SitesBLAST
Comparing GFF1175 FitnessBrowser__Phaeo:GFF1175 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)
5gxdA Structure of acryloyl-coa lyase prpe from dinoroseobacter shibae dfl 12
82% identity, 100% coverage: 2:627/629 of query aligns to 1:626/627 of 5gxdA
- active site: T238 (= T239), T390 (= T391), E391 (= E392), N498 (= N499), R503 (= R504), K587 (= K588)
- binding adenosine monophosphate: G364 (= G365), E365 (= E366), R366 (= R367), H386 (= H387), W387 (= W388), W388 (= W389), Q389 (= Q390), T390 (= T391), D477 (= D478), I489 (= I490), R492 (= R493), N498 (= N499), R503 (= R504)
- binding coenzyme a: F139 (= F140), G140 (= G141), G141 (= G142), E167 (= E168), R170 (= R171), S279 (= S280), K307 (= K308), P308 (= P309), A332 (= A333), T334 (= T335), A363 (= A364), A500 (= A501), H502 (= H503), K532 (= K533), R562 (= R563), P567 (= P568), V568 (= V569)
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)
41% identity, 99% coverage: 3:623/629 of query aligns to 23:643/648 of Q89WV5
- G263 (= G241) mutation to I: Loss of activity.
- G266 (= G244) mutation to I: Great decrease in activity.
- K269 (= K247) mutation to G: Great decrease in activity.
- E414 (= E392) mutation to Q: Great decrease in activity.
5jrhA Crystal structure of salmonella enterica acetyl-coa synthetase (acs) in complex with camp and coenzyme a (see paper)
38% identity, 99% coverage: 2:623/629 of query aligns to 19:639/640 of 5jrhA
- active site: T260 (= T239), T412 (= T391), E413 (= E392), N517 (= N499), R522 (= R504), K605 (= K588)
- binding (r,r)-2,3-butanediol: W93 (≠ Y74), E140 (= E121), G169 (≠ V150), K266 (≠ Q245), P267 (= P246)
- binding adenosine-3',5'-cyclic-monophosphate: G383 (= G365), E384 (= E366), P385 (≠ R367), T408 (≠ H387), W409 (= W388), W410 (= W389), Q411 (= Q390), T412 (= T391), D496 (= D478), I508 (= I490), N517 (= N499), R522 (= R504)
- binding coenzyme a: F159 (= F140), G160 (= G141), G161 (= G142), R187 (≠ E168), S519 (≠ A501), R580 (= R563), P585 (= P568)
- binding magnesium ion: V533 (≠ A515), H535 (= H517), I538 (≠ V520)
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)
37% identity, 99% coverage: 2:625/629 of query aligns to 23:648/652 of P27550
- K609 (= K588) modified: N6-acetyllysine; by autocatalysis
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)
38% identity, 99% coverage: 2:625/629 of query aligns to 23:648/652 of Q8ZKF6
- R194 (= R171) 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 (≠ V286) binding
- N335 (≠ G311) binding
- A357 (= A333) 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 (= D495) 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 (≠ A501) binding
- G524 (= G502) 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 (= R504) 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 (= R563) 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 (= K588) 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)
38% identity, 99% coverage: 2:623/629 of query aligns to 18:636/637 of 2p2fA
- active site: T259 (= T239), T411 (= T391), E412 (= E392), N516 (= N499), R521 (= R504), K604 (= K588)
- binding adenosine monophosphate: G382 (= G365), E383 (= E366), P384 (≠ R367), T407 (≠ H387), W408 (= W388), W409 (= W389), Q410 (= Q390), T411 (= T391), D495 (= D478), I507 (= I490), R510 (= R493), N516 (= N499), R521 (= R504)
- binding coenzyme a: F158 (= F140), R186 (≠ E168), W304 (= W284), T306 (≠ V286), P329 (= P309), A352 (= A333), A355 (= A336), S518 (≠ A501), R579 (= R563), P584 (= P568)
2p20A Acetyl-coa synthetase, r584a mutation (see paper)
38% identity, 99% coverage: 2:623/629 of query aligns to 19:640/641 of 2p20A
- active site: T260 (= T239), T412 (= T391), E413 (= E392), N517 (= N499), R522 (= R504), K605 (= K588)
- binding adenosine-5'-monophosphate-propyl ester: G383 (= G365), E384 (= E366), P385 (≠ R367), T408 (≠ H387), W409 (= W388), W410 (= W389), Q411 (= Q390), T412 (= T391), D496 (= D478), I508 (= I490), R511 (= R493), R522 (= R504)
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)
37% identity, 100% coverage: 3:629/629 of query aligns to 40:680/683 of P52910
- K506 (≠ T468) modified: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)
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)
40% identity, 99% coverage: 3:623/629 of query aligns to 35:655/662 of P78773
- T596 (≠ K565) modified: Phosphothreonine
1pg3A Acetyl coa synthetase, acetylated on lys609 (see paper)
38% identity, 99% coverage: 2:623/629 of query aligns to 19:633/634 of 1pg3A
- active site: T260 (= T239), T412 (= T391), E413 (= E392), N517 (= N499), R522 (= R504), K605 (= K588)
- binding coenzyme a: F159 (= F140), G160 (= G141), R187 (≠ E168), R190 (= R171), A301 (≠ S280), T307 (≠ V286), P330 (= P309), A356 (= A336), S519 (≠ A501), R580 (= R563), P585 (= P568)
- binding magnesium ion: V533 (≠ A515), H535 (= H517), I538 (≠ V520)
- binding adenosine-5'-monophosphate-propyl ester: G383 (= G365), E384 (= E366), P385 (≠ R367), T408 (≠ H387), W409 (= W388), W410 (= W389), Q411 (= Q390), T412 (= T391), D496 (= D478), R511 (= R493), R522 (= R504)
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)
38% identity, 98% coverage: 4:621/629 of query aligns to 26:650/651 of P9WQD1
- K617 (= K588) modified: N6-acetyllysine; mutation to R: Complete loss of acetyl-coenzyme A synthetase activity.
1ry2A Crystal structure of yeast acetyl-coenzyme a synthetase in complex with amp (see paper)
39% identity, 88% coverage: 45:597/629 of query aligns to 52:599/615 of 1ry2A
- active site: T247 (= T239), T399 (= T391), N507 (= N499), K590 (= K588)
- binding adenosine monophosphate: G370 (= G365), E371 (= E366), P372 (≠ R367), T395 (≠ H387), Y396 (≠ W388), W397 (= W389), Q398 (= Q390), T399 (= T391), D486 (= D478), I498 (= I490), R501 (= R493)
7kvyA Crystal structure of acetyl-coa synthetase in complex with adenosine- 5'-ethylphosphate and co-enzyme a from coccidioides immitis rs
39% identity, 96% coverage: 3:604/629 of query aligns to 34:631/633 of 7kvyA
- active site: T271 (= T239), T422 (= T391), E423 (= E392), N529 (= N499), R534 (= R504), K612 (= K583)
- binding coenzyme a: F172 (= F140), G174 (= G142), R200 (≠ E168), G312 (≠ S280), Y362 (≠ F331), V363 (≠ T332), A364 (= A333), S531 (≠ A501), G532 (= G502), R592 (= R563), F598 (≠ V569)
- binding 5'-O-[(S)-ethoxy(hydroxy)phosphoryl]adenosine: G393 (= G365), E394 (= E366), P395 (≠ R367), T418 (≠ H387), Y419 (≠ W388), W420 (= W389), Q421 (= Q390), T422 (= T391), D508 (= D478), I520 (= I490), R523 (= R493), R534 (= R504)
8w0dA Acetyl-coenzyme A synthetase 2
36% identity, 99% coverage: 3:622/629 of query aligns to 37:660/666 of 8w0dA
- binding 5'-O-{(R)-hydroxy[(propan-2-yl)oxy]phosphoryl}adenosine: G398 (= G365), E399 (= E366), P400 (≠ R367), T423 (≠ H387), Y424 (≠ W388), W425 (= W389), Q426 (= Q390), T427 (= T391), D513 (= D478), I525 (= I490), R528 (= R493), R539 (= R504)
8v4rA Crystal structure of acetyl-coa synthetase 2 in complex with amp and coa from candida albicans
36% identity, 99% coverage: 3:622/629 of query aligns to 37:660/666 of 8v4rA
- binding adenosine monophosphate: G398 (= G365), E399 (= E366), P400 (≠ R367), T423 (≠ H387), Y424 (≠ W388), Q426 (= Q390), T427 (= T391), D513 (= D478), I525 (= I490), R528 (= R493), R539 (= R504)
- binding coenzyme a: F175 (= F140), R203 (≠ E168), R206 (= R171), G316 (≠ S280), H538 (= H503), R599 (= R563), F605 (≠ V569)
8w0cA Acetyl-coenzyme A synthetase 2
36% identity, 99% coverage: 3:622/629 of query aligns to 38:661/667 of 8w0cA
- binding 5'-O-[(S)-(cyclopentyloxy)(hydroxy)phosphoryl]adenosine: G399 (= G365), E400 (= E366), P401 (≠ R367), T424 (≠ H387), Y425 (≠ W388), W426 (= W389), Q427 (= Q390), T428 (= T391), D514 (= D478), R529 (= R493), R540 (= R504)
8w0bA Acetyl-coenzyme A synthetase 2
36% identity, 99% coverage: 3:622/629 of query aligns to 38:661/667 of 8w0bA
- binding 5'-O-[(R)-(cyclopropyloxy)(hydroxy)phosphoryl]adenosine: V398 (≠ A364), G399 (= G365), E400 (= E366), P401 (≠ R367), T424 (≠ H387), Y425 (≠ W388), W426 (= W389), Q427 (= Q390), T428 (= T391), D514 (= D478), I526 (= I490), R529 (= R493), R540 (= R504)
8w0jA Acetyl-coenzyme A synthetase 2
36% identity, 99% coverage: 2:622/629 of query aligns to 37:656/662 of 8w0jA
- binding 5'-O-{(S)-hydroxy[(prop-2-yn-1-yl)oxy]phosphoryl}adenosine: G399 (= G365), E400 (= E366), P401 (≠ R367), T424 (≠ H387), Y425 (≠ W388), W426 (= W389), Q427 (= Q390), T428 (= T391), D514 (= D478), I526 (= I490), R529 (= R493), R540 (= R504)
8v4pA Crystal structure of acetyl-coa synthetase 2 in complex with adenosine-5'-allylphosphate from candida albicans
36% identity, 99% coverage: 2:622/629 of query aligns to 36:655/660 of 8v4pA
- binding 5'-O-{(S)-hydroxy[(prop-2-en-1-yl)oxy]phosphoryl}adenosine: P152 (= P117), A176 (≠ G141), G177 (= G142), R203 (≠ E168), T208 (≠ V173), D317 (= D281), E342 (= E306), G343 (= G307), P345 (= P309), G398 (= G365), E399 (= E366), P400 (≠ R367), T423 (≠ H387), W425 (= W389), Q426 (= Q390), T427 (= T391), D513 (= D478), I525 (= I490), R528 (= R493), R539 (= R504)
8v4oA Crystal structure of acetyl-coa synthetase 2 in complex with amp from candida albicans
36% identity, 99% coverage: 2:622/629 of query aligns to 36:655/660 of 8v4oA
- binding adenosine monophosphate: G398 (= G365), E399 (= E366), P400 (≠ R367), T423 (≠ H387), Y424 (≠ W388), W425 (= W389), Q426 (= Q390), T427 (= T391), D513 (= D478), I525 (= I490), R528 (= R493), R539 (= R504)
Query Sequence
>GFF1175 FitnessBrowser__Phaeo:GFF1175
MSYSEVYEGWKANPEQFWMEAAEAISWDSAPTKALTDKGDGLYEWFADARVNTCYNAVDR
HVEQGRGEQTAIIYDSPITHTKREISYVELRNRVATLAGALRAKGVEKGDRVIIYMPMIP
EALEAMLACARLGAVHSVVFGGFAANELAVRIDDATPKAIIAASCGLEPGRTVHYKPLLD
GAIDLATHKPDFCVIFQREQEVAELIEGRDVNWHGFQYGVEPAECVPVEGNHPAYILYTS
GTTGQPKGVIRHTAGQLVALNWTMKNIYNVDPGDVFWAASDVGWVVGHSYICYGPLIHGN
TTIVFEGKPIGTPDAGTFWRVISEHKVKSFFTAPTAFRAVKREDPKGEFVKKYDLSCLKQ
VYLAGERADPDTITWAQEQLKVPVIDHWWQTETGWSIAANPLGIEELPTKLGSPAVPMPG
YTVDILDEGGHPVAPGELGAIAVKLPLPPGTLPTLWNAEDRFKKSYLTTFPGYYETGDAG
MKDEDGYLYIMARTDDVINVAGHRLSTGAMEEVLAGHPDVAECAVIGVSDSLKGQAPVGF
LCLNAGCDTPHEDVVAQVVKLVREKIGPVAAFKLACVVDRLPKTRSGKILRGTMVNIADG
TDWKMPATIDDPAILDEITTALQGLGYAK
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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