SitesBLAST
Comparing WP_011445127.1 NCBI__GCF_000013325.1:WP_011445127.1 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)
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)
28% identity, 93% coverage: 11:504/530 of query aligns to 38:542/590 of Q4WR83
Sites not aligning to the query:
- 6:14 PTS2-type peroxisomal targeting signal
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, 93% coverage: 19:511/530 of query aligns to 39:522/546 of Q84P21
Sites not aligning to the query:
- 530 K→N: Lossed enzymatic 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)
28% identity, 98% coverage: 11:529/530 of query aligns to 3:496/503 of P9WQ37
- R9 (≠ L17) mutation to A: Alteration of the strength of the membrane binding; when associated with A-9; A-195; A-197 and A-244.
- R17 (≠ E25) mutation to A: Alteration of the strength of the membrane binding; when associated with A-9; A-17; A-197 and A-244.
- K172 (= K198) mutation to A: Slight reduction of the fatty acyl-CoA ligase activity. Slight increase of susceptibility to proteolysis.
- R195 (= R216) mutation to A: Alteration of the strength of the membrane binding; when associated with A-9; A-17; A-197 and A-244.
- R197 (= R218) mutation to A: Alteration of the strength of the membrane binding; when associated with A-9; A-17; A-195 and A-244.
- V209 (≠ I236) 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 (≠ S238) mutation to G: Slight increase of the fatty acyl-CoA ligase activity. Reduced rate of proteolytic degradation.
- T214 (≠ P241) 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 (≠ A271) mutation to A: Alteration of the strength of the membrane binding; when associated with A-17; A-195; A-195 and A-197.
- A302 (≠ G329) 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 (= W408) 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 (= D413) 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 (= R428) mutation to A: Reduction of binding affinity for fatty acids.
- S404 (≠ V435) mutation to A: Slight reduction of the fatty acyl-CoA ligase activity. Enhanced affinity towards palmitic acid binding.
- G406 (= G437) mutation to L: No effect on the formation of acyl-adenylate intermediate. However, it shows very poor catalytic efficiency to form acyl-CoA.
- K487 (= K520) mutation to A: Strong reduction of the fatty acyl-CoA ligase activity. Reduction of binding affinity for ATP.
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, 94% coverage: 33:530/530 of query aligns to 57:545/559 of Q67W82
- G395 (= G379) mutation to R: In ral1; reduced lignin content and increased accumulation of 4-coumarate and ferulate in roots; confers increased tolerance to aluminum.
6e8oA Crystal structure of aryl acid adenylating enzyme fscc from fuscachelin nrps in complex with amp
31% identity, 98% coverage: 11:530/530 of query aligns to 23:531/536 of 6e8oA
- active site: S190 (≠ T190), S210 (≠ G210), H234 (= H235), A336 (≠ T331), E337 (= E332), N437 (≠ K434), K442 (≠ N439), K521 (= K520)
- binding adenosine monophosphate: H234 (= H235), G310 (≠ Y302), A311 (≠ L303), K312 (≠ F304), V332 (≠ A327), F333 (≠ C328), G334 (= G329), M335 (= M330), A336 (≠ T331), D416 (= D413), V428 (≠ F425), K442 (≠ N439)
5bsmA Crystal structure of 4-coumarate:coa ligase complexed with magnesium and adenosine triphosphate (see paper)
29% identity, 93% coverage: 37:530/530 of query aligns to 47:529/530 of 5bsmA
- active site: S182 (≠ T190), S202 (≠ G210), H230 (= H235), T329 (= T331), E330 (= E332), K434 (= K434), Q439 (≠ N439), K519 (= K520)
- binding adenosine-5'-triphosphate: S182 (≠ T190), S183 (= S191), G184 (= G192), T185 (= T193), T186 (= T194), K190 (= K198), H230 (= H235), A302 (= A307), A303 (≠ P308), P304 (= P309), Y326 (≠ C328), G327 (= G329), M328 (= M330), T329 (= T331), D413 (= D413), I425 (≠ F425), R428 (= R428), K519 (= K520)
5bsvA Crystal structure of 4-coumarate:coa ligase complexed with feruloyl adenylate (see paper)
29% identity, 93% coverage: 37:530/530 of query aligns to 47:529/529 of 5bsvA
- active site: S182 (≠ T190), S202 (≠ G210), H230 (= H235), T329 (= T331), E330 (= E332), K434 (= K434), Q439 (≠ N439), K519 (= K520)
- binding 5'-O-[(R)-hydroxy{[(2E)-3-(5-methoxy-4-oxocyclohexa-1,5-dien-1-yl)prop-2-enoyl]oxy}phosphoryl]adenosine: H230 (= H235), Y232 (≠ G237), S236 (≠ A240), A302 (= A307), A303 (≠ P308), P304 (= P309), G325 (≠ A327), G327 (= G329), M328 (= M330), T329 (= T331), P333 (≠ G335), V334 (= V336), D413 (= D413), K430 (= K430), K434 (= K434), Q439 (≠ N439)
5bsuA Crystal structure of 4-coumarate:coa ligase complexed with caffeoyl adenylate (see paper)
29% identity, 93% coverage: 37:530/530 of query aligns to 47:529/529 of 5bsuA
- active site: S182 (≠ T190), S202 (≠ G210), H230 (= H235), T329 (= T331), E330 (= E332), K434 (= K434), Q439 (≠ N439), K519 (= K520)
- binding 5'-O-[(R)-{[(2E)-3-(3,4-dioxocyclohexa-1,5-dien-1-yl)prop-2-enoyl]oxy}(hydroxy)phosphoryl]adenosine: H230 (= H235), Y232 (≠ G237), S236 (≠ A240), M299 (≠ F304), A302 (= A307), A303 (≠ P308), P304 (= P309), G325 (≠ A327), G327 (= G329), M328 (= M330), T329 (= T331), P333 (≠ G335), D413 (= D413), K430 (= K430), K434 (= K434), Q439 (≠ N439)
5bstA Crystal structure of 4-coumarate:coa ligase complexed with coumaroyl adenylate (see paper)
29% identity, 93% coverage: 37:530/530 of query aligns to 47:529/529 of 5bstA
- active site: S182 (≠ T190), S202 (≠ G210), H230 (= H235), T329 (= T331), E330 (= E332), K434 (= K434), Q439 (≠ N439), K519 (= K520)
- binding 5'-O-[(R)-hydroxy{[(2E)-3-(4-oxocyclohexa-1,5-dien-1-yl)prop-2-enoyl]oxy}phosphoryl]adenosine: H230 (= H235), Y232 (≠ G237), S236 (≠ A240), A302 (= A307), A303 (≠ P308), P304 (= P309), G325 (≠ A327), Y326 (≠ C328), G327 (= G329), M328 (= M330), T329 (= T331), P333 (≠ G335), V334 (= V336), D413 (= D413), K430 (= K430), K434 (= K434), Q439 (≠ N439)
5bsrA Crystal structure of 4-coumarate:coa ligase complexed with adenosine monophosphate and coenzyme a (see paper)
29% identity, 93% coverage: 37:530/530 of query aligns to 46:528/528 of 5bsrA
- active site: S181 (≠ T190), S201 (≠ G210), H229 (= H235), T328 (= T331), E329 (= E332), K433 (= K434), Q438 (≠ N439), K518 (= K520)
- binding adenosine monophosphate: A301 (= A307), G326 (= G329), T328 (= T331), D412 (= D413), K429 (= K430), K433 (= K434), Q438 (≠ N439)
- binding coenzyme a: L102 (≠ R93), P226 (= P232), H229 (= H235), Y231 (≠ G237), F253 (= F258), K435 (≠ G436), G436 (= G437), F437 (≠ E438), F498 (≠ S499)
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, 93% coverage: 37:530/530 of query aligns to 54:536/542 of O24146
- S189 (≠ T190) binding ATP
- S190 (= S191) binding ATP
- G191 (= G192) binding ATP
- T192 (= T193) binding ATP
- T193 (= T194) binding ATP; mutation to A: Reduced activity against 4-coumarate.
- K197 (= K198) binding ATP; mutation to A: Reduced activity against 4-coumarate.
- H237 (= H235) mutation to A: Strongly reduced activity against 4-coumarate.
- Y239 (≠ G237) binding (E)-4-coumaroyl-AMP; binding (E)-caffeoyl-AMP; binding (E)-feruloyl-AMP; mutation to A: Strongly reduced activity against 4-coumarate.; mutation to F: Reduced activity against 4-coumarate.
- S243 (≠ A240) binding (E)-4-coumaroyl-AMP; binding (E)-caffeoyl-AMP; binding (E)-feruloyl-AMP
- K260 (≠ Y257) binding CoA
- A309 (= A307) binding (E)-4-coumaroyl-AMP; binding (E)-caffeoyl-AMP; binding (E)-feruloyl-AMP
- Q331 (= Q326) binding ATP
- G332 (≠ A327) binding (E)-4-coumaroyl-AMP; binding (E)-caffeoyl-AMP; binding (E)-feruloyl-AMP; binding AMP; binding ATP
- T336 (= T331) binding (E)-4-coumaroyl-AMP; binding (E)-caffeoyl-AMP; binding (E)-feruloyl-AMP; binding AMP; binding ATP; mutation to A: Strongly reduced activity against 4-coumarate.
- V341 (= V336) mutation to G: Reduced activity against 4-coumarate.; mutation Missing: Reduced activity against 4-coumarate, but acquired ability to use sinapate as substrate.
- M344 (≠ L339) binding (E)-4-coumaroyl-AMP; binding (E)-caffeoyl-AMP; binding (E)-feruloyl-AMP; mutation to A: Reduced activity against 4-coumarate.
- D420 (= D413) binding (E)-4-coumaroyl-AMP; binding (E)-caffeoyl-AMP; binding (E)-feruloyl-AMP; binding AMP; binding ATP
- R435 (= R428) binding (E)-4-coumaroyl-AMP; binding (E)-caffeoyl-AMP; binding (E)-feruloyl-AMP; binding ATP; mutation to A: Strongly reduced activity against 4-coumarate.
- K437 (= K430) binding (E)-4-coumaroyl-AMP; binding (E)-caffeoyl-AMP; binding (E)-feruloyl-AMP; binding AMP
- K441 (= K434) binding (E)-4-coumaroyl-AMP; binding (E)-caffeoyl-AMP; binding (E)-feruloyl-AMP; binding AMP; mutation to A: Abolished activity against 4-coumarate.
- K443 (≠ G436) binding CoA; mutation to A: Normal activity against 4-coumarate.
- G444 (= G437) binding CoA
- Q446 (≠ N439) binding AMP
- K526 (= K520) binding ATP; mutation to A: Abolished activity against 4-coumarate.
4gxqA Crystal structure of atp bound rpmatb-bxbclm chimera b1 (see paper)
30% identity, 93% coverage: 33:527/530 of query aligns to 26:498/506 of 4gxqA
- active site: T163 (= T190), N183 (≠ G210), H207 (= H235), T303 (= T331), E304 (= E332), I403 (≠ K434), N408 (= N439), A491 (≠ K520)
- binding adenosine-5'-triphosphate: T163 (= T190), S164 (= S191), G165 (= G192), T166 (= T193), T167 (= T194), H207 (= H235), S277 (≠ A307), A278 (≠ P308), P279 (= P309), E298 (≠ Q326), M302 (= M330), T303 (= T331), D382 (= D413), R397 (= R428)
- binding carbonate ion: H207 (= H235), S277 (≠ A307), R299 (≠ A327), G301 (= G329)
6e97B Crystal structure of the aryl acid adenylating enzyme fscc from fuscachelin nrps in complex with dhb-adenylate
31% identity, 98% coverage: 11:530/530 of query aligns to 23:532/537 of 6e97B
- active site: S190 (≠ T190), S210 (≠ G210), H234 (= H235), A336 (≠ T331), E337 (= E332), N437 (≠ K434), K442 (≠ N439), K522 (= K520)
- binding 5'-O-[(S)-[(2,3-dihydroxybenzene-1-carbonyl)oxy](hydroxy)phosphoryl]adenosine: H234 (= H235), N235 (≠ I236), F236 (≠ G237), S240 (≠ P241), G310 (≠ Y302), A311 (≠ L303), K312 (≠ F304), V332 (≠ A327), F333 (≠ C328), G334 (= G329), M335 (= M330), A336 (≠ T331), D416 (= D413), K433 (= K430), K442 (≠ N439)
P0DX84 3-methylmercaptopropionyl-CoA ligase; MMPA-CoA ligase; EC 6.2.1.44 from Ruegeria lacuscaerulensis (strain DSM 11314 / KCTC 2953 / ITI-1157) (Silicibacter lacuscaerulensis) (see paper)
27% identity, 99% coverage: 5:530/530 of query aligns to 5:533/539 of P0DX84
- H231 (= H235) mutation to A: Retains 74% of wild-type activity.
- W235 (≠ L239) mutation to A: Almost completely abolishes the activity.
- G302 (vs. gap) mutation to P: Almost completely abolishes the activity.
- G303 (vs. gap) mutation to P: Almost completely abolishes the activity.
- W326 (≠ C328) mutation to A: Retains 7.7% of wild-type activity.
- P333 (≠ G335) mutation to A: Retains 69% of wild-type activity.
- R432 (= R428) mutation to A: Retains 4.3% of wild-type activity.
- K434 (= K430) mutation to A: Retains 36% of wild-type activity.
- D435 (= D431) mutation to A: Retains 76% of wild-type activity.
- K438 (= K434) mutation to A: Retains 5.6% of wild-type activity.
- G440 (= G436) mutation to P: Retains 3.6% of wild-type activity.
- G441 (= G437) mutation to P: Retains 2.7% of wild-type activity.
- E442 (= E438) mutation to A: Retains 27% of wild-type activity.
- W443 (≠ N439) mutation to A: Retains 60% of wild-type activity.
- E474 (= E470) mutation to A: Retains 33% of wild-type activity.
- K523 (= K520) Plays an important role in catalysis; mutation to A: Retains 1.6% of wild-type activity.; mutation to E: Retains 1.4% of wild-type activity.; mutation to R: Retains 57% of wild-type activity.
- K526 (= K523) mutation to A: Retains 48% of wild-type activity.
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)
29% identity, 98% coverage: 11:529/530 of query aligns to 5:508/514 of Q9SMT7
- TSGTT 170:174 (= TSGTT 190:194) binding ATP
- H214 (= H235) binding ATP; mutation to A: Abolished activity.
- S289 (≠ F304) binding oxalate; mutation to A: Abolished activity.
- SAS 289:291 (≠ FLI 304:306) binding ATP
- EA 310:311 (≠ QA 326:327) binding ATP
- M314 (= M330) binding oxalate
- T315 (= T331) binding ATP
- H319 (≠ G335) binding oxalate; mutation to A: Abolished activity.
- D394 (= D413) binding ATP
- R409 (= R428) binding ATP; mutation to A: Abolished activity.
- K500 (≠ I521) binding ATP; binding oxalate; mutation to A: Abolished activity.
5ie2A Crystal structure of a plant enzyme (see paper)
30% identity, 98% coverage: 11:529/530 of query aligns to 5:503/506 of 5ie2A
- active site: T165 (= T190), S185 (≠ G210), H209 (= H235), T310 (= T331), E311 (= E332), N410 (≠ K434), K415 (≠ N439), K495 (≠ I521)
- binding adenosine-5'-triphosphate: T165 (= T190), S166 (= S191), G167 (= G192), T168 (= T193), T169 (= T194), S284 (≠ F304), A285 (≠ L305), S286 (≠ I306), Y307 (≠ C328), A308 (≠ G329), M309 (= M330), T310 (= T331), D389 (= D413), L401 (≠ F425), R404 (= R428), K495 (≠ I521)
6ijbB Structure of 3-methylmercaptopropionate coa ligase mutant k523a in complex with amp and mmpa (see paper)
27% identity, 99% coverage: 5:530/530 of query aligns to 5:533/538 of 6ijbB
- active site: T185 (= T190), H205 (≠ R209), H231 (= H235), S329 (≠ T331), E330 (= E332), K438 (= K434), W443 (≠ N439), A523 (≠ K520)
- binding 3-(methylsulfanyl)propanoic acid: W235 (≠ L239), G303 (vs. gap), A325 (= A327), W326 (≠ C328), G327 (= G329), M328 (= M330)
- binding adenosine monophosphate: G303 (vs. gap), A304 (vs. gap), A305 (≠ I306), H324 (≠ Q326), W326 (≠ C328), G327 (= G329), M328 (= M330), S329 (≠ T331), Q359 (= Q353), D417 (= D413)
3r44A Mycobacterium tuberculosis fatty acyl coa synthetase (see paper)
28% identity, 98% coverage: 8:529/530 of query aligns to 3:496/502 of 3r44A
3ni2A Crystal structures and enzymatic mechanisms of a populus tomentosa 4- coumarate:coa ligase (see paper)
28% identity, 90% coverage: 33:511/530 of query aligns to 43:511/528 of 3ni2A
- active site: S182 (≠ T190), S202 (≠ G210), H230 (= H235), T329 (= T331), E330 (= E332), K434 (= K434), Q439 (≠ N439)
- binding 5'-O-{(S)-hydroxy[3-(4-hydroxyphenyl)propoxy]phosphoryl}adenosine: Y232 (≠ G237), S236 (≠ A240), G302 (≠ A307), A303 (≠ P308), P304 (= P309), G325 (≠ A327), G327 (= G329), T329 (= T331), P333 (≠ G335), V334 (= V336), D413 (= D413), K430 (= K430), K434 (= K434), Q439 (≠ N439)
Sites not aligning to the query:
3a9vA Crystal structures and enzymatic mechanisms of a populus tomentosa 4- coumarate--coa ligase (see paper)
28% identity, 90% coverage: 33:511/530 of query aligns to 43:511/528 of 3a9vA
- active site: S182 (≠ T190), S202 (≠ G210), H230 (= H235), T329 (= T331), E330 (= E332), K434 (= K434), Q439 (≠ N439)
- binding adenosine monophosphate: H230 (= H235), G302 (≠ A307), A303 (≠ P308), P304 (= P309), Y326 (≠ C328), G327 (= G329), M328 (= M330), T329 (= T331), D413 (= D413), K430 (= K430), K434 (= K434), Q439 (≠ N439)
Sites not aligning to the query:
Query Sequence
>WP_011445127.1 NCBI__GCF_000013325.1:WP_011445127.1
MPVTVTTEVATVGDLLLRAADLHAERTALALPGVAVSYRELRDGAFRVARALIGLGIARG
EHVALLMPNSVEFAEALFGIMLAGCVAVPLNARHRAAEIGYIIDNSQARILLTSRHDSDP
VNFIEVIEQALPTPSAAPALRYVALLRGEGSGDVLGREAFLSQGVRTDPAEVEHTRRSVR
VRDAALIIYTSGTTANPKGCVLPHEAVTRGPVERARYRLSANGVDVTWAGGPLFHIGSLA
PFIGSVGVAGTFLADSYFEPGRAIALMEKHAVTLAWPWFAAIVQGIIDHPEFSAEKFAHL
KYLFLIAPPTLVERVQDLLPHTEIIQACGMTETSGVFALCDTDEDRESRIFTQGKACPGI
EIRIVDPETGQDLPDGTMGEILVRGYNVMDGYWDAPEKTSEALVGHGWLKTGDLYTRQPN
GSLIFGGRCKDMLKVGGENVAAIEVEAFLCTHPAVKTAEVVGRPDPRLDEVPVAFIELYD
GETINEEELIAFCRGRIASYKVPRAIRFMSAADWPMSATKIDKRALRAQL
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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