SitesBLAST
Comparing 8499218 FitnessBrowser__Miya:8499218 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)
39% identity, 96% coverage: 22:554/557 of query aligns to 39:572/577 of Q08AH3
- Q139 (= Q116) binding
- 221:229 (vs. 204:212, 67% identical) binding
- ESYGQT 359:364 (≠ EGYGQT 343:348) binding
- T364 (= T348) binding
- D446 (= D430) binding
- R461 (= R445) binding
- SGY 469:471 (= SGY 453:455) binding
- R472 (= R456) binding
- R501 (= R485) binding
- S513 (≠ A497) to L: in dbSNP:rs1133607
- K532 (= K514) binding
- YPR 540:542 (= YPR 522:524) binding
- K557 (= K539) binding
3c5eA Crystal structure of human acyl-coa synthetase medium-chain family member 2a (l64p mutation) in complex with atp (see paper)
39% identity, 95% coverage: 22:549/557 of query aligns to 6:534/536 of 3c5eA
- active site: T188 (≠ S204), T331 (= T348), E332 (= E349), N434 (≠ K451), R439 (= R456), K524 (= K539)
- binding adenosine-5'-triphosphate: T188 (≠ S204), S189 (= S205), G190 (= G206), T191 (= T207), S192 (≠ T208), G305 (= G322), E306 (= E323), S307 (≠ L324), G329 (= G346), Q330 (= Q347), T331 (= T348), D413 (= D430), F425 (= F442), R428 (= R445), K524 (= K539)
- binding magnesium ion: M450 (≠ V467), H452 (= H469), V455 (= V472)
3eq6A Crystal structure of human acyl-coa synthetase medium-chain family member 2a (l64p mutation) in a ternary complex with products (see paper)
39% identity, 95% coverage: 22:549/557 of query aligns to 3:531/533 of 3eq6A
- active site: T185 (≠ S204), T328 (= T348), E329 (= E349), N431 (≠ K451), R436 (= R456), K521 (= K539)
- binding adenosine monophosphate: G302 (= G322), E303 (= E323), S304 (≠ L324), E323 (= E343), S324 (≠ G344), Y325 (= Y345), G326 (= G346), Q327 (= Q347), T328 (= T348), D410 (= D430), F422 (= F442), R425 (= R445), R436 (= R456)
- binding Butyryl Coenzyme A: W229 (= W248), F255 (= F275), I277 (≠ T297), V301 (≠ A321), S433 (= S453), G434 (= G454), Y435 (= Y455), P501 (= P519), Y502 (= Y520), Y504 (= Y522), R506 (= R524)
2wd9A Crystal structure of human acyl-coa synthetase medium-chain family member 2a (l64p mutation) in complex with ibuprofen (see paper)
39% identity, 95% coverage: 22:549/557 of query aligns to 3:531/533 of 2wd9A
- active site: T185 (≠ S204), T328 (= T348), E329 (= E349), N431 (≠ K451), R436 (= R456), K521 (= K539)
- binding ibuprofen: I230 (≠ G249), L231 (≠ K250), G326 (= G346), Q327 (= Q347), T328 (= T348), R436 (= R456)
2vzeA Crystal structure of human acyl-coa synthetase medium-chain family member 2a (l64p mutation) in complex with amp (see paper)
39% identity, 95% coverage: 22:549/557 of query aligns to 3:531/533 of 2vzeA
- active site: T185 (≠ S204), T328 (= T348), E329 (= E349), N431 (≠ K451), R436 (= R456), K521 (= K539)
- binding adenosine monophosphate: W229 (= W248), G302 (= G322), E303 (= E323), S304 (≠ L324), E323 (= E343), Y325 (= Y345), G326 (= G346), Q327 (= Q347), T328 (= T348), D410 (= D430), F422 (= F442), R425 (= R445), R436 (= R456)
3b7wA Crystal structure of human acyl-coa synthetase medium-chain family member 2a, with l64p mutation (see paper)
39% identity, 95% coverage: 22:549/557 of query aligns to 7:535/537 of 3b7wA
3gpcA Crystal structure of human acyl-coa synthetase medium-chain family member 2a (l64p mutation) in a complex with coa (see paper)
39% identity, 95% coverage: 22:549/557 of query aligns to 4:530/532 of 3gpcA
- active site: T186 (≠ S204), T327 (= T348), E328 (= E349), N430 (≠ K451), R435 (= R456), K520 (= K539)
- binding coenzyme a: G301 (= G322), E302 (= E323), S303 (≠ L324), E322 (= E343), Y324 (= Y345), G325 (= G346), Q326 (= Q347), T327 (= T348), D409 (= D430), F421 (= F442), R424 (= R445), T516 (= T535), K520 (= K539), Q522 (≠ K541)
- binding magnesium ion: H448 (= H469), V451 (= V472)
3dayA Crystal structure of human acyl-coa synthetase medium-chain family member 2a (l64p mutation) in complex with amp-cpp (see paper)
39% identity, 95% coverage: 22:549/557 of query aligns to 7:533/535 of 3dayA
- active site: T189 (≠ S204), T332 (= T348), E333 (= E349), N435 (≠ K451), R440 (= R456), K523 (= K539)
- binding diphosphomethylphosphonic acid adenosyl ester: T189 (≠ S204), S190 (= S205), G191 (= G206), T192 (= T207), S193 (≠ T208), K197 (= K212), G306 (= G322), E307 (= E323), S308 (≠ L324), Y329 (= Y345), G330 (= G346), Q331 (= Q347), T332 (= T348), D414 (= D430), F426 (= F442), R429 (= R445), K523 (= K539)
- binding magnesium ion: M451 (≠ V467), H453 (= H469), V456 (= V472)
8biqB Crystal structure of acyl-coa synthetase from metallosphaera sedula in complex with acetyl-amp
39% identity, 93% coverage: 27:545/557 of query aligns to 35:541/561 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 (≠ L324), D340 (≠ E343), F341 (≠ G344), Y342 (= Y345), G343 (= G346), Q344 (= Q347), T345 (= T348), D426 (= D430), F438 (= F442), K447 (= K451), R452 (= R456)
8biqA Crystal structure of acyl-coa synthetase from metallosphaera sedula in complex with acetyl-amp
39% identity, 93% coverage: 27:545/557 of query aligns to 36:542/562 of 8biqA
8bitA Crystal structure of acyl-coa synthetase from metallosphaera sedula in complex with coenzyme a and acetyl-amp
39% identity, 93% coverage: 27:545/557 of query aligns to 37:543/562 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 (= W253), G321 (= G322), E322 (= E323), P323 (≠ L324), D342 (≠ E343), F343 (≠ G344), Y344 (= Y345), Q346 (= Q347), T347 (= T348), D428 (= D430), F440 (= F442), K449 (= K451), R454 (= R456)
- binding coenzyme a: N128 (≠ Q116), W247 (= W248), K249 (= K250), K273 (= K274), L274 (≠ F275), Q300 (≠ F301), D452 (≠ G454), Y453 (= Y455), R483 (= R485), P517 (= P519)
4wv3B Crystal structure of the anthranilate coa ligase auaeii in complex with anthranoyl-amp (see paper)
32% identity, 89% coverage: 57:553/557 of query aligns to 34:516/518 of 4wv3B
- active site: S175 (= S204), T320 (= T348), E321 (= E349), K418 (= K451), W423 (≠ R456), K502 (= K539)
- binding 5'-O-[(S)-[(2-aminobenzoyl)oxy](hydroxy)phosphoryl]adenosine: F220 (≠ W248), T221 (≠ G249), F222 (≠ K250), A293 (= A321), S294 (≠ G322), E295 (= E323), A296 (≠ L324), G316 (= G344), I317 (≠ Y345), G318 (= G346), C319 (≠ Q347), T320 (= T348), D397 (= D430), H409 (≠ F442), R412 (= R445), K502 (= K539)
8w0dA Acetyl-coenzyme A synthetase 2
31% identity, 94% coverage: 27:547/557 of query aligns to 87:632/666 of 8w0dA
- binding 5'-O-{(R)-hydroxy[(propan-2-yl)oxy]phosphoryl}adenosine: G398 (= G322), E399 (= E323), P400 (≠ L324), T423 (≠ G344), Y424 (= Y345), W425 (≠ G346), Q426 (= Q347), T427 (= T348), D513 (= D430), I525 (≠ F442), R528 (= R445), R539 (= R456)
8v4rA Crystal structure of acetyl-coa synthetase 2 in complex with amp and coa from candida albicans
31% identity, 94% coverage: 27:547/557 of query aligns to 87:632/666 of 8v4rA
- binding adenosine monophosphate: G398 (= G322), E399 (= E323), P400 (≠ L324), T423 (≠ G344), Y424 (= Y345), Q426 (= Q347), T427 (= T348), D513 (= D430), I525 (≠ F442), R528 (= R445), R539 (= R456)
- binding coenzyme a: F175 (≠ P114), R203 (vs. gap), R206 (vs. gap), G316 (≠ A244), H538 (≠ Y455), R599 (≠ K514), F605 (≠ Y520)
8w0cA Acetyl-coenzyme A synthetase 2
31% identity, 94% coverage: 27:547/557 of query aligns to 88:633/667 of 8w0cA
- binding 5'-O-[(S)-(cyclopentyloxy)(hydroxy)phosphoryl]adenosine: G399 (= G322), E400 (= E323), P401 (≠ L324), T424 (≠ G344), Y425 (= Y345), W426 (≠ G346), Q427 (= Q347), T428 (= T348), D514 (= D430), R529 (= R445), R540 (= R456)
8w0bA Acetyl-coenzyme A synthetase 2
31% identity, 94% coverage: 27:547/557 of query aligns to 88:633/667 of 8w0bA
- binding 5'-O-[(R)-(cyclopropyloxy)(hydroxy)phosphoryl]adenosine: V398 (≠ A321), G399 (= G322), E400 (= E323), P401 (≠ L324), T424 (≠ G344), Y425 (= Y345), W426 (≠ G346), Q427 (= Q347), T428 (= T348), D514 (= D430), I526 (≠ F442), R529 (= R445), R540 (= R456)
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)
32% identity, 89% coverage: 51:547/557 of query aligns to 99:614/648 of Q89WV5
- G263 (= G206) mutation to I: Loss of activity.
- G266 (= G209) mutation to I: Great decrease in activity.
- K269 (= K212) mutation to G: Great decrease in activity.
- E414 (= E349) mutation to Q: Great decrease in activity.
7kdsA Crystal structure of acetyl-coa synthetase 2 in complex with adenosine-5'-propylphosphate from candida albicans
31% identity, 94% coverage: 27:547/557 of query aligns to 87:628/654 of 7kdsA
- active site: T275 (≠ S204), T427 (= T348), E428 (= E349), N534 (≠ K451), R539 (= R456), K620 (= K539)
- binding adenosine-5'-monophosphate-propyl ester: I321 (≠ G249), G398 (= G322), E399 (= E323), P400 (≠ L324), D422 (≠ E343), T423 (≠ G344), Y424 (= Y345), W425 (≠ G346), Q426 (= Q347), T427 (= T348), D513 (= D430), R528 (= R445), N534 (≠ K451), R539 (= R456)
8v4pA Crystal structure of acetyl-coa synthetase 2 in complex with adenosine-5'-allylphosphate from candida albicans
31% identity, 94% coverage: 27:547/557 of query aligns to 87:627/660 of 8v4pA
- binding 5'-O-{(S)-hydroxy[(prop-2-en-1-yl)oxy]phosphoryl}adenosine: P152 (≠ Y91), A176 (= A115), G177 (≠ Q116), R203 (vs. gap), T208 (≠ H138), D317 (= D245), E342 (≠ D270), G343 (≠ F271), P345 (≠ G273), G398 (= G322), E399 (= E323), P400 (≠ L324), T423 (≠ G344), W425 (≠ G346), Q426 (= Q347), T427 (= T348), D513 (= D430), I525 (≠ F442), R528 (= R445), R539 (= R456)
8v4oA Crystal structure of acetyl-coa synthetase 2 in complex with amp from candida albicans
31% identity, 94% coverage: 27:547/557 of query aligns to 87:627/660 of 8v4oA
- binding adenosine monophosphate: G398 (= G322), E399 (= E323), P400 (≠ L324), T423 (≠ G344), Y424 (= Y345), W425 (≠ G346), Q426 (= Q347), T427 (= T348), D513 (= D430), I525 (≠ F442), R528 (= R445), R539 (= R456)
Query Sequence
>8499218 FitnessBrowser__Miya:8499218
MTYTTKFTAKDYKEFCATFRIDAPDTFNFAFDVLDPIAAADPGRLCIAHVDDAGVRRDYT
FAWMAEASAKLANALRLRGIRKGDRVMLVLYRRIEFWVSMLALHRLGAVAIPAPAQLTPK
DIVFRVERAKTRCVIVDHSITERVEAARPDCPGLAVCVQVGGDALPRGWVDYDTIFTPAE
ARFPRPESPLEFAGGEDPLLIFFSSGTTGMPKMVEHVHTYPLGHLLTGMYWHDLVPGDLH
LTLADTGWGKAVWGKFYGQWMAGASVFVYDFRGKFEPAALLDVLAAHAVTTFCAPPTVYR
FLVRQDLSAYDLSKLRHCTTAGELLNDSVFHDWKAATGLEIHEGYGQTETTLQIATLPCM
TPKAGSIGRPMPGWDVVLQDAAGNICPPGEEGEICVRVAEGLPVGLFRGYLEEPEKTASV
MFGGYYHTGDKAWMDEDGYYWFLGRVDDLIKSSGYRIGPFEVESALVAHPAVVEAAVTGV
PDPLRGQAVKATVVLAAGYTASDALTKELQDHVKKVTAPYKYPRIIDYVAELPKTISGKI
KRAEIRERDQQASGPGA
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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