SitesBLAST
Comparing Ac3H11_1843 FitnessBrowser__acidovorax_3H11:Ac3H11_1843 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)
50% identity, 100% coverage: 1:558/560 of query aligns to 1:550/561 of P69451
- Y213 (= Y217) mutation to A: Loss of activity.
- T214 (= T218) mutation to A: 10% of wild-type activity.
- G216 (= G220) mutation to A: Decreases activity.
- T217 (= T221) mutation to A: Decreases activity.
- G219 (= G223) mutation to A: Decreases activity.
- K222 (= K226) mutation to A: Decreases activity.
- E361 (= E368) mutation to A: Loss of activity.
4gxqA Crystal structure of atp bound rpmatb-bxbclm chimera b1 (see paper)
35% identity, 63% coverage: 210:559/560 of query aligns to 155:499/506 of 4gxqA
- active site: T163 (= T218), N183 (≠ A238), H207 (= H269), T303 (≠ S367), E304 (= E368), I403 (≠ L467), N408 (= N472), A491 (≠ K551)
- binding adenosine-5'-triphosphate: T163 (= T218), S164 (≠ G219), G165 (= G220), T166 (= T221), T167 (= T222), H207 (= H269), S277 (≠ G341), A278 (≠ M342), P279 (≠ A343), E298 (= E362), M302 (= M366), T303 (≠ S367), D382 (= D446), R397 (= R461)
- binding carbonate ion: H207 (= H269), S277 (≠ G341), R299 (≠ G363), G301 (= G365)
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)
30% identity, 92% coverage: 46:559/560 of query aligns to 27:495/503 of P9WQ37
- K172 (= K226) mutation to A: Slight reduction of the fatty acyl-CoA ligase activity. Slight increase of susceptibility to proteolysis.
- R195 (≠ L256) mutation to A: Alteration of the strength of the membrane binding; when associated with A-9; A-17; A-197 and A-244.
- R197 (≠ K258) mutation to A: Alteration of the strength of the membrane binding; when associated with A-9; A-17; A-195 and A-244.
- V209 (≠ I270) 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 (= A272) mutation to G: Slight increase of the fatty acyl-CoA ligase activity. Reduced rate of proteolytic degradation.
- T214 (≠ L275) 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 (≠ P306) mutation to A: Alteration of the strength of the membrane binding; when associated with A-17; A-195; A-195 and A-197.
- A302 (≠ G365) 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 (≠ F441) 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 (= D446) 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 (= R461) mutation to A: Reduction of binding affinity for fatty acids.
- S404 (≠ V468) mutation to A: Slight reduction of the fatty acyl-CoA ligase activity. Enhanced affinity towards palmitic acid binding.
- G406 (= G470) mutation to L: No effect on the formation of acyl-adenylate intermediate. However, it shows very poor catalytic efficiency to form acyl-CoA.
- K487 (= K551) 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.
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)
30% identity, 91% coverage: 50:558/560 of query aligns to 61:542/559 of Q67W82
- G395 (= G412) mutation to R: In ral1; reduced lignin content and increased accumulation of 4-coumarate and ferulate in roots; confers increased tolerance to aluminum.
5bsmA Crystal structure of 4-coumarate:coa ligase complexed with magnesium and adenosine triphosphate (see paper)
30% identity, 91% coverage: 47:558/560 of query aligns to 44:526/530 of 5bsmA
- active site: S182 (≠ T218), S202 (≠ A238), H230 (= H269), T329 (≠ S367), E330 (= E368), K434 (≠ L467), Q439 (≠ N472), K519 (= K551)
- binding adenosine-5'-triphosphate: S182 (≠ T218), S183 (≠ G219), G184 (= G220), T185 (= T221), T186 (= T222), K190 (= K226), H230 (= H269), A302 (≠ G341), A303 (≠ M342), P304 (≠ A343), Y326 (≠ W364), G327 (= G365), M328 (= M366), T329 (≠ S367), D413 (= D446), I425 (= I458), R428 (= R461), K519 (= K551)
5bsvA Crystal structure of 4-coumarate:coa ligase complexed with feruloyl adenylate (see paper)
30% identity, 91% coverage: 47:558/560 of query aligns to 44:526/529 of 5bsvA
- active site: S182 (≠ T218), S202 (≠ A238), H230 (= H269), T329 (≠ S367), E330 (= E368), K434 (≠ L467), Q439 (≠ N472), K519 (= K551)
- binding 5'-O-[(R)-hydroxy{[(2E)-3-(5-methoxy-4-oxocyclohexa-1,5-dien-1-yl)prop-2-enoyl]oxy}phosphoryl]adenosine: H230 (= H269), Y232 (≠ F271), S236 (≠ L275), A302 (≠ G341), A303 (≠ M342), P304 (≠ A343), G325 (= G363), G327 (= G365), M328 (= M366), T329 (≠ S367), P333 (vs. gap), V334 (vs. gap), D413 (= D446), K430 (= K463), K434 (≠ L467), Q439 (≠ N472)
5bsuA Crystal structure of 4-coumarate:coa ligase complexed with caffeoyl adenylate (see paper)
30% identity, 91% coverage: 47:558/560 of query aligns to 44:526/529 of 5bsuA
- active site: S182 (≠ T218), S202 (≠ A238), H230 (= H269), T329 (≠ S367), E330 (= E368), K434 (≠ L467), Q439 (≠ N472), K519 (= K551)
- binding 5'-O-[(R)-{[(2E)-3-(3,4-dioxocyclohexa-1,5-dien-1-yl)prop-2-enoyl]oxy}(hydroxy)phosphoryl]adenosine: H230 (= H269), Y232 (≠ F271), S236 (≠ L275), M299 (≠ Q338), A302 (≠ G341), A303 (≠ M342), P304 (≠ A343), G325 (= G363), G327 (= G365), M328 (= M366), T329 (≠ S367), P333 (vs. gap), D413 (= D446), K430 (= K463), K434 (≠ L467), Q439 (≠ N472)
5bstA Crystal structure of 4-coumarate:coa ligase complexed with coumaroyl adenylate (see paper)
30% identity, 91% coverage: 47:558/560 of query aligns to 44:526/529 of 5bstA
- active site: S182 (≠ T218), S202 (≠ A238), H230 (= H269), T329 (≠ S367), E330 (= E368), K434 (≠ L467), Q439 (≠ N472), K519 (= K551)
- binding 5'-O-[(R)-hydroxy{[(2E)-3-(4-oxocyclohexa-1,5-dien-1-yl)prop-2-enoyl]oxy}phosphoryl]adenosine: H230 (= H269), Y232 (≠ F271), S236 (≠ L275), A302 (≠ G341), A303 (≠ M342), P304 (≠ A343), G325 (= G363), Y326 (≠ W364), G327 (= G365), M328 (= M366), T329 (≠ S367), P333 (vs. gap), V334 (vs. gap), D413 (= D446), K430 (= K463), K434 (≠ L467), Q439 (≠ N472)
5bsrA Crystal structure of 4-coumarate:coa ligase complexed with adenosine monophosphate and coenzyme a (see paper)
30% identity, 91% coverage: 47:558/560 of query aligns to 43:525/528 of 5bsrA
- active site: S181 (≠ T218), S201 (≠ A238), H229 (= H269), T328 (≠ S367), E329 (= E368), K433 (≠ L467), Q438 (≠ N472), K518 (= K551)
- binding adenosine monophosphate: A301 (≠ G341), G326 (= G365), T328 (≠ S367), D412 (= D446), K429 (= K463), K433 (≠ L467), Q438 (≠ N472)
- binding coenzyme a: L102 (= L106), P226 (= P266), H229 (= H269), Y231 (≠ F271), F253 (≠ R293), K435 (≠ S469), G436 (= G470), F437 (= F471), F498 (≠ G531)
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)
30% identity, 91% coverage: 47:558/560 of query aligns to 51:533/542 of O24146
- S189 (≠ T218) binding
- S190 (≠ G219) binding
- G191 (= G220) binding
- T192 (= T221) binding
- T193 (= T222) binding ; mutation to A: Reduced activity against 4-coumarate.
- K197 (= K226) binding ; mutation to A: Reduced activity against 4-coumarate.
- H237 (= H269) mutation to A: Strongly reduced activity against 4-coumarate.
- Y239 (≠ F271) binding ; binding ; binding ; mutation to A: Strongly reduced activity against 4-coumarate.; mutation to F: Reduced activity against 4-coumarate.
- S243 (≠ L275) binding ; binding ; binding
- K260 (≠ P292) binding
- A309 (≠ G341) binding ; binding ; binding
- Q331 (≠ E362) binding
- G332 (= G363) binding ; binding ; binding ; binding ; binding
- T336 (≠ S367) binding ; binding ; binding ; binding ; binding ; mutation to A: Strongly reduced activity against 4-coumarate.
- V341 (vs. gap) mutation to G: Reduced activity against 4-coumarate.; mutation Missing: Reduced activity against 4-coumarate, but acquired ability to use sinapate as substrate.
- M344 (vs. gap) binding ; binding ; binding ; mutation to A: Reduced activity against 4-coumarate.
- D420 (= D446) binding ; binding ; binding ; binding ; binding
- R435 (= R461) binding ; binding ; binding ; binding ; mutation to A: Strongly reduced activity against 4-coumarate.
- K437 (= K463) binding ; binding ; binding ; binding
- K441 (≠ L467) binding ; binding ; binding ; binding ; mutation to A: Abolished activity against 4-coumarate.
- K443 (≠ S469) binding ; mutation to A: Normal activity against 4-coumarate.
- G444 (= G470) binding
- Q446 (≠ N472) binding
- K526 (= K551) binding ; mutation to A: Abolished activity against 4-coumarate.
3r44A Mycobacterium tuberculosis fatty acyl coa synthetase (see paper)
29% identity, 92% coverage: 46:559/560 of query aligns to 30:495/502 of 3r44A
Sites not aligning to the query:
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)
27% identity, 91% coverage: 50:558/560 of query aligns to 65:547/556 of Q9S725
- K211 (= K226) mutation to S: Drastically reduces the activity.
- M293 (≠ P311) mutation M->A,P: Affects the substrate specificity.
- K320 (≠ Q338) mutation K->L,A: Affects the substrate specificity.
- E401 (= E413) mutation to Q: Slighlty reduces the substrate specificity.
- C403 (= C415) mutation to A: Significantly reduces the substrate specificity.
- R449 (= R461) mutation to Q: Drastically reduces the activity.
- K457 (≠ S469) mutation to S: Drastically reduces the activity.
- K540 (= K551) mutation to N: Abolishes the activity.
6e97B Crystal structure of the aryl acid adenylating enzyme fscc from fuscachelin nrps in complex with dhb-adenylate
31% identity, 96% coverage: 21:559/560 of query aligns to 12:530/537 of 6e97B
- active site: S190 (≠ T218), S210 (≠ T239), H234 (= H269), A336 (≠ S367), E337 (= E368), N437 (≠ L467), K442 (≠ N472), K522 (= K551)
- binding 5'-O-[(S)-[(2,3-dihydroxybenzene-1-carbonyl)oxy](hydroxy)phosphoryl]adenosine: H234 (= H269), N235 (≠ I270), F236 (= F271), S240 (≠ L275), G310 (= G341), A311 (≠ M342), K312 (≠ A343), V332 (≠ G363), F333 (≠ W364), G334 (= G365), M335 (= M366), A336 (≠ S367), D416 (= D446), K433 (= K463), K442 (≠ N472)
5u95B Structure of the open conformation of 4-coumarate-coa ligase from nicotiana tabacum
30% identity, 91% coverage: 47:558/560 of query aligns to 43:522/527 of 5u95B
3ni2A Crystal structures and enzymatic mechanisms of a populus tomentosa 4- coumarate:coa ligase (see paper)
27% identity, 91% coverage: 50:559/560 of query aligns to 47:527/528 of 3ni2A
- active site: S182 (≠ T218), S202 (≠ A238), H230 (= H269), T329 (≠ S367), E330 (= E368), K434 (≠ L467), Q439 (≠ N472), K519 (= K551)
- binding 5'-O-{(S)-hydroxy[3-(4-hydroxyphenyl)propoxy]phosphoryl}adenosine: Y232 (≠ F271), S236 (≠ T274), G302 (= G341), A303 (≠ M342), P304 (≠ A343), G325 (= G363), G327 (= G365), T329 (≠ S367), P333 (= P377), V334 (= V378), D413 (= D446), K430 (= K463), K434 (≠ L467), Q439 (≠ N472)
3a9vA Crystal structures and enzymatic mechanisms of a populus tomentosa 4- coumarate--coa ligase (see paper)
27% identity, 91% coverage: 50:559/560 of query aligns to 47:527/528 of 3a9vA
- active site: S182 (≠ T218), S202 (≠ A238), H230 (= H269), T329 (≠ S367), E330 (= E368), K434 (≠ L467), Q439 (≠ N472), K519 (= K551)
- binding adenosine monophosphate: H230 (= H269), G302 (= G341), A303 (≠ M342), P304 (≠ A343), Y326 (≠ W364), G327 (= G365), M328 (= M366), T329 (≠ S367), D413 (= D446), K430 (= K463), K434 (≠ L467), Q439 (≠ N472)
5wm3A Crystal structure of cahj in complex with salicyl adenylate (see paper)
29% identity, 96% coverage: 23:559/560 of query aligns to 27:532/537 of 5wm3A
- active site: S193 (≠ T218), N213 (≠ T239), H237 (= H269), A336 (≠ S367), E337 (= E368), N437 (≠ L467), K442 (≠ N472), K524 (= K551)
- binding 9-(5-O-{(S)-hydroxy[(2-hydroxybenzene-1-carbonyl)oxy]phosphoryl}-alpha-L-lyxofuranosyl)-9H-purin-6-amine: N238 (≠ I270), F239 (= F271), G310 (= G341), S311 (≠ M342), K312 (≠ A343), V332 (≠ G363), F333 (≠ W364), G334 (= G365), M335 (= M366), A336 (≠ S367), D416 (= D446), K433 (= K463), K442 (≠ N472)
- binding magnesium ion: S301 (= S332), L303 (= L334), G326 (= G357)
5wm6A Crystal structure of cahj in complex with benzoyl adenylate (see paper)
29% identity, 96% coverage: 23:559/560 of query aligns to 27:532/535 of 5wm6A
- active site: S193 (≠ T218), N213 (≠ T239), H237 (= H269), A336 (≠ S367), E337 (= E368), N437 (≠ L467), K442 (≠ N472), K524 (= K551)
- binding magnesium ion: S301 (= S332), L303 (= L334), G326 (= G357)
- binding 5'-O-[(R)-(benzoyloxy)(hydroxy)phosphoryl]adenosine: F239 (= F271), G310 (= G341), S311 (≠ M342), K312 (≠ A343), V332 (≠ G363), F333 (≠ W364), G334 (= G365), M335 (= M366), A336 (≠ S367), D416 (= D446), K433 (= K463), K442 (≠ N472)
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, 90% coverage: 54:555/560 of query aligns to 40:504/514 of Q9SMT7
- TSGTT 170:174 (≠ TGGTT 218:222) binding
- H214 (= H269) binding ; mutation to A: Abolished activity.
- S289 (≠ V336) binding ; mutation to A: Abolished activity.
- SAS 289:291 (≠ VSQ 336:338) binding
- EA 310:311 (≠ EG 362:363) binding
- M314 (= M366) binding
- T315 (≠ S367) binding
- H319 (≠ A371) binding ; mutation to A: Abolished activity.
- D394 (= D446) binding
- R409 (= R461) binding ; mutation to A: Abolished activity.
- K500 (= K551) binding ; binding ; mutation to A: Abolished activity.
5wm2A Crystal structure of cahj in complex with salicylic acid and amp (see paper)
29% identity, 96% coverage: 23:559/560 of query aligns to 27:532/536 of 5wm2A
- active site: S193 (≠ T218), N213 (≠ T239), H237 (= H269), A336 (≠ S367), E337 (= E368), N437 (≠ L467), K442 (≠ N472), K524 (= K551)
- binding adenosine monophosphate: G310 (= G341), S311 (≠ M342), K312 (≠ A343), V332 (≠ G363), F333 (≠ W364), G334 (= G365), M335 (= M366), A336 (≠ S367), E337 (= E368), D416 (= D446), V428 (≠ I458), K433 (= K463), K442 (≠ N472)
Query Sequence
>Ac3H11_1843 FitnessBrowser__acidovorax_3H11:Ac3H11_1843
MEKIWLKSYPPGVPHDVKPEQYRSVAHLLEESFRKHAKSPFSVCMDQWMTYGELERRSAA
LGAYLQSLGLEPGARVAIMLPNIPQFGVTMAAVLRAGYTCVNVNPLYTARELEHQLKDSG
ATAIVILENFAHTLADVIDHTAVKHVVMASMGDLLGFWFGQWITFAVRHLAKMVPAYDLP
LTGGRKVVTFKKALSVGEHKSLAPSQATLDSIAFLQYTGGTTGLSKGAVLTHRNIVAATL
QAEAWFTPALSKVGDLSKANSIAALPLYHIFALTLCLLAIRQGSSLTLIPNPRDIPKFVA
ELKKRPFHMLPAVNTLFNALLQNPQFKTLDFSHLCVSQAGGMAASEGTAKQWQKVTGSTM
IEGWGMSETCAIGTNNPVISTTFSGNIGLPLPGIDIAIKDDDGNSLPQGESGEICIRGPN
VMVGYYNQPEENAKAFTPDGFMRTGDIGIMDPQGYTRIIDRKKDMILVSGFNVFPNELEQ
VISLCPGVVECAAIGVPDEKQGEAIKVFIIKNDPALTEDEVANYCHQNLTGYKRPKYIEF
RDELPKSNVGKILRRELRKA
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