SitesBLAST
Comparing WP_028313942.1 NCBI__GCF_000429905.1:WP_028313942.1 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)
3eq6A Crystal structure of human acyl-coa synthetase medium-chain family member 2a (l64p mutation) in a ternary complex with products (see paper)
48% identity, 96% coverage: 20:540/543 of query aligns to 3:532/533 of 3eq6A
- active site: T185 (= T194), T328 (= T338), E329 (= E339), N431 (≠ L441), R436 (= R446), K521 (= K529)
- binding adenosine monophosphate: G302 (= G312), E303 (= E313), S304 (≠ P314), E323 (≠ D333), S324 (≠ G334), Y325 (= Y335), G326 (= G336), Q327 (= Q337), T328 (= T338), D410 (= D420), F422 (= F432), R425 (= R435), R436 (= R446)
- binding Butyryl Coenzyme A: W229 (= W239), F255 (= F265), I277 (≠ T287), V301 (≠ A311), S433 (= S443), G434 (= G444), Y435 (= Y445), P501 (= P509), Y502 (= Y510), Y504 (= Y512), R506 (= R514)
2wd9A Crystal structure of human acyl-coa synthetase medium-chain family member 2a (l64p mutation) in complex with ibuprofen (see paper)
48% identity, 96% coverage: 20:540/543 of query aligns to 3:532/533 of 2wd9A
- active site: T185 (= T194), T328 (= T338), E329 (= E339), N431 (≠ L441), R436 (= R446), K521 (= K529)
- binding ibuprofen: I230 (≠ A240), L231 (≠ K241), G326 (= G336), Q327 (= Q337), T328 (= T338), R436 (= R446)
2vzeA Crystal structure of human acyl-coa synthetase medium-chain family member 2a (l64p mutation) in complex with amp (see paper)
48% identity, 96% coverage: 20:540/543 of query aligns to 3:532/533 of 2vzeA
- active site: T185 (= T194), T328 (= T338), E329 (= E339), N431 (≠ L441), R436 (= R446), K521 (= K529)
- binding adenosine monophosphate: W229 (= W239), G302 (= G312), E303 (= E313), S304 (≠ P314), E323 (≠ D333), Y325 (= Y335), G326 (= G336), Q327 (= Q337), T328 (= T338), D410 (= D420), F422 (= F432), R425 (= R435), R436 (= R446)
3b7wA Crystal structure of human acyl-coa synthetase medium-chain family member 2a, with l64p mutation (see paper)
48% identity, 96% coverage: 20:540/543 of query aligns to 7:536/537 of 3b7wA
3c5eA Crystal structure of human acyl-coa synthetase medium-chain family member 2a (l64p mutation) in complex with atp (see paper)
48% identity, 96% coverage: 20:540/543 of query aligns to 6:535/536 of 3c5eA
- active site: T188 (= T194), T331 (= T338), E332 (= E339), N434 (≠ L441), R439 (= R446), K524 (= K529)
- binding adenosine-5'-triphosphate: T188 (= T194), S189 (= S195), G190 (= G196), T191 (= T197), S192 (≠ V198), G305 (= G312), E306 (= E313), S307 (≠ P314), G329 (= G336), Q330 (= Q337), T331 (= T338), D413 (= D420), F425 (= F432), R428 (= R435), K524 (= K529)
- binding magnesium ion: M450 (≠ I457), H452 (= H459), V455 (= V462)
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)
48% identity, 96% coverage: 20:540/543 of query aligns to 39:568/577 of Q08AH3
- Q139 (= Q113) binding CoA
- 221:229 (vs. 194:202, 78% identical) binding ATP
- ESYGQT 359:364 (≠ DGYGQT 333:338) binding ATP
- T364 (= T338) binding substrate
- D446 (= D420) binding ATP
- R461 (= R435) binding ATP
- SGY 469:471 (= SGY 443:445) binding CoA
- R472 (= R446) binding substrate
- R501 (= R475) binding CoA
- S513 (≠ G487) to L: in dbSNP:rs1133607
- K532 (= K504) binding CoA
- YPR 540:542 (= YPR 512:514) binding CoA
- K557 (= K529) binding ATP
