SitesBLAST
Comparing 352309 FitnessBrowser__Btheta:352309 to proteins with known functional sites using BLASTp with E ≤ 0.001.
Or try Sites on a Tree, PaperBLAST, Conserved Domains, or compare to all protein structures
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)
38% identity, 99% coverage: 2:544/549 of query aligns to 33:580/590 of Q4WR83
Sites not aligning to the query:
- 6:14 PTS2-type peroxisomal targeting signal
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)
30% identity, 91% coverage: 34:535/549 of query aligns to 49:551/561 of P69451
- Y213 (= Y196) mutation to A: Loss of activity.
- T214 (= T197) mutation to A: 10% of wild-type activity.
- G216 (= G199) mutation to A: Decreases activity.
- T217 (= T200) mutation to A: Decreases activity.
- G219 (= G202) mutation to A: Decreases activity.
- K222 (= K205) mutation to A: Decreases activity.
- E361 (= E340) mutation to A: Loss of activity.
4gxqA Crystal structure of atp bound rpmatb-bxbclm chimera b1 (see paper)
29% identity, 92% coverage: 33:535/549 of query aligns to 28:499/506 of 4gxqA
- active site: T163 (= T197), N183 (= N217), H207 (= H241), T303 (= T339), E304 (= E340), I403 (= I442), N408 (= N447), A491 (≠ K527)
- binding adenosine-5'-triphosphate: T163 (= T197), S164 (= S198), G165 (= G199), T166 (= T200), T167 (= T201), H207 (= H241), S277 (≠ G313), A278 (≠ S314), P279 (≠ L315), E298 (≠ S334), M302 (≠ L338), T303 (= T339), D382 (= D421), R397 (= R436)
- binding carbonate ion: H207 (= H241), S277 (≠ G313), R299 (≠ V335), G301 (= G337)
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)
28% identity, 93% coverage: 34:541/549 of query aligns to 64:551/556 of Q9S725
- K211 (= K205) mutation to S: Drastically reduces the activity.
- M293 (≠ Y283) mutation M->A,P: Affects the substrate specificity.
- K320 (≠ M311) mutation K->L,A: Affects the substrate specificity.
- E401 (= E388) mutation to Q: Slighlty reduces the substrate specificity.
- C403 (= C390) mutation to A: Significantly reduces the substrate specificity.
- R449 (= R436) mutation to Q: Drastically reduces the activity.
- K457 (≠ G444) mutation to S: Drastically reduces the activity.
- K540 (= K527) mutation to N: Abolishes the 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)
27% identity, 97% coverage: 6:535/549 of query aligns to 2:495/503 of P9WQ37
- R9 (≠ E13) mutation to A: Alteration of the strength of the membrane binding; when associated with A-9; A-195; A-197 and A-244.
- R17 (≠ D21) mutation to A: Alteration of the strength of the membrane binding; when associated with A-9; A-17; A-197 and A-244.
- K172 (= K205) mutation to A: Slight reduction of the fatty acyl-CoA ligase activity. Slight increase of susceptibility to proteolysis.
- R195 (≠ T228) mutation to A: Alteration of the strength of the membrane binding; when associated with A-9; A-17; A-197 and A-244.
- R197 (≠ D230) mutation to A: Alteration of the strength of the membrane binding; when associated with A-9; A-17; A-195 and A-244.
- V209 (≠ C242) 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 (≠ G244) mutation to G: Slight increase of the fatty acyl-CoA ligase activity. Reduced rate of proteolytic degradation.
- T214 (≠ L247) 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 (= R278) mutation to A: Alteration of the strength of the membrane binding; when associated with A-17; A-195; A-195 and A-197.
- A302 (≠ G337) 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 (≠ F416) 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 (= D421) 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 (= R436) mutation to A: Reduction of binding affinity for fatty acids.
- S404 (≠ R443) mutation to A: Slight reduction of the fatty acyl-CoA ligase activity. Enhanced affinity towards palmitic acid binding.
- G406 (= G445) mutation to L: No effect on the formation of acyl-adenylate intermediate. However, it shows very poor catalytic efficiency to form acyl-CoA.
- K487 (= K527) mutation to A: Strong reduction of the fatty acyl-CoA ligase activity. Reduction of binding affinity for ATP.
3r44A Mycobacterium tuberculosis fatty acyl coa synthetase (see paper)
27% identity, 97% coverage: 6:535/549 of query aligns to 5:495/502 of 3r44A
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)
28% identity, 93% coverage: 34:541/549 of query aligns to 53:537/542 of O24146
- S189 (≠ T197) binding
- S190 (= S198) binding
- G191 (= G199) binding
- T192 (= T200) binding
- T193 (= T201) binding ; mutation to A: Reduced activity against 4-coumarate.
- K197 (= K205) binding ; mutation to A: Reduced activity against 4-coumarate.
- H237 (= H241) mutation to A: Strongly reduced activity against 4-coumarate.
- Y239 (≠ F243) binding ; binding ; binding ; mutation to A: Strongly reduced activity against 4-coumarate.; mutation to F: Reduced activity against 4-coumarate.
- S243 (≠ L247) binding ; binding ; binding
- K260 (≠ R264) binding
- A309 (≠ S314) binding ; binding ; binding
- Q331 (vs. gap) binding
- G332 (vs. gap) binding ; binding ; binding ; binding ; binding
- T336 (= T339) 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 (= M345) binding ; binding ; binding ; mutation to A: Reduced activity against 4-coumarate.
- D420 (= D421) binding ; binding ; binding ; binding ; binding
- R435 (= R436) binding ; binding ; binding ; binding ; mutation to A: Strongly reduced activity against 4-coumarate.
- K437 (= K438) binding ; binding ; binding ; binding
- K441 (≠ I442) binding ; binding ; binding ; binding ; mutation to A: Abolished activity against 4-coumarate.
- K443 (≠ G444) binding ; mutation to A: Normal activity against 4-coumarate.
- G444 (= G445) binding
- Q446 (≠ N447) binding
- K526 (= K527) 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)
28% identity, 93% coverage: 34:541/549 of query aligns to 46:530/530 of 5bsmA
- active site: S182 (≠ T197), S202 (≠ N217), H230 (= H241), T329 (= T339), E330 (= E340), K434 (≠ I442), Q439 (≠ N447), K519 (= K527)
- binding adenosine-5'-triphosphate: S182 (≠ T197), S183 (= S198), G184 (= G199), T185 (= T200), T186 (= T201), K190 (= K205), H230 (= H241), A302 (≠ S314), A303 (≠ V318), P304 (≠ E319), Y326 (= Y336), G327 (= G337), M328 (≠ L338), T329 (= T339), D413 (= D421), I425 (= I433), R428 (= R436), K519 (= K527)
5bsvA Crystal structure of 4-coumarate:coa ligase complexed with feruloyl adenylate (see paper)
28% identity, 92% coverage: 34:540/549 of query aligns to 46:529/529 of 5bsvA
- active site: S182 (≠ T197), S202 (≠ N217), H230 (= H241), T329 (= T339), E330 (= E340), K434 (≠ I442), Q439 (≠ N447), K519 (= K527)
- binding 5'-O-[(R)-hydroxy{[(2E)-3-(5-methoxy-4-oxocyclohexa-1,5-dien-1-yl)prop-2-enoyl]oxy}phosphoryl]adenosine: H230 (= H241), Y232 (≠ F243), S236 (≠ L247), A302 (≠ S314), A303 (≠ V318), P304 (≠ E319), G325 (vs. gap), G327 (= G337), M328 (≠ L338), T329 (= T339), P333 (= P343), V334 (vs. gap), D413 (= D421), K430 (= K438), K434 (≠ I442), Q439 (≠ N447)
5bsuA Crystal structure of 4-coumarate:coa ligase complexed with caffeoyl adenylate (see paper)
28% identity, 92% coverage: 34:540/549 of query aligns to 46:529/529 of 5bsuA
- active site: S182 (≠ T197), S202 (≠ N217), H230 (= H241), T329 (= T339), E330 (= E340), K434 (≠ I442), Q439 (≠ N447), K519 (= K527)
- binding 5'-O-[(R)-{[(2E)-3-(3,4-dioxocyclohexa-1,5-dien-1-yl)prop-2-enoyl]oxy}(hydroxy)phosphoryl]adenosine: H230 (= H241), Y232 (≠ F243), S236 (≠ L247), M299 (= M311), A302 (≠ S314), A303 (≠ V318), P304 (≠ E319), G325 (vs. gap), G327 (= G337), M328 (≠ L338), T329 (= T339), P333 (= P343), D413 (= D421), K430 (= K438), K434 (≠ I442), Q439 (≠ N447)
5bstA Crystal structure of 4-coumarate:coa ligase complexed with coumaroyl adenylate (see paper)
28% identity, 92% coverage: 34:540/549 of query aligns to 46:529/529 of 5bstA
- active site: S182 (≠ T197), S202 (≠ N217), H230 (= H241), T329 (= T339), E330 (= E340), K434 (≠ I442), Q439 (≠ N447), K519 (= K527)
- binding 5'-O-[(R)-hydroxy{[(2E)-3-(4-oxocyclohexa-1,5-dien-1-yl)prop-2-enoyl]oxy}phosphoryl]adenosine: H230 (= H241), Y232 (≠ F243), S236 (≠ L247), A302 (≠ S314), A303 (≠ V318), P304 (≠ E319), G325 (vs. gap), Y326 (= Y336), G327 (= G337), M328 (≠ L338), T329 (= T339), P333 (= P343), V334 (vs. gap), D413 (= D421), K430 (= K438), K434 (≠ I442), Q439 (≠ N447)
6k4cA Ancestral luciferase anclamp in complex with dlsa (see paper)
27% identity, 91% coverage: 35:536/549 of query aligns to 50:536/538 of 6k4cA
- binding 5'-o-[n-(dehydroluciferyl)-sulfamoyl] adenosine: H243 (= H241), F245 (= F243), T249 (≠ A248), G314 (= G313), A315 (≠ S314), P316 (≠ L315), G337 (≠ V335), Y338 (= Y336), G339 (= G337), L340 (= L338), T341 (= T339), A346 (= A347), D420 (= D421), I432 (= I433), K527 (= K527)
5bsrA Crystal structure of 4-coumarate:coa ligase complexed with adenosine monophosphate and coenzyme a (see paper)
28% identity, 92% coverage: 34:540/549 of query aligns to 45:528/528 of 5bsrA
- active site: S181 (≠ T197), S201 (≠ N217), H229 (= H241), T328 (= T339), E329 (= E340), K433 (≠ I442), Q438 (≠ N447), K518 (= K527)
- binding adenosine monophosphate: A301 (≠ S314), G326 (= G337), T328 (= T339), D412 (= D421), K429 (= K438), K433 (≠ I442), Q438 (≠ N447)
- binding coenzyme a: L102 (≠ N91), P226 (= P238), H229 (= H241), Y231 (≠ F243), F253 (= F265), K435 (≠ G444), G436 (= G445), F437 (≠ E446), F498 (≠ R507)
6k4dA Ancestral luciferase anclamp in complex with atp and d-luciferin (see paper)
27% identity, 91% coverage: 35:536/549 of query aligns to 50:536/539 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 (= H241), F245 (= F243), T249 (≠ A248), G314 (= G313), A315 (≠ S314), P316 (≠ L315), G337 (≠ V335), Y338 (= Y336), G339 (= G337), L340 (= L338), T341 (= T339), S345 (≠ T346), A346 (= A347), D420 (= D421), I432 (= I433), K527 (= K527)
- binding (4S)-2-(6-hydroxy-1,3-benzothiazol-2-yl)-4,5-dihydro-1,3-thiazole-4-carboxylic acid: F245 (= F243), R335 (≠ T333), G337 (≠ V335), G339 (= G337), L340 (= L338), A346 (= A347)
5ie2A Crystal structure of a plant enzyme (see paper)
29% identity, 95% coverage: 7:530/549 of query aligns to 5:498/506 of 5ie2A
- active site: T165 (= T197), S185 (≠ N217), H209 (= H241), T310 (= T339), E311 (= E340), N410 (≠ I442), K415 (≠ N447), K495 (= K527)
- binding adenosine-5'-triphosphate: T165 (= T197), S166 (= S198), G167 (= G199), T168 (= T200), T169 (= T201), S284 (≠ A312), A285 (≠ G313), S286 (= S314), Y307 (= Y336), A308 (≠ G337), M309 (≠ L338), T310 (= T339), D389 (= D421), L401 (≠ I433), R404 (= R436), K495 (= K527)
5u95B Structure of the open conformation of 4-coumarate-coa ligase from nicotiana tabacum
28% identity, 93% coverage: 34:541/549 of query aligns to 45:526/527 of 5u95B
O74976 Oxalate--CoA ligase; Oxalyl-CoA synthetase; Peroxisomal-coenzyme A synthetase; EC 6.2.1.8 from Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast) (see paper)
27% identity, 92% coverage: 25:530/549 of query aligns to 19:497/512 of O74976
- S283 (≠ A312) modified: Phosphoserine
- S284 (≠ G313) modified: Phosphoserine
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, 93% coverage: 34:541/549 of query aligns to 60:546/559 of Q67W82
- G395 (= G387) mutation to R: In ral1; reduced lignin content and increased accumulation of 4-coumarate and ferulate in roots; confers increased tolerance to aluminum.
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, 95% coverage: 7:530/549 of query aligns to 5:503/514 of Q9SMT7
- TSGTT 170:174 (= TSGTT 197:201) binding
- H214 (= H241) binding ; mutation to A: Abolished activity.
- S289 (≠ A312) binding ; mutation to A: Abolished activity.
- SAS 289:291 (≠ AGS 312:314) binding
- EA 310:311 (≠ SV 334:335) binding
- M314 (≠ L338) binding
- T315 (= T339) binding
- H319 (≠ P343) binding ; mutation to A: Abolished activity.
- D394 (= D421) binding
- R409 (= R436) binding ; mutation to A: Abolished activity.
- K500 (= K527) binding ; binding ; mutation to A: Abolished activity.
3ni2A Crystal structures and enzymatic mechanisms of a populus tomentosa 4- coumarate:coa ligase (see paper)
27% identity, 91% coverage: 34:535/549 of query aligns to 46:527/528 of 3ni2A
- active site: S182 (≠ T197), S202 (≠ N213), H230 (= H241), T329 (= T339), E330 (= E340), K434 (≠ I442), Q439 (≠ N447), K519 (= K527)
- binding 5'-O-{(S)-hydroxy[3-(4-hydroxyphenyl)propoxy]phosphoryl}adenosine: Y232 (≠ F243), S236 (≠ L247), G302 (= G313), A303 (≠ S314), P304 (≠ L315), G325 (≠ V335), G327 (= G337), T329 (= T339), P333 (= P343), V334 (vs. gap), D413 (= D421), K430 (= K438), K434 (≠ I442), Q439 (≠ N447)
Query Sequence
>352309 FitnessBrowser__Btheta:352309
MQLFERTLGQWLEHWAEETPDKEYIVYSDRNLRFTWSQLNQRVDDMAKGLIAVGVERGTH
VGIWAANVPDWLTLLYACAKIGAVYVTVNTNYKQAELEYLCQNSDMHTLCIVNGEKDSDF
VQMTYTMLPELKTCERGHLKSERFPYMKNVIYVGQEKHRGMYNTAEILLLGNNVEDDRLT
ELKSKVDCHDVVNMQYTSGTTGFPKGVMLTHYNIANNGFLTGEHMKFTADDKLCCCVPLF
HCFGVVLATMNCLTHGCTQVMVERFDPLVVLASIHKERCTALYGVPTMFIAELHHPMFDL
FDMSCLRTGIMAGSLCPVELMKQVEEKMYMKVTSVYGLTEAAPGMTATRIDDSFDVRCNT
VGRDFEFTEVRVIDPETGEECPVGVQGEMCNRGYNTMKGYYKNPEATAEVIDKDNFLHSG
DLGIKDEDGNYRITGRIKDMIIRGGENIYPREIEEFLYKLDGVKDVQVAGIPSKKYGEAV
GAFIILQEGVEMHESDVRDFCKNKISRYKIPKYVFFVKEFPMTGSGKIQKFRLKDLGLQL
CKEQGIEII
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