SitesBLAST
Comparing 8501039 FitnessBrowser__Miya:8501039 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)
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)
59% identity, 93% coverage: 39:661/667 of query aligns to 22:642/648 of Q89WV5
- G263 (= G282) mutation to I: Loss of activity.
- G266 (= G285) mutation to I: Great decrease in activity.
- K269 (= K288) mutation to G: Great decrease in activity.
- E414 (= E433) mutation to Q: Great decrease in activity.
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)
59% identity, 94% coverage: 38:661/667 of query aligns to 22:645/652 of Q8ZKF6
- R194 (= R210) 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 (= T327) binding
- N335 (≠ S351) binding
- A357 (= A373) 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 (= D533) 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 (= S539) binding
- G524 (= G540) 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 (= R542) 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 (= R600) 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 (= K625) modified: N6-acetyllysine; by Pat; mutation to A: No acetyl-coenzyme A synthetase 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)
59% identity, 93% coverage: 39:661/667 of query aligns to 23:645/652 of P27550
- K609 (= K625) modified: N6-acetyllysine; by autocatalysis
5jrhA Crystal structure of salmonella enterica acetyl-coa synthetase (acs) in complex with camp and coenzyme a (see paper)
59% identity, 94% coverage: 38:661/667 of query aligns to 18:638/640 of 5jrhA
- active site: T260 (= T280), T412 (= T432), E413 (= E433), N517 (= N537), R522 (= R542), K605 (= K625)
- binding (r,r)-2,3-butanediol: W93 (= W113), E140 (= E160), G169 (≠ N189), K266 (= K286), P267 (= P287)
- binding adenosine-3',5'-cyclic-monophosphate: G383 (= G403), E384 (= E404), P385 (= P405), T408 (= T428), W409 (= W429), W410 (= W430), Q411 (= Q431), T412 (= T432), D496 (= D516), I508 (≠ V528), N517 (= N537), R522 (= R542)
- binding coenzyme a: F159 (= F179), G160 (≠ A180), G161 (= G181), R187 (= R207), S519 (= S539), R580 (= R600), P585 (= P605)
- binding magnesium ion: V533 (= V553), H535 (= H555), I538 (≠ V558)
2p20A Acetyl-coa synthetase, r584a mutation (see paper)
59% identity, 94% coverage: 38:661/667 of query aligns to 18:639/641 of 2p20A
- active site: T260 (= T280), T412 (= T432), E413 (= E433), N517 (= N537), R522 (= R542), K605 (= K625)
- binding adenosine-5'-monophosphate-propyl ester: G383 (= G403), E384 (= E404), P385 (= P405), T408 (= T428), W409 (= W429), W410 (= W430), Q411 (= Q431), T412 (= T432), D496 (= D516), I508 (≠ V528), R511 (= R531), R522 (= R542)
2p2fA Acetyl-coa synthetase, wild-type with acetate, amp, and coa bound (see paper)
58% identity, 94% coverage: 38:661/667 of query aligns to 17:635/637 of 2p2fA
- active site: T259 (= T280), T411 (= T432), E412 (= E433), N516 (= N537), R521 (= R542), K604 (= K625)
- binding adenosine monophosphate: G382 (= G403), E383 (= E404), P384 (= P405), T407 (= T428), W408 (= W429), W409 (= W430), Q410 (= Q431), T411 (= T432), D495 (= D516), I507 (≠ V528), R510 (= R531), N516 (= N537), R521 (= R542)
- binding coenzyme a: F158 (= F179), R186 (= R207), W304 (= W325), T306 (= T327), P329 (= P350), A352 (= A373), A355 (≠ V376), S518 (= S539), R579 (= R600), P584 (= P605)
1pg3A Acetyl coa synthetase, acetylated on lys609 (see paper)
58% identity, 94% coverage: 38:661/667 of query aligns to 18:632/634 of 1pg3A
- active site: T260 (= T280), T412 (= T432), E413 (= E433), N517 (= N537), R522 (= R542), K605 (= K625)
- binding coenzyme a: F159 (= F179), G160 (≠ A180), R187 (= R207), R190 (= R210), A301 (= A321), T307 (= T327), P330 (= P350), A356 (≠ V376), S519 (= S539), R580 (= R600), P585 (= P605)
