (= K210), G306 (= G318), E307 (= E319), S308 (≠ P320), Y329 (≠ F341), G330 (= G342), Q331 (= Q343), T332 (= T344), D414 (= D426), F426 (≠ Y438), R429 (= R441), K523 (= K534)
- binding magnesium ion: M451 (≠ I463), H453 (= H465), V456 (≠ I468)
3gpcA Crystal structure of human acyl-coa synthetase medium-chain family member 2a (l64p mutation) in a complex with coa (see paper)
33% identity, 90% coverage: 35:544/567 of query aligns to 8:530/532 of 3gpcA
- active site: T186 (= T202), T327 (= T344), E328 (= E345), N430 (≠ K447), R435 (= R452), K520 (= K534)
- binding coenzyme a: G301 (= G318), E302 (= E319), S303 (≠ P320), E322 (≠ D339), Y324 (≠ F341), G325 (= G342), Q326 (= Q343), T327 (= T344), D409 (= D426), F421 (≠ Y438), R424 (= R441), T516 (= T530), K520 (= K534), Q522 (≠ R536)
- binding magnesium ion: H448 (= H465), V451 (≠ I468)
Q89WV5 Acetyl-coenzyme A synthetase; AcCoA synthetase; Acs; Acetate--CoA ligase; Acyl-activating enzyme; EC 6.2.1.1 from Bradyrhizobium diazoefficiens (strain JCM 10833 / BCRC 13528 / IAM 13628 / NBRC 14792 / USDA 110) (see paper)
31% identity, 90% coverage: 48:556/567 of query aligns to 88:625/648 of Q89WV5
- G263 (= G204) mutation to I: Loss of activity.
- G266 (≠ S207) mutation to I: Great decrease in activity.
- K269 (= K210) mutation to G: Great decrease in activity.
- E414 (= E345) mutation to Q: Great decrease in activity.
6m2uA The crystal structure of benzoate coenzyme a ligase double mutant (h333a/i334a) in complex with 2-chloro-1,3-thiazole-5-carboxylate-amp (see paper)
32% identity, 90% coverage: 31:541/567 of query aligns to 3:514/518 of 6m2uA
- active site: S176 (≠ T202), T196 (≠ V221), T324 (= T344), E325 (= E345), K422 (= K447), Y427 (≠ R452), K507 (= K534)
- binding adenosine monophosphate: G298 (= G318), E299 (= E319), A300 (≠ P320), D319 (= D339), G320 (= G340), I321 (≠ F341), G322 (= G342), T324 (= T344), D401 (= D426), R416 (= R441), K422 (= K447), Y427 (≠ R452)
- binding 2-chloranyl-1,3-thiazole-5-carboxylic acid: Y223 (≠ K248), A297 (= A317), G322 (= G342), S323 (≠ Q343), A328 (≠ C348)
6m2tA The crystal structure of benzoate coenzyme a ligase double mutant (h333a/i334a) in complex with 2-methyl-thiazole-5 carboxylate-amp
32% identity, 90% coverage: 31:541/567 of query aligns to 3:514/518 of 6m2tA
- active site: S176 (≠ T202), T196 (≠ V221), T324 (= T344), E325 (= E345), K422 (= K447), Y427 (≠ R452), K507 (= K534)
- binding 2-methyl-1,3-thiazole-5-carboxylic acid: Y223 (≠ K248), G322 (= G342), S323 (≠ Q343), A328 (≠ C348)
- binding adenosine monophosphate: G298 (= G318), E299 (= E319), A300 (≠ P320), G320 (= G340), I321 (≠ F341), S323 (≠ Q343), T324 (= T344), D401 (= D426), R416 (= R441), K422 (= K447), Y427 (≠ R452)
4zjzA Crystal structure of a benzoate coenzyme a ligase with benzoyl-amp (see paper)
32% identity, 90% coverage: 31:541/567 of query aligns to 3:514/517 of 4zjzA
- active site: S176 (≠ T202), T196 (≠ V221), T324 (= T344), E325 (= E345), K422 (= K447), Y427 (≠ R452), K507 (= K534)
- binding 5'-O-[(R)-(benzoyloxy)(hydroxy)phosphoryl]adenosine: A222 (= A247), Y223 (≠ K248), A297 (= A317), G298 (= G318), E299 (= E319), A300 (≠ P320), G320 (= G340), I321 (≠ F341), G322 (= G342), S323 (≠ Q343), T324 (= T344), H328 (vs. gap), I329 (≠ C348), D401 (= D426), R416 (= R441), K422 (= K447), Y427 (≠ R452)
4rm2A Crystal structure of a benzoate coenzyme a ligase with 2-fluoro benzoic acid (see paper)
32% identity, 90% coverage: 31:541/567 of query aligns to 3:514/516 of 4rm2A
