SitesBLAST
Comparing RR42_RS15595 FitnessBrowser__Cup4G11:RR42_RS15595 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)
4wd1A Acetoacetyl-coa synthetase from streptomyces lividans (see paper)
47% identity, 97% coverage: 8:666/678 of query aligns to 2:644/646 of 4wd1A
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)
28% identity, 91% coverage: 39:658/678 of query aligns to 21:636/648 of Q89WV5
- G263 (= G287) mutation to I: Loss of activity.
- G266 (= G290) mutation to I: Great decrease in activity.
- K269 (= K293) mutation to G: Great decrease in activity.
- E414 (≠ D435) mutation to Q: Great decrease in activity.
Q99NB1 Acetyl-coenzyme A synthetase 2-like, mitochondrial; Acetate--CoA ligase 2; Acetyl-CoA synthetase 2; AceCS2; Acyl-CoA synthetase short-chain family member 1; Propionate--CoA ligase; EC 6.2.1.1; EC 6.2.1.17 from Mus musculus (Mouse) (see paper)
26% identity, 94% coverage: 41:675/678 of query aligns to 51:682/682 of Q99NB1
- K635 (= K627) modified: N6-acetyllysine
Q9NUB1 Acetyl-coenzyme A synthetase 2-like, mitochondrial; Acetate--CoA ligase 2; Acetyl-CoA synthetase 2; AceCS2; Acyl-CoA synthetase short-chain family member 1; Propionate--CoA ligase; EC 6.2.1.1; EC 6.2.1.17 from Homo sapiens (Human) (see 3 papers)
27% identity, 93% coverage: 41:671/678 of query aligns to 58:689/689 of Q9NUB1
- V488 (≠ L473) to M: in dbSNP:rs6050249
- K642 (= K627) modified: N6-acetyllysine; mutation to Q: Loss of activity.
Sites not aligning to the query:
- 1:37 modified: transit peptide, Mitochondrion
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)
26% identity, 91% coverage: 41:657/678 of query aligns to 40:666/683 of P52910
- K506 (≠ D508) modified: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)
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)
29% identity, 91% coverage: 44:658/678 of query aligns to 28:645/651 of P9WQD1
- K617 (= K627) modified: N6-acetyllysine; mutation to R: Complete loss of acetyl-coenzyme A synthetase activity.
8sf3A Crystal structure of acetyl-coenzyme a synthetase from leishmania infantum (amp, acetate and coa bound)
27% identity, 92% coverage: 44:669/678 of query aligns to 28:662/662 of 8sf3A
- binding adenosine monophosphate: G398 (= G406), E399 (≠ S407), P400 (= P408), T423 (≠ I425), W424 (= W426), Q426 (≠ A428), T427 (≠ P429), D511 (= D518), R526 (= R533), R537 (= R544)
- binding coenzyme a: F171 (≠ A179), G172 (≠ P180), G173 (≠ D181), R199 (≠ Y207), K202 (= K210), R595 (= R602), P600 (≠ S607)
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)
28% identity, 92% coverage: 37:658/678 of query aligns to 31:648/662 of P78773
- T596 (≠ A604) modified: Phosphothreonine
8u2rA Crystal structure of acetyl-coenzyme a synthetase from leishmania infantum (ethyl amp bound)
27% identity, 92% coverage: 44:669/678 of query aligns to 27:664/664 of 8u2rA
- binding 5'-O-[(S)-ethoxy(hydroxy)phosphoryl]adenosine: I323 (= I331), G400 (= G406), E401 (≠ S407), P402 (= P408), T425 (≠ I425), W426 (= W426), W427 (≠ L427), Q428 (≠ A428), T429 (≠ P429), D513 (= D518), I525 (= I530), R528 (= R533), R539 (= R544)
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)
25% identity, 91% coverage: 41:654/678 of query aligns to 24:635/652 of Q8ZKF6
- R194 (≠ D213) 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 (≠ M332) binding
- N335 (≠ A354) binding
- A357 (≠ G376) 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 (= D535) 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 (≠ H541) binding
- G524 (= G542) 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 (= R544) 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 (= R602) 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 (= K627) modified: N6-acetyllysine; by Pat; mutation to A: No acetyl-coenzyme A synthetase activity.
2p2fA Acetyl-coa synthetase, wild-type with acetate, amp, and coa bound (see paper)
25% identity, 90% coverage: 41:647/678 of query aligns to 19:624/637 of 2p2fA
- active site: T259 (≠ S285), T411 (≠ P429), E412 (≠ M430), N516 (= N539), R521 (= R544), K604 (= K627)
- binding adenosine monophosphate: G382 (= G406), E383 (≠ S407), P384 (= P408), T407 (≠ I425), W408 (= W426), W409 (≠ L427), Q410 (≠ A428), T411 (≠ P429), D495 (= D518), I507 (= I530), R510 (= R533), N516 (= N539), R521 (= R544)
- binding coenzyme a: F158 (≠ A179), R186 (≠ K210), W304 (= W330), T306 (≠ M332), P329 (= P353), A352 (≠ G376), A355 (≠ F379), S518 (≠ H541), R579 (= R602), P584 (≠ S607)
5jrhA Crystal structure of salmonella enterica acetyl-coa synthetase (acs) in complex with camp and coenzyme a (see paper)
25% identity, 91% coverage: 41:654/678 of query aligns to 20:628/640 of 5jrhA
- active site: T260 (≠ S285), T412 (≠ P429), E413 (≠ M430), N517 (= N539), R522 (= R544), K605 (= K627)
- binding (r,r)-2,3-butanediol: W93 (≠ Y114), E140 (≠ A160), G169 (≠ D189), K266 (≠ M291), P267 (= P292)
- binding adenosine-3',5'-cyclic-monophosphate: G383 (= G406), E384 (≠ S407), P385 (= P408), T408 (≠ I425), W409 (= W426), W410 (≠ L427), Q411 (≠ A428), T412 (≠ P429), D496 (= D518), I508 (= I530), N517 (= N539), R522 (= R544)
- binding coenzyme a: F159 (≠ A179), G160 (≠ P180), G161 (≠ D181), R187 (≠ K210), S519 (≠ H541), R580 (= R602), P585 (≠ S607)
- binding magnesium ion: V533 (≠ E555), H535 (≠ L557), I538 (≠ V560)
1pg3A Acetyl coa synthetase, acetylated on lys609 (see paper)
26% identity, 89% coverage: 41:643/678 of query aligns to 20:621/634 of 1pg3A
- active site: T260 (≠ S285), T412 (≠ P429), E413 (≠ M430), N517 (= N539), R522 (= R544), K605 (= K627)
- binding coenzyme a: F159 (≠ W175), G160 (≠ S176), R187 (= R206), R190 (≠ G209), A301 (≠ S326), T307 (≠ M332), P330 (= P353), A356 (≠ F379), S519 (≠ H541), R580 (= R602), P585 (≠ S607)
- binding magnesium ion: V533 (≠ E555), H535 (≠ L557), I538 (≠ V560)
- binding adenosine-5'-monophosphate-propyl ester: G383 (= G406), E384 (≠ S407), P385 (= P408), T408 (≠ I425), W409 (= W426), W410 (≠ L427), Q411 (≠ A428), T412 (≠ P429), D496 (= D518), R511 (= R533), R522 (= R544)
2p20A Acetyl-coa synthetase, r584a mutation (see paper)
25% identity, 91% coverage: 41:654/678 of query aligns to 20:629/641 of 2p20A
- active site: T260 (≠ S285), T412 (≠ P429), E413 (≠ M430), N517 (= N539), R522 (= R544), K605 (= K627)
- binding adenosine-5'-monophosphate-propyl ester: G383 (= G406), E384 (≠ S407), P385 (= P408), T408 (≠ I425), W409 (= W426), W410 (≠ L427), Q411 (≠ A428), T412 (≠ P429), D496 (= D518), I508 (= I530), R511 (= R533), R522 (= R544)
8w0cA Acetyl-coenzyme A synthetase 2
25% identity, 96% coverage: 8:658/678 of query aligns to 14:655/667 of 8w0cA
- binding 5'-O-[(S)-(cyclopentyloxy)(hydroxy)phosphoryl]adenosine: G399 (= G406), E400 (≠ S407), P401 (= P408), T424 (≠ D424), Y425 (≠ I425), W426 (= W426), Q427 (vs. gap), T428 (vs. gap), D514 (= D518), R529 (= R533), R540 (= R544)
8w0bA Acetyl-coenzyme A synthetase 2
25% identity, 96% coverage: 8:658/678 of query aligns to 14:655/667 of 8w0bA
- binding 5'-O-[(R)-(cyclopropyloxy)(hydroxy)phosphoryl]adenosine: V398 (≠ T405), G399 (= G406), E400 (≠ S407), P401 (= P408), T424 (≠ D424), Y425 (≠ I425), W426 (= W426), Q427 (vs. gap), T428 (vs. gap), D514 (= D518), I526 (= I530), R529 (= R533), R540 (= R544)
8w0dA Acetyl-coenzyme A synthetase 2
25% identity, 96% coverage: 8:658/678 of query aligns to 13:654/666 of 8w0dA
- binding 5'-O-{(R)-hydroxy[(propan-2-yl)oxy]phosphoryl}adenosine: G398 (= G406), E399 (≠ S407), P400 (= P408), T423 (≠ D424), Y424 (≠ I425), W425 (= W426), Q426 (vs. gap), T427 (vs. gap), D513 (= D518), I525 (= I530), R528 (= R533), R539 (= R544)
8v4rA Crystal structure of acetyl-coa synthetase 2 in complex with amp and coa from candida albicans
25% identity, 96% coverage: 8:658/678 of query aligns to 13:654/666 of 8v4rA
- binding adenosine monophosphate: G398 (= G406), E399 (≠ S407), P400 (= P408), T423 (≠ D424), Y424 (≠ I425), Q426 (vs. gap), T427 (vs. gap), D513 (= D518), I525 (= I530), R528 (= R533), R539 (= R544)
- binding coenzyme a: F175 (≠ A179), R203 (≠ Y207), R206 (≠ K210), G316 (≠ S326), H538 (≠ I543), R599 (= R602), F605 (≠ R608)
8v4pA Crystal structure of acetyl-coa synthetase 2 in complex with adenosine-5'-allylphosphate from candida albicans
25% identity, 96% coverage: 8:658/678 of query aligns to 13:649/660 of 8v4pA
- binding 5'-O-{(S)-hydroxy[(prop-2-en-1-yl)oxy]phosphoryl}adenosine: P152 (= P156), A176 (≠ P180), G177 (≠ D181), R203 (≠ Y207), T208 (≠ Y212), D317 (≠ S327), E342 (≠ D350), G343 (= G351), P345 (= P353), G398 (= G406), E399 (≠ S407), P400 (= P408), T423 (≠ D424), W425 (= W426), Q426 (vs. gap), T427 (vs. gap), D513 (= D518), I525 (= I530), R528 (= R533), R539 (= R544)
8v4oA Crystal structure of acetyl-coa synthetase 2 in complex with amp from candida albicans
25% identity, 96% coverage: 8:658/678 of query aligns to 13:649/660 of 8v4oA
- binding adenosine monophosphate: G398 (= G406), E399 (≠ S407), P400 (= P408), T423 (≠ D424), Y424 (≠ I425), W425 (= W426), Q426 (vs. gap), T427 (vs. gap), D513 (= D518), I525 (= I530), R528 (= R533), R539 (= R544)
Query Sequence
>RR42_RS15595 FitnessBrowser__Cup4G11:RR42_RS15595
MTTLEEGQLRWTPSQAFRDGSRIAHFMRWLESERGLAFADYGALWQWSVTDLEAFWDAIR
AYFDLRFDTPAERVLGSAQMPGARWFEGASLNYVQQVFRHAGSGAARERTAIRYAGESIA
VTDLSWDVLEQQVASLAHALRGMGVARGDRVAGYLPNIPATVVAFLATASLGAIWSGCAP
DMGQVAVSDRFRQIEPKVLIAVDGYRYGGKAYDRAPVLADLAAALPSLTDLVLVPGEHTD
AHAAPNAIALPANVRRHAWQAVLAHRVPLAIESVPFDHPLWIVYSSGTTGMPKPIVHGHG
GIVIEQLKLMAFHNNLGPDDVFHWYSSSGWIMWNAQIAGLLLGSTIALYDGNPAWPDAGV
LWRFVDAARVTAFGAGAAFFTAGMKAGIEPARVADLSRLRALGSTGSPLPAEAYDWIYRH
VSADIWLAPMSGGTDFAGSFVAGCPILPVYSGEMQCRCLGAKVEAFDEAGNALVGEVGEL
VCTAPMPSMPLFLWGDTNGQRYRDSYFDTYPGVWRHGDWIKITAHGGAIIYGRSDATINR
HGIRMGTSELYRVVEDLPEVLDSMVVDLEYLGRDSYMPLFVVLREGMVLDDALRDTMRAR
IRSALSSRHVPNEILQVPGVPRTLSGKKMEVPIKKLLLGHAPDKIANRDAMANPETLDWY
FAYAERFIAARASESAAA
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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