SitesBLAST
Comparing WP_017599801.1 NCBI__GCF_000341125.1:WP_017599801.1 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)
8biqA Crystal structure of acyl-coa synthetase from metallosphaera sedula in complex with acetyl-amp
42% identity, 88% coverage: 41:542/572 of query aligns to 35:542/562 of 8biqA
8bitA Crystal structure of acyl-coa synthetase from metallosphaera sedula in complex with coenzyme a and acetyl-amp
42% identity, 88% coverage: 41:542/572 of query aligns to 36:543/562 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 (≠ Y256), G321 (= G323), E322 (= E324), P323 (= P325), D342 (= D344), F343 (≠ G345), Y344 (≠ F346), Q346 (= Q348), T347 (= T349), D428 (= D428), F440 (≠ Y440), K449 (= K449), R454 (= R454)
- binding coenzyme a: N128 (≠ I131), W247 (= W251), K249 (= K253), K273 (≠ R276), L274 (≠ F277), Q300 (≠ M303), D452 (= D452), Y453 (= Y453), R483 (= R483), P517 (= P517)
8biqB Crystal structure of acyl-coa synthetase from metallosphaera sedula in complex with acetyl-amp
42% identity, 88% coverage: 41:542/572 of query aligns to 34:541/561 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 (≠ G345), Y342 (≠ F346), G343 (= G347), Q344 (= Q348), T345 (= T349), D426 (= D428), F438 (≠ Y440), K447 (= K449), R452 (= R454)
3c5eA Crystal structure of human acyl-coa synthetase medium-chain family member 2a (l64p mutation) in complex with atp (see paper)
32% identity, 89% coverage: 39:546/572 of query aligns to 8:534/536 of 3c5eA
- active site: T188 (= T207), T331 (= T349), E332 (= E350), N434 (≠ K449), R439 (= R454), K524 (= K536)
- binding adenosine-5'-triphosphate: T188 (= T207), S189 (= S208), G190 (= G209), T191 (= T210), S192 (≠ T211), G305 (= G323), E306 (= E324), S307 (≠ P325), G329 (= G347), Q330 (= Q348), T331 (= T349), D413 (= D428), F425 (≠ Y440), R428 (= R443), K524 (= K536)
- binding magnesium ion: M450 (≠ V465), H452 (= H467), V455 (= V470)
3eq6A Crystal structure of human acyl-coa synthetase medium-chain family member 2a (l64p mutation) in a ternary complex with products (see paper)
32% identity, 89% coverage: 39:546/572 of query aligns to 5:531/533 of 3eq6A
- active site: T185 (= T207), T328 (= T349), E329 (= E350), N431 (≠ K449), R436 (= R454), K521 (= K536)
- binding adenosine monophosphate: G302 (= G323), E303 (= E324), S304 (≠ P325), E323 (≠ D344), S324 (≠ G345), Y325 (≠ F346), G326 (= G347), Q327 (= Q348), T328 (= T349), D410 (= D428), F422 (≠ Y440), R425 (= R443), R436 (= R454)
- binding Butyryl Coenzyme A: W229 (= W251), F255 (= F277), I277 (≠ T299), V301 (≠ A322), S433 (= S451), G434 (≠ D452), Y435 (= Y453), P501 (= P517), Y502 (= Y518), Y504 (≠ R520), R506 (= R522)
2wd9A Crystal structure of human acyl-coa synthetase medium-chain family member 2a (l64p mutation) in complex with ibuprofen (see paper)
32% identity, 89% coverage: 39:546/572 of query aligns to 5:531/533 of 2wd9A
- active site: T185 (= T207), T328 (= T349), E329 (= E350), N431 (≠ K449), R436 (= R454), K521 (= K536)
- binding ibuprofen: I230 (≠ G252), L231 (≠ K253), G326 (= G347), Q327 (= Q348), T328 (= T349), R436 (= R454)
2vzeA Crystal structure of human acyl-coa synthetase medium-chain family member 2a (l64p mutation) in complex with amp (see paper)
32% identity, 89% coverage: 39:546/572 of query aligns to 5:531/533 of 2vzeA
- active site: T185 (= T207), T328 (= T349), E329 (= E350), N431 (≠ K449), R436 (= R454), K521 (= K536)
- binding adenosine monophosphate: W229 (= W251), G302 (= G323), E303 (= E324), S304 (≠ P325), E323 (≠ D344), Y325 (≠ F346), G326 (= G347), Q327 (= Q348), T328 (= T349), D410 (= D428), F422 (≠ Y440), R425 (= R443), R436 (= R454)
3b7wA Crystal structure of human acyl-coa synthetase medium-chain family member 2a, with l64p mutation (see paper)
32% identity, 89% coverage: 39:546/572 of query aligns to 9:535/537 of 3b7wA
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)
32% identity, 89% coverage: 39:546/572 of query aligns to 41:567/577 of Q08AH3
- Q139 (≠ I131) binding CoA
- 221:229 (vs. 207:215, 67% identical) binding ATP
- ESYGQT 359:364 (≠ DGFGQT 344:349) binding ATP
- T364 (= T349) binding substrate
- D446 (= D428) binding ATP
- R461 (= R443) binding ATP
- SGY 469:471 (≠ SDY 451:453) binding CoA
- R472 (= R454) binding substrate
- R501 (= R483) binding CoA
- S513 (≠ E495) to L: in dbSNP:rs1133607
- K532 (≠ R512) binding CoA
- YPR 540:542 (≠ RVR 520:522) binding CoA
- K557 (= K536) binding ATP
3gpcA Crystal structure of human acyl-coa synthetase medium-chain family member 2a (l64p mutation) in a complex with coa (see paper)
32% identity, 89% coverage: 39:546/572 of query aligns to 6:530/532 of 3gpcA
- active site: T186 (= T207), T327 (= T349), E328 (= E350), N430 (≠ K449), R435 (= R454), K520 (= K536)
- binding coenzyme a: G301 (= G323), E302 (= E324), S303 (≠ P325), E322 (≠ D344), Y324 (≠ F346), G325 (= G347), Q326 (= Q348), T327 (= T349), D409 (= D428), F421 (≠ Y440), R424 (= R443), T516 (= T532), K520 (= K536), Q522 (≠ R538)
- binding magnesium ion: H448 (= H467), V451 (= V470)
3dayA Crystal structure of human acyl-coa synthetase medium-chain family member 2a (l64p mutation) in complex with amp-cpp (see paper)
32% identity, 89% coverage: 39:546/572 of query aligns to 9:533/535 of 3dayA
- active site: T189 (= T207), T332 (= T349), E333 (= E350), N435 (≠ K449), R440 (= R454), K523 (= K536)
- binding diphosphomethylphosphonic acid adenosyl ester: T189 (= T207), S190 (= S208), G191 (= G209), T192 (= T210), S193 (≠ T211), K197 (= K215), G306 (= G323), E307 (= E324), S308 (≠ P325), Y329 (≠ F346), G330 (= G347), Q331 (= Q348), T332 (= T349), D414 (= D428), F426 (≠ Y440), R429 (= R443), K523 (= K536)
- binding magnesium ion: M451 (≠ V465), H453 (= H467), V456 (= V470)
8rplB Amp-forming acetyl-coa synthetase from chloroflexota bacterium with bound acetyl amp (see paper)
30% identity, 90% coverage: 34:546/572 of query aligns to 71:621/630 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 (= G323), E392 (= E324), P393 (= P325), T416 (≠ G345), W417 (≠ F346), W418 (≠ G347), Q419 (= Q348), T420 (= T349), D502 (= D428), R517 (= R443), K523 (= K449), R528 (= R454)
- binding magnesium ion: V539 (= V465), H541 (= H467)
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)
29% identity, 91% coverage: 34:554/572 of query aligns to 66:625/648 of Q89WV5
- G263 (= G209) mutation to I: Loss of activity.
- G266 (≠ S212) mutation to I: Great decrease in activity.
- K269 (= K215) mutation to G: Great decrease in activity.
- E414 (= E350) mutation to Q: Great decrease in activity.
4wv3B Crystal structure of the anthranilate coa ligase auaeii in complex with anthranoyl-amp (see paper)
29% identity, 87% coverage: 50:545/572 of query aligns to 14:511/518 of 4wv3B
- active site: S175 (≠ T207), T320 (= T349), E321 (= E350), K418 (= K449), W423 (≠ R454), K502 (= K536)
- binding 5'-O-[(S)-[(2-aminobenzoyl)oxy](hydroxy)phosphoryl]adenosine: F220 (≠ W251), T221 (≠ G252), F222 (≠ K253), A293 (= A322), S294 (≠ G323), E295 (= E324), A296 (≠ P325), G316 (= G345), I317 (≠ F346), G318 (= G347), C319 (≠ Q348), T320 (= T349), D397 (= D428), H409 (≠ Y440), R412 (= R443), K502 (= K536)
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)
29% identity, 86% coverage: 57:547/572 of query aligns to 100:629/662 of P78773
- T596 (≠ R514) modified: Phosphothreonine
4rm3A Crystal structure of a benzoate coenzyme a ligase with 2-furoic acid (see paper)
30% identity, 89% coverage: 37:543/572 of query aligns to 4:515/518 of 4rm3A
- active site: S177 (≠ T207), T197 (≠ V226), T325 (= T349), E326 (= E350), K423 (= K449), Y428 (≠ R454), K508 (= K536)
- binding 2-furoic acid: A223 (≠ G252), Y224 (≠ K253), A298 (= A322), G323 (= G347), H329 (vs. gap), I330 (≠ M353), K423 (= K449)
4rmnA Crystal structure of a benzoate coenzyme a ligase with 2-thiophene carboxylic acid (see paper)
29% identity, 89% coverage: 37:543/572 of query aligns to 3:514/518 of 4rmnA
- active site: S176 (≠ T207), T196 (≠ V226), T324 (= T349), E325 (= E350), K422 (= K449), Y427 (≠ R454), K507 (= K536)
- binding thiophene-2-carboxylic acid: A217 (≠ S247), F221 (≠ W251), Y223 (≠ K253), G269 (≠ A296), A270 (≠ P297), A297 (= A322), G298 (= G323), G322 (= G347), S323 (≠ Q348), H328 (vs. gap), I329 (≠ M353), K422 (= K449), G425 (≠ D452)
4rlfB Crystal structure of a benzoate coenzyme a ligase with p-toluic acid and o-toluic acid (see paper)
30% identity, 89% coverage: 37:543/572 of query aligns to 3:514/519 of 4rlfB
- active site: S176 (≠ T207), T196 (≠ V226), T324 (= T349), E325 (= E350), K422 (= K449), Y427 (≠ R454), K507 (= K536)
- binding 2-methylbenzoic acid: A222 (≠ G252), Y223 (≠ K253), G298 (= G323), I321 (≠ F346), G322 (= G347), S323 (≠ Q348), H328 (vs. gap)
- binding 4-methylbenzoic acid: A216 (≠ I246), P246 (≠ F277), P248 (= P279), G269 (≠ A296), A270 (≠ P297), G273 (≠ V300)
4zjzA Crystal structure of a benzoate coenzyme a ligase with benzoyl-amp (see paper)
29% identity, 89% coverage: 37:543/572 of query aligns to 3:514/517 of 4zjzA
- active site: S176 (≠ T207), T196 (≠ V226), T324 (= T349), E325 (= E350), K422 (= K449), Y427 (≠ R454), K507 (= K536)
- binding 5'-O-[(R)-(benzoyloxy)(hydroxy)phosphoryl]adenosine: A222 (≠ G252), Y223 (≠ K253), A297 (= A322), G298 (= G323), E299 (= E324), A300 (≠ P325), G320 (= G345), I321 (≠ F346), G322 (= G347), S323 (≠ Q348), T324 (= T349), H328 (vs. gap), I329 (≠ M353), D401 (= D428), R416 (= R443), K422 (= K449), Y427 (≠ R454)
4rm2A Crystal structure of a benzoate coenzyme a ligase with 2-fluoro benzoic acid (see paper)
29% identity, 89% coverage: 37:543/572 of query aligns to 3:514/516 of 4rm2A
- active site: S176 (≠ T207), T196 (≠ V226), T324 (= T349), E325 (= E350), K422 (= K449), Y427 (≠ R454), K507 (= K536)
- binding 2-fluorobenzoic acid: A216 (≠ I246), A222 (≠ G252), Y223 (≠ K253), P246 (≠ F277), T247 (≠ D278), V251 (vs. gap), F267 (≠ M294), G269 (≠ A296), A270 (≠ P297), G273 (≠ V300), M277 (= M303), A297 (= A322), G298 (= G323), I321 (≠ F346), G322 (= G347), S323 (≠ Q348), H328 (vs. gap), K422 (= K449)
Query Sequence
>WP_017599801.1 NCBI__GCF_000341125.1:WP_017599801.1
MSKERAAEGAAEFRAARDLLLRHREDQPRAHREFSWPRPDRFNWALDYFDALAETIPDRT
ALWIVEEDGSEAKYTYQHLSERSNQVANWLIGQGVHPGDRIMLMLGNQVELWETTLAAIK
LGAVVCPTAPILTESDLVDRLDRGDVAHVVCSPAETEKFAHLRGHWTRVCVGYMDGWLSY
PDSEHAALDFTPPRPVGADDPLLLYFTSGTTSRPKLVSHSQRSYPVGHLSTMYWLGLQPA
DIHLNISSPGWGKHAYSSVFAPWNAEATSLVVNQARFDPERLLDQVVRCGVTTMCAPPTV
WRMLIQTDLTSWSVRLREAAAAGEPLNPEVVDKVRDAWGITVRDGFGQTETTMLVGNAPG
QSVVPGSMGRPLPGYDIVLTDPTTDERTETGEICVDLSGDPVGVMTGYADGTDMTRDVTR
LGLYHTGDLAARDPRGYITYIGRIDDVFKASDYRISPFELESVLVEHEFVAEAAVVPSPD
PLRLSVAKAYIALAEGVPPDADTARAILTYSRERLSPYKRVRRLEFTDLPKTVSGKIRRV
QLRRAEAERGTVTDGQRNQREFWEEDLPGLKD
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