- active site: S176 (≠ T202), T196 (≠ V221), T324 (= T344), E325 (= E345), K422 (= K447), Y427 (≠ R452), K507 (= K534)
- binding 2-fluorobenzoic acid: A216 (≠ I241), A222 (= A247), Y223 (≠ K248), P246 (≠ F272), T247 (≠ V273), V251 (vs. gap), F267 (≠ V289), G269 (≠ A291), A270 (≠ P292), G273 (≠ V295), M277 (= M298), A297 (= A317), G298 (= G318), I321 (≠ F341), G322 (= G342), S323 (≠ Q343), H328 (vs. gap), K422 (= K447)
4rm3A Crystal structure of a benzoate coenzyme a ligase with 2-furoic acid (see paper)
32% identity, 90% coverage: 31:541/567 of query aligns to 4:515/518 of 4rm3A
- active site: S177 (≠ T202), T197 (≠ V221), T325 (= T344), E326 (= E345), K423 (= K447), Y428 (≠ R452), K508 (= K534)
- binding 2-furoic acid: A223 (= A247), Y224 (≠ K248), A298 (= A317), G323 (= G342), H329 (vs. gap), I330 (≠ C348), K423 (= K447)
4rmnA Crystal structure of a benzoate coenzyme a ligase with 2-thiophene carboxylic acid (see paper)
32% identity, 90% coverage: 31:541/567 of query aligns to 3:514/518 of 4rmnA
- active site: S176 (≠ T202), T196 (≠ V221), T324 (= T344), E325 (= E345), K422 (= K447), Y427 (≠ R452), K507 (= K534)
- binding thiophene-2-carboxylic acid: A217 (≠ S242), F221 (≠ W246), Y223 (≠ K248), G269 (≠ A291), A270 (≠ P292), A297 (= A317), G298 (= G318), G322 (= G342), S323 (≠ Q343), H328 (vs. gap), I329 (≠ C348), K422 (= K447), G425 (≠ D450)
4rlfB Crystal structure of a benzoate coenzyme a ligase with p-toluic acid and o-toluic acid (see paper)
32% identity, 90% coverage: 31:541/567 of query aligns to 3:514/519 of 4rlfB
- active site: S176 (≠ T202), T196 (≠ V221), T324 (= T344), E325 (= E345), K422 (= K447), Y427 (≠ R452), K507 (= K534)
- binding 2-methylbenzoic acid: A222 (= A247), Y223 (≠ K248), G298 (= G318), I321 (≠ F341), G322 (= G342), S323 (≠ Q343), H328 (vs. gap)
- binding 4-methylbenzoic acid: A216 (≠ I241), P246 (≠ F272), P248 (= P274), G269 (≠ A291), A270 (≠ P292), G273 (≠ V295)
5jrhA Crystal structure of salmonella enterica acetyl-coa synthetase (acs) in complex with camp and coenzyme a (see paper)
31% identity, 89% coverage: 36:542/567 of query aligns to 71:613/640 of 5jrhA
- active site: T260 (= T202), T412 (= T344), E413 (= E345), N517 (≠ K447), R522 (= R452), K605 (= K534)
- binding (r,r)-2,3-butanediol: W93 (≠ I57), E140 (= E104), G169 (≠ D133), K266 (= K208), P267 (= P209)
- binding adenosine-3',5'-cyclic-monophosphate: G383 (= G318), E384 (= E319), P385 (= P320), T408 (≠ G340), W409 (≠ F341), W410 (≠ G342), Q411 (= Q343), T412 (= T344), D496 (= D426), I508 (≠ Y438), N517 (≠ K447), R522 (= R452)
- binding coenzyme a: F159 (≠ T123), G160 (≠ T124), G161 (≠ Q125), R187 (vs. gap), S519 (= S449), R580 (= R510), P585 (= P515)
- binding magnesium ion: V533 (≠ I463), H535 (= H465), I538 (= I468)
Query Sequence
>H281DRAFT_01203 H281DRAFT_01203 acetyl-CoA synthetase
MTAAKAFFDARDLLLRHRTDYERAYREFAWPALEQFNWALDYFDVIARDNDNTALWIVDD
PASEGLRLSYAQMSERSARMANFLRSVGVKRGDRVLLMLPNRVELWDVMLAAMKLGAIVL
PATTQLSADDVRDRVQIGGANFVVVDSAELSKFDSLDVPLTRLSVGTPRAGWTDLAAAYD
ASPQFTPDGVTRAADPLLLYFTSGTTSKPKLVEHTHQSYPVGHLSTMYWIGLQPGDIHWN
ISSPGWAKHAWSCFFAPWNAQACVFVFNFARFVPKDTLDVLVRFNVTTVCAPPTVWRMLV
QEHLTDYPVKLREIVGAGEPLNPEIIERVKHAWGITIRDGFGQTETTCQIGNSPGQPVVA
GSMGRPLPGYRIELLDADDQPVTEGEIALPIGPDGKQRPLGLMTGYANSEQATAQAMRNG
FYRTSDVALRREDGYYVYVGRADDVFKSSDYRLSPFELESVLIEHEAIGEAAVVPSADAL
RLSVPKAFVTVRHGYQAGPELARAVFAFSREKLAPYKRIRRLQFSELPKTISGKIRRVEL
RRREMERQAEPARLPDEYWEEDFPDLR
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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