3dayA Crystal structure of human acyl-coa synthetase medium-chain family member 2a (l64p mutation) in complex with amp-cpp (see paper)
48% identity, 96% coverage: 20:540/543 of query aligns to 7:534/535 of 3dayA
- active site: T189 (= T194), T332 (= T338), E333 (= E339), N435 (≠ L441), R440 (= R446), K523 (= K529)
- binding diphosphomethylphosphonic acid adenosyl ester: T189 (= T194), S190 (= S195), G191 (= G196), T192 (= T197), S193 (≠ V198), K197 (= K202), G306 (= G312), E307 (= E313), S308 (≠ P314), Y329 (= Y335), G330 (= G336), Q331 (= Q337), T332 (= T338), D414 (= D420), F426 (= F432), R429 (= R435), K523 (= K529)
- binding magnesium ion: M451 (≠ I457), H453 (= H459), V456 (= V462)
3gpcA Crystal structure of human acyl-coa synthetase medium-chain family member 2a (l64p mutation) in a complex with coa (see paper)
48% identity, 96% coverage: 20:540/543 of query aligns to 4:531/532 of 3gpcA
- active site: T186 (= T194), T327 (= T338), E328 (= E339), N430 (≠ L441), R435 (= R446), K520 (= K529)
- binding coenzyme a: G301 (= G312), E302 (= E313), S303 (≠ P314), E322 (≠ D333), Y324 (= Y335), G325 (= G336), Q326 (= Q337), T327 (= T338), D409 (= D420), F421 (= F432), R424 (= R435), T516 (= T525), K520 (= K529), Q522 (≠ R531)
- binding magnesium ion: H448 (= H459), V451 (= V462)
8bitA Crystal structure of acyl-coa synthetase from metallosphaera sedula in complex with coenzyme a and acetyl-amp
42% identity, 94% coverage: 25:535/543 of query aligns to 37:543/562 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 (= W244), G321 (= G312), E322 (= E313), P323 (= P314), D342 (= D333), F343 (≠ G334), Y344 (= Y335), Q346 (= Q337), T347 (= T338), D428 (= D420), F440 (= F432), K449 (≠ L441), R454 (= R446)
- binding coenzyme a: N128 (≠ Q113), W247 (= W239), K249 (= K241), K273 (≠ R264), L274 (≠ F265), Q300 (≠ M291), D452 (≠ G444), Y453 (= Y445), R483 (= R475), P517 (= P509)
8biqB Crystal structure of acyl-coa synthetase from metallosphaera sedula in complex with acetyl-amp
42% identity, 94% coverage: 25:535/543 of query aligns to 35:541/561 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 (= G312), E320 (= E313), P321 (= P314), D340 (= D333), F341 (≠ G334), Y342 (= Y335), G343 (= G336), Q344 (= Q337), T345 (= T338), D426 (= D420), F438 (= F432), K447 (≠ L441), R452 (= R446)
8biqA Crystal structure of acyl-coa synthetase from metallosphaera sedula in complex with acetyl-amp
42% identity, 94% coverage: 25:535/543 of query aligns to 36:542/562 of 8biqA
8rplB Amp-forming acetyl-coa synthetase from chloroflexota bacterium with bound acetyl amp (see paper)
32% identity, 97% coverage: 17:542/543 of query aligns to 71:624/630 of 8rplB
- 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: G391 (= G312), E392 (= E313), P393 (= P314), T416 (≠ G334), W417 (≠ Y335), W418 (≠ G336), Q419 (= Q337), T420 (= T338), D502 (= D420), R517 (= R435), K523 (≠ L441), R528 (= R446)
- binding magnesium ion: V539 (≠ I457), H541 (= H459)
4wv3B Crystal structure of the anthranilate coa ligase auaeii in complex with anthranoyl-amp (see paper)
30% identity, 95% coverage: 20:537/543 of query aligns to 5:510/518 of 4wv3B
- active site: S175 (≠ T194), T320 (= T338), E321 (= E339), K418 (≠ L441), W423 (≠ R446), K502 (= K529)
- binding 5'-O-[(S)-[(2-aminobenzoyl)oxy](hydroxy)phosphoryl]adenosine: F220 (≠ W239), T221 (≠ A240), F222 (≠ K241), A293 (= A311), S294 (≠ G312), E295 (= E313), A296 (≠ P314), G316 (= G334), I317 (≠ Y335), G318 (= G336), C319 (≠ Q337), T320 (= T338), D397 (= D420), H409 (≠ F432), R412 (= R435), K502 (= K529)
P27550 Acetyl-coenzyme A synthetase; AcCoA synthetase; Acs; Acetate--CoA ligase; Acyl-activating enzyme; EC 6.2.1.1 from Escherichia coli (strain K12) (see paper)
31% identity, 96% coverage: 17:536/543 of query aligns to 67:616/652 of P27550
- K609 (= K529) modified: N6-acetyllysine; by autocatalysis
2p2fA Acetyl-coa synthetase, wild-type with acetate, amp, and coa bound (see paper)
29% identity, 96% coverage: 17:536/543 of query aligns to 62:611/637 of 2p2fA
- active site: T259 (= T194), T411 (= T338), E412 (= E339), N516 (≠ L441), R521 (= R446), K604 (= K529)
- binding adenosine monophosphate: G382 (= G312), E383 (= E313), P384 (= P314), T407 (≠ G334), W408 (≠ Y335), W409 (≠ G336), Q410 (= Q337), T411 (= T338), D495 (= D420), I507 (≠ F432), R510 (= R435), N516 (≠ L441), R521 (= R446)
- binding coenzyme a: F158 (≠ T111), R186 (vs. gap), W304 (= W239), T306 (≠ K241), P329 (vs. gap), A352 (= A285), A355 (≠ I288), S518 (= S443), R579 (≠ K504), P584 (= P509)
Q8ZKF6 Acetyl-coenzyme A synthetase; AcCoA synthetase; Acs; Acetate--CoA ligase; Acyl-activating enzyme; EC 6.2.1.1 from Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720) (see 4 papers)
29% identity, 96% coverage: 17:536/543 of query aligns to 67:616/652 of Q8ZKF6
- R194 (vs. gap) mutation to A: Results in a 2-fold reduction in the catalytic efficiency for both ATP and CoA. 2-fold increase in the affinity for ATP and 3-fold reduction for CoA.; mutation to E: Results in a 2-fold reduction in the catalytic efficiency for both ATP and CoA. 2-fold increase in the affinity for ATP and 2-fold reduction for CoA.
- T311 (≠ K241) binding CoA
- N335 (≠ D263) binding CoA
- A357 (= A285) mutation to V: Results in a 2-fold reduction in the catalytic efficiency for both ATP and CoA. 3-fold increase in the affinity for ATP and 3-fold reduction for CoA.
- D517 (= D437) mutation to G: Results in a 2-fold reduction in the catalytic efficiency for both ATP and CoA. 2-fold increase in the affinity for ATP and 10-fold reduction for CoA.; mutation to P: Results in a 2-fold reduction in the catalytic efficiency for both ATP and CoA. 3-fold reduction in the affinity for ATP and 4.5-fold reduction for CoA.
- S523 (= S443) binding CoA
- G524 (= G444) mutation to L: No acetyl-coenzyme A synthetase activity.; mutation to S: Results in a 2-fold reduction in the catalytic efficiency for both ATP and CoA. Almost the same affinity as the wild-type for ATP, but 9-fold reduction in the affinity for CoA.
- R526 (= R446) mutation to A: Results in a 2-fold reduction in the catalytic efficiency for both ATP and CoA. 3-fold increase in the affinity for ATP and 4-fold reduction for CoA.
- R584 (≠ K504) binding CoA; mutation to A: Results in a 2-fold reduction in the catalytic efficiency for both ATP and CoA. 2-fold increase in the affinity for ATP and 7-fold reduction for CoA.; mutation to E: Results in a 2-fold reduction in the catalytic efficiency for both ATP and CoA. 3-fold increase in the affinity for ATP and 8-fold reduction for CoA.
- K609 (= K529) modified: N6-acetyllysine; by Pat; mutation to A: No acetyl-coenzyme A synthetase activity.
5jrhA Crystal structure of salmonella enterica acetyl-coa synthetase (acs) in complex with camp and coenzyme a (see paper)
29% identity, 96% coverage: 17:536/543 of query aligns to 63:612/640 of 5jrhA
- active site: T260 (= T194), T412 (= T338), E413 (= E339), N517 (≠ L441), R522 (= R446), K605 (= K529)
- binding (r,r)-2,3-butanediol: W93 (= W46), E140 (= E92), G169 (≠ F121), K266 (≠ F200), P267 (= P201)
- binding adenosine-3',5'-cyclic-monophosphate: G383 (= G312), E384 (= E313), P385 (= P314), T408 (≠ G334), W409 (≠ Y335), W410 (≠ G336), Q411 (= Q337), T412 (= T338), D496 (= D420), I508 (≠ F432), N517 (≠ L441), R522 (= R446)
- binding coenzyme a: F159 (≠ T111), G160 (≠ T112), G161 (≠ Q113), R187 (vs. gap), S519 (= S443), R580 (≠ K504), P585 (= P509)
- binding magnesium ion: V533 (≠ I457), H535 (= H459), I538 (≠ V462)
P78773 Probable acetyl-coenzyme A synthetase; Acetate--CoA ligase; Acyl-activating enzyme; EC 6.2.1.1 from Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast) (see paper)
31% identity, 94% coverage: 30:537/543 of query aligns to 90:626/662 of P78773
- T596 (≠ V506) modified: Phosphothreonine
8w0cA Crystal structure of acetyl-coa synthetase 2 from candida albicans in complex with a cyclopentyl ester amp inhibitor
32% identity, 95% coverage: 19:536/543 of query aligns to 82:632/667 of 8w0cA
- binding 5'-O-[(S)-(cyclopentyloxy)(hydroxy)phosphoryl]adenosine: G399 (= G312), E400 (= E313), P401 (= P314), T424 (≠ G334), Y425 (= Y335), W426 (≠ G336), Q427 (= Q337), T428 (= T338), D514 (= D420), R529 (= R435), R540 (= R446)
8w0bA Crystal structure of acetyl-coa synthetase 2 from candida albicans in complex with a cyclopropyl amp ester inhibitor
32% identity, 95% coverage: 19:536/543 of query aligns to 82:632/667 of 8w0bA
- binding 5'-O-[(R)-(cyclopropyloxy)(hydroxy)phosphoryl]adenosine: V398 (≠ A311), G399 (= G312), E400 (= E313), P401 (= P314), T424 (≠ G334), Y425 (= Y335), W426 (≠ G336), Q427 (= Q337), T428 (= T338), D514 (= D420), I526 (≠ F432), R529 (= R435), R540 (= R446)
Query Sequence
>WP_028313942.1 NCBI__GCF_000429905.1:WP_028313942.1
MGKTPNMTDYQKEYDEFKWEVPEYFNFAGDVIDKWAQDPEKLAMLWVDDDGNEVRKTFAQ
LSAASKKLANLLTSLGVGQGDVVMVVLPRNIEWWEVFTACIRMGALLAPGTTQLTSKDLQ
FRANKAEASCIITNPELAEKFDKVADECPTVKSKIIITEPREDWTFYTEAVEAASDQFET
AKTKSSDNCLVYFTSGTVGFPKMALHTHASYPIGHQVTGKYWLDLKPEDMHWNVSDTGWA
KAAWSSYFGPWNMGAAQFIHHTDRFDPIKTLELLAQYPITTMCGAPTIYRMLVLQDLAKF
KFPTLRHCVGAGEPLNPEIIEVWKKATGCVIRDGYGQTETVLLAGSFPCIEPRFGSMGRP
TPGIELKVIDEDCNELPPNTEGDIAIKVKPNRPVGLFKEYWKEPDRTASVYRGDYYLTGD
RAYVDEDGYFWFVGRADDVILTSGYRIGPFEVESALIEHPAVAESAVVSSPDETRGEVVK
AFVILAGGFTASDELAKELQEHVKNVTAPYKYPRKIEFVDVLPKTVSGKIRRVQLRNQEW
GKE
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