SitesBLAST
Comparing HSERO_RS04625 FitnessBrowser__HerbieS:HSERO_RS04625 to proteins with known functional sites using BLASTp with E ≤ 0.001.
Or try Sites on a Tree, PaperBLAST, Conserved Domains, or compare to all protein structures
Found 20 (the maximum) hits to proteins with known functional sites (download)
8biqB Crystal structure of acyl-coa synthetase from metallosphaera sedula in complex with acetyl-amp
33% identity, 90% coverage: 45:544/556 of query aligns to 44:541/561 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 (= G323), E320 (= E324), P321 (= P325), D340 (= D344), F341 (≠ H345), Y342 (= Y346), G343 (= G347), Q344 (= Q348), T345 (= T349), D426 (= D429), F438 (= F441), K447 (≠ T450), R452 (= R455)
8biqA Crystal structure of acyl-coa synthetase from metallosphaera sedula in complex with acetyl-amp
33% identity, 90% coverage: 45:544/556 of query aligns to 45:542/562 of 8biqA
8bitA Crystal structure of acyl-coa synthetase from metallosphaera sedula in complex with coenzyme a and acetyl-amp
33% identity, 90% coverage: 45:544/556 of query aligns to 46:543/562 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 (≠ Y254), G321 (= G323), E322 (= E324), P323 (= P325), D342 (= D344), F343 (≠ H345), Y344 (= Y346), Q346 (= Q348), T347 (= T349), D428 (= D429), F440 (= F441), K449 (≠ T450), R454 (= R455)
- binding coenzyme a: N128 (≠ A124), W247 (= W249), K249 (≠ Y251), K273 (≠ A273), L274 (≠ F274), Q300 (≠ M300), D452 (≠ G453), Y453 (= Y454), R483 (= R484), P517 (≠ A518)
3c5eA Crystal structure of human acyl-coa synthetase medium-chain family member 2a (l64p mutation) in complex with atp (see paper)
33% identity, 89% coverage: 54:548/556 of query aligns to 35:534/536 of 3c5eA
- active site: T188 (= T205), T331 (= T349), E332 (= E350), N434 (≠ T450), R439 (= R455), K524 (= K538)
- binding adenosine-5'-triphosphate: T188 (= T205), S189 (= S206), G190 (= G207), T191 (= T208), S192 (≠ T209), G305 (= G323), E306 (= E324), S307 (≠ P325), G329 (= G347), Q330 (= Q348), T331 (= T349), D413 (= D429), F425 (= F441), R428 (= R444), K524 (= K538)
- binding magnesium ion: M450 (≠ L466), H452 (= H468), V455 (= V471)
3eq6A Crystal structure of human acyl-coa synthetase medium-chain family member 2a (l64p mutation) in a ternary complex with products (see paper)
33% identity, 89% coverage: 54:548/556 of query aligns to 32:531/533 of 3eq6A
- active site: T185 (= T205), T328 (= T349), E329 (= E350), N431 (≠ T450), R436 (= R455), K521 (= K538)
- binding adenosine monophosphate: G302 (= G323), E303 (= E324), S304 (≠ P325), E323 (≠ D344), S324 (≠ H345), Y325 (= Y346), G326 (= G347), Q327 (= Q348), T328 (= T349), D410 (= D429), F422 (= F441), R425 (= R444), R436 (= R455)
- binding Butyryl Coenzyme A: W229 (= W249), F255 (= F274), I277 (≠ T296), V301 (≠ A322), S433 (≠ A452), G434 (= G453), Y435 (= Y454), P501 (≠ A518), Y502 (≠ H519), Y504 (= Y521), R506 (= R523)
3b7wA Crystal structure of human acyl-coa synthetase medium-chain family member 2a, with l64p mutation (see paper)
33% identity, 89% coverage: 54:548/556 of query aligns to 36:535/537 of 3b7wA
2wd9A Crystal structure of human acyl-coa synthetase medium-chain family member 2a (l64p mutation) in complex with ibuprofen (see paper)
33% identity, 89% coverage: 54:548/556 of query aligns to 32:531/533 of 2wd9A
- active site: T185 (= T205), T328 (= T349), E329 (= E350), N431 (≠ T450), R436 (= R455), K521 (= K538)
- binding ibuprofen: I230 (≠ A250), L231 (≠ Y251), G326 (= G347), Q327 (= Q348), T328 (= T349), R436 (= R455)
2vzeA Crystal structure of human acyl-coa synthetase medium-chain family member 2a (l64p mutation) in complex with amp (see paper)
33% identity, 89% coverage: 54:548/556 of query aligns to 32:531/533 of 2vzeA
- active site: T185 (= T205), T328 (= T349), E329 (= E350), N431 (≠ T450), R436 (= R455), K521 (= K538)
- binding adenosine monophosphate: W229 (= W249), G302 (= G323), E303 (= E324), S304 (≠ P325), E323 (≠ D344), Y325 (= Y346), G326 (= G347), Q327 (= Q348), T328 (= T349), D410 (= D429), F422 (= F441), R425 (= R444), R436 (= R455)
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)
33% identity, 89% coverage: 54:548/556 of query aligns to 68:567/577 of Q08AH3
- Q139 (≠ A124) binding
- 221:229 (vs. 205:213, 67% identical) binding
- ESYGQT 359:364 (≠ DHYGQT 344:349) binding
- T364 (= T349) binding
- D446 (= D429) binding
- R461 (= R444) binding
- SGY 469:471 (≠ AGY 452:454) binding
- R472 (= R455) binding
- R501 (= R484) binding
- S513 (≠ D496) to L: in dbSNP:rs1133607
- K532 (= K513) binding
- YPR 540:542 (= YPR 521:523) binding
- K557 (= K538) binding
3dayA Crystal structure of human acyl-coa synthetase medium-chain family member 2a (l64p mutation) in complex with amp-cpp (see paper)
33% identity, 89% coverage: 54:548/556 of query aligns to 36:533/535 of 3dayA
- active site: T189 (= T205), T332 (= T349), E333 (= E350), N435 (≠ T450), R440 (= R455), K523 (= K538)
- binding diphosphomethylphosphonic acid adenosyl ester: T189 (= T205), S190 (= S206), G191 (= G207), T192 (= T208), S193 (≠ T209), K197 (= K213), G306 (= G323), E307 (= E324), S308 (≠ P325), Y329 (= Y346), G330 (= G347), Q331 (= Q348), T332 (= T349), D414 (= D429), F426 (= F441), R429 (= R444), K523 (= K538)
- binding magnesium ion: M451 (≠ L466), H453 (= H468), V456 (= V471)
3gpcA Crystal structure of human acyl-coa synthetase medium-chain family member 2a (l64p mutation) in a complex with coa (see paper)
33% identity, 89% coverage: 54:548/556 of query aligns to 33:530/532 of 3gpcA
- active site: T186 (= T205), T327 (= T349), E328 (= E350), N430 (≠ T450), R435 (= R455), K520 (= K538)
- binding coenzyme a: G301 (= G323), E302 (= E324), S303 (≠ P325), E322 (≠ D344), Y324 (= Y346), G325 (= G347), Q326 (= Q348), T327 (= T349), D409 (= D429), F421 (= F441), R424 (= R444), T516 (= T534), K520 (= K538), Q522 (= Q540)
- binding magnesium ion: H448 (= H468), V451 (= V471)
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)
30% identity, 93% coverage: 37:554/556 of query aligns to 73:633/651 of P9WQD1
- K617 (= K538) modified: N6-acetyllysine; mutation to R: Complete loss of acetyl-coenzyme A synthetase activity.
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)
29% identity, 93% coverage: 33:549/556 of query aligns to 70:620/652 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 (≠ Y251) binding
- N335 (vs. gap) binding
- A357 (= A294) 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 (= D446) 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 (≠ A452) binding
- G524 (= G453) 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 (= R455) 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 (≠ K513) 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 (= K538) modified: N6-acetyllysine; by Pat; mutation to A: No acetyl-coenzyme A synthetase activity.
5jrhA Crystal structure of salmonella enterica acetyl-coa synthetase (acs) in complex with camp and coenzyme a (see paper)
29% identity, 93% coverage: 33:549/556 of query aligns to 66:616/640 of 5jrhA
- active site: T260 (= T205), T412 (= T349), E413 (= E350), N517 (≠ T450), R522 (= R455), K605 (= K538)
- binding (r,r)-2,3-butanediol: W93 (≠ F57), E140 (= E103), G169 (≠ H132), K266 (≠ A211), P267 (≠ A212)
- binding adenosine-3',5'-cyclic-monophosphate: G383 (= G323), E384 (= E324), P385 (= P325), T408 (≠ H345), W409 (≠ Y346), W410 (≠ G347), Q411 (= Q348), T412 (= T349), D496 (= D429), I508 (≠ F441), N517 (≠ T450), R522 (= R455)
- binding coenzyme a: F159 (= F122), G160 (≠ T123), G161 (≠ A124), R187 (vs. gap), S519 (≠ A452), R580 (≠ K513), P585 (≠ A518)
- binding magnesium ion: V533 (≠ L466), H535 (= H468), I538 (≠ V471)
2p2fA Acetyl-coa synthetase, wild-type with acetate, amp, and coa bound (see paper)
29% identity, 93% coverage: 33:549/556 of query aligns to 65:615/637 of 2p2fA
- active site: T259 (= T205), T411 (= T349), E412 (= E350), N516 (≠ T450), R521 (= R455), K604 (= K538)
- binding adenosine monophosphate: G382 (= G323), E383 (= E324), P384 (= P325), T407 (≠ H345), W408 (≠ Y346), W409 (≠ G347), Q410 (= Q348), T411 (= T349), D495 (= D429), I507 (≠ F441), R510 (= R444), N516 (≠ T450), R521 (= R455)
- binding coenzyme a: F158 (= F122), R186 (vs. gap), W304 (= W249), T306 (≠ Y251), P329 (≠ F274), A352 (= A294), A355 (= A297), S518 (≠ A452), R579 (≠ K513), P584 (≠ A518)
2p20A Acetyl-coa synthetase, r584a mutation (see paper)
29% identity, 93% coverage: 33:549/556 of query aligns to 66:616/641 of 2p20A
- active site: T260 (= T205), T412 (= T349), E413 (= E350), N517 (≠ T450), R522 (= R455), K605 (= K538)
- binding adenosine-5'-monophosphate-propyl ester: G383 (= G323), E384 (= E324), P385 (= P325), T408 (≠ H345), W409 (≠ Y346), W410 (≠ G347), Q411 (= Q348), T412 (= T349), D496 (= D429), I508 (≠ F441), R511 (= R444), R522 (= R455)
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)
29% identity, 93% coverage: 29:547/556 of query aligns to 91:651/689 of Q9NUB1
- V488 (≠ L389) to M: in dbSNP:rs6050249
- K642 (= K538) modified: N6-acetyllysine; mutation to Q: Loss of activity.
Sites not aligning to the query:
- 1:37 modified: transit peptide, Mitochondrion
1ry2A Crystal structure of yeast acetyl-coenzyme a synthetase in complex with amp (see paper)
31% identity, 95% coverage: 23:550/556 of query aligns to 41:602/615 of 1ry2A
- active site: T247 (= T205), T399 (= T349), N507 (≠ T450), K590 (= K538)
- binding adenosine monophosphate: G370 (= G323), E371 (= E324), P372 (= P325), T395 (≠ H345), Y396 (= Y346), W397 (≠ G347), Q398 (= Q348), T399 (= T349), D486 (= D429), I498 (≠ F441), R501 (= R444)
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)
28% identity, 93% coverage: 33:549/556 of query aligns to 70:620/652 of P27550
- K609 (= K538) modified: N6-acetyllysine; by autocatalysis
1pg3A Acetyl coa synthetase, acetylated on lys609 (see paper)
29% identity, 93% coverage: 33:549/556 of query aligns to 66:616/634 of 1pg3A
- active site: T260 (= T205), T412 (= T349), E413 (= E350), N517 (≠ T450), R522 (= R455), K605 (= K538)
- binding coenzyme a: F159 (= F122), G160 (≠ T123), R187 (vs. gap), R190 (vs. gap), A301 (= A245), T307 (≠ Y251), P330 (≠ F274), A356 (= A297), S519 (≠ A452), R580 (≠ K513), P585 (≠ A518)
- binding magnesium ion: V533 (≠ L466), H535 (= H468), I538 (≠ V471)
- binding adenosine-5'-monophosphate-propyl ester: G383 (= G323), E384 (= E324), P385 (= P325), T408 (≠ H345), W409 (≠ Y346), W410 (≠ G347), Q411 (= Q348), T412 (= T349), D496 (= D429), R511 (= R444), R522 (= R455)
Query Sequence
>HSERO_RS04625 FitnessBrowser__HerbieS:HSERO_RS04625
MPELIPAPRQPDYADVYAGFRIETLREQFQGDFETGINACVECCDRHVKGDNIALEFVSL
HGEHQQYSFAQVRSMAARVANLLRQQGIQPGQIVAGMLPRTPELLATVLGTLRAGAVYQP
LFTAFGPKAIEHRLALSGASLIVTNVANRDKLDEIANCPQVCTVRESNDPLRAGDIDFRA
AVDAQSDDFAPVLRSGADLMLMMSTSGTTGAAKGVPVPLSALQAFSVYMREAVGLLPQDK
FWNMADPGWAYGLYYAIIGPLAIGHGITFNEAAFTVSGTYETIRRLGITSLAGAPTAYRM
MMAAGEEAAASVKGRLRAVSSAGEPLNAEVVRWFASALDVPIHDHYGQTELGMVVNNHHA
LRHEVVPGSAGFAMPGYRVVVLDENHQELGANQPGELAIDIARSPLYWFSGYWKQDTPAI
AHGYYSTGDNVELEPNGSISFIGRSDDVITSAGYRIGPFDVESALLEHPAVADVAVIGLP
DPERTEIVKAFVVLSDQFKASDALREQLAQHVKRRLSAHAYPRAIEFLDALPKTPSGKLQ
RFVLRKMEADRRAGHP
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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