SitesBLAST
Comparing H281DRAFT_05129 FitnessBrowser__Burk376:H281DRAFT_05129 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)
55% identity, 92% coverage: 48:606/610 of query aligns to 4:556/561 of P69451
- Y213 (= Y259) mutation to A: Loss of activity.
- T214 (= T260) mutation to A: 10% of wild-type activity.
- G216 (= G262) mutation to A: Decreases activity.
- T217 (= T263) mutation to A: Decreases activity.
- G219 (= G265) mutation to A: Decreases activity.
- K222 (= K268) mutation to A: Decreases activity.
- E361 (= E407) mutation to A: Loss of activity.
P9WQ37 Long-chain-fatty-acid--CoA ligase FadD13; Fatty acyl-CoA ligase; FACL; FACL13; Fatty acyl-CoA synthetase; ACS; FACS; Very-long-chain fatty-acyl-CoA synthetase; ACSVL; EC 6.2.1.3 from Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv) (see 4 papers)
31% identity, 85% coverage: 85:602/610 of query aligns to 20:496/503 of P9WQ37
- K172 (= K268) mutation to A: Slight reduction of the fatty acyl-CoA ligase activity. Slight increase of susceptibility to proteolysis.
- R195 (≠ G294) mutation to A: Alteration of the strength of the membrane binding; when associated with A-9; A-17; A-197 and A-244.
- R197 (≠ V296) mutation to A: Alteration of the strength of the membrane binding; when associated with A-9; A-17; A-195 and A-244.
- V209 (≠ I308) mutation to D: Strong reduction of the fatty acyl-CoA ligase activity. No significant change in the total expression level, however the cytoplasmic expression is reduced. Slight increase of susceptibility to proteolysis.
- A211 (≠ S310) mutation to G: Slight increase of the fatty acyl-CoA ligase activity. Reduced rate of proteolytic degradation.
- T214 (≠ V313) mutation to W: Shows a marked decrease in the activity with lauric and palmitic acid (C12 and C16 fatty acid) with a simultaneous increase in the activity with caprylic acid (C8 fatty acid).
- R244 (≠ K345) mutation to A: Alteration of the strength of the membrane binding; when associated with A-17; A-195; A-195 and A-197.
- A302 (≠ G404) mutation to G: Slight increase of the fatty acyl-CoA ligase activity. Reduced rate of proteolytic degradation.; mutation to W: Does not show activity with small, medium or long acyl chains.
- W377 (= W483) mutation to A: Strong reduction of the fatty acyl-CoA ligase activity. Enhanced affinity towards palmitic acid binding. No significant change in the total expression level, however the cytoplasmic expression is low. Slight increase of susceptibility to proteolysis.
- D382 (= D488) mutation to A: Strong reduction of the fatty acyl-CoA ligase activity. No significant change in the total expression level, however the cytoplasmic expression is reduced.
- R397 (= R503) mutation to A: Reduction of binding affinity for fatty acids.
- S404 (≠ V510) mutation to A: Slight reduction of the fatty acyl-CoA ligase activity. Enhanced affinity towards palmitic acid binding.
- G406 (= G512) mutation to L: No effect on the formation of acyl-adenylate intermediate. However, it shows very poor catalytic efficiency to form acyl-CoA.
- K487 (= K593) mutation to A: Strong reduction of the fatty acyl-CoA ligase activity. Reduction of binding affinity for ATP.
Sites not aligning to the query:
- 9 R→A: Alteration of the strength of the membrane binding; when associated with A-9; A-195; A-197 and A-244.
- 17 R→A: Alteration of the strength of the membrane binding; when associated with A-9; A-17; A-197 and A-244.
3r44A Mycobacterium tuberculosis fatty acyl coa synthetase (see paper)
31% identity, 85% coverage: 85:602/610 of query aligns to 23:496/502 of 3r44A
Sites not aligning to the query:
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)
30% identity, 85% coverage: 81:599/610 of query aligns to 44:536/546 of Q84P21
- K530 (= K593) mutation to N: Lossed enzymatic 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)
29% identity, 84% coverage: 90:600/610 of query aligns to 57:542/559 of Q67W82
- G395 (= G454) mutation to R: In ral1; reduced lignin content and increased accumulation of 4-coumarate and ferulate in roots; confers increased tolerance to aluminum.
Q4WR83 Acyl-CoA ligase sidI; Siderophore biosynthesis protein I; EC 6.2.1.- from Aspergillus fumigatus (strain ATCC MYA-4609 / CBS 101355 / FGSC A1100 / Af293) (Neosartorya fumigata) (see paper)
29% identity, 85% coverage: 82:600/610 of query aligns to 54:570/590 of Q4WR83
Sites not aligning to the query:
- 6:14 PTS2-type peroxisomal targeting signal
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)
26% identity, 86% coverage: 75:600/610 of query aligns to 44:547/556 of Q9S725
- K211 (= K268) mutation to S: Drastically reduces the activity.
- M293 (≠ T350) mutation M->A,P: Affects the substrate specificity.
- K320 (≠ M377) mutation K->L,A: Affects the substrate specificity.
- E401 (= E455) mutation to Q: Slighlty reduces the substrate specificity.
- C403 (= C457) mutation to A: Significantly reduces the substrate specificity.
- R449 (= R503) mutation to Q: Drastically reduces the activity.
- K457 (≠ S511) mutation to S: Drastically reduces the activity.
- K540 (= K593) mutation to N: Abolishes the activity.
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)
29% identity, 86% coverage: 75:600/610 of query aligns to 33:533/542 of O24146
- S189 (≠ T260) binding
- S190 (≠ G261) binding
- G191 (= G262) binding
- T192 (= T263) binding
- T193 (= T264) binding ; mutation to A: Reduced activity against 4-coumarate.
- K197 (= K268) binding ; mutation to A: Reduced activity against 4-coumarate.
- H237 (= H307) mutation to A: Strongly reduced activity against 4-coumarate.
- Y239 (= Y309) binding ; binding ; binding ; mutation to A: Strongly reduced activity against 4-coumarate.; mutation to F: Reduced activity against 4-coumarate.
- S243 (≠ A315) binding ; binding ; binding
- K260 (≠ P331) binding
- A309 (≠ G380) binding ; binding ; binding
- Q331 (≠ E401) binding
- G332 (= G402) binding ; binding ; binding ; binding ; binding
- T336 (= T406) binding ; binding ; binding ; binding ; binding ; mutation to A: Strongly reduced activity against 4-coumarate.
- V341 (≠ I411) mutation to G: Reduced activity against 4-coumarate.; mutation Missing: Reduced activity against 4-coumarate, but acquired ability to use sinapate as substrate.
- M344 (= M414) binding ; binding ; binding ; mutation to A: Reduced activity against 4-coumarate.
- D420 (= D488) binding ; binding ; binding ; binding ; binding
- R435 (= R503) binding ; binding ; binding ; binding ; mutation to A: Strongly reduced activity against 4-coumarate.
- K437 (= K505) binding ; binding ; binding ; binding
- K441 (≠ L509) binding ; binding ; binding ; binding ; mutation to A: Abolished activity against 4-coumarate.
- K443 (≠ S511) binding ; mutation to A: Normal activity against 4-coumarate.
- G444 (= G512) binding
- Q446 (≠ N514) binding
- K526 (= K593) binding ; mutation to A: Abolished activity against 4-coumarate.
5bsmA Crystal structure of 4-coumarate:coa ligase complexed with magnesium and adenosine triphosphate (see paper)
29% identity, 86% coverage: 75:600/610 of query aligns to 26:526/530 of 5bsmA
- active site: S182 (≠ T260), S202 (≠ N280), H230 (= H307), T329 (= T406), E330 (= E407), K434 (≠ L509), Q439 (≠ N514), K519 (= K593)
- binding adenosine-5'-triphosphate: S182 (≠ T260), S183 (≠ G261), G184 (= G262), T185 (= T263), T186 (= T264), K190 (= K268), H230 (= H307), A302 (≠ G380), A303 (≠ M381), P304 (≠ A382), Y326 (= Y403), G327 (= G404), M328 (≠ L405), T329 (= T406), D413 (= D488), I425 (≠ L500), R428 (= R503), K519 (= K593)
5bsrA Crystal structure of 4-coumarate:coa ligase complexed with adenosine monophosphate and coenzyme a (see paper)
29% identity, 86% coverage: 75:600/610 of query aligns to 25:525/528 of 5bsrA
- active site: S181 (≠ T260), S201 (≠ N280), H229 (= H307), T328 (= T406), E329 (= E407), K433 (≠ L509), Q438 (≠ N514), K518 (= K593)
- binding adenosine monophosphate: A301 (≠ G380), G326 (= G404), T328 (= T406), D412 (= D488), K429 (= K505), K433 (≠ L509), Q438 (≠ N514)
- binding coenzyme a: L102 (= L150), P226 (= P304), H229 (= H307), Y231 (= Y309), F253 (≠ R332), K435 (≠ S511), G436 (= G512), F437 (= F513), F498 (≠ G573)
5bsvA Crystal structure of 4-coumarate:coa ligase complexed with feruloyl adenylate (see paper)
29% identity, 86% coverage: 75:600/610 of query aligns to 26:526/529 of 5bsvA
- active site: S182 (≠ T260), S202 (≠ N280), H230 (= H307), T329 (= T406), E330 (= E407), K434 (≠ L509), Q439 (≠ N514), K519 (= K593)
- binding 5'-O-[(R)-hydroxy{[(2E)-3-(5-methoxy-4-oxocyclohexa-1,5-dien-1-yl)prop-2-enoyl]oxy}phosphoryl]adenosine: H230 (= H307), Y232 (= Y309), S236 (≠ A315), A302 (≠ G380), A303 (≠ M381), P304 (≠ A382), G325 (= G402), G327 (= G404), M328 (≠ L405), T329 (= T406), P333 (= P410), V334 (≠ I411), D413 (= D488), K430 (= K505), K434 (≠ L509), Q439 (≠ N514)
5bsuA Crystal structure of 4-coumarate:coa ligase complexed with caffeoyl adenylate (see paper)
29% identity, 86% coverage: 75:600/610 of query aligns to 26:526/529 of 5bsuA
- active site: S182 (≠ T260), S202 (≠ N280), H230 (= H307), T329 (= T406), E330 (= E407), K434 (≠ L509), Q439 (≠ N514), K519 (= K593)
- binding 5'-O-[(R)-{[(2E)-3-(3,4-dioxocyclohexa-1,5-dien-1-yl)prop-2-enoyl]oxy}(hydroxy)phosphoryl]adenosine: H230 (= H307), Y232 (= Y309), S236 (≠ A315), M299 (= M377), A302 (≠ G380), A303 (≠ M381), P304 (≠ A382), G325 (= G402), G327 (= G404), M328 (≠ L405), T329 (= T406), P333 (= P410), D413 (= D488), K430 (= K505), K434 (≠ L509), Q439 (≠ N514)
5bstA Crystal structure of 4-coumarate:coa ligase complexed with coumaroyl adenylate (see paper)
29% identity, 86% coverage: 75:600/610 of query aligns to 26:526/529 of 5bstA
- active site: S182 (≠ T260), S202 (≠ N280), H230 (= H307), T329 (= T406), E330 (= E407), K434 (≠ L509), Q439 (≠ N514), K519 (= K593)
- binding 5'-O-[(R)-hydroxy{[(2E)-3-(4-oxocyclohexa-1,5-dien-1-yl)prop-2-enoyl]oxy}phosphoryl]adenosine: H230 (= H307), Y232 (= Y309), S236 (≠ A315), A302 (≠ G380), A303 (≠ M381), P304 (≠ A382), G325 (= G402), Y326 (= Y403), G327 (= G404), M328 (≠ L405), T329 (= T406), P333 (= P410), V334 (≠ I411), D413 (= D488), K430 (= K505), K434 (≠ L509), Q439 (≠ N514)
3ni2A Crystal structures and enzymatic mechanisms of a populus tomentosa 4- coumarate:coa ligase (see paper)
29% identity, 84% coverage: 90:602/610 of query aligns to 43:528/528 of 3ni2A
- active site: S182 (≠ T260), S202 (≠ N280), H230 (= H307), T329 (= T406), E330 (= E407), K434 (≠ L509), Q439 (≠ N514), K519 (= K593)
- binding 5'-O-{(S)-hydroxy[3-(4-hydroxyphenyl)propoxy]phosphoryl}adenosine: Y232 (= Y309), S236 (≠ A315), G302 (= G380), A303 (≠ M381), P304 (≠ A382), G325 (= G402), G327 (= G404), T329 (= T406), P333 (= P410), V334 (≠ I411), D413 (= D488), K430 (= K505), K434 (≠ L509), Q439 (≠ N514)
3a9vA Crystal structures and enzymatic mechanisms of a populus tomentosa 4- coumarate--coa ligase (see paper)
29% identity, 84% coverage: 90:602/610 of query aligns to 43:528/528 of 3a9vA
- active site: S182 (≠ T260), S202 (≠ N280), H230 (= H307), T329 (= T406), E330 (= E407), K434 (≠ L509), Q439 (≠ N514), K519 (= K593)
- binding adenosine monophosphate: H230 (= H307), G302 (= G380), A303 (≠ M381), P304 (≠ A382), Y326 (= Y403), G327 (= G404), M328 (≠ L405), T329 (= T406), D413 (= D488), K430 (= K505), K434 (≠ L509), Q439 (≠ N514)
4gxqA Crystal structure of atp bound rpmatb-bxbclm chimera b1 (see paper)
30% identity, 84% coverage: 88:601/610 of query aligns to 24:499/506 of 4gxqA
- active site: T163 (= T260), N183 (= N280), H207 (= H307), T303 (= T406), E304 (= E407), I403 (≠ L509), N408 (= N514), A491 (≠ K593)
- binding adenosine-5'-triphosphate: T163 (= T260), S164 (≠ G261), G165 (= G262), T166 (= T263), T167 (= T264), H207 (= H307), S277 (≠ G380), A278 (≠ M381), P279 (≠ A382), E298 (= E401), M302 (≠ L405), T303 (= T406), D382 (= D488), R397 (= R503)
- binding carbonate ion: H207 (= H307), S277 (≠ G380), R299 (≠ G402), G301 (= G404)
5u95B Structure of the open conformation of 4-coumarate-coa ligase from nicotiana tabacum
29% identity, 86% coverage: 75:600/610 of query aligns to 25:522/527 of 5u95B
Q17577 Acyl-CoA synthetase 7; EC 6.2.1.- from Caenorhabditis elegans (see paper)
27% identity, 86% coverage: 82:608/610 of query aligns to 32:537/540 of Q17577
- SS 186:187 (≠ TG 260:261) mutation to AA: Loss of catalytic activity; when associated with A-339.
- E339 (= E407) mutation to A: Severe loss of catalytic activity. Loss of catalytic activity; when associated with 186-A-A-187.
Q9SMT7 Oxalate--CoA ligase; 4-coumarate--CoA ligase isoform 8; At4CL8; 4-coumarate--CoA ligase-like 10; Acyl-activating enzyme 3; Adenosine monophosphate binding protein 3; AtMPBP3; Oxalyl-CoA synthetase; EC 6.2.1.8 from Arabidopsis thaliana (Mouse-ear cress) (see paper)
28% identity, 86% coverage: 83:606/610 of query aligns to 21:513/514 of Q9SMT7
- TSGTT 170:174 (≠ TGGTT 260:264) binding
- H214 (= H307) binding ; mutation to A: Abolished activity.
- S289 (≠ G380) binding ; mutation to A: Abolished activity.
- SAS 289:291 (≠ GMA 380:382) binding
- EA 310:311 (≠ EG 401:402) binding
- M314 (≠ L405) binding
- T315 (= T406) binding
- H319 (≠ P410) binding ; mutation to A: Abolished activity.
- D394 (= D488) binding
- R409 (= R503) binding ; mutation to A: Abolished activity.
- K500 (= K593) binding ; binding ; mutation to A: Abolished activity.
5ie3A Crystal structure of a plant enzyme (see paper)
29% identity, 84% coverage: 83:597/610 of query aligns to 21:497/504 of 5ie3A
- active site: T163 (= T260), S183 (≠ N280), H207 (= H307), T308 (= T406), E309 (= E407), N408 (≠ L509), K413 (≠ N514), K493 (= K593)
- binding adenosine monophosphate: S164 (≠ G261), S282 (≠ G380), A283 (≠ M381), S284 (≠ A382), Y305 (= Y403), A306 (≠ G404), M307 (≠ L405), T308 (= T406), D387 (= D488), L399 (= L500), R402 (= R503), K493 (= K593)
- binding oxalic acid: V208 (≠ I308), S282 (≠ G380), A306 (≠ G404), M307 (≠ L405), H312 (≠ P410), K493 (= K593)
Query Sequence
>H281DRAFT_05129 FitnessBrowser__Burk376:H281DRAFT_05129
MTQPTQASLSPAAANQATGPAHADAAATPHAMQDATGHTNHAPNTDGIWYASYPADVPHE
IDVGKYESVVHFFDECIAQFRERVAYVSVGASMTYGELGRKATAFAAYLQSIGVKPGARV
AIMLPNTFQYPVSLFGVLKAGAVVVNVNPLYTVRELAHQLKDSGAQTIIVFENFAKTVQD
ALPGSKVQNVIVTGLGDLLADGLNLKGRVLNFMLRHVKKMVPAYSLPNAVPLLKALAIGY
TRPLTPVRPTHHDIAFLQYTGGTTGVAKGAMLTHRNIIANLLQAKAWAEGQLSGEVETVL
TPLPLYHIYSLTVNALIFMGLGGRNILIANPRDMKRVMMIIRHEKFTGMTAVNTLYNAFL
ENEEFCKRDFSDLKLAMAGGMATQRSVAERFKAVTGKPIIEGYGLTECSPIVSMNPVDIS
NLRDFEGSIGLPAPSTQVRFRKDDGSWANIGEAGELCVKGPQVMKGYWNRPEETAKVIDD
EGWLATGDIGVMDSRGFIRLIDRKKDMILVSGFNVYPNEIEDVIAAHPDVREVAAIGVPD
DAQGERVKVFIVKRNPSLTAEQVIAHCRKNLTGYKVPKVVEFRDELPQTNVGKILRRALR
DEELAKQKTA
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