SitesBLAST
Comparing RR42_RS10085 FitnessBrowser__Cup4G11:RR42_RS10085 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)
37% identity, 63% coverage: 10:656/1020 of query aligns to 3:633/646 of 4wd1A
4zxiA Crystal structure of holo-ab3403 a four domain nonribosomal peptide synthetase bound to amp and glycine (see paper)
26% identity, 50% coverage: 501:1015/1020 of query aligns to 840:1309/1314 of 4zxiA
Sites not aligning to the query:
- active site: 625, 750
- binding adenosine monophosphate: 626, 735, 736, 737, 756, 757
- binding glycine: 665, 666, 758, 760, 764
- binding 4'-phosphopantetheine: 25, 29, 39, 300, 335, 336, 339, 346, 351
4zxhA Crystal structure of holo-ab3403 a four domain nonribosomal peptide synthetase from acinetobacter baumanii (see paper)
26% identity, 50% coverage: 501:1015/1020 of query aligns to 840:1309/1314 of 4zxhA
Sites not aligning to the query:
P11454 Enterobactin synthase component F; Enterochelin synthase F; Nonribosomal peptide synthetase EntF; EC 6.3.2.14; EC 6.2.1.72 from Escherichia coli (strain K12) (see 5 papers)
26% identity, 80% coverage: 102:917/1020 of query aligns to 464:1223/1293 of P11454
- S1006 (= S708) modified: O-(pantetheine 4'-phosphoryl)serine
- F1077 (≠ S776) mutation to A: Retains 2% of activity.
- W1079 (≠ M778) mutation to A: Abolishes enterobactin production.
- Q1080 (≠ E779) mutation to A: Retains 50% of activity.
- S1138 (= S837) mutation to A: No enterobactin synthase activity. This mutant holo-EntF is still able to adenylate serine and to autoacylate itself with serine.; mutation to C: 1000-fold decrease in kcat. Releases both enterobactin an linear dimers (DHB-Ser)2.
- D1165 (= D864) mutation to A: 20-fold decrease in kcat.; mutation to S: 200-fold decrease in kcat.
Sites not aligning to the query:
- 1271 H→A: 10000-fold decrease in kcat. Releases only enterobactin, but accumulates both DHB-Ser-O-TE and (DHB-Ser)2-O-TE acyl enzyme intermediates.
5ja2A Entf, a terminal nonribosomal peptide synthetase module bound to the non-native mbth-like protein pa2412 (see paper)
26% identity, 80% coverage: 102:917/1020 of query aligns to 441:1171/1238 of 5ja2A
- active site: T580 (≠ S278), E727 (≠ D425), K838 (≠ N527), R843 (≠ N532)
- binding 5'-({[(2R,3S)-3-amino-4-hydroxy-2-{[2-({N-[(2R)-2-hydroxy-3,3-dimethyl-4-(phosphonooxy)butanoyl]-beta-alanyl}amino)ethyl]sulfanyl}butyl]sulfonyl}amino)-5'-deoxyadenosine: F624 (≠ W323), D625 (≠ M324), R650 (≠ V349), V670 (≠ S367), S699 (≠ T396), G700 (= G397), E701 (≠ A398), A702 (≠ V399), Y723 (≠ S421), G724 (= G422), P725 (≠ G423), T726 (= T424), V730 (≠ C429), D731 (≠ F430), D817 (= D506), Y829 (≠ L518), K838 (≠ N527), R840 (= R529), G841 (= G530), Q842 (≠ I531), R843 (≠ N532), S976 (= S708)
- binding Meso-2,3-Butanediol: S583 (≠ T281), S799 (≠ K488), R800 (≠ G489)
Sites not aligning to the query:
7kdsA Crystal structure of acetyl-coa synthetase 2 in complex with adenosine-5'-propylphosphate from candida albicans
23% identity, 60% coverage: 46:655/1020 of query aligns to 30:646/654 of 7kdsA
