SitesBLAST
Comparing GFF1013 FitnessBrowser__Phaeo:GFF1013 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)
3eq6A Crystal structure of human acyl-coa synthetase medium-chain family member 2a (l64p mutation) in a ternary complex with products (see paper)
31% identity, 95% coverage: 20:510/516 of query aligns to 3:530/533 of 3eq6A
- active site: T185 (= T176), T328 (= T318), E329 (= E319), N431 (≠ T416), R436 (= R421), K521 (= K501)
- binding adenosine monophosphate: G302 (= G292), E303 (= E293), S304 (≠ P294), E323 (= E313), S324 (≠ F314), Y325 (= Y315), G326 (= G316), Q327 (= Q317), T328 (= T318), D410 (= D396), F422 (= F407), R425 (= R410), R436 (= R421)
- binding Butyryl Coenzyme A: W229 (= W222), F255 (= F248), I277 (≠ T270), V301 (≠ G291), S433 (≠ A418), G434 (= G419), Y435 (= Y420), P501 (≠ K481), Y502 (= Y482), Y504 (= Y484), R506 (= R486)
2wd9A Crystal structure of human acyl-coa synthetase medium-chain family member 2a (l64p mutation) in complex with ibuprofen (see paper)
31% identity, 95% coverage: 20:510/516 of query aligns to 3:530/533 of 2wd9A
- active site: T185 (= T176), T328 (= T318), E329 (= E319), N431 (≠ T416), R436 (= R421), K521 (= K501)
- binding ibuprofen: I230 (= I223), L231 (≠ G224), G326 (= G316), Q327 (= Q317), T328 (= T318), R436 (= R421)
2vzeA Crystal structure of human acyl-coa synthetase medium-chain family member 2a (l64p mutation) in complex with amp (see paper)
31% identity, 95% coverage: 20:510/516 of query aligns to 3:530/533 of 2vzeA
- active site: T185 (= T176), T328 (= T318), E329 (= E319), N431 (≠ T416), R436 (= R421), K521 (= K501)
- binding adenosine monophosphate: W229 (= W222), G302 (= G292), E303 (= E293), S304 (≠ P294), E323 (= E313), Y325 (= Y315), G326 (= G316), Q327 (= Q317), T328 (= T318), D410 (= D396), F422 (= F407), R425 (= R410), R436 (= R421)
3b7wA Crystal structure of human acyl-coa synthetase medium-chain family member 2a, with l64p mutation (see paper)
31% identity, 96% coverage: 17:510/516 of query aligns to 4:534/537 of 3b7wA
3c5eA Crystal structure of human acyl-coa synthetase medium-chain family member 2a (l64p mutation) in complex with atp (see paper)
31% identity, 96% coverage: 17:510/516 of query aligns to 3:533/536 of 3c5eA
- active site: T188 (= T176), T331 (= T318), E332 (= E319), N434 (≠ T416), R439 (= R421), K524 (= K501)
- binding adenosine-5'-triphosphate: T188 (= T176), S189 (= S177), G190 (= G178), T191 (= T179), S192 (≠ T180), G305 (= G292), E306 (= E293), S307 (≠ P294), G329 (= G316), Q330 (= Q317), T331 (= T318), D413 (= D396), F425 (= F407), R428 (= R410), K524 (= K501)
- binding magnesium ion: M450 (= M432), H452 (= H434), V455 (= V437)
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)
31% identity, 96% coverage: 17:510/516 of query aligns to 36:566/577 of Q08AH3
- Q139 (vs. gap) binding
- 221:229 (vs. 176:184, 67% identical) binding
- ESYGQT 359:364 (≠ EFYGQT 313:318) binding
- T364 (= T318) binding
- D446 (= D396) binding
- R461 (= R410) binding
- SGY 469:471 (≠ AGY 418:420) binding
- R472 (= R421) binding
- R501 (= R450) binding
- S513 (≠ P462) to L: in dbSNP:rs1133607
- K532 (= K476) binding
- YPR 540:542 (= YPR 484:486) binding
- K557 (= K501) binding
3dayA Crystal structure of human acyl-coa synthetase medium-chain family member 2a (l64p mutation) in complex with amp-cpp (see paper)
31% identity, 96% coverage: 17:510/516 of query aligns to 4:532/535 of 3dayA
- active site: T189 (= T176), T332 (= T318), E333 (= E319), N435 (≠ T416), R440 (= R421), K523 (= K501)
- binding diphosphomethylphosphonic acid adenosyl ester: T189 (= T176), S190 (= S177), G191 (= G178), T192 (= T179), S193 (≠ T180), K197 (= K184), G306 (= G292), E307 (= E293), S308 (≠ P294), Y329 (= Y315), G330 (= G316), Q331 (= Q317), T332 (= T318), D414 (= D396), F426 (= F407), R429 (= R410), K523 (= K501)
- binding magnesium ion: M451 (= M432), H453 (= H434), V456 (= V437)
3gpcA Crystal structure of human acyl-coa synthetase medium-chain family member 2a (l64p mutation) in a complex with coa (see paper)
31% identity, 96% coverage: 17:510/516 of query aligns to 1:529/532 of 3gpcA
- active site: T186 (= T176), T327 (= T318), E328 (= E319), N430 (≠ T416), R435 (= R421), K520 (= K501)
- binding coenzyme a: G301 (= G292), E302 (= E293), S303 (≠ P294), E322 (= E313), Y324 (= Y315), G325 (= G316), Q326 (= Q317), T327 (= T318), D409 (= D396), F421 (= F407), R424 (= R410), T516 (= T497), K520 (= K501), Q522 (≠ I503)
- binding magnesium ion: H448 (= H434), V451 (= V437)
8biqB Crystal structure of acyl-coa synthetase from metallosphaera sedula in complex with acetyl-amp
31% identity, 91% coverage: 38:507/516 of query aligns to 53:541/561 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 (= G292), E320 (= E293), P321 (= P294), D340 (≠ E313), F341 (= F314), Y342 (= Y315), G343 (= G316), Q344 (= Q317), T345 (= T318), D426 (= D396), F438 (= F407), K447 (≠ T416), R452 (= R421)
8biqA Crystal structure of acyl-coa synthetase from metallosphaera sedula in complex with acetyl-amp
31% identity, 91% coverage: 38:507/516 of query aligns to 54:542/562 of 8biqA
8bitA Crystal structure of acyl-coa synthetase from metallosphaera sedula in complex with coenzyme a and acetyl-amp
31% identity, 91% coverage: 38:507/516 of query aligns to 55:543/562 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 (= W222), G321 (= G292), E322 (= E293), P323 (= P294), D342 (≠ E313), F343 (= F314), Y344 (= Y315), Q346 (= Q317), T347 (= T318), D428 (= D396), F440 (= F407), K449 (≠ T416), R454 (= R421)
- binding coenzyme a: N128 (≠ L108), W247 (= W215), K249 (≠ D219), K273 (≠ R244), L274 (= L245), Q300 (vs. gap), D452 (≠ G419), Y453 (= Y420), R483 (= R450), P517 (≠ K481)
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)
30% identity, 95% coverage: 18:508/516 of query aligns to 101:649/689 of Q9NUB1
- V488 (≠ T357) to M: in dbSNP:rs6050249
- K642 (= K501) modified: N6-acetyllysine; mutation to Q: Loss of activity.
Sites not aligning to the query:
- 1:37 modified: transit peptide, Mitochondrion
Q99NB1 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 Mus musculus (Mouse) (see paper)
29% identity, 95% coverage: 18:508/516 of query aligns to 94:642/682 of Q99NB1
- K635 (= K501) modified: N6-acetyllysine
8w0dA Acetyl-coenzyme A synthetase 2
27% identity, 99% coverage: 7:516/516 of query aligns to 67:639/666 of 8w0dA
- binding 5'-O-{(R)-hydroxy[(propan-2-yl)oxy]phosphoryl}adenosine: G398 (= G292), E399 (= E293), P400 (= P294), T423 (≠ F314), Y424 (= Y315), W425 (≠ G316), Q426 (= Q317), T427 (= T318), D513 (= D396), I525 (≠ F407), R528 (= R410), R539 (= R421)
8v4rA Crystal structure of acetyl-coa synthetase 2 in complex with amp and coa from candida albicans
27% identity, 99% coverage: 7:516/516 of query aligns to 67:639/666 of 8v4rA
- binding adenosine monophosphate: G398 (= G292), E399 (= E293), P400 (= P294), T423 (≠ F314), Y424 (= Y315), Q426 (= Q317), T427 (= T318), D513 (= D396), I525 (≠ F407), R528 (= R410), R539 (= R421)
- binding coenzyme a: F175 (= F106), R203 (≠ D129), R206 (≠ G132), G316 (≠ A218), H538 (≠ Y420), R599 (≠ K476), F605 (≠ Y482)
8w0cA Acetyl-coenzyme A synthetase 2
27% identity, 99% coverage: 7:516/516 of query aligns to 68:640/667 of 8w0cA
- binding 5'-O-[(S)-(cyclopentyloxy)(hydroxy)phosphoryl]adenosine: G399 (= G292), E400 (= E293), P401 (= P294), T424 (≠ F314), Y425 (= Y315), W426 (≠ G316), Q427 (= Q317), T428 (= T318), D514 (= D396), R529 (= R410), R540 (= R421)
8w0bA Acetyl-coenzyme A synthetase 2
27% identity, 99% coverage: 7:516/516 of query aligns to 68:640/667 of 8w0bA
- binding 5'-O-[(R)-(cyclopropyloxy)(hydroxy)phosphoryl]adenosine: V398 (≠ G291), G399 (= G292), E400 (= E293), P401 (= P294), T424 (≠ F314), Y425 (= Y315), W426 (≠ G316), Q427 (= Q317), T428 (= T318), D514 (= D396), I526 (≠ F407), R529 (= R410), R540 (= R421)
8v4pA Crystal structure of acetyl-coa synthetase 2 in complex with adenosine-5'-allylphosphate from candida albicans
27% identity, 99% coverage: 7:516/516 of query aligns to 67:634/660 of 8v4pA
- binding 5'-O-{(S)-hydroxy[(prop-2-en-1-yl)oxy]phosphoryl}adenosine: P152 (≠ S83), A176 (≠ K107), G177 (≠ L108), R203 (≠ D129), T208 (≠ A134), D317 (= D219), E342 (≠ R244), G343 (≠ L245), P345 (≠ K247), G398 (= G292), E399 (= E293), P400 (= P294), T423 (≠ F314), W425 (≠ G316), Q426 (= Q317), T427 (= T318), D513 (= D396), I525 (≠ F407), R528 (= R410), R539 (= R421)
8v4oA Crystal structure of acetyl-coa synthetase 2 in complex with amp from candida albicans
27% identity, 99% coverage: 7:516/516 of query aligns to 67:634/660 of 8v4oA
- binding adenosine monophosphate: G398 (= G292), E399 (= E293), P400 (= P294), T423 (≠ F314), Y424 (= Y315), W425 (≠ G316), Q426 (= Q317), T427 (= T318), D513 (= D396), I525 (≠ F407), R528 (= R410), R539 (= R421)
8w0jA Acetyl-coenzyme A synthetase 2
27% identity, 99% coverage: 7:516/516 of query aligns to 68:635/662 of 8w0jA
- binding 5'-O-{(S)-hydroxy[(prop-2-yn-1-yl)oxy]phosphoryl}adenosine: G399 (= G292), E400 (= E293), P401 (= P294), T424 (≠ F314), Y425 (= Y315), W426 (≠ G316), Q427 (= Q317), T428 (= T318), D514 (= D396), I526 (≠ F407), R529 (= R410), R540 (= R421)
Query Sequence
>GFF1013 FitnessBrowser__Phaeo:GFF1013
MSGVGGHTLYPGLRTDGGWQFPSCLNMAAQALDHPDEQLALIDLTTGARRDIRYGELRQM
VDAVARDLMQRVQPGDRVGVLLSQSVDCAVAHLAIWKIGAISVPLFKLFQHDALASRIGD
AGLELVLTDGGGTAQLGSLAQPLLVADILSASTGQSDHLLPYAETTPETPAVLIYTSGTT
GSAKGALHGHRVLSGHLPGVAISHDHLGQPGDCLWTPADWAWIGGLFDVLMPGLALGVPV
VAARLDKFTPEACAEIIRQGDVRNVFFPPTALRLLKAAGQGLDGLRSVASGGEPLGAEML
AWGQRHLGVTINEFYGQTECNMTVSSCVADFPVRPGCIGRPVPGCTVEVLDDTGTPTKDE
GDVAVRRGAASMMLEYWNRPDATAEKFHADWLITGDRGIWEGDYLRFVGREDDVITSAGY
RIGPAEIEDCLMTHPAVATVGVVGKPDELRTEIVKAYVVLKPGHSPSESDLQDYVKSRLA
KYSYPREVEFLDALPMTVTGKVIRKELKARAAGKVN
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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