SitesBLAST
Comparing BPHYT_RS31920 FitnessBrowser__BFirm:BPHYT_RS31920 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)
P9WQD1 Acetyl-coenzyme A synthetase; AcCoA synthetase; Acs; Acetate--CoA ligase; Acyl-activating enzyme; EC 6.2.1.1 from Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv) (see 2 papers)
33% identity, 91% coverage: 50:640/650 of query aligns to 36:648/651 of P9WQD1
- K617 (= K609) modified: N6-acetyllysine; mutation to R: Complete loss of acetyl-coenzyme A synthetase activity.
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)
30% identity, 93% coverage: 33:637/650 of query aligns to 23:636/648 of Q89WV5
- G263 (= G274) mutation to I: Loss of activity.
- G266 (= G277) mutation to I: Great decrease in activity.
- K269 (= K280) mutation to G: Great decrease in activity.
- E414 (= E420) mutation to Q: Great decrease in activity.
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)
30% identity, 94% coverage: 31:641/650 of query aligns to 22:643/652 of P27550
- K609 (= K609) modified: N6-acetyllysine; by autocatalysis
2p20A Acetyl-coa synthetase, r584a mutation (see paper)
30% identity, 94% coverage: 33:641/650 of query aligns to 20:637/641 of 2p20A
- active site: T260 (= T272), T412 (≠ S419), E413 (= E420), N517 (≠ K522), R522 (= R527), K605 (= K609)
- binding adenosine-5'-monophosphate-propyl ester: G383 (= G393), E384 (= E394), P385 (≠ V395), T408 (≠ F415), W409 (≠ T416), W410 (≠ G417), Q411 (≠ G418), T412 (≠ S419), D496 (= D501), I508 (≠ L513), R511 (= R516), R522 (= R527)
5jrhA Crystal structure of salmonella enterica acetyl-coa synthetase (acs) in complex with camp and coenzyme a (see paper)
30% identity, 94% coverage: 33:641/650 of query aligns to 20:636/640 of 5jrhA
- active site: T260 (= T272), T412 (≠ S419), E413 (= E420), N517 (≠ K522), R522 (= R527), K605 (= K609)
- binding (r,r)-2,3-butanediol: W93 (≠ A107), E140 (= E153), G169 (≠ A182), K266 (= K278), P267 (= P279)
- binding adenosine-3',5'-cyclic-monophosphate: G383 (= G393), E384 (= E394), P385 (≠ V395), T408 (≠ F415), W409 (≠ T416), W410 (≠ G417), Q411 (≠ G418), T412 (≠ S419), D496 (= D501), I508 (≠ L513), N517 (≠ K522), R522 (= R527)
- binding coenzyme a: F159 (= F172), G160 (≠ S173), G161 (= G174), R187 (= R200), S519 (≠ A524), R580 (≠ S584), P585 (≠ K589)
- binding magnesium ion: V533 (= V538), H535 (≠ I540), I538 (≠ V543)
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)
30% identity, 94% coverage: 33:641/650 of query aligns to 24:643/652 of Q8ZKF6
- R194 (≠ K203) 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 (≠ A319) binding
- N335 (= N342) binding
- A357 (≠ S364) 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 (= D518) 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 (≠ A524) binding
- G524 (= G525) 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 (= R527) 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 (≠ S584) binding ; 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 (= K609) modified: N6-acetyllysine; by Pat; mutation to A: No acetyl-coenzyme A synthetase activity.
8w0jA Acetyl-coenzyme A synthetase 2
30% identity, 94% coverage: 30:639/650 of query aligns to 35:652/662 of 8w0jA
- binding 5'-O-{(S)-hydroxy[(prop-2-yn-1-yl)oxy]phosphoryl}adenosine: G399 (= G393), E400 (= E394), P401 (≠ V395), T424 (≠ F415), Y425 (≠ T416), W426 (≠ G417), Q427 (≠ G418), T428 (≠ S419), D514 (= D501), I526 (≠ L513), R529 (= R516), R540 (= R527)
8v4pA Crystal structure of acetyl-coa synthetase 2 in complex with adenosine-5'-allylphosphate from candida albicans
30% identity, 94% coverage: 30:639/650 of query aligns to 34:651/660 of 8v4pA
- binding 5'-O-{(S)-hydroxy[(prop-2-en-1-yl)oxy]phosphoryl}adenosine: P152 (≠ E149), A176 (≠ S173), G177 (= G174), R203 (= R200), T208 (≠ V205), D317 (= D314), E342 (≠ D338), G343 (= G339), P345 (= P341), G398 (= G393), E399 (= E394), P400 (≠ V395), T423 (≠ F415), W425 (≠ G417), Q426 (≠ G418), T427 (≠ S419), D513 (= D501), I525 (≠ L513), R528 (= R516), R539 (= R527)
8v4oA Crystal structure of acetyl-coa synthetase 2 in complex with amp from candida albicans
30% identity, 94% coverage: 30:639/650 of query aligns to 34:651/660 of 8v4oA
- binding adenosine monophosphate: G398 (= G393), E399 (= E394), P400 (≠ V395), T423 (≠ F415), Y424 (≠ T416), W425 (≠ G417), Q426 (≠ G418), T427 (≠ S419), D513 (= D501), I525 (≠ L513), R528 (= R516), R539 (= R527)
8w0dA Acetyl-coenzyme A synthetase 2
30% identity, 94% coverage: 30:639/650 of query aligns to 34:656/666 of 8w0dA
- binding 5'-O-{(R)-hydroxy[(propan-2-yl)oxy]phosphoryl}adenosine: G398 (= G393), E399 (= E394), P400 (≠ V395), T423 (≠ F415), Y424 (≠ T416), W425 (≠ G417), Q426 (≠ G418), T427 (≠ S419), D513 (= D501), I525 (≠ L513), R528 (= R516), R539 (= R527)
8v4rA Crystal structure of acetyl-coa synthetase 2 in complex with amp and coa from candida albicans
30% identity, 94% coverage: 30:639/650 of query aligns to 34:656/666 of 8v4rA
- binding adenosine monophosphate: G398 (= G393), E399 (= E394), P400 (≠ V395), T423 (≠ F415), Y424 (≠ T416), Q426 (≠ G418), T427 (≠ S419), D513 (= D501), I525 (≠ L513), R528 (= R516), R539 (= R527)
- binding coenzyme a: F175 (= F172), R203 (= R200), R206 (≠ K203), G316 (≠ A313), H538 (≠ K526), R599 (≠ S584), F605 (≠ P590)
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)
30% identity, 94% coverage: 30:639/650 of query aligns to 32:650/662 of P78773
- T596 (≠ R586) modified: Phosphothreonine
8w0cA Acetyl-coenzyme A synthetase 2
29% identity, 94% coverage: 30:639/650 of query aligns to 35:657/667 of 8w0cA
- binding 5'-O-[(S)-(cyclopentyloxy)(hydroxy)phosphoryl]adenosine: G399 (= G393), E400 (= E394), P401 (≠ V395), T424 (≠ F415), Y425 (≠ T416), W426 (≠ G417), Q427 (≠ G418), T428 (≠ S419), D514 (= D501), R529 (= R516), R540 (= R527)
8w0bA Acetyl-coenzyme A synthetase 2
29% identity, 94% coverage: 30:639/650 of query aligns to 35:657/667 of 8w0bA
- binding 5'-O-[(R)-(cyclopropyloxy)(hydroxy)phosphoryl]adenosine: V398 (≠ A392), G399 (= G393), E400 (= E394), P401 (≠ V395), T424 (≠ F415), Y425 (≠ T416), W426 (≠ G417), Q427 (≠ G418), T428 (≠ S419), D514 (= D501), I526 (≠ L513), R529 (= R516), R540 (= R527)
P52910 Acetyl-coenzyme A synthetase 2; Acetate--CoA ligase 2; Acyl-activating enzyme 2; EC 6.2.1.1 from Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) (see paper)
32% identity, 94% coverage: 30:639/650 of query aligns to 37:669/683 of P52910
- K506 (≠ R491) modified: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)
7kdsA Crystal structure of acetyl-coa synthetase 2 in complex with adenosine-5'-propylphosphate from candida albicans
30% identity, 94% coverage: 30:639/650 of query aligns to 34:646/654 of 7kdsA
- active site: T275 (= T272), T427 (≠ S419), E428 (= E420), N534 (≠ K522), R539 (= R527), K620 (= K609)
- binding adenosine-5'-monophosphate-propyl ester: I321 (≠ V318), G398 (= G393), E399 (= E394), P400 (≠ V395), D422 (≠ N414), T423 (≠ F415), Y424 (≠ T416), W425 (≠ G417), Q426 (≠ G418), T427 (≠ S419), D513 (= D501), R528 (= R516), N534 (≠ K522), R539 (= R527)
1ry2A Crystal structure of yeast acetyl-coenzyme a synthetase in complex with amp (see paper)
30% identity, 95% coverage: 31:645/650 of query aligns to 1:615/615 of 1ry2A
- active site: T247 (= T272), T399 (≠ S419), N507 (≠ K522), K590 (= K609)
- binding adenosine monophosphate: G370 (= G393), E371 (= E394), P372 (≠ V395), T395 (≠ F415), Y396 (≠ T416), W397 (≠ G417), Q398 (≠ G418), T399 (≠ S419), D486 (= D501), I498 (≠ L513), R501 (= R516)
2p2fA Acetyl-coa synthetase, wild-type with acetate, amp, and coa bound (see paper)
30% identity, 94% coverage: 33:641/650 of query aligns to 19:633/637 of 2p2fA
- active site: T259 (= T272), T411 (≠ S419), E412 (= E420), N516 (≠ K522), R521 (= R527), K604 (= K609)
- binding adenosine monophosphate: G382 (= G393), E383 (= E394), P384 (≠ V395), T407 (≠ F415), W408 (≠ T416), W409 (≠ G417), Q410 (≠ G418), T411 (≠ S419), D495 (= D501), I507 (≠ L513), R510 (= R516), N516 (≠ K522), R521 (= R527)
- binding coenzyme a: F158 (= F172), R186 (= R200), W304 (= W317), T306 (≠ A319), P329 (= P341), A352 (≠ S364), A355 (≠ L367), S518 (≠ A524), R579 (≠ S584), P584 (≠ K589)
1pg3A Acetyl coa synthetase, acetylated on lys609 (see paper)
29% identity, 94% coverage: 33:641/650 of query aligns to 20:630/634 of 1pg3A
- active site: T260 (= T272), T412 (≠ S419), E413 (= E420), N517 (≠ K522), R522 (= R527), K605 (= K609)
- binding coenzyme a: F159 (= F172), G160 (≠ S173), R187 (= R200), R190 (≠ K203), A301 (= A313), T307 (≠ A319), P330 (= P341), A356 (≠ L367), S519 (≠ A524), R580 (≠ S584), P585 (≠ K589)
- binding magnesium ion: V533 (= V538), H535 (≠ I540), I538 (≠ V543)
- binding adenosine-5'-monophosphate-propyl ester: G383 (= G393), E384 (= E394), P385 (≠ V395), T408 (≠ F415), W409 (≠ T416), W410 (≠ G417), Q411 (≠ G418), T412 (≠ S419), D496 (= D501), R511 (= R516), R522 (= R527)
7l4gB Crystal structure of acetyl-coa synthetase in complex with acetyl adenylate from cryptococcus neoformans h99
29% identity, 87% coverage: 77:641/650 of query aligns to 86:665/668 of 7l4gB
- active site: T280 (= T272), T432 (≠ S419), E433 (= E420), N539 (≠ K522), R544 (= R527), K631 (= K609)
- 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: W325 (= W317), G403 (= G393), E404 (= E394), P405 (≠ V395), T428 (≠ F415), Y429 (≠ T416), W430 (≠ G417), M431 (≠ G418), T432 (≠ S419), D518 (= D501), I530 (≠ L513), R533 (= R516)
Query Sequence
>BPHYT_RS31920 FitnessBrowser__BFirm:BPHYT_RS31920
MPSQPDPVWWPTATDVSNAQVTSLIRALGLRDYDELYAYSIANPGEYWHRLMVWLGIRWQ
APYSAYVDLSDGKPFPQWFPGGKLNWVDSIFECEADKERLQRIALIAEDESGRVTQRTYA
ELREDVQSFAAGLMTSKLGPGDCVGLLMESSVESVVTYLALSYIGAIAVPLFSGFGADAI
VARLQGCDAKGLVATAGFMRRGKPVLTRDAIESSIPALPSLEVLVVKPMRGSQGSVHAGA
LDWYDVLAAGRAEPLDHAVPAEANTPCMIVYTSGTTGKPKGTVHTHGGFPLKIAHDAAVY
FNLGAGDRWLWPADMGWVAGPITIAGAFLRGATLVCYDGAPNCPDWSRLPQLIRRYAVTH
FGASPTLIRTLSAHESSIAPDDLSSVRLAITAGEVIDSESFRWYGERFACPVINFTGGSE
VSGGLLGNVVVKPIVPGGFNAIAPGIRVDVRGADGKQVRGEVGELAVLEPFVGMTRSFWK
NPERYLDTYWRNVPDVWIHGDLAIQFDDHAFVLCGRSDDTLKIAGKRVGPSEIEDVIVEI
AEVAEAAAVGISDPVKGQRLVVFVVADKERCTVAFREQIVDMVSRRLGKPFAPSQVYVVG
ELPKTRSGKIMRRLIKRAYEGQPLGDTASLENPWAIEMIREVMKLPIEPA
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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