- active site: T275 (≠ S278), T427 (≠ S419), E428 (≠ I420), N534 (= N527), R539 (≠ N532), K620 (= K625)
- binding adenosine-5'-monophosphate-propyl ester: I321 (≠ M324), G398 (= G397), E399 (≠ A398), P400 (≠ V399), D422 (≠ P414), T423 (≠ L415), Y424 (≠ P416), W425 (≠ L417), Q426 (= Q418), T427 (≠ S419), D513 (= D506), R528 (= R521), N534 (= N527), R539 (≠ N532)
8v4pA Crystal structure of acetyl-coa synthetase 2 in complex with adenosine-5'-allylphosphate from candida albicans
23% identity, 60% coverage: 46:655/1020 of query aligns to 30:651/660 of 8v4pA
- binding 5'-O-{(S)-hydroxy[(prop-2-en-1-yl)oxy]phosphoryl}adenosine: P152 (≠ R156), A176 (= A180), G177 (≠ E181), R203 (≠ E207), T208 (≠ M212), D317 (≠ T320), E342 (≠ D343), G343 (= G344), P345 (≠ I346), G398 (= G397), E399 (≠ A398), P400 (≠ V399), T423 (≠ L415), W425 (≠ L417), Q426 (= Q418), T427 (≠ S419), D513 (= D506), I525 (≠ L518), R528 (= R521), R539 (≠ N532)
8v4oA Crystal structure of acetyl-coa synthetase 2 in complex with amp from candida albicans
23% identity, 60% coverage: 46:655/1020 of query aligns to 30:651/660 of 8v4oA
- binding adenosine monophosphate: G398 (= G397), E399 (≠ A398), P400 (≠ V399), T423 (≠ L415), Y424 (≠ P416), W425 (≠ L417), Q426 (= Q418), T427 (≠ S419), D513 (= D506), I525 (≠ L518), R528 (= R521), R539 (≠ N532)
8w0jA Acetyl-coenzyme A synthetase 2
23% identity, 60% coverage: 46:655/1020 of query aligns to 31:652/662 of 8w0jA
- binding 5'-O-{(S)-hydroxy[(prop-2-yn-1-yl)oxy]phosphoryl}adenosine: G399 (= G397), E400 (≠ A398), P401 (≠ V399), T424 (≠ L415), Y425 (≠ P416), W426 (≠ L417), Q427 (= Q418), T428 (≠ S419), D514 (= D506), I526 (≠ L518), R529 (= R521), R540 (≠ N532)
8w0cA Acetyl-coenzyme A synthetase 2
23% identity, 60% coverage: 46:655/1020 of query aligns to 31:657/667 of 8w0cA
- binding 5'-O-[(S)-(cyclopentyloxy)(hydroxy)phosphoryl]adenosine: G399 (= G397), E400 (≠ A398), P401 (≠ V399), T424 (≠ L415), Y425 (≠ P416), W426 (≠ L417), Q427 (= Q418), T428 (≠ S419), D514 (= D506), R529 (= R521), R540 (≠ N532)
8w0bA Acetyl-coenzyme A synthetase 2
23% identity, 60% coverage: 46:655/1020 of query aligns to 31:657/667 of 8w0bA
- binding 5'-O-[(R)-(cyclopropyloxy)(hydroxy)phosphoryl]adenosine: V398 (≠ T396), G399 (= G397), E400 (≠ A398), P401 (≠ V399), T424 (≠ L415), Y425 (≠ P416), W426 (≠ L417), Q427 (= Q418), T428 (≠ S419), D514 (= D506), I526 (≠ L518), R529 (= R521), R540 (≠ N532)
8w0dA Acetyl-coenzyme A synthetase 2
23% identity, 60% coverage: 46:655/1020 of query aligns to 30:656/666 of 8w0dA
- binding 5'-O-{(R)-hydroxy[(propan-2-yl)oxy]phosphoryl}adenosine: G398 (= G397), E399 (≠ A398), P400 (≠ V399), T423 (≠ L415), Y424 (≠ P416), W425 (≠ L417), Q426 (= Q418), T427 (≠ S419), D513 (= D506), I525 (≠ L518), R528 (= R521), R539 (≠ N532)
8v4rA Crystal structure of acetyl-coa synthetase 2 in complex with amp and coa from candida albicans
23% identity, 60% coverage: 46:655/1020 of query aligns to 30:656/666 of 8v4rA
- binding adenosine monophosphate: G398 (= G397), E399 (≠ A398), P400 (≠ V399), T423 (≠ L415), Y424 (≠ P416), Q426 (= Q418), T427 (≠ S419), D513 (= D506), I525 (≠ L518), R528 (= R521), R539 (≠ N532)
- binding coenzyme a: F175 (≠ A179), R203 (≠ E207), R206 (≠ T210), G316 (≠ T319), H538 (≠ I531), R599 (= R596), F605 (≠ A606)
2p20A Acetyl-coa synthetase, r584a mutation (see paper)
26% identity, 52% coverage: 128:655/1020 of query aligns to 108:635/641 of 2p20A
- active site: T260 (≠ S278), T412 (= T424), E413 (≠ D425), N517 (= N527), R522 (≠ N532), K605 (= K625)
- binding adenosine-5'-monophosphate-propyl ester: G383 (= G397), E384 (≠ A398), P385 (≠ V399), T408 (≠ I420), W409 (≠ S421), W410 (≠ G422), Q411 (≠ G423), T412 (= T424), D496 (= D506), I508 (≠ L518), R511 (= R521), R522 (≠ N532)
5gxdA Structure of acryloyl-coa lyase prpe from dinoroseobacter shibae dfl 12
24% identity, 56% coverage: 86:655/1020 of query aligns to 43:617/627 of 5gxdA
- active site: T238 (≠ S278), T390 (= T424), E391 (≠ D425), N498 (= N527), R503 (≠ N532), K587 (= K625)
- binding adenosine monophosphate: G364 (= G397), E365 (≠ A398), R366 (≠ V399), H386 (≠ I420), W387 (≠ S421), W388 (≠ G422), Q389 (≠ G423), T390 (= T424), D477 (= D506), I489 (≠ L518), R492 (= R521), N498 (= N527), R503 (≠ N532)
- binding coenzyme a: F139 (≠ A179), G140 (≠ A180), G141 (≠ E181), E167 (= E207), R170 (vs. gap), S279 (≠ T319), K307 (vs. gap), P308 (= P345), A332 (≠ S367), T334 (≠ A369), A363 (≠ T396), A500 (≠ R529), H502 (≠ I531), K532 (≠ A561), R562 (≠ A600), P567 (= P605), V568 (≠ A606)
5jrhA Crystal structure of salmonella enterica acetyl-coa synthetase (acs) in complex with camp and coenzyme a (see paper)
26% identity, 52% coverage: 128:655/1020 of query aligns to 108:634/640 of 5jrhA
- active site: T260 (≠ S278), T412 (= T424), E413 (≠ D425), N517 (= N527), R522 (≠ N532), K605 (= K625)
- binding (r,r)-2,3-butanediol: E140 (≠ D160), G169 (≠ D189), K266 (= K284), P267 (= P285)
- binding adenosine-3',5'-cyclic-monophosphate: G383 (= G397), E384 (≠ A398), P385 (≠ V399), T408 (≠ I420), W409 (≠ S421), W410 (≠ G422), Q411 (≠ G423), T412 (= T424), D496 (= D506), I508 (≠ L518), N517 (= N527), R522 (≠ N532)
- binding coenzyme a: F159 (≠ A179), G160 (≠ A180), G161 (≠ E181), R187 (≠ E207), S519 (≠ R529), R580 (≠ A600), P585 (= P605)
- binding magnesium ion: V533 (≠ S543), H535 (≠ I545), I538 (= I548)
Sites not aligning to the query:
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)
26% identity, 52% coverage: 128:655/1020 of query aligns to 112:641/652 of Q8ZKF6
- R194 (≠ T210) 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 (≠ M325) binding
- N335 (≠ S347) binding
- A357 (≠ S367) 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 (= D523) 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 (≠ R529) binding
- G524 (= G530) 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 (≠ N532) 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 (≠ A600) 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.
Q04747 Surfactin synthase subunit 2 from Bacillus subtilis (strain 168) (see paper)
25% identity, 65% coverage: 106:767/1020 of query aligns to 1506:2099/3583 of Q04747
- S2040 (= S708) modified: O-(pantetheine 4'-phosphoryl)serine
Sites not aligning to the query:
- 999 modified: O-(pantetheine 4'-phosphoryl)serine
2p2fA Acetyl-coa synthetase, wild-type with acetate, amp, and coa bound (see paper)
25% identity, 52% coverage: 128:655/1020 of query aligns to 107:631/637 of 2p2fA
- active site: T259 (≠ S278), T411 (= T424), E412 (≠ D425), N516 (= N527), R521 (≠ N532), K604 (= K625)
- binding adenosine monophosphate: G382 (= G397), E383 (≠ A398), P384 (≠ V399), T407 (≠ I420), W408 (≠ S421), W409 (≠ G422), Q410 (≠ G423), T411 (= T424), D495 (= D506), I507 (≠ L518), R510 (= R521), N516 (= N527), R521 (≠ N532)
- binding coenzyme a: F158 (≠ A179), R186 (≠ E207), W304 (= W323), T306 (≠ M325), P329 (≠ I346), A352 (≠ S367), A355 (≠ Y370), S518 (≠ R529), R579 (≠ A600), P584 (= P605)
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)
24% identity, 60% coverage: 40:655/1020 of query aligns to 56:674/689 of Q9NUB1
- V488 (≠ E457) to M: in dbSNP:rs6050249
- K642 (= K625) modified: N6-acetyllysine; mutation to Q: Loss of activity.
Sites not aligning to the query:
- 1:37 modified: transit peptide, Mitochondrion
Query Sequence
>RR42_RS10085 FitnessBrowser__Cup4G11:RR42_RS10085
MPSVTMRRLPIYGSTSERAAASQMTAFTTALQAYTGQVFGDYDTLHDFSVREYRTFWQCF
VQWSHGLAWSGSTEPVCVGDECEHARFFPQVQLNYADNLLGQAVAAPDTPALTACHADGR
RVRLTRGELRNRVARLAHALSELGLRDGDRVVGVMRNDADAVVAALAVTALGATLSTAAA
EMSVETILDRFAPLAPRLLFAHVAEREFDTGMSLADNVADLAAALPSLQGVVRLDDGTLP
GTVKQRIYSLGELIDSGDAGSFVWRRFPFNHPLFIMFSSGTTGKPKCIVHGAGGSLLEHL
KEHRLHCDLRPGDRLYFHTTCAWMMWNWQLSALASGAEIVTYDGPISTVDALWRLVADER
VTVFGTSPAYLKMCEDAGLVPGQQFDLGALRAMMSTGAVLFDAQFEWVRDHVKPLPLQSI
SGGTDILGCFVLGNPNLPIYAGEAQCKSLALDVQAWEQGAHTSRIGELVCANPFPSRPLG
FFGDMDGKGFHAAYFTRNPGVWTHGDRIEFSPEGTARLHGRSDGILNVRGINVGPGEIYR
VLSDIRDIREALVVEQRSCAAPPDRTHAERYDQRIVLLLVLQDGVALTGALATRVRRDLA
RRASPAHVPDLIIAVDELPVTHNGKLSEAAARNAINGLPVGNAAALRNPGCLDSIQNHPA
LNLAARELPPACDSREQLERHLQVLWEKLFHFAPIGRDDNFFDLGGHSLLGARLLADVHQ
STGRTIPLATLLIAPTIARLAAAIDEGAPPPPSPILVPVRAGTGTPLFLVHGLSGSVMEC
WGLVCALRSPRPVYGLQARGLDGEQLTQRRVEDMAASYIEQMRTVQPDGPYALAGYSFGG
LVAFAIAQQLSCAGEHIEFLCLLDTYVHEHFLPWSAWMQHRCSYLGERWRKLRAVPASQL
FGYLTYMLGRAADRVRMSRGRMRRRPDPFTESLPPALRRVRETMGLAMTTYRPRPYHAGP
IVYVRAAIRQQDRGDPISLWRRVARGGLMISEVPSGHNDMLVEPNLQVVAALLDEGLANA
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