SitesBLAST
Comparing 7024497 FitnessBrowser__ANA3:7024497 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
62% identity, 96% coverage: 20:634/640 of query aligns to 12:626/627 of 5gxdA
- active site: T238 (= T246), T390 (= T398), E391 (= E399), N498 (= N506), R503 (= R511), K587 (= K595)
- binding adenosine monophosphate: G364 (= G372), E365 (= E373), R366 (= R374), H386 (= H394), W387 (= W395), W388 (= W396), Q389 (= Q397), T390 (= T398), D477 (= D485), I489 (= I497), R492 (= R500), N498 (= N506), R503 (= R511)
- binding coenzyme a: F139 (= F147), G140 (= G148), G141 (= G149), E167 (= E175), R170 (≠ G178), S279 (= S287), K307 (= K315), P308 (= P316), A332 (= A340), T334 (= T342), A363 (= A371), A500 (= A508), H502 (= H510), K532 (= K540), R562 (= R570), P567 (= P575), V568 (= V576)
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)
41% identity, 95% coverage: 14:623/640 of query aligns to 28:639/652 of Q8ZKF6
- R194 (≠ G178) 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 (≠ V293) binding
- N335 (≠ G318) binding
- A357 (= A340) 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 (= D502) 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 (≠ A508) binding
- G524 (= G509) 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 (= R511) 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 (= R570) 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 (= K595) modified: N6-acetyllysine; by Pat; mutation to A: No acetyl-coenzyme A synthetase activity.
2p20A Acetyl-coa synthetase, r584a mutation (see paper)
41% identity, 95% coverage: 14:623/640 of query aligns to 24:633/641 of 2p20A
- active site: T260 (= T246), T412 (= T398), E413 (= E399), N517 (= N506), R522 (= R511), K605 (= K595)
- binding adenosine-5'-monophosphate-propyl ester: G383 (= G372), E384 (= E373), P385 (≠ R374), T408 (≠ H394), W409 (= W395), W410 (= W396), Q411 (= Q397), T412 (= T398), D496 (= D485), I508 (= I497), R511 (= R500), R522 (= R511)
5jrhA Crystal structure of salmonella enterica acetyl-coa synthetase (acs) in complex with camp and coenzyme a (see paper)
41% identity, 94% coverage: 14:617/640 of query aligns to 24:632/640 of 5jrhA
- active site: T260 (= T246), T412 (= T398), E413 (= E399), N517 (= N506), R522 (= R511), K605 (= K595)
- binding (r,r)-2,3-butanediol: W93 (≠ Y81), E140 (= E128), G169 (≠ T157), K266 (≠ Q252), P267 (= P253)
- binding adenosine-3',5'-cyclic-monophosphate: G383 (= G372), E384 (= E373), P385 (≠ R374), T408 (≠ H394), W409 (= W395), W410 (= W396), Q411 (= Q397), T412 (= T398), D496 (= D485), I508 (= I497), N517 (= N506), R522 (= R511)
- binding coenzyme a: F159 (= F147), G160 (= G148), G161 (= G149), R187 (≠ E175), S519 (≠ A508), R580 (= R570), P585 (= P575)
- binding magnesium ion: V533 (≠ C522), H535 (= H524), I538 (≠ V527)
2p2fA Acetyl-coa synthetase, wild-type with acetate, amp, and coa bound (see paper)
41% identity, 95% coverage: 14:623/640 of query aligns to 23:629/637 of 2p2fA
- active site: T259 (= T246), T411 (= T398), E412 (= E399), N516 (= N506), R521 (= R511), K604 (= K595)
- binding adenosine monophosphate: G382 (= G372), E383 (= E373), P384 (≠ R374), T407 (≠ H394), W408 (= W395), W409 (= W396), Q410 (= Q397), T411 (= T398), D495 (= D485), I507 (= I497), R510 (= R500), N516 (= N506), R521 (= R511)
- binding coenzyme a: F158 (= F147), R186 (≠ E175), W304 (= W291), T306 (≠ V293), P329 (= P316), A352 (= A340), A355 (= A343), S518 (≠ A508), R579 (= R570), P584 (= P575)
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, 96% coverage: 11:622/640 of query aligns to 24:629/648 of Q89WV5
- G263 (= G248) mutation to I: Loss of activity.
- G266 (= G251) mutation to I: Great decrease in activity.
- K269 (= K254) mutation to G: Great decrease in activity.
- E414 (= E399) mutation to Q: Great decrease in activity.
1pg3A Acetyl coa synthetase, acetylated on lys609 (see paper)
42% identity, 93% coverage: 14:605/640 of query aligns to 24:615/634 of 1pg3A
- active site: T260 (= T246), T412 (= T398), E413 (= E399), N517 (= N506), R522 (= R511), K605 (= K595)
- binding coenzyme a: F159 (= F147), G160 (= G148), R187 (≠ E175), R190 (≠ G178), A301 (≠ S287), T307 (≠ V293), P330 (= P316), A356 (= A343), S519 (≠ A508), R580 (= R570), P585 (= P575)
- binding magnesium ion: V533 (≠ C522), H535 (= H524), I538 (≠ V527)
- binding adenosine-5'-monophosphate-propyl ester: G383 (= G372), E384 (= E373), P385 (≠ R374), T408 (≠ H394), W409 (= W395), W410 (= W396), Q411 (= Q397), T412 (= T398), D496 (= D485), R511 (= R500), R522 (= R511)
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)
40% identity, 96% coverage: 11:623/640 of query aligns to 25:639/652 of P27550
- K609 (= K595) modified: N6-acetyllysine; by autocatalysis
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)
40% identity, 97% coverage: 8:626/640 of query aligns to 23:648/651 of P9WQD1
- K617 (= K595) modified: N6-acetyllysine; mutation to R: Complete loss of acetyl-coenzyme A synthetase activity.
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)
39% identity, 97% coverage: 8:625/640 of query aligns to 33:650/662 of P78773
- T596 (≠ E572) modified: Phosphothreonine
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)
39% identity, 97% coverage: 4:622/640 of query aligns to 32:666/683 of P52910
- K506 (≠ S475) modified: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)
1ry2A Crystal structure of yeast acetyl-coenzyme a synthetase in complex with amp (see paper)
39% identity, 93% coverage: 11:607/640 of query aligns to 4:602/615 of 1ry2A
- active site: T247 (= T246), T399 (= T398), N507 (= N506), K590 (= K595)
- binding adenosine monophosphate: G370 (= G372), E371 (= E373), P372 (≠ R374), T395 (≠ H394), Y396 (≠ W395), W397 (= W396), Q398 (= Q397), T399 (= T398), D486 (= D485), I498 (= I497), R501 (= R500)
8w0cA Acetyl-coenzyme A synthetase 2
38% identity, 96% coverage: 11:623/640 of query aligns to 39:655/667 of 8w0cA
- binding 5'-O-[(S)-(cyclopentyloxy)(hydroxy)phosphoryl]adenosine: G399 (= G372), E400 (= E373), P401 (≠ R374), T424 (≠ H394), Y425 (≠ W395), W426 (= W396), Q427 (= Q397), T428 (= T398), D514 (= D485), R529 (= R500), R540 (= R511)
8w0bA Acetyl-coenzyme A synthetase 2
38% identity, 96% coverage: 11:623/640 of query aligns to 39:655/667 of 8w0bA
- binding 5'-O-[(R)-(cyclopropyloxy)(hydroxy)phosphoryl]adenosine: V398 (≠ A371), G399 (= G372), E400 (= E373), P401 (≠ R374), T424 (≠ H394), Y425 (≠ W395), W426 (= W396), Q427 (= Q397), T428 (= T398), D514 (= D485), I526 (= I497), R529 (= R500), R540 (= R511)
8w0dA Acetyl-coenzyme A synthetase 2
38% identity, 96% coverage: 11:623/640 of query aligns to 38:654/666 of 8w0dA
- binding 5'-O-{(R)-hydroxy[(propan-2-yl)oxy]phosphoryl}adenosine: G398 (= G372), E399 (= E373), P400 (≠ R374), T423 (≠ H394), Y424 (≠ W395), W425 (= W396), Q426 (= Q397), T427 (= T398), D513 (= D485), I525 (= I497), R528 (= R500), R539 (= R511)
8v4rA Crystal structure of acetyl-coa synthetase 2 in complex with amp and coa from candida albicans
38% identity, 96% coverage: 11:623/640 of query aligns to 38:654/666 of 8v4rA
- binding adenosine monophosphate: G398 (= G372), E399 (= E373), P400 (≠ R374), T423 (≠ H394), Y424 (≠ W395), Q426 (= Q397), T427 (= T398), D513 (= D485), I525 (= I497), R528 (= R500), R539 (= R511)
- binding coenzyme a: F175 (= F147), R203 (≠ E175), R206 (≠ G178), G316 (≠ S287), H538 (= H510), R599 (= R570), F605 (≠ V576)
8v4pA Crystal structure of acetyl-coa synthetase 2 in complex with adenosine-5'-allylphosphate from candida albicans
38% identity, 96% coverage: 11:623/640 of query aligns to 38:649/660 of 8v4pA
- binding 5'-O-{(S)-hydroxy[(prop-2-en-1-yl)oxy]phosphoryl}adenosine: P152 (= P124), A176 (≠ G148), G177 (= G149), R203 (≠ E175), T208 (≠ V180), D317 (= D288), E342 (= E313), G343 (= G314), P345 (= P316), G398 (= G372), E399 (= E373), P400 (≠ R374), T423 (≠ H394), W425 (= W396), Q426 (= Q397), T427 (= T398), D513 (= D485), I525 (= I497), R528 (= R500), R539 (= R511)
8v4oA Crystal structure of acetyl-coa synthetase 2 in complex with amp from candida albicans
38% identity, 96% coverage: 11:623/640 of query aligns to 38:649/660 of 8v4oA
- binding adenosine monophosphate: G398 (= G372), E399 (= E373), P400 (≠ R374), T423 (≠ H394), Y424 (≠ W395), W425 (= W396), Q426 (= Q397), T427 (= T398), D513 (= D485), I525 (= I497), R528 (= R500), R539 (= R511)
8w0jA Acetyl-coenzyme A synthetase 2
38% identity, 96% coverage: 11:623/640 of query aligns to 39:650/662 of 8w0jA
- binding 5'-O-{(S)-hydroxy[(prop-2-yn-1-yl)oxy]phosphoryl}adenosine: G399 (= G372), E400 (= E373), P401 (≠ R374), T424 (≠ H394), Y425 (≠ W395), W426 (= W396), Q427 (= Q397), T428 (= T398), D514 (= D485), I526 (= I497), R529 (= R500), R540 (= R511)
7kdsA Crystal structure of acetyl-coa synthetase 2 in complex with adenosine-5'-propylphosphate from candida albicans
38% identity, 96% coverage: 11:623/640 of query aligns to 38:644/654 of 7kdsA
- active site: T275 (= T246), T427 (= T398), E428 (= E399), N534 (= N506), R539 (= R511), K620 (= K595)
- binding adenosine-5'-monophosphate-propyl ester: I321 (≠ V292), G398 (= G372), E399 (= E373), P400 (≠ R374), D422 (= D393), T423 (≠ H394), Y424 (≠ W395), W425 (= W396), Q426 (= Q397), T427 (= T398), D513 (= D485), R528 (= R500), N534 (= N506), R539 (= R511)
Query Sequence
>7024497 FitnessBrowser__ANA3:7024497
MMGGLMTDAGQQLHQTSIANKQAFWQQAAKALDWVTPSKQILDESEAPFYHWFSDGELNT
CYNAVDRHVLAGRGEQIAIHYVSPVTETEYSITYRELQAQVARLAGYLQSVGVAKGDRVV
IYMPMVPETAYAMLACARIGAIHSVVFGGFAANELATRINDAKPKLVMSASCGIEPSGVV
PYKPLLDKALNEAVHKVEHCLILNRPQYEAQMQAGRDKDWQTALCTSDSADCVTVKATDP
LYVLYTSGTTGQPKGVVRDNGGHAVALAWSMANIYDIAQGDVFWAASDVGWVVGHSYIVY
GPLLVGATTLLYEGKPVGTPDPGAFWRTIAKYRVKSFFTAPTAIRAIKREDPDGEFILGV
DLSCLKNVFLAGERCDPDTLHWAEAKLHKPVIDHWWQTETGWPVAANLMGVAPIAVKAGS
PGRPVPGYEVDVVDELGAKVAANVSGNVVIKLPLPPGTLTTLWQNNKRYQDSYLSMYPGY
YLTGDAGYMDEDGYLYIMSRIDDIINVAGHRLSTGRFEEVLCQHPDVAEAAVIGVDDKLK
GQVPLGLVVLKKGVTITDEELHKQLIALVRQEIGPVASFRLVSAIQKLPKTRSGKILRGT
MRKIADNQQYTAPATIEDPQTLDLVRTTLTRMGYADALVG
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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