SitesBLAST
Comparing 206897 MicrobesOnline__882:206897 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)
39% identity, 98% coverage: 3:556/564 of query aligns to 5:559/561 of P69451
- Y213 (= Y209) mutation to A: Loss of activity.
- T214 (= T210) mutation to A: 10% of wild-type activity.
- G216 (= G212) mutation to A: Decreases activity.
- T217 (= T213) mutation to A: Decreases activity.
- G219 (= G215) mutation to A: Decreases activity.
- K222 (= K218) mutation to A: Decreases activity.
- E361 (= E355) mutation to A: Loss of 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)
32% identity, 90% coverage: 47:556/564 of query aligns to 54:542/542 of O24146
- S189 (≠ T210) binding
- S190 (≠ G211) binding
- G191 (= G212) binding
- T192 (= T213) binding
- T193 (= T214) binding ; mutation to A: Reduced activity against 4-coumarate.
- K197 (= K218) binding ; mutation to A: Reduced activity against 4-coumarate.
- H237 (= H256) mutation to A: Strongly reduced activity against 4-coumarate.
- Y239 (= Y258) binding ; binding ; binding ; mutation to A: Strongly reduced activity against 4-coumarate.; mutation to F: Reduced activity against 4-coumarate.
- S243 (≠ T262) binding ; binding ; binding
- K260 (≠ R279) binding
- A309 (≠ S328) binding ; binding ; binding
- Q331 (≠ E349) binding
- G332 (= G350) binding ; binding ; binding ; binding ; binding
- T336 (= T354) binding ; binding ; binding ; binding ; binding ; mutation to A: Strongly reduced activity against 4-coumarate.
- V341 (= V359) mutation to G: Reduced activity against 4-coumarate.; mutation Missing: Reduced activity against 4-coumarate, but acquired ability to use sinapate as substrate.
- M344 (≠ L362) binding ; binding ; binding ; mutation to A: Reduced activity against 4-coumarate.
- D420 (= D434) binding ; binding ; binding ; binding ; binding
- R435 (= R449) binding ; binding ; binding ; binding ; mutation to A: Strongly reduced activity against 4-coumarate.
- K437 (= K451) binding ; binding ; binding ; binding
- K441 (≠ I455) binding ; binding ; binding ; binding ; mutation to A: Abolished activity against 4-coumarate.
- K443 (≠ G457) binding ; mutation to A: Normal activity against 4-coumarate.
- G444 (= G458) binding
- Q446 (≠ N460) binding
- K526 (= K540) binding ; mutation to A: Abolished activity against 4-coumarate.
5bsrA Crystal structure of 4-coumarate:coa ligase complexed with adenosine monophosphate and coenzyme a (see paper)
32% identity, 89% coverage: 47:549/564 of query aligns to 46:527/528 of 5bsrA
- active site: S181 (≠ T210), S201 (≠ N230), H229 (= H256), T328 (= T354), E329 (= E355), K433 (≠ I455), Q438 (≠ N460), K518 (= K540)
- binding adenosine monophosphate: A301 (≠ S328), G326 (= G352), T328 (= T354), D412 (= D434), K429 (= K451), K433 (≠ I455), Q438 (≠ N460)
- binding coenzyme a: L102 (= L103), P226 (= P253), H229 (= H256), Y231 (= Y258), F253 (≠ Y280), K435 (≠ G457), G436 (= G458), F437 (≠ Y459), F498 (≠ N520)
5bsmA Crystal structure of 4-coumarate:coa ligase complexed with magnesium and adenosine triphosphate (see paper)
32% identity, 89% coverage: 47:549/564 of query aligns to 47:528/530 of 5bsmA
- active site: S182 (≠ T210), S202 (≠ N230), H230 (= H256), T329 (= T354), E330 (= E355), K434 (≠ I455), Q439 (≠ N460), K519 (= K540)
- binding adenosine-5'-triphosphate: S182 (≠ T210), S183 (≠ G211), G184 (= G212), T185 (= T213), T186 (= T214), K190 (= K218), H230 (= H256), A302 (≠ S328), A303 (= A329), P304 (= P330), Y326 (≠ F351), G327 (= G352), M328 (≠ L353), T329 (= T354), D413 (= D434), I425 (= I446), R428 (= R449), K519 (= K540)
5bsvA Crystal structure of 4-coumarate:coa ligase complexed with feruloyl adenylate (see paper)
32% identity, 89% coverage: 47:549/564 of query aligns to 47:528/529 of 5bsvA
- active site: S182 (≠ T210), S202 (≠ N230), H230 (= H256), T329 (= T354), E330 (= E355), K434 (≠ I455), Q439 (≠ N460), K519 (= K540)
- binding 5'-O-[(R)-hydroxy{[(2E)-3-(5-methoxy-4-oxocyclohexa-1,5-dien-1-yl)prop-2-enoyl]oxy}phosphoryl]adenosine: H230 (= H256), Y232 (= Y258), S236 (≠ T262), A302 (≠ S328), A303 (= A329), P304 (= P330), G325 (= G350), G327 (= G352), M328 (≠ L353), T329 (= T354), P333 (= P358), V334 (= V359), D413 (= D434), K430 (= K451), K434 (≠ I455), Q439 (≠ N460)
5bsuA Crystal structure of 4-coumarate:coa ligase complexed with caffeoyl adenylate (see paper)
32% identity, 89% coverage: 47:549/564 of query aligns to 47:528/529 of 5bsuA
- active site: S182 (≠ T210), S202 (≠ N230), H230 (= H256), T329 (= T354), E330 (= E355), K434 (≠ I455), Q439 (≠ N460), K519 (= K540)
- binding 5'-O-[(R)-{[(2E)-3-(3,4-dioxocyclohexa-1,5-dien-1-yl)prop-2-enoyl]oxy}(hydroxy)phosphoryl]adenosine: H230 (= H256), Y232 (= Y258), S236 (≠ T262), M299 (≠ I325), A302 (≠ S328), A303 (= A329), P304 (= P330), G325 (= G350), G327 (= G352), M328 (≠ L353), T329 (= T354), P333 (= P358), D413 (= D434), K430 (= K451), K434 (≠ I455), Q439 (≠ N460)
5bstA Crystal structure of 4-coumarate:coa ligase complexed with coumaroyl adenylate (see paper)
32% identity, 89% coverage: 47:549/564 of query aligns to 47:528/529 of 5bstA
- active site: S182 (≠ T210), S202 (≠ N230), H230 (= H256), T329 (= T354), E330 (= E355), K434 (≠ I455), Q439 (≠ N460), K519 (= K540)
- binding 5'-O-[(R)-hydroxy{[(2E)-3-(4-oxocyclohexa-1,5-dien-1-yl)prop-2-enoyl]oxy}phosphoryl]adenosine: H230 (= H256), Y232 (= Y258), S236 (≠ T262), A302 (≠ S328), A303 (= A329), P304 (= P330), G325 (= G350), Y326 (≠ F351), G327 (= G352), M328 (≠ L353), T329 (= T354), P333 (= P358), V334 (= V359), D413 (= D434), K430 (= K451), K434 (≠ I455), Q439 (≠ N460)
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)
32% identity, 96% coverage: 8:549/564 of query aligns to 25:544/559 of Q67W82
- G395 (= G401) mutation to R: In ral1; reduced lignin content and increased accumulation of 4-coumarate and ferulate in roots; confers increased tolerance to aluminum.
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)
31% identity, 90% coverage: 47:556/564 of query aligns to 65:556/556 of Q9S725
- K211 (= K218) mutation to S: Drastically reduces the activity.
- M293 (≠ P298) mutation M->A,P: Affects the substrate specificity.
- K320 (≠ I325) mutation K->L,A: Affects the substrate specificity.
- E401 (= E402) mutation to Q: Slighlty reduces the substrate specificity.
- C403 (≠ I404) mutation to A: Significantly reduces the substrate specificity.
- R449 (= R449) mutation to Q: Drastically reduces the activity.
- K457 (≠ G457) mutation to S: Drastically reduces the activity.
- K540 (= K540) mutation to N: Abolishes the activity.
5u95B Structure of the open conformation of 4-coumarate-coa ligase from nicotiana tabacum
32% identity, 89% coverage: 47:549/564 of query aligns to 46:524/527 of 5u95B
3ni2A Crystal structures and enzymatic mechanisms of a populus tomentosa 4- coumarate:coa ligase (see paper)
30% identity, 93% coverage: 21:547/564 of query aligns to 19:526/528 of 3ni2A
- active site: S182 (≠ T210), S202 (≠ N230), H230 (= H256), T329 (= T354), E330 (= E355), K434 (≠ I455), Q439 (≠ N460), K519 (= K540)
- binding 5'-O-{(S)-hydroxy[3-(4-hydroxyphenyl)propoxy]phosphoryl}adenosine: Y232 (= Y258), S236 (≠ T262), G302 (≠ S328), A303 (= A329), P304 (= P330), G325 (= G350), G327 (= G352), T329 (= T354), P333 (= P358), V334 (= V359), D413 (= D434), K430 (= K451), K434 (≠ I455), Q439 (≠ N460)
3a9vA Crystal structures and enzymatic mechanisms of a populus tomentosa 4- coumarate--coa ligase (see paper)
30% identity, 93% coverage: 21:547/564 of query aligns to 19:526/528 of 3a9vA
- active site: S182 (≠ T210), S202 (≠ N230), H230 (= H256), T329 (= T354), E330 (= E355), K434 (≠ I455), Q439 (≠ N460), K519 (= K540)
- binding adenosine monophosphate: H230 (= H256), G302 (≠ S328), A303 (= A329), P304 (= P330), Y326 (≠ F351), G327 (= G352), M328 (≠ L353), T329 (= T354), D413 (= D434), K430 (= K451), K434 (≠ I455), Q439 (≠ N460)
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, 89% coverage: 45:546/564 of query aligns to 57:536/546 of Q84P21
- K530 (= K540) mutation to N: Lossed enzymatic 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)
31% identity, 93% coverage: 22:546/564 of query aligns to 6:506/514 of Q9SMT7
- TSGTT 170:174 (≠ TGGTT 210:214) binding
- H214 (= H256) binding ; mutation to A: Abolished activity.
- S289 (= S328) binding ; mutation to A: Abolished activity.
- SAS 289:291 (≠ SAP 328:330) binding
- EA 310:311 (≠ EG 349:350) binding
- M314 (≠ L353) binding
- T315 (= T354) binding
- H319 (≠ P358) binding ; mutation to A: Abolished activity.
- D394 (= D434) binding
- R409 (= R449) binding ; mutation to A: Abolished activity.
- K500 (= K540) binding ; binding ; mutation to A: Abolished activity.
4gxqA Crystal structure of atp bound rpmatb-bxbclm chimera b1 (see paper)
31% identity, 89% coverage: 45:547/564 of query aligns to 28:498/506 of 4gxqA
- active site: T163 (= T210), N183 (= N230), H207 (= H256), T303 (= T354), E304 (= E355), I403 (= I455), N408 (= N460), A491 (≠ K540)
- binding adenosine-5'-triphosphate: T163 (= T210), S164 (≠ G211), G165 (= G212), T166 (= T213), T167 (= T214), H207 (= H256), S277 (= S328), A278 (= A329), P279 (= P330), E298 (= E349), M302 (≠ L353), T303 (= T354), D382 (= D434), R397 (= R449)
- binding carbonate ion: H207 (= H256), S277 (= S328), R299 (≠ G350), G301 (= G352)
5ie2A Crystal structure of a plant enzyme (see paper)
31% identity, 93% coverage: 22:546/564 of query aligns to 6:501/506 of 5ie2A
- active site: T165 (= T210), S185 (≠ N230), H209 (= H256), T310 (= T354), E311 (= E355), N410 (≠ I455), K415 (≠ N460), K495 (= K540)
- binding adenosine-5'-triphosphate: T165 (= T210), S166 (≠ G211), G167 (= G212), T168 (= T213), T169 (= T214), S284 (= S328), A285 (= A329), S286 (≠ P330), Y307 (≠ F351), A308 (≠ G352), M309 (≠ L353), T310 (= T354), D389 (= D434), L401 (≠ I446), R404 (= R449), K495 (= K540)
5ie3A Crystal structure of a plant enzyme (see paper)
30% identity, 93% coverage: 22:546/564 of query aligns to 6:499/504 of 5ie3A
- active site: T163 (= T210), S183 (≠ N230), H207 (= H256), T308 (= T354), E309 (= E355), N408 (≠ I455), K413 (≠ N460), K493 (= K540)
- binding adenosine monophosphate: S164 (≠ G211), S282 (= S328), A283 (= A329), S284 (≠ P330), Y305 (≠ F351), A306 (≠ G352), M307 (≠ L353), T308 (= T354), D387 (= D434), L399 (≠ I446), R402 (= R449), K493 (= K540)
- binding oxalic acid: V208 (= V257), S282 (= S328), A306 (≠ G352), M307 (≠ L353), H312 (≠ P358), K493 (= K540)
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, 90% coverage: 43:549/564 of query aligns to 27:496/503 of P9WQ37
- K172 (= K218) mutation to A: Slight reduction of the fatty acyl-CoA ligase activity. Slight increase of susceptibility to proteolysis.
- R195 (= R243) mutation to A: Alteration of the strength of the membrane binding; when associated with A-9; A-17; A-197 and A-244.
- R197 (= R245) mutation to A: Alteration of the strength of the membrane binding; when associated with A-9; A-17; A-195 and A-244.
- V209 (= V257) 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 (≠ G259) mutation to G: Slight increase of the fatty acyl-CoA ligase activity. Reduced rate of proteolytic degradation.
- T214 (= T262) 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 (≠ K293) mutation to A: Alteration of the strength of the membrane binding; when associated with A-17; A-195; A-195 and A-197.
- A302 (≠ G352) 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 (= W429) 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 (= D434) 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 (= R449) mutation to A: Reduction of binding affinity for fatty acids.
- S404 (≠ V456) mutation to A: Slight reduction of the fatty acyl-CoA ligase activity. Enhanced affinity towards palmitic acid binding.
- G406 (= G458) mutation to L: No effect on the formation of acyl-adenylate intermediate. However, it shows very poor catalytic efficiency to form acyl-CoA.
- K487 (= K540) 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.
6k4dA Ancestral luciferase anclamp in complex with atp and d-luciferin (see paper)
31% identity, 89% coverage: 46:547/564 of query aligns to 49:534/539 of 6k4dA
- binding [[(2R,3S,4R,5R)-5-(6-aminopurin-9-yl)-3,4-bis(oxidanyl)oxolan-2-yl]methoxy-oxidanyl-phosphoryl] (4S)-2-(6-oxidanyl-1,3-benzothiazol-2-yl)-4,5-dihydro-1,3-thiazole-4-carboxylate: H243 (= H256), F245 (≠ Y258), T249 (= T262), G314 (≠ S328), A315 (= A329), P316 (= P330), G337 (= G350), Y338 (≠ F351), G339 (= G352), L340 (= L353), T341 (= T354), S345 (≠ P358), A346 (≠ V359), D420 (= D434), I432 (= I446), K527 (= K540)
- binding (4S)-2-(6-hydroxy-1,3-benzothiazol-2-yl)-4,5-dihydro-1,3-thiazole-4-carboxylic acid: F245 (≠ Y258), R335 (≠ Q346), G337 (= G350), G339 (= G352), L340 (= L353), A346 (≠ V359)
6k4cA Ancestral luciferase anclamp in complex with dlsa (see paper)
31% identity, 89% coverage: 45:547/564 of query aligns to 48:534/538 of 6k4cA
- binding 5'-o-[n-(dehydroluciferyl)-sulfamoyl] adenosine: H243 (= H256), F245 (≠ Y258), T249 (= T262), G314 (≠ S328), A315 (= A329), P316 (= P330), G337 (= G350), Y338 (≠ F351), G339 (= G352), L340 (= L353), T341 (= T354), A346 (≠ V359), D420 (= D434), I432 (= I446), K527 (= K540)
Query Sequence
>206897 MicrobesOnline__882:206897
MPWLQSYDKDVPARIDYEVAPLFAFLDEAAERHPKQTAIIFRNYKVSYAKLRLLAERFAA
NLRAQGVLPGDRVSVMLPNVPQAIIAFWGLLKAGCTVVMTNPLYMEKELVHQIHDSGAEY
MIALDLVWPKIEPLRDRLGIRKFFITRISDALGFPLNLLYRFKAKREGTWRDVPFDGETV
IPWKTLFKKKEGYSAKVENPREALALLQYTGGTTGISKGVMLTHYNLSVNVQQIKAILGE
STRMRHTFLGLMPYFHVYGLTTCLTLPTALGATIIPFPRYVPRDVLVGIDKHKPTIFPGA
PSIYISLMQQKDVGEFDLKSIKYCISGSAPMPLEHIRRFHELTGAQVIEGFGLTEASPVT
HLNPIHGVQKPGSIGVPFPDTEARVVDMEVGLVPLPPGKIGELIIRGPQVMQGYLNRPDE
TANTLRNGWLYTGDIATMDEDGYFFIVDRKKDMIIVGGYNVYPREIDEVLHEHPKVKEAV
TVGVPHATRGEIIKAYIVPREGVKLTKAEIVAHCREQLANYKVPKQVEFRNELPKTIVGK
VLRRILRAEEEERLKNAPAGNGED
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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