SitesBLAST
Comparing AO356_26340 FitnessBrowser__pseudo5_N2C3_1:AO356_26340 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)
Q08AH3 Acyl-coenzyme A synthetase ACSM2A, mitochondrial; Acyl-CoA synthetase medium-chain family member 2A; Benzoate--CoA ligase; Butyrate--CoA ligase 2A; Butyryl-coenzyme A synthetase 2A; Middle-chain acyl-CoA synthetase 2A; EC 6.2.1.2; EC 6.2.1.25 from Homo sapiens (Human) (see 4 papers)
34% identity, 91% coverage: 45:550/554 of query aligns to 68:577/577 of Q08AH3
- Q139 (≠ A115) binding
- 221:229 (vs. 197:205, 67% identical) binding
- ESYGQT 359:364 (≠ DHYGQT 336:341) binding
- T364 (= T341) binding
- D446 (= D421) binding
- R461 (= R436) binding
- SGY 469:471 (= SGY 444:446) binding
- R472 (= R447) binding
- R501 (= R476) binding
- S513 (= S488) to L: in dbSNP:rs1133607
- K532 (≠ R505) binding
- YPR 540:542 (= YPR 513:515) binding
- K557 (= K530) binding
3c5eA Crystal structure of human acyl-coa synthetase medium-chain family member 2a (l64p mutation) in complex with atp (see paper)
35% identity, 90% coverage: 41:540/554 of query aligns to 31:534/536 of 3c5eA
- active site: T188 (= T197), T331 (= T341), E332 (= E342), N434 (≠ T442), R439 (= R447), K524 (= K530)
- binding adenosine-5'-triphosphate: T188 (= T197), S189 (= S198), G190 (= G199), T191 (= T200), S192 (≠ T201), G305 (= G315), E306 (= E316), S307 (≠ P317), G329 (= G339), Q330 (= Q340), T331 (= T341), D413 (= D421), F425 (= F433), R428 (= R436), K524 (= K530)
- binding magnesium ion: M450 (≠ I458), H452 (= H460), V455 (= V463)
3eq6A Crystal structure of human acyl-coa synthetase medium-chain family member 2a (l64p mutation) in a ternary complex with products (see paper)
35% identity, 90% coverage: 41:540/554 of query aligns to 28:531/533 of 3eq6A
- active site: T185 (= T197), T328 (= T341), E329 (= E342), N431 (≠ T442), R436 (= R447), K521 (= K530)
- binding adenosine monophosphate: G302 (= G315), E303 (= E316), S304 (≠ P317), E323 (≠ D336), S324 (≠ H337), Y325 (= Y338), G326 (= G339), Q327 (= Q340), T328 (= T341), D410 (= D421), F422 (= F433), R425 (= R436), R436 (= R447)
- binding Butyryl Coenzyme A: W229 (= W241), F255 (≠ Y262), I277 (≠ T288), V301 (≠ A314), S433 (= S444), G434 (= G445), Y435 (= Y446), P501 (≠ A510), Y502 (≠ H511), Y504 (= Y513), R506 (= R515)
2wd9A Crystal structure of human acyl-coa synthetase medium-chain family member 2a (l64p mutation) in complex with ibuprofen (see paper)
35% identity, 90% coverage: 41:540/554 of query aligns to 28:531/533 of 2wd9A
- active site: T185 (= T197), T328 (= T341), E329 (= E342), N431 (≠ T442), R436 (= R447), K521 (= K530)
- binding ibuprofen: I230 (≠ A242), L231 (≠ Y243), G326 (= G339), Q327 (= Q340), T328 (= T341), R436 (= R447)
2vzeA Crystal structure of human acyl-coa synthetase medium-chain family member 2a (l64p mutation) in complex with amp (see paper)
35% identity, 90% coverage: 41:540/554 of query aligns to 28:531/533 of 2vzeA
- active site: T185 (= T197), T328 (= T341), E329 (= E342), N431 (≠ T442), R436 (= R447), K521 (= K530)
- binding adenosine monophosphate: W229 (= W241), G302 (= G315), E303 (= E316), S304 (≠ P317), E323 (≠ D336), Y325 (= Y338), G326 (= G339), Q327 (= Q340), T328 (= T341), D410 (= D421), F422 (= F433), R425 (= R436), R436 (= R447)
3b7wA Crystal structure of human acyl-coa synthetase medium-chain family member 2a, with l64p mutation (see paper)
35% identity, 90% coverage: 41:540/554 of query aligns to 32:535/537 of 3b7wA
3dayA Crystal structure of human acyl-coa synthetase medium-chain family member 2a (l64p mutation) in complex with amp-cpp (see paper)
34% identity, 90% coverage: 41:540/554 of query aligns to 32:533/535 of 3dayA
- active site: T189 (= T197), T332 (= T341), E333 (= E342), N435 (≠ T442), R440 (= R447), K523 (= K530)
- binding diphosphomethylphosphonic acid adenosyl ester: T189 (= T197), S190 (= S198), G191 (= G199), T192 (= T200), S193 (≠ T201), K197 (= K205), G306 (= G315), E307 (= E316), S308 (≠ P317), Y329 (= Y338), G330 (= G339), Q331 (= Q340), T332 (= T341), D414 (= D421), F426 (= F433), R429 (= R436), K523 (= K530)
- binding magnesium ion: M451 (≠ I458), H453 (= H460), V456 (= V463)
3gpcA Crystal structure of human acyl-coa synthetase medium-chain family member 2a (l64p mutation) in a complex with coa (see paper)
34% identity, 90% coverage: 41:540/554 of query aligns to 29:530/532 of 3gpcA
- active site: T186 (= T197), T327 (= T341), E328 (= E342), N430 (≠ T442), R435 (= R447), K520 (= K530)
- binding coenzyme a: G301 (= G315), E302 (= E316), S303 (≠ P317), E322 (≠ D336), Y324 (= Y338), G325 (= G339), Q326 (= Q340), T327 (= T341), D409 (= D421), F421 (= F433), R424 (= R436), T516 (= T526), K520 (= K530), Q522 (= Q532)
- binding magnesium ion: H448 (= H460), V451 (= V463)
8biqB Crystal structure of acyl-coa synthetase from metallosphaera sedula in complex with acetyl-amp
36% identity, 89% coverage: 43:533/554 of query aligns to 53:538/561 of 8biqB
- 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: G319 (= G315), E320 (= E316), P321 (= P317), D340 (= D336), F341 (≠ H337), Y342 (= Y338), G343 (= G339), Q344 (= Q340), T345 (= T341), D426 (= D421), F438 (= F433), K447 (≠ T442), R452 (= R447)
8bitA Crystal structure of acyl-coa synthetase from metallosphaera sedula in complex with coenzyme a and acetyl-amp
36% identity, 89% coverage: 43:533/554 of query aligns to 55:540/562 of 8bitA
- 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: W252 (≠ Y246), G321 (= G315), E322 (= E316), P323 (= P317), D342 (= D336), F343 (≠ H337), Y344 (= Y338), Q346 (= Q340), T347 (= T341), D428 (= D421), F440 (= F433), K449 (≠ T442), R454 (= R447)
- binding coenzyme a: N128 (≠ A115), W247 (= W241), K249 (≠ Y243), K273 (≠ P265), L274 (≠ F266), Q300 (≠ L292), D452 (≠ G445), Y453 (= Y446), R483 (= R476), P517 (≠ A510)
8biqA Crystal structure of acyl-coa synthetase from metallosphaera sedula in complex with acetyl-amp
36% identity, 89% coverage: 43:533/554 of query aligns to 54:539/562 of 8biqA
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)
32% identity, 92% coverage: 28:538/554 of query aligns to 75:617/652 of P27550
- K609 (= K530) 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)
32% identity, 92% coverage: 28:538/554 of query aligns to 75:617/652 of Q8ZKF6
- R194 (vs. gap) 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 (≠ Y243) binding
- N335 (vs. gap) binding
- A357 (≠ S286) 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 (= D438) 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 (= S444) binding
- G524 (= G445) 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 (= R447) 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 (= R505) 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 (= K530) 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)
32% identity, 92% coverage: 28:538/554 of query aligns to 70:612/637 of 2p2fA
- active site: T259 (= T197), T411 (= T341), E412 (= E342), N516 (≠ T442), R521 (= R447), K604 (= K530)
- binding adenosine monophosphate: G382 (= G315), E383 (= E316), P384 (= P317), T407 (≠ H337), W408 (≠ Y338), W409 (≠ G339), Q410 (= Q340), T411 (= T341), D495 (= D421), I507 (≠ F433), R510 (= R436), N516 (≠ T442), R521 (= R447)
- binding coenzyme a: F158 (= F113), R186 (vs. gap), W304 (= W241), T306 (≠ Y243), P329 (vs. gap), A352 (≠ S286), A355 (= A289), S518 (= S444), R579 (= R505), P584 (≠ A510)
5jrhA Crystal structure of salmonella enterica acetyl-coa synthetase (acs) in complex with camp and coenzyme a (see paper)
32% identity, 92% coverage: 28:538/554 of query aligns to 71:613/640 of 5jrhA
- active site: T260 (= T197), T412 (= T341), E413 (= E342), N517 (≠ T442), R522 (= R447), K605 (= K530)
- binding (r,r)-2,3-butanediol: W93 (= W48), E140 (= E94), G169 (≠ H123), K266 (≠ P203), P267 (≠ A204)
- binding adenosine-3',5'-cyclic-monophosphate: G383 (= G315), E384 (= E316), P385 (= P317), T408 (≠ H337), W409 (≠ Y338), W410 (≠ G339), Q411 (= Q340), T412 (= T341), D496 (= D421), I508 (≠ F433), N517 (≠ T442), R522 (= R447)
- binding coenzyme a: F159 (= F113), G160 (≠ T114), G161 (≠ A115), R187 (vs. gap), S519 (= S444), R580 (= R505), P585 (≠ A510)
- binding magnesium ion: V533 (≠ I458), H535 (= H460), I538 (≠ V463)
2p20A Acetyl-coa synthetase, r584a mutation (see paper)
31% identity, 92% coverage: 28:538/554 of query aligns to 71:613/641 of 2p20A
- active site: T260 (= T197), T412 (= T341), E413 (= E342), N517 (≠ T442), R522 (= R447), K605 (= K530)
- binding adenosine-5'-monophosphate-propyl ester: G383 (= G315), E384 (= E316), P385 (= P317), T408 (≠ H337), W409 (≠ Y338), W410 (≠ G339), Q411 (= Q340), T412 (= T341), D496 (= D421), I508 (≠ F433), R511 (= R436), R522 (= R447)
1pg3A Acetyl coa synthetase, acetylated on lys609 (see paper)
31% identity, 92% coverage: 28:538/554 of query aligns to 71:613/634 of 1pg3A
- active site: T260 (= T197), T412 (= T341), E413 (= E342), N517 (≠ T442), R522 (= R447), K605 (= K530)
- binding coenzyme a: F159 (= F113), G160 (≠ T114), R187 (vs. gap), R190 (vs. gap), A301 (= A237), T307 (≠ Y243), P330 (vs. gap), A356 (= A289), S519 (= S444), R580 (= R505), P585 (≠ A510)
- binding magnesium ion: V533 (≠ I458), H535 (= H460), I538 (≠ V463)
- binding adenosine-5'-monophosphate-propyl ester: G383 (= G315), E384 (= E316), P385 (= P317), T408 (≠ H337), W409 (≠ Y338), W410 (≠ G339), Q411 (= Q340), T412 (= T341), D496 (= D421), R511 (= R436), R522 (= R447)
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)
30% identity, 97% coverage: 2:538/554 of query aligns to 55:626/662 of P78773
- T596 (≠ R507) modified: Phosphothreonine
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)
32% identity, 92% coverage: 28:538/554 of query aligns to 73:625/651 of P9WQD1
- K617 (= K530) modified: N6-acetyllysine; mutation to R: Complete loss of acetyl-coenzyme A synthetase activity.
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)
31% identity, 92% coverage: 28:538/554 of query aligns to 74:614/648 of Q89WV5
- G263 (= G199) mutation to I: Loss of activity.
- G266 (= G202) mutation to I: Great decrease in activity.
- K269 (= K205) mutation to G: Great decrease in activity.
- E414 (= E342) mutation to Q: Great decrease in activity.
Query Sequence
>AO356_26340 FitnessBrowser__pseudo5_N2C3_1:AO356_26340
MRDYSSATSQFDYQHTVNTALHGSLEALNACVECCDRHALPGRIALFWEGRDGSEATWTY
RDLQDNAARFANFLRAQGVGKGDKVAGLLPRTAELLIVVLATWRIGAVYQPLFTAFGPKA
IEHRLGSSGARIVVTDAVNRPKLNEVAGCPTIVTVGGEKGQGIVRGDYSFWAEVANQSSQ
CEPLMLTGEDPFLLMFTSGTTGPAKALSVPLKAIVAFQSYTRDAVDLRPEDAFWNVADPG
WAYGIYFGVTGPLAMGHPITFYDGPFTLESTCRVINKYGITNLTGSPTAYRLLIAGGEQF
ARSIKGKLRIVSSAGEPLNPEVIRWFADNLNVVIHDHYGQTELGMVLCNHHGLEHPVHLG
AAGFASPGHRIVVLDEEQRELGVGQPGILAVDRSQSPMCWFAGYEGAPTKAFVGDYYLSG
DTVELNPDGSISFVGRSDDVITTSGYRVGPFDVESALIEHPAVVETAVIGKPDPERTELV
KAFVVLSSQYRASPELAEELRLHVRKRLAAHAYPREIEFVSDLPKTPSGKLQRFILRNQE
IAKAQEAAAQNVSA
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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