SitesBLAST
Comparing 202759 SO3664 long-chain-fatty-acid--CoA ligase (NCBI ptt file) 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)
P69451 Long-chain-fatty-acid--CoA ligase; Long-chain acyl-CoA synthetase; Acyl-CoA synthetase; EC 6.2.1.3 from Escherichia coli (strain K12) (see paper)
48% identity, 99% coverage: 4:532/532 of query aligns to 12:551/561 of P69451
- Y213 (= Y190) mutation to A: Loss of activity.
- T214 (= T191) mutation to A: 10% of wild-type activity.
- G216 (= G193) mutation to A: Decreases activity.
- T217 (= T194) mutation to A: Decreases activity.
- G219 (= G196) mutation to A: Decreases activity.
- K222 (= K199) mutation to A: Decreases activity.
- E361 (= E338) mutation to A: Loss of activity.
4gxqA Crystal structure of atp bound rpmatb-bxbclm chimera b1 (see paper)
30% identity, 95% coverage: 29:531/532 of query aligns to 26:498/506 of 4gxqA
- active site: T163 (= T191), N183 (= N211), H207 (= H238), T303 (≠ S337), E304 (= E338), I403 (= I436), N408 (= N441), A491 (≠ K524)
- binding adenosine-5'-triphosphate: T163 (= T191), S164 (≠ G192), G165 (= G193), T166 (= T194), T167 (= T195), H207 (= H238), S277 (≠ G311), A278 (≠ T312), P279 (≠ A313), E298 (= E332), M302 (≠ L336), T303 (≠ S337), D382 (= D415), R397 (= R430)
- binding carbonate ion: H207 (= H238), S277 (≠ G311), R299 (≠ G333), G301 (= G335)
5bsmA Crystal structure of 4-coumarate:coa ligase complexed with magnesium and adenosine triphosphate (see paper)
31% identity, 92% coverage: 42:531/532 of query aligns to 47:526/530 of 5bsmA
- active site: S182 (≠ T191), S202 (≠ N211), H230 (= H238), T329 (≠ S337), E330 (= E338), K434 (≠ I436), Q439 (≠ N441), K519 (= K524)
- binding adenosine-5'-triphosphate: S182 (≠ T191), S183 (≠ G192), G184 (= G193), T185 (= T194), T186 (= T195), K190 (= K199), H230 (= H238), A302 (≠ G311), A303 (≠ T312), P304 (≠ A313), Y326 (= Y334), G327 (= G335), M328 (≠ L336), T329 (≠ S337), D413 (= D415), I425 (= I427), R428 (= R430), K519 (= K524)
5bsvA Crystal structure of 4-coumarate:coa ligase complexed with feruloyl adenylate (see paper)
31% identity, 92% coverage: 42:531/532 of query aligns to 47:526/529 of 5bsvA
- active site: S182 (≠ T191), S202 (≠ N211), H230 (= H238), T329 (≠ S337), E330 (= E338), K434 (≠ I436), Q439 (≠ N441), K519 (= K524)
- binding 5'-O-[(R)-hydroxy{[(2E)-3-(5-methoxy-4-oxocyclohexa-1,5-dien-1-yl)prop-2-enoyl]oxy}phosphoryl]adenosine: H230 (= H238), Y232 (= Y240), S236 (≠ L246), A302 (≠ G311), A303 (≠ T312), P304 (≠ A313), G325 (= G333), G327 (= G335), M328 (≠ L336), T329 (≠ S337), P333 (= P341), V334 (= V342), D413 (= D415), K430 (= K432), K434 (≠ I436), Q439 (≠ N441)
5bsuA Crystal structure of 4-coumarate:coa ligase complexed with caffeoyl adenylate (see paper)
31% identity, 92% coverage: 42:531/532 of query aligns to 47:526/529 of 5bsuA
- active site: S182 (≠ T191), S202 (≠ N211), H230 (= H238), T329 (≠ S337), E330 (= E338), K434 (≠ I436), Q439 (≠ N441), K519 (= K524)
- binding 5'-O-[(R)-{[(2E)-3-(3,4-dioxocyclohexa-1,5-dien-1-yl)prop-2-enoyl]oxy}(hydroxy)phosphoryl]adenosine: H230 (= H238), Y232 (= Y240), S236 (≠ L246), M299 (≠ I308), A302 (≠ G311), A303 (≠ T312), P304 (≠ A313), G325 (= G333), G327 (= G335), M328 (≠ L336), T329 (≠ S337), P333 (= P341), D413 (= D415), K430 (= K432), K434 (≠ I436), Q439 (≠ N441)
5bstA Crystal structure of 4-coumarate:coa ligase complexed with coumaroyl adenylate (see paper)
31% identity, 92% coverage: 42:531/532 of query aligns to 47:526/529 of 5bstA
- active site: S182 (≠ T191), S202 (≠ N211), H230 (= H238), T329 (≠ S337), E330 (= E338), K434 (≠ I436), Q439 (≠ N441), K519 (= K524)
- binding 5'-O-[(R)-hydroxy{[(2E)-3-(4-oxocyclohexa-1,5-dien-1-yl)prop-2-enoyl]oxy}phosphoryl]adenosine: H230 (= H238), Y232 (= Y240), S236 (≠ L246), A302 (≠ G311), A303 (≠ T312), P304 (≠ A313), G325 (= G333), Y326 (= Y334), G327 (= G335), M328 (≠ L336), T329 (≠ S337), P333 (= P341), V334 (= V342), D413 (= D415), K430 (= K432), K434 (≠ I436), Q439 (≠ N441)
5bsrA Crystal structure of 4-coumarate:coa ligase complexed with adenosine monophosphate and coenzyme a (see paper)
31% identity, 92% coverage: 42:531/532 of query aligns to 46:525/528 of 5bsrA
- active site: S181 (≠ T191), S201 (≠ N211), H229 (= H238), T328 (≠ S337), E329 (= E338), K433 (≠ I436), Q438 (≠ N441), K518 (= K524)
- binding adenosine monophosphate: A301 (≠ G311), G326 (= G335), T328 (≠ S337), D412 (= D415), K429 (= K432), K433 (≠ I436), Q438 (≠ N441)
- binding coenzyme a: L102 (= L99), P226 (= P235), H229 (= H238), Y231 (= Y240), F253 (≠ R263), K435 (≠ S438), G436 (= G439), F437 (= F440), F498 (≠ A504)
O24146 4-coumarate--CoA ligase 2; 4CL 2; Nt4CL-19; Nt4CL-2; 4-coumaroyl-CoA synthase 2; Caffeate--CoA ligase; Cinnamate--CoA ligase; Ferulate--CoA ligase; EC 6.2.1.12; EC 6.2.1.-; EC 6.2.1.-; EC 6.2.1.34 from Nicotiana tabacum (Common tobacco) (see paper)
31% identity, 92% coverage: 42:531/532 of query aligns to 54:533/542 of O24146
- S189 (≠ T191) binding
- S190 (≠ G192) binding
- G191 (= G193) binding
- T192 (= T194) binding
- T193 (= T195) binding ; mutation to A: Reduced activity against 4-coumarate.
- K197 (= K199) binding ; mutation to A: Reduced activity against 4-coumarate.
- H237 (= H238) mutation to A: Strongly reduced activity against 4-coumarate.
- Y239 (= Y240) binding ; binding ; binding ; mutation to A: Strongly reduced activity against 4-coumarate.; mutation to F: Reduced activity against 4-coumarate.
- S243 (≠ L246) binding ; binding ; binding
- K260 (≠ P262) binding
- A309 (≠ G311) binding ; binding ; binding
- Q331 (≠ E332) binding
- G332 (= G333) binding ; binding ; binding ; binding ; binding
- T336 (≠ S337) binding ; binding ; binding ; binding ; binding ; mutation to A: Strongly reduced activity against 4-coumarate.
- V341 (= V342) mutation to G: Reduced activity against 4-coumarate.; mutation Missing: Reduced activity against 4-coumarate, but acquired ability to use sinapate as substrate.
- M344 (≠ L345) binding ; binding ; binding ; mutation to A: Reduced activity against 4-coumarate.
- D420 (= D415) binding ; binding ; binding ; binding ; binding
- R435 (= R430) binding ; binding ; binding ; binding ; mutation to A: Strongly reduced activity against 4-coumarate.
- K437 (= K432) binding ; binding ; binding ; binding
- K441 (≠ I436) binding ; binding ; binding ; binding ; mutation to A: Abolished activity against 4-coumarate.
- K443 (≠ S438) binding ; mutation to A: Normal activity against 4-coumarate.
- G444 (= G439) binding
- Q446 (≠ N441) binding
- K526 (= K524) binding ; mutation to A: Abolished activity against 4-coumarate.
Q9S725 4-coumarate--CoA ligase 2; 4CL 2; 4-coumarate--CoA ligase isoform 2; At4CL2; 4-coumaroyl-CoA synthase 2; Caffeate--CoA ligase; EC 6.2.1.12; EC 6.2.1.- from Arabidopsis thaliana (Mouse-ear cress) (see 3 papers)
29% identity, 94% coverage: 33:531/532 of query aligns to 51:547/556 of Q9S725
- K211 (= K199) mutation to S: Drastically reduces the activity.
- M293 (≠ A281) mutation M->A,P: Affects the substrate specificity.
- K320 (≠ I308) mutation K->L,A: Affects the substrate specificity.
- E401 (= E382) mutation to Q: Slighlty reduces the substrate specificity.
- C403 (≠ A384) mutation to A: Significantly reduces the substrate specificity.
- R449 (= R430) mutation to Q: Drastically reduces the activity.
- K457 (≠ S438) mutation to S: Drastically reduces the activity.
- K540 (= K524) mutation to N: Abolishes the activity.
Q67W82 4-coumarate--CoA ligase 4; 4CL 4; Os4CL4; (E)-ferulate--CoA ligase; 4-coumaroyl-CoA synthase 4; Protein RESISTANCE TO ALUMINUM 1; EC 6.2.1.12; EC 6.2.1.34 from Oryza sativa subsp. japonica (Rice) (see paper)
28% identity, 95% coverage: 26:531/532 of query aligns to 40:542/559 of Q67W82
- G395 (= G381) mutation to R: In ral1; reduced lignin content and increased accumulation of 4-coumarate and ferulate in roots; confers increased tolerance to aluminum.
Q84P21 Peroxisomal OPC-8:0-CoA ligase 1; 4-coumarate--CoA ligase isoform 9; At4CL9; 4-coumarate--CoA ligase-like 5; EC 6.2.1.- from Arabidopsis thaliana (Mouse-ear cress) (see paper)
28% identity, 95% coverage: 24:530/532 of query aligns to 39:536/546 of Q84P21
- K530 (= K524) mutation to N: Lossed enzymatic activity.
5u95B Structure of the open conformation of 4-coumarate-coa ligase from nicotiana tabacum
31% identity, 92% coverage: 42:531/532 of query aligns to 46:522/527 of 5u95B
3ni2A Crystal structures and enzymatic mechanisms of a populus tomentosa 4- coumarate:coa ligase (see paper)
30% identity, 95% coverage: 26:532/532 of query aligns to 26:527/528 of 3ni2A
- active site: S182 (≠ T191), S202 (≠ N211), H230 (= H238), T329 (≠ S337), E330 (= E338), K434 (≠ I436), Q439 (≠ N441), K519 (= K524)
- binding 5'-O-{(S)-hydroxy[3-(4-hydroxyphenyl)propoxy]phosphoryl}adenosine: Y232 (= Y240), S236 (≠ L246), G302 (= G311), A303 (≠ T312), P304 (≠ A313), G325 (= G333), G327 (= G335), T329 (≠ S337), P333 (= P341), V334 (= V342), D413 (= D415), K430 (= K432), K434 (≠ I436), Q439 (≠ N441)
3a9vA Crystal structures and enzymatic mechanisms of a populus tomentosa 4- coumarate--coa ligase (see paper)
30% identity, 95% coverage: 26:532/532 of query aligns to 26:527/528 of 3a9vA
- active site: S182 (≠ T191), S202 (≠ N211), H230 (= H238), T329 (≠ S337), E330 (= E338), K434 (≠ I436), Q439 (≠ N441), K519 (= K524)
- binding adenosine monophosphate: H230 (= H238), G302 (= G311), A303 (≠ T312), P304 (≠ A313), Y326 (= Y334), G327 (= G335), M328 (≠ L336), T329 (≠ S337), D413 (= D415), K430 (= K432), K434 (≠ I436), Q439 (≠ N441)
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)
28% identity, 96% coverage: 21:532/532 of query aligns to 57:565/577 of Q08AH3
- Q139 (≠ L99) binding
- 221:229 (vs. 191:199, 67% identical) binding
- ESYGQT 359:364 (≠ EGYGLS 332:337) binding
- T364 (≠ S337) binding
- D446 (= D415) binding
- R461 (= R430) binding
- SGY 469:471 (≠ SGF 438:440) binding
- R472 (≠ N441) binding
- R501 (≠ S470) binding
- S513 (≠ D482) to L: in dbSNP:rs1133607
- K532 (≠ R499) binding
- YPR 540:542 (≠ LPK 507:509) binding
- K557 (= K524) binding
3eq6A Crystal structure of human acyl-coa synthetase medium-chain family member 2a (l64p mutation) in a ternary complex with products (see paper)
28% identity, 96% coverage: 21:532/532 of query aligns to 21:529/533 of 3eq6A
- active site: T185 (= T191), T328 (≠ S337), E329 (= E338), N431 (≠ I436), R436 (≠ N441), K521 (= K524)
- binding adenosine monophosphate: G302 (= G311), E303 (≠ T312), S304 (≠ A313), E323 (= E332), S324 (≠ G333), Y325 (= Y334), G326 (= G335), Q327 (≠ L336), T328 (≠ S337), D410 (= D415), F422 (≠ I427), R425 (= R430), R436 (≠ N441)
- binding Butyryl Coenzyme A: W229 (≠ H238), F255 (vs. gap), I277 (≠ T285), V301 (≠ G310), S433 (= S438), G434 (= G439), Y435 (≠ F440), P501 (≠ A504), Y502 (= Y505), Y504 (≠ L507), R506 (≠ K509)
2wd9A Crystal structure of human acyl-coa synthetase medium-chain family member 2a (l64p mutation) in complex with ibuprofen (see paper)
28% identity, 96% coverage: 21:532/532 of query aligns to 21:529/533 of 2wd9A
- active site: T185 (= T191), T328 (≠ S337), E329 (= E338), N431 (≠ I436), R436 (≠ N441), K521 (= K524)
- binding ibuprofen: I230 (= I239), L231 (≠ Y240), G326 (= G335), Q327 (≠ L336), T328 (≠ S337), R436 (≠ N441)
2vzeA Crystal structure of human acyl-coa synthetase medium-chain family member 2a (l64p mutation) in complex with amp (see paper)
28% identity, 96% coverage: 21:532/532 of query aligns to 21:529/533 of 2vzeA
- active site: T185 (= T191), T328 (≠ S337), E329 (= E338), N431 (≠ I436), R436 (≠ N441), K521 (= K524)
- binding adenosine monophosphate: W229 (≠ H238), G302 (= G311), E303 (≠ T312), S304 (≠ A313), E323 (= E332), Y325 (= Y334), G326 (= G335), Q327 (≠ L336), T328 (≠ S337), D410 (= D415), F422 (≠ I427), R425 (= R430), R436 (≠ N441)
3b7wA Crystal structure of human acyl-coa synthetase medium-chain family member 2a, with l64p mutation (see paper)
28% identity, 96% coverage: 21:532/532 of query aligns to 25:533/537 of 3b7wA
3c5eA Crystal structure of human acyl-coa synthetase medium-chain family member 2a (l64p mutation) in complex with atp (see paper)
28% identity, 96% coverage: 21:532/532 of query aligns to 24:532/536 of 3c5eA
- active site: T188 (= T191), T331 (≠ S337), E332 (= E338), N434 (≠ I436), R439 (≠ N441), K524 (= K524)
- binding adenosine-5'-triphosphate: T188 (= T191), S189 (≠ G192), G190 (= G193), T191 (= T194), S192 (≠ T195), G305 (= G311), E306 (≠ T312), S307 (≠ A313), G329 (= G335), Q330 (≠ L336), T331 (≠ S337), D413 (= D415), F425 (≠ I427), R428 (= R430), K524 (= K524)
- binding magnesium ion: M450 (≠ A452), H452 (= H454), V455 (≠ I457)
Query Sequence
>202759 SO3664 long-chain-fatty-acid--CoA ligase (NCBI ptt file)
MAYDQESQLELGKYSSLIDLIERTSQRFGDKTAYACLGKNSSFNEIERDSRYFAAYLQNN
TNLKPGDRIAIQLPNITQFVIAAYGALRAGLILVNTNPLYTERELIHQFNDSGAKALVVL
SDLLPTLAKVVATTPIELVISTHPLDLIDPQVQPKTGLKNVEFCHVLQQGALLPFTRFVP
TLSDLAALQYTGGTTGLSKGAMLTHGNMLANAAQVKSRIGSVISEGEDIFVAPLPIYHIY
AFMVNLVLYFECGGCSVLIPNPRDINGLIKTLAKYPFTGFAGLNTLFVALCHQPEFKALN
FSHLKITISGGTALTAAAANLWQQTTGNTISEGYGLSETSPVISLNAPGYQKIGTIGKPV
LGTEVKLLDESGNEVTQGTAGELAARGPQVMLGYWNNPQETANVMTPDGFFKTGDIAILN
EEGFHQIVDRKKDMIIVSGFNVYPNEVENVLASHPNIIECAVVGVKDDHSGEAVKAFIVL
KDDSQDHEKIKTAILNFCREQLTAYKLPKQIEFMSQLPKSTVGKILRRELKN
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