SitesBLAST
Comparing WP_012568177.1 NCBI__GCF_000016185.1:WP_012568177.1 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)
8bitA Crystal structure of acyl-coa synthetase from metallosphaera sedula in complex with coenzyme a and acetyl-amp
45% identity, 89% coverage: 38:540/567 of query aligns to 33:543/562 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 (= W255), G321 (= G322), E322 (= E323), P323 (= P324), D342 (= D343), F343 (≠ G344), Y344 (≠ F345), Q346 (= Q347), T347 (= T348), D428 (= D426), F440 (≠ Y438), K449 (= K447), R454 (= R452)
- binding coenzyme a: N128 (≠ L130), W247 (= W250), K249 (= K252), K273 (≠ R275), L274 (≠ F276), Q300 (≠ M302), D452 (= D450), Y453 (= Y451), R483 (= R481), P517 (= P515)
8biqA Crystal structure of acyl-coa synthetase from metallosphaera sedula in complex with acetyl-amp
45% identity, 89% coverage: 38:540/567 of query aligns to 32:542/562 of 8biqA
8biqB Crystal structure of acyl-coa synthetase from metallosphaera sedula in complex with acetyl-amp
45% identity, 89% coverage: 38:540/567 of query aligns to 31:541/561 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 (= G322), E320 (= E323), P321 (= P324), D340 (= D343), F341 (≠ G344), Y342 (≠ F345), G343 (= G346), Q344 (= Q347), T345 (= T348), D426 (= D426), F438 (≠ Y438), K447 (= K447), R452 (= R452)
3eq6A Crystal structure of human acyl-coa synthetase medium-chain family member 2a (l64p mutation) in a ternary complex with products (see paper)
34% identity, 89% coverage: 42:544/567 of query aligns to 8:531/533 of 3eq6A
- active site: T185 (= T206), T328 (= T348), E329 (= E349), N431 (≠ K447), R436 (= R452), K521 (= K534)
- binding adenosine monophosphate: G302 (= G322), E303 (= E323), S304 (≠ P324), E323 (≠ D343), S324 (≠ G344), Y325 (≠ F345), G326 (= G346), Q327 (= Q347), T328 (= T348), D410 (= D426), F422 (≠ Y438), R425 (= R441), R436 (= R452)
- binding Butyryl Coenzyme A: W229 (= W250), F255 (= F276), I277 (≠ T298), V301 (≠ A321), S433 (= S449), G434 (≠ D450), Y435 (= Y451), P501 (= P515), Y502 (= Y516), Y504 (≠ R518), R506 (= R520)
2wd9A Crystal structure of human acyl-coa synthetase medium-chain family member 2a (l64p mutation) in complex with ibuprofen (see paper)
34% identity, 89% coverage: 42:544/567 of query aligns to 8:531/533 of 2wd9A
- active site: T185 (= T206), T328 (= T348), E329 (= E349), N431 (≠ K447), R436 (= R452), K521 (= K534)
- binding ibuprofen: I230 (≠ A251), L231 (≠ K252), G326 (= G346), Q327 (= Q347), T328 (= T348), R436 (= R452)
2vzeA Crystal structure of human acyl-coa synthetase medium-chain family member 2a (l64p mutation) in complex with amp (see paper)
34% identity, 89% coverage: 42:544/567 of query aligns to 8:531/533 of 2vzeA
- active site: T185 (= T206), T328 (= T348), E329 (= E349), N431 (≠ K447), R436 (= R452), K521 (= K534)
- binding adenosine monophosphate: W229 (= W250), G302 (= G322), E303 (= E323), S304 (≠ P324), E323 (≠ D343), Y325 (≠ F345), G326 (= G346), Q327 (= Q347), T328 (= T348), D410 (= D426), F422 (≠ Y438), R425 (= R441), R436 (= R452)
3b7wA Crystal structure of human acyl-coa synthetase medium-chain family member 2a, with l64p mutation (see paper)
34% identity, 89% coverage: 42:544/567 of query aligns to 12:535/537 of 3b7wA
3c5eA Crystal structure of human acyl-coa synthetase medium-chain family member 2a (l64p mutation) in complex with atp (see paper)
34% identity, 89% coverage: 42:544/567 of query aligns to 11:534/536 of 3c5eA
- active site: T188 (= T206), T331 (= T348), E332 (= E349), N434 (≠ K447), R439 (= R452), K524 (= K534)
- binding adenosine-5'-triphosphate: T188 (= T206), S189 (= S207), G190 (= G208), T191 (= T209), S192 (≠ T210), G305 (= G322), E306 (= E323), S307 (≠ P324), G329 (= G346), Q330 (= Q347), T331 (= T348), D413 (= D426), F425 (≠ Y438), R428 (= R441), K524 (= K534)
- binding magnesium ion: M450 (≠ I463), H452 (= H465), V455 (= V468)
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: 42:544/567 of query aligns to 44:567/577 of Q08AH3
- Q139 (≠ L130) binding CoA
- 221:229 (vs. 206:214, 67% identical) binding ATP
- ESYGQT 359:364 (≠ DGFGQT 343:348) binding ATP
- T364 (= T348) binding substrate
- D446 (= D426) binding ATP
- R461 (= R441) binding ATP
- SGY 469:471 (≠ SDY 449:451) binding CoA
- R472 (= R452) binding substrate
- R501 (= R481) binding CoA
- S513 (≠ A493) to L: in dbSNP:rs1133607
- K532 (≠ R510) binding CoA
- YPR 540:542 (≠ RVR 518:520) binding CoA
- K557 (= K534) binding ATP
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: 42:544/567 of query aligns to 9:530/532 of 3gpcA
- active site: T186 (= T206), T327 (= T348), E328 (= E349), N430 (≠ K447), R435 (= R452), K520 (= K534)
- binding coenzyme a: G301 (= G322), E302 (= E323), S303 (≠ P324), E322 (≠ D343), Y324 (≠ F345), G325 (= G346), Q326 (= Q347), T327 (= T348), D409 (= D426), F421 (≠ Y438), R424 (= R441), T516 (= T530), K520 (= K534), Q522 (≠ R536)
- binding magnesium ion: H448 (= H465), V451 (= V468)
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: 42:544/567 of query aligns to 12:533/535 of 3dayA
- active site: T189 (= T206), T332 (= T348), E333 (= E349), N435 (≠ K447), R440 (= R452), K523 (= K534)
- binding diphosphomethylphosphonic acid adenosyl ester: T189 (= T206), S190 (= S207), G191 (= G208), T192 (= T209), S193 (≠ T210), K197 (= K214), G306 (= G322), E307 (= E323), S308 (≠ P324), Y329 (≠ F345), G330 (= G346), Q331 (= Q347), T332 (= T348), D414 (= D426), F426 (≠ Y438), R429 (= R441), K523 (= K534)
- binding magnesium ion: M451 (≠ I463), H453 (= H465), V456 (= V468)
8rplB Amp-forming acetyl-coa synthetase from chloroflexota bacterium with bound acetyl amp (see paper)
31% identity, 91% coverage: 34:551/567 of query aligns to 71:628/630 of 8rplB
- 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: G391 (= G322), E392 (= E323), P393 (= P324), T416 (≠ G344), W417 (≠ F345), W418 (≠ G346), Q419 (= Q347), T420 (= T348), D502 (= D426), R517 (= R441), K523 (= K447), R528 (= R452)
- binding magnesium ion: V539 (≠ I463), H541 (= H465)
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)
31% identity, 88% coverage: 52:552/567 of query aligns to 97:636/662 of P78773
- T596 (= T512) modified: Phosphothreonine
7kvyA Crystal structure of acetyl-coa synthetase in complex with adenosine- 5'-ethylphosphate and co-enzyme a from coccidioides immitis rs
30% identity, 92% coverage: 16:538/567 of query aligns to 53:621/633 of 7kvyA
- active site: T271 (= T206), T422 (= T348), E423 (= E349), N529 (≠ K447), R534 (= R452), K612 (= K529)
- binding coenzyme a: F172 (≠ T128), G174 (≠ L130), R200 (vs. gap), G312 (≠ S246), Y362 (≠ C294), V363 (≠ A295), A364 (≠ P296), S531 (= S449), G532 (≠ D450), R592 (= R510), F598 (≠ Y516)
- binding 5'-O-[(S)-ethoxy(hydroxy)phosphoryl]adenosine: G393 (= G322), E394 (= E323), P395 (= P324), T418 (≠ G344), Y419 (≠ F345), W420 (≠ G346), Q421 (= Q347), T422 (= T348), D508 (= D426), I520 (≠ Y438), R523 (= R441), R534 (= R452)
4wv3B Crystal structure of the anthranilate coa ligase auaeii in complex with anthranoyl-amp (see paper)
31% identity, 87% coverage: 50:541/567 of query aligns to 14:509/518 of 4wv3B
- active site: S175 (≠ T206), T320 (= T348), E321 (= E349), K418 (= K447), W423 (≠ R452), K502 (= K534)
- binding 5'-O-[(S)-[(2-aminobenzoyl)oxy](hydroxy)phosphoryl]adenosine: F220 (≠ W250), T221 (≠ A251), F222 (≠ K252), A293 (= A321), S294 (≠ G322), E295 (= E323), A296 (≠ P324), G316 (= G344), I317 (≠ F345), G318 (= G346), C319 (≠ Q347), T320 (= T348), D397 (= D426), H409 (≠ Y438), R412 (= R441), K502 (= K534)
7l3qA Crystal structure of acetyl-coa synthetase in complex with adenosine- 5'-methylphosphate and co-enzyme a from coccidioides immitis rs
30% identity, 88% coverage: 16:516/567 of query aligns to 54:599/631 of 7l3qA
- active site: T272 (= T206), T423 (= T348), E424 (= E349), N530 (≠ K447), R535 (= R452)
- binding coenzyme a: F173 (≠ T128), A174 (≠ T129), G175 (≠ L130), R201 (vs. gap), G313 (≠ S246), Y363 (≠ C294), A365 (≠ P296), S532 (= S449), G533 (≠ D450), R593 (= R510), P598 (= P515), F599 (≠ Y516)
- binding 5'-O-[(R)-hydroxy(methoxy)phosphoryl]adenosine: I318 (≠ A251), G394 (= G322), E395 (= E323), P396 (= P324), T419 (≠ G344), Y420 (≠ F345), Q422 (= Q347), T423 (= T348), D509 (= D426), R524 (= R441), R535 (= R452)
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)
30% identity, 90% coverage: 34:542/567 of query aligns to 66:614/648 of Q89WV5
- G263 (= G208) mutation to I: Loss of activity.
- G266 (≠ A211) mutation to I: Great decrease in activity.
- K269 (= K214) mutation to G: Great decrease in activity.
- E414 (= E349) mutation to Q: Great decrease in activity.
7kdnA Crystal structure of acetyl-coa synthetase in complex with adenosine- 5'-propylphosphate from aspergillus fumigatus
30% identity, 89% coverage: 36:542/567 of query aligns to 78:620/622 of 7kdnA
- active site: T271 (= T206), T422 (= T348), E423 (= E349), N529 (≠ K447), R534 (= R452), K612 (= K534)
- binding adenosine-5'-monophosphate-propyl ester: G393 (= G322), E394 (= E323), P395 (= P324), T418 (≠ G344), Y419 (≠ F345), W420 (≠ G346), Q421 (= Q347), T422 (= T348), D508 (= D426), I520 (≠ Y438), R523 (= R441), R534 (= R452)
6m2uA The crystal structure of benzoate coenzyme a ligase double mutant (h333a/i334a) in complex with 2-chloro-1,3-thiazole-5-carboxylate-amp (see paper)
32% identity, 83% coverage: 71:541/567 of query aligns to 32:514/518 of 6m2uA
- active site: S176 (≠ T206), T196 (≠ V225), T324 (= T348), E325 (= E349), K422 (= K447), Y427 (≠ R452), K507 (= K534)
- binding adenosine monophosphate: G298 (= G322), E299 (= E323), A300 (≠ P324), D319 (= D343), G320 (= G344), I321 (≠ F345), G322 (= G346), T324 (= T348), D401 (= D426), R416 (= R441), K422 (= K447), Y427 (≠ R452)
- binding 2-chloranyl-1,3-thiazole-5-carboxylic acid: Y223 (≠ K252), A297 (= A321), G322 (= G346), S323 (≠ Q347), A328 (= A352)
6m2tA The crystal structure of benzoate coenzyme a ligase double mutant (h333a/i334a) in complex with 2-methyl-thiazole-5 carboxylate-amp
32% identity, 83% coverage: 71:541/567 of query aligns to 32:514/518 of 6m2tA
- active site: S176 (≠ T206), T196 (≠ V225), T324 (= T348), E325 (= E349), K422 (= K447), Y427 (≠ R452), K507 (= K534)
- binding 2-methyl-1,3-thiazole-5-carboxylic acid: Y223 (≠ K252), G322 (= G346), S323 (≠ Q347), A328 (= A352)
- binding adenosine monophosphate: G298 (= G322), E299 (= E323), A300 (≠ P324), G320 (= G344), I321 (≠ F345), S323 (≠ Q347), T324 (= T348), D401 (= D426), R416 (= R441), K422 (= K447), Y427 (≠ R452)
Query Sequence
>WP_012568177.1 NCBI__GCF_000016185.1:WP_012568177.1
MTDGTMKDGTGAFMAARDILLAAGTDYDRARREFRWPDTGPFNWALDYFDVIARDNPQPA
LRVVSEDGSEETVSYAEMAARSARTATWLRGLGVGRGDRILLMLPNIPPLWEVMLAAMKL
GAVVIPATTLLAGEELRDRVERGGARFVIVAAGQCDRFDDLPGVTRIAVGGAPSGWIAYE
ESRGAPAEFSPDGETRPDDPMLLYFTSGTTAKPKLVLHTHRSYPVGHLSTMYWIGLRPED
VHWNISSPGWAKHAWSNVFAPWNAQATVFVYNYARFQARAVLDVLVGHGVTTLCAPPTVW
RMLIQEDLKSWPVRLREVVGAGEPLNAEVIEQVRSAWGLTVRDGFGQTETTAQVGNSPGQ
PVKPGSMGRPLPGYDVVLLDADGNEAEEGEIALRLSPRPAGLMAGYQSAAGEPVQPPAGG
WYRTGDVASRDADGYLTYVGRADDVFKASDYRISPFELESALIEHPAVAEAAVVPSPDPV
RLAVPKAFLVLAAGYEPDADLARDIFRHIRATLPPYKRVRRIEFADLPKTISGKIRRVEL
RREEQGRADGDGRHPQEFWEEDFPDLR
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