SitesBLAST
Comparing WP_083439307.1 NCBI__GCF_001189915.1:WP_083439307.1 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)
4gxqA Crystal structure of atp bound rpmatb-bxbclm chimera b1 (see paper)
50% identity, 56% coverage: 390:892/899 of query aligns to 1:503/506 of 4gxqA
- active site: T163 (= T557), N183 (= N577), H207 (= H601), T303 (= T697), E304 (= E698), I403 (= I796), N408 (= N801), A491 (≠ K880)
- binding adenosine-5'-triphosphate: T163 (= T557), S164 (= S558), G165 (= G559), T166 (= T560), T167 (= T561), H207 (= H601), S277 (= S671), A278 (= A672), P279 (= P673), E298 (= E692), M302 (= M696), T303 (= T697), D382 (= D775), R397 (= R790)
- binding carbonate ion: H207 (= H601), S277 (= S671), R299 (= R693), G301 (= G695)
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)
33% identity, 54% coverage: 410:895/899 of query aligns to 21:502/503 of P9WQ37
- K172 (= K565) mutation to A: Slight reduction of the fatty acyl-CoA ligase activity. Slight increase of susceptibility to proteolysis.
- R195 (≠ G588) mutation to A: Alteration of the strength of the membrane binding; when associated with A-9; A-17; A-197 and A-244.
- R197 (≠ N590) mutation to A: Alteration of the strength of the membrane binding; when associated with A-9; A-17; A-195 and A-244.
- V209 (≠ A602) 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 (≠ G604) mutation to G: Slight increase of the fatty acyl-CoA ligase activity. Reduced rate of proteolytic degradation.
- T214 (≠ I607) 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 (≠ T638) mutation to A: Alteration of the strength of the membrane binding; when associated with A-17; A-195; A-195 and A-197.
- A302 (≠ G695) 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 (= W770) 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 (= D775) 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 (= R790) mutation to A: Reduction of binding affinity for fatty acids.
- S404 (= S797) mutation to A: Slight reduction of the fatty acyl-CoA ligase activity. Enhanced affinity towards palmitic acid binding.
- G406 (= G799) mutation to L: No effect on the formation of acyl-adenylate intermediate. However, it shows very poor catalytic efficiency to form acyl-CoA.
- K487 (= K880) 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.
8wevA Crystal structure of feruoyl-coa synthetase complexed with amp from amycolatopsis thermoflava
35% identity, 52% coverage: 419:887/899 of query aligns to 30:484/486 of 8wevA
Sites not aligning to the query:
3r44A Mycobacterium tuberculosis fatty acyl coa synthetase (see paper)
33% identity, 54% coverage: 410:895/899 of query aligns to 24:502/502 of 3r44A
Sites not aligning to the query:
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)
29% identity, 58% coverage: 368:888/899 of query aligns to 4:551/561 of P69451
- Y213 (= Y556) mutation to A: Loss of activity.
- T214 (= T557) mutation to A: 10% of wild-type activity.
- G216 (= G559) mutation to A: Decreases activity.
- T217 (= T560) mutation to A: Decreases activity.
- G219 (= G562) mutation to A: Decreases activity.
- K222 (= K565) mutation to A: Decreases activity.
- E361 (= E698) mutation to A: Loss of activity.
Q4G176 Malonate--CoA ligase ACSF3, mitochondrial; Acyl-CoA synthetase family member 3; EC 6.2.1.76 from Homo sapiens (Human) (see 2 papers)
36% identity, 37% coverage: 552:886/899 of query aligns to 197:569/576 of Q4G176
- R354 (= R693) mutation to A: Impairs malonyl-CoA synthase activity.; mutation to L: Impairs malonyl-CoA synthase activity.
- V372 (≠ R711) to M: in dbSNP:rs3743979
Sites not aligning to the query:
- 2 L → P: in dbSNP:rs7188200
- 17 A → P: in dbSNP:rs11547019
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)
32% identity, 53% coverage: 407:886/899 of query aligns to 11:506/514 of Q9SMT7
- TSGTT 170:174 (= TSGTT 557:561) binding ATP
- H214 (= H601) binding ATP; mutation to A: Abolished activity.
- S289 (= S671) binding oxalate; mutation to A: Abolished activity.
- SAS 289:291 (≠ SAP 671:673) binding ATP
- EA 310:311 (≠ ER 692:693) binding ATP
- M314 (= M696) binding oxalate
- T315 (= T697) binding ATP
- H319 (vs. gap) binding oxalate; mutation to A: Abolished activity.
- D394 (= D775) binding ATP
- R409 (= R790) binding ATP; mutation to A: Abolished activity.
- K500 (= K880) binding ATP; binding oxalate; mutation to A: Abolished activity.
6qjzA Identificationand characterization of an oxalylfrom grass pea (lathyrus sativuscoa-synthetase l.) (see paper)
32% identity, 51% coverage: 414:875/899 of query aligns to 18:494/504 of 6qjzA
- active site: T169 (= T557), S189 (≠ N577), H213 (= H601), T314 (= T697), E315 (= E698), N414 (≠ I796), K419 (≠ N801)
- binding adenosine monophosphate: H213 (= H601), S288 (= S671), A289 (= A672), S290 (≠ P673), A312 (≠ G695), M313 (= M696), T314 (= T697), D393 (= D775), L405 (≠ I787), K410 (= K792), K419 (≠ N801)
5ie3A Crystal structure of a plant enzyme (see paper)
32% identity, 53% coverage: 407:886/899 of query aligns to 11:499/504 of 5ie3A
- active site: T163 (= T557), S183 (≠ N577), H207 (= H601), T308 (= T697), E309 (= E698), N408 (≠ I796), K413 (≠ N801), K493 (= K880)
- binding adenosine monophosphate: S164 (= S558), S282 (= S671), A283 (= A672), S284 (≠ P673), Y305 (= Y694), A306 (≠ G695), M307 (= M696), T308 (= T697), D387 (= D775), L399 (≠ I787), R402 (= R790), K493 (= K880)
- binding oxalic acid: V208 (≠ A602), S282 (= S671), A306 (≠ G695), M307 (= M696), H312 (vs. gap), K493 (= K880)
5ie2A Crystal structure of a plant enzyme (see paper)
33% identity, 53% coverage: 407:886/899 of query aligns to 11:501/506 of 5ie2A
- active site: T165 (= T557), S185 (≠ N577), H209 (= H601), T310 (= T697), E311 (= E698), N410 (≠ I796), K415 (≠ N801), K495 (= K880)
- binding adenosine-5'-triphosphate: T165 (= T557), S166 (= S558), G167 (= G559), T168 (= T560), T169 (= T561), S284 (= S671), A285 (= A672), S286 (≠ P673), Y307 (= Y694), A308 (≠ G695), M309 (= M696), T310 (= T697), D389 (= D775), L401 (≠ I787), R404 (= R790), K495 (= K880)
3nyrA Malonyl-coa ligase ternary product complex with malonyl-coa and amp bound (see paper)
34% identity, 48% coverage: 445:875/899 of query aligns to 44:460/460 of 3nyrA
- active site: T137 (= T557), T157 (≠ N577), H181 (= H601), T281 (= T697), E282 (= E698), K379 (≠ I796), K384 (≠ N801)
- binding adenosine monophosphate: S255 (= S671), A256 (= A672), A257 (≠ P673), R277 (= R693), Y278 (= Y694), G279 (= G695), M280 (= M696), T281 (= T697), D357 (= D775), K379 (≠ I796), K384 (≠ N801)
- binding malonyl-coenzyme a: P178 (= P598), H181 (= H601), T226 (= T645), R230 (= R649), S255 (= S671), R277 (= R693), G279 (= G695), G381 (= G798), G382 (= G799), Y383 (= Y800)
3nyqA Malonyl-coa ligase ternary product complex with methylmalonyl-coa and amp bound (see paper)
34% identity, 48% coverage: 445:875/899 of query aligns to 44:460/460 of 3nyqA
- active site: T137 (= T557), T157 (≠ N577), H181 (= H601), T281 (= T697), E282 (= E698), K379 (≠ I796), K384 (≠ N801)
- binding adenosine monophosphate: S255 (= S671), A256 (= A672), A257 (≠ P673), R277 (= R693), Y278 (= Y694), G279 (= G695), M280 (= M696), T281 (= T697), D357 (= D775), K379 (≠ I796), K384 (≠ N801)
- binding methylmalonyl-coenzyme a: P178 (= P598), H181 (= H601), H183 (= H603), T226 (= T645), R230 (= R649), S255 (= S671), R277 (= R693), G279 (= G695), M280 (= M696), M285 (≠ I701), G381 (= G798), G382 (= G799), Y383 (= Y800)
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)
29% identity, 53% coverage: 419:897/899 of query aligns to 28:511/512 of O74976
- S283 (= S671) modified: Phosphoserine
- S284 (≠ A672) modified: Phosphoserine
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, 52% coverage: 430:899/899 of query aligns to 76:582/590 of Q4WR83
Sites not aligning to the query:
- 6:14 PTS2-type peroxisomal targeting signal
6k4cA Ancestral luciferase anclamp in complex with dlsa (see paper)
27% identity, 55% coverage: 393:889/899 of query aligns to 23:536/538 of 6k4cA
- binding 5'-o-[n-(dehydroluciferyl)-sulfamoyl] adenosine: H243 (= H601), F245 (≠ H603), T249 (≠ S608), G314 (≠ S671), A315 (= A672), P316 (= P673), G337 (≠ R693), Y338 (= Y694), G339 (= G695), L340 (≠ M696), T341 (= T697), A346 (= A700), D420 (= D775), I432 (= I787), K527 (= K880)
6k4dA Ancestral luciferase anclamp in complex with atp and d-luciferin (see paper)
27% identity, 55% coverage: 393:889/899 of query aligns to 23:536/539 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 (= H601), F245 (≠ H603), T249 (≠ S608), G314 (≠ S671), A315 (= A672), P316 (= P673), G337 (≠ R693), Y338 (= Y694), G339 (= G695), L340 (≠ M696), T341 (= T697), S345 (= S699), A346 (= A700), D420 (= D775), I432 (= I787), K527 (= K880)
- binding (4S)-2-(6-hydroxy-1,3-benzothiazol-2-yl)-4,5-dihydro-1,3-thiazole-4-carboxylic acid: F245 (≠ H603), R335 (≠ L691), G337 (≠ R693), G339 (= G695), L340 (≠ M696), A346 (= A700)
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)
29% identity, 54% coverage: 406:889/899 of query aligns to 45:539/546 of Q84P21
- K530 (= K880) mutation to N: Lossed enzymatic activity.
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)
29% identity, 55% coverage: 398:887/899 of query aligns to 43:547/556 of Q9S725
- K211 (= K565) mutation to S: Drastically reduces the activity.
- M293 (≠ V641) mutation M->A,P: Affects the substrate specificity.
- K320 (≠ I668) mutation K->L,A: Affects the substrate specificity.
- E401 (≠ G742) mutation to Q: Slighlty reduces the substrate specificity.
- C403 (≠ Q744) mutation to A: Significantly reduces the substrate specificity.
- R449 (= R790) mutation to Q: Drastically reduces the activity.
- K457 (≠ G798) mutation to S: Drastically reduces the activity.
- K540 (= K880) mutation to N: Abolishes the activity.
Q5SKN9 Long-chain-fatty-acid--CoA ligase; Long-chain fatty acyl-CoA synthetase; LC-FACS; EC 6.2.1.3 from Thermus thermophilus (strain ATCC 27634 / DSM 579 / HB8) (see paper)
28% identity, 57% coverage: 380:892/899 of query aligns to 4:536/541 of Q5SKN9
- T184 (= T557) binding Mg(2+)
- G302 (= G670) binding tetradecanoyl-AMP
- Q322 (≠ E692) binding tetradecanoyl-AMP
- G323 (≠ R693) binding tetradecanoyl-AMP
- T327 (= T697) binding tetradecanoyl-AMP
- E328 (= E698) binding Mg(2+)
- D418 (= D775) binding tetradecanoyl-AMP
- K435 (= K792) binding tetradecanoyl-AMP
- K439 (≠ I796) binding tetradecanoyl-AMP
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, 55% coverage: 398:887/899 of query aligns to 39:542/559 of Q67W82
- G395 (= G741) mutation to R: In ral1; reduced lignin content and increased accumulation of 4-coumarate and ferulate in roots; confers increased tolerance to aluminum.
Query Sequence
>WP_083439307.1 NCBI__GCF_001189915.1:WP_083439307.1
MSQASFTGATAESRLAALFDPDCRTPLISASHLKMMRGNVAGRQVLAVATDPQVDKGAVG
VAECSDLRRAVQLAQETGAALVLLIDSAGARLYEGLPIQGALRRLMRELLDARLDGLPVL
ALLGRNVFGGASMLAQAASQRCYAPATLLAMTGPRVLQQGGDAYATVIAAIDGNARSHCG
ITANSEQLLDDTPGTYTAALQRWVSRLGDSAAPDLDAERRQLAQRLQTTTLVPNADMILT
GATLRCHGQIPAGCADALRLAEMIDAAGPGALQLQLDYNGHSTALADERLLLSQYLAHLA
ASIRRRVRRGHPVHLHINGPISGGIYIAAAGAASSVVMTPGSSVRTLPQSALDDILARPA
GIDAAADITLERYPELGLADTISTLPVTAMNANIFATFEHIARDAGEAVFIETPEAQTLS
YAGMLALTARYANALQNLGVNPGDRVAVQVDKSVENFCLYLATLRMSAIYLPLNTAYHPN
EVQYFMQDAAPRIFICTPANLAALSILASANGVAHTFSLADDGSGSFIDYVAANTTAGAG
FDTAHANADDVALIIYTSGTTGRPKGAMLTHANLLSNGRALTTLWEFGKNDVLLHALPLF
HAHGLFISSHCALLSASRILFLKKFDAAQVVTLLPCATVMVGVPTFYSRLLAQAGFNTAA
AAGMRLFISGSAPLLAETNHEFSQRSGHVVLERYGMTESAIISSNPCSGERRIGAVGPAI
DGVEVRIADTDDRPLGADTVGGIQIRGSGVMKGYWRNPEKTAQEFTADGWFRTGDLGTLS
ADAYLTIVGRAKDLVISGGYNVYPKEVEMAIDALPGVIESAVIGVPDRDFGEAVNAVVVC
SDSTLSAPDIILSLKAQMASYKVPKQVHFVTELPRNAMGKVLKNVLRDIYGNTAPARQA
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