- binding magnesium ion: V533 (= V553), H535 (= H555), I538 (≠ V558)
- binding adenosine-5'-monophosphate-propyl ester: G383 (= G403), E384 (= E404), P385 (= P405), T408 (= T428), W409 (= W429), W410 (= W430), Q411 (= Q431), T412 (= T432), D496 (= D516), R511 (= R531), R522 (= R542)
Q9QXG4 Acetyl-coenzyme A synthetase, cytoplasmic; Acetate--CoA ligase; Acetyl-CoA synthetase; ACS; AceCS; Acetyl-CoA synthetase 1; AceCS1; Acyl-CoA synthetase short-chain family member 2; Acyl-activating enzyme; Propionate--CoA ligase; EC 6.2.1.1; EC 6.2.1.17 from Mus musculus (Mouse) (see paper)
50% identity, 96% coverage: 23:665/667 of query aligns to 30:700/701 of Q9QXG4
- K661 (= K625) modified: N6-acetyllysine
8u2rA Crystal structure of acetyl-coenzyme a synthetase from leishmania infantum (ethyl amp bound)
51% identity, 92% coverage: 52:664/667 of query aligns to 36:662/664 of 8u2rA
- binding 5'-O-[(S)-ethoxy(hydroxy)phosphoryl]adenosine: I323 (= I326), G400 (= G403), E401 (= E404), P402 (= P405), T425 (= T428), W426 (= W429), W427 (= W430), Q428 (= Q431), T429 (= T432), D513 (= D516), I525 (≠ V528), R528 (= R531), R539 (= R542)
8sf3A Crystal structure of acetyl-coenzyme a synthetase from leishmania infantum (amp, acetate and coa bound)
51% identity, 92% coverage: 52:664/667 of query aligns to 37:660/662 of 8sf3A
- binding adenosine monophosphate: G398 (= G403), E399 (= E404), P400 (= P405), T423 (= T428), W424 (= W429), Q426 (= Q431), T427 (= T432), D511 (= D516), R526 (= R531), R537 (= R542)
- binding coenzyme a: F171 (= F179), G172 (≠ A180), G173 (= G181), R199 (= R207), K202 (≠ R210), R595 (= R600), P600 (= P605)
7l4gB Crystal structure of acetyl-coa synthetase in complex with acetyl adenylate from cryptococcus neoformans h99
50% identity, 97% coverage: 10:657/667 of query aligns to 9:663/668 of 7l4gB
- active site: T280 (= T280), T432 (= T432), E433 (= E433), N539 (= N537), R544 (= R542), K631 (= K625)
- 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 (= W325), G403 (= G403), E404 (= E404), P405 (= P405), T428 (= T428), Y429 (≠ W429), W430 (= W430), M431 (≠ Q431), T432 (= T432), D518 (= D516), I530 (≠ V528), R533 (= R531)
5u29A Crystal structure of cryptococcus neoformans h99 acetyl-coa synthetase in complex with ac-ams
50% identity, 97% coverage: 10:657/667 of query aligns to 9:663/668 of 5u29A
- active site: T280 (= T280), T432 (= T432), E433 (= E433), N539 (= N537), R544 (= R542), K631 (= K625)
- binding 5'-O-(acetylsulfamoyl)adenosine: W325 (= W325), G403 (= G403), E404 (= E404), P405 (= P405), T428 (= T428), Y429 (≠ W429), W430 (= W430), M431 (≠ Q431), T432 (= T432), D518 (= D516), I530 (≠ V528), R533 (= R531)
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)
48% identity, 99% coverage: 1:660/667 of query aligns to 1:653/662 of P78773
- T596 (≠ E602) modified: Phosphothreonine
8g0vA Crystal structure of acetyl-coa synthetase in complex with a propyne ester amp inhibitor from cryptococcus neoformans h99
49% identity, 97% coverage: 10:657/667 of query aligns to 9:661/666 of 8g0vA
- binding 5'-O-{(S)-hydroxy[(prop-2-yn-1-yl)oxy]phosphoryl}adenosine: W323 (= W325), I324 (= I326), V400 (= V402), G401 (= G403), E402 (= E404), P403 (= P405), T426 (= T428), Y427 (≠ W429), W428 (= W430), M429 (≠ Q431), T430 (= T432), D516 (= D516)
8g0uA Crystal structure of acetyl-coa synthetase in complex with an isopropyl ester amp inhibitor from cryptococcus neoformans h99
49% identity, 97% coverage: 10:657/667 of query aligns to 9:661/666 of 8g0uA
- binding 5'-O-{(R)-hydroxy[(propan-2-yl)oxy]phosphoryl}adenosine: W323 (= W325), I324 (= I326), G401 (= G403), E402 (= E404), P403 (= P405), T426 (= T428), Y427 (≠ W429), W428 (= W430), M429 (≠ Q431), T430 (= T432), D516 (= D516), I528 (≠ V528), R531 (= R531)
7knoA Crystal structure of acetyl-coa synthetase in complex with adenosine- 5'-ethylphosphate from cryptococcus neoformans var. Grubii serotype a (h99)
49% identity, 97% coverage: 10:657/667 of query aligns to 9:661/666 of 7knoA
- active site: T280 (= T280), T430 (= T432), E431 (= E433), N537 (= N537), R542 (= R542), K629 (= K625)
- binding 5'-O-[(S)-ethoxy(hydroxy)phosphoryl]adenosine: W323 (= W325), I324 (= I326), G401 (= G403), E402 (= E404), P403 (= P405), T426 (= T428), Y427 (≠ W429), W428 (= W430), M429 (≠ Q431), T430 (= T432), D516 (= D516), R531 (= R531)
7mmzA Crystal structure of acetyl-coenzyme a synthetase from legionella pneumophila philadelphia 1 in complex with ethyl-amp (see paper)
53% identity, 84% coverage: 54:615/667 of query aligns to 10:559/559 of 7mmzA
- active site: T231 (= T280), T383 (= T432), E384 (= E433), N486 (= N537), R491 (= R542)
- binding 5'-O-[(S)-ethoxy(hydroxy)phosphoryl]adenosine: I277 (= I326), G354 (= G403), E355 (= E404), P356 (= P405), T379 (= T428), W380 (= W429), W381 (= W430), Q382 (= Q431), T383 (= T432), D465 (= D516), I477 (≠ V528), R480 (= R531), R491 (= R542)
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)
51% identity, 97% coverage: 10:653/667 of query aligns to 3:643/651 of P9WQD1
- K617 (= K625) modified: N6-acetyllysine; mutation to R: Complete loss of acetyl-coenzyme A synthetase activity.
5k8fA Crystal structure of acetyl-coa synthetase in complex with atp and acetyl-amp from cryptococcus neoformans h99
50% identity, 94% coverage: 10:637/667 of query aligns to 9:643/656 of 5k8fA
- active site: T280 (= T280), T432 (= T432), E433 (= E433), N539 (= N537), R544 (= R542), K631 (= K625)
- 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 (= W325), I326 (= I326), G403 (= G403), E404 (= E404), P405 (= P405), T428 (= T428), Y429 (≠ W429), W430 (= W430), M431 (≠ Q431), T432 (= T432), D518 (= D516), I530 (≠ V528), R533 (= R531), K631 (= K625)
- binding adenosine-5'-triphosphate: T280 (= T280), S281 (= S281), G282 (= G282), S283 (= S283), T284 (= T284), K288 (= K288), G403 (= G403), E404 (= E404), P405 (= P405), T428 (= T428), Y429 (≠ W429), M431 (≠ Q431), T432 (= T432), D518 (= D516), I530 (≠ V528), R533 (= R531), K631 (= K625)
8v5gA Crystal structure of acetyl-coa synthetase from cryptococcus neoformans h99 in complex with an ethylsulfamide amp inhibitor
50% identity, 95% coverage: 10:641/667 of query aligns to 8:644/655 of 8v5gA
- binding 5'-deoxy-5'-(ethylsulfamamido)adenosine: V401 (= V402), G402 (= G403), E403 (= E404), P404 (= P405), T427 (= T428), Y428 (≠ W429), W429 (= W430), M430 (≠ Q431), D517 (= D516), I529 (≠ V528), K628 (= K625)
Query Sequence
>8501039 FitnessBrowser__Miya:8501039
MSQNKSDKIESMMDEKRLFAPPAAPSGDRRRPHVNGMDEYLAHRERADKDPEGFWGDRAR
QLLDWFTPWDKVMDADMNEPRIEWFKGATLNVAYNCLDRHLVNGRRNKAAIIWQGEPEDD
VRVLTYQMLYDEVCRFASVLQGLGVQKGDRVALYMPMIPELAVAMLACARIGAVHSIVFA
GFSAVSLQNRIQDCEAKVVVTADAVLRAGRSIPLKVNVDEALKDCPSVERVVVVDRAHSN
CAMREGRDMWWHEAMADRTLDTSCPCAKMDSEDMLFILYTSGSTGKPKGVVHTTGGYLAY
AAHTTQWVFDLHDDDVYWCTADIGWITGHSYIVYGPLALGGTTLMFEGVPSWPGPDRFWH
IVEKFRVNIFYTAPTVIRALMREGAHWTQKHDLSSLRVLGSVGEPINPEAWMWYHEHIGH
SRLPIVDTWWQTETGGIMISALPYATTLKPGSATMPLPGIDAAVVKADGTPCGPNEGGHL
VVRKPWPGMLRGVFGSPERYKSTYFERFPGMYESGDGARTDEDGYTWVMGRLDDVINVSG
HRMGTAEVESALVSHPAVAEAAVVGMPHAIKGEAIYAYVTLSAGTEETEELRAALRTWVR
KEIGPIATPEVIQFAEGLPKTRSGKIMRRILRKIASGAGSDFGDTSTLADPGVVQDLIEG
RVQLTGH
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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