SitesBLAST
Comparing WP_012116043.1 NCBI__GCF_000017645.1:WP_012116043.1 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)
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)
37% identity, 91% coverage: 45:518/521 of query aligns to 29:496/503 of P9WQ37
- K172 (= K190) mutation to A: Slight reduction of the fatty acyl-CoA ligase activity. Slight increase of susceptibility to proteolysis.
- R195 (≠ E213) mutation to A: Alteration of the strength of the membrane binding; when associated with A-9; A-17; A-197 and A-244.
- R197 (≠ G215) mutation to A: Alteration of the strength of the membrane binding; when associated with A-9; A-17; A-195 and A-244.
- V209 (≠ M227) 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 (≠ G229) mutation to G: Slight increase of the fatty acyl-CoA ligase activity. Reduced rate of proteolytic degradation.
- T214 (≠ G232) 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 (= R263) mutation to A: Alteration of the strength of the membrane binding; when associated with A-17; A-195; A-195 and A-197.
- A302 (≠ G323) 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 (≠ Y399) 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 (= D404) 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 (= R419) mutation to A: Reduction of binding affinity for fatty acids.
- S404 (≠ R426) mutation to A: Slight reduction of the fatty acyl-CoA ligase activity. Enhanced affinity towards palmitic acid binding.
- G406 (= G428) mutation to L: No effect on the formation of acyl-adenylate intermediate. However, it shows very poor catalytic efficiency to form acyl-CoA.
- K487 (= K509) 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.
3r44A Mycobacterium tuberculosis fatty acyl coa synthetase (see paper)
35% identity, 96% coverage: 17:518/521 of query aligns to 2:496/502 of 3r44A
8wevA Crystal structure of feruoyl-coa synthetase complexed with amp from amycolatopsis thermoflava
37% identity, 94% coverage: 28:518/521 of query aligns to 8:486/486 of 8wevA
5gtdA O-succinylbenzoate coa synthetase (mene) from bacillus subtilis in complex with the acyl-adenylate intermediate osb-amp (see paper)
30% identity, 94% coverage: 33:521/521 of query aligns to 15:482/484 of 5gtdA
- active site: T151 (= T182), S171 (= S202), H195 (= H226), T288 (= T325), E289 (= E326)
- binding adenosine-5'-monophosphate: G263 (= G298), G264 (≠ A299), Y285 (= Y322), G286 (= G323), M287 (≠ A324), T288 (= T325), D366 (= D404), V378 (= V416)
- binding magnesium ion: F314 (≠ P351), S315 (≠ C352)
- binding 2-succinylbenzoate: H195 (= H226), S197 (≠ T228), A237 (≠ M269), L260 (≠ A295), G262 (= G297), G263 (= G298), G286 (= G323), M287 (≠ A324), S292 (= S329), Q293 (≠ P330)
5x8fB Ternary complex structure of a double mutant i454ra456k of o- succinylbenzoate coa synthetase (mene) from bacillus subtilis bound with amp and its product analogue osb-ncoa at 1.76 angstrom (see paper)
30% identity, 94% coverage: 33:521/521 of query aligns to 15:482/485 of 5x8fB
- active site: T151 (= T182), S171 (= S202), H195 (= H226), T288 (= T325), E289 (= E326), I387 (≠ N425), N392 (≠ K430), K470 (= K509)
- binding magnesium ion: Y23 (≠ G41), E24 (≠ G42), H70 (≠ L88), N178 (≠ A209), L202 (≠ V233), L214 (= L246), T296 (≠ I333), L297 (= L334), S298 (≠ P335)
- binding o-succinylbenzoyl-N-coenzyme A: K85 (≠ R103), L191 (≠ V222), P192 (= P223), H195 (= H226), I196 (≠ M227), S197 (≠ T228), A237 (≠ M269), V238 (= V270), L260 (≠ A295), G262 (= G297), G286 (= G323), M287 (≠ A324), S292 (= S329), Q293 (≠ P330), S388 (≠ R426), G389 (≠ A427), G390 (= G428), E391 (≠ Y429), K420 (≠ V458), W421 (≠ L459), K450 (≠ D488), Y451 (= Y489)
5burA O-succinylbenzoate coenzyme a synthetase (mene) from bacillus subtilis, in complex with atp and magnesium ion (see paper)
30% identity, 94% coverage: 28:517/521 of query aligns to 5:475/475 of 5burA
- active site: T150 (= T182), S170 (= S202), H194 (= H226), T287 (= T325), E288 (= E326)
- binding adenosine-5'-triphosphate: T150 (= T182), S151 (= S183), T153 (= T185), T154 (= T186), K158 (= K190), G263 (≠ A299), S283 (≠ V321), T287 (= T325), D365 (= D404), V377 (= V416), R380 (= R419)
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)
31% identity, 91% coverage: 45:520/521 of query aligns to 64:574/590 of Q4WR83
Sites not aligning to the query:
- 6:14 PTS2-type peroxisomal targeting signal
5busA O-succinylbenzoate coenzyme a synthetase (mene) from bacillus subtilis, in complex with amp (see paper)
30% identity, 95% coverage: 28:521/521 of query aligns to 5:479/481 of 5busA
- active site: T150 (= T182), S170 (= S202), H194 (= H226), T287 (= T325), E288 (= E326)
- binding adenosine monophosphate: H194 (= H226), G262 (= G298), G263 (≠ A299), S283 (≠ V321), M286 (≠ A324), T287 (= T325), D365 (= D404), V377 (= V416), R380 (= R419), K467 (= K509)
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, 97% coverage: 17:521/521 of query aligns to 20:555/561 of P69451
- Y213 (= Y181) mutation to A: Loss of activity.
- T214 (= T182) mutation to A: 10% of wild-type activity.
- G216 (= G184) mutation to A: Decreases activity.
- T217 (= T185) mutation to A: Decreases activity.
- G219 (= G187) mutation to A: Decreases activity.
- K222 (= K190) mutation to A: Decreases activity.
- E361 (= E326) mutation to A: Loss of activity.
4gxqA Crystal structure of atp bound rpmatb-bxbclm chimera b1 (see paper)
32% identity, 91% coverage: 45:517/521 of query aligns to 28:499/506 of 4gxqA
- active site: T163 (= T182), N183 (≠ S202), H207 (= H226), T303 (= T325), E304 (= E326), I403 (≠ N425), N408 (≠ K430), A491 (≠ K509)
- binding adenosine-5'-triphosphate: T163 (= T182), S164 (= S183), G165 (= G184), T166 (= T185), T167 (= T186), H207 (= H226), S277 (≠ G298), A278 (= A299), P279 (= P300), E298 (≠ N320), M302 (≠ A324), T303 (= T325), D382 (= D404), R397 (= R419)
- binding carbonate ion: H207 (= H226), S277 (≠ G298), R299 (≠ V321), G301 (= G323)
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, 91% coverage: 44:515/521 of query aligns to 56:536/546 of Q84P21
- K530 (= K509) mutation to N: Lossed enzymatic activity.
7tz4A Salicylate adenylate pchd from pseudomonas aeruginosa containing 4- cyanosalicyl-ams (see paper)
33% identity, 94% coverage: 31:518/521 of query aligns to 33:526/530 of 7tz4A
- binding 5'-O-[(4-cyano-2-hydroxybenzoyl)sulfamoyl]adenosine: H232 (= H226), N233 (≠ M227), F234 (≠ T228), C238 (vs. gap), G305 (= G298), S306 (≠ A299), R307 (≠ P300), V327 (= V321), L328 (≠ Y322), G329 (= G323), M330 (≠ A324), A331 (≠ T325), I335 (≠ V331), D411 (= D404), V423 (= V416), K517 (= K509)
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, 91% coverage: 47:521/521 of query aligns to 65:552/556 of Q9S725
- K211 (= K190) mutation to S: Drastically reduces the activity.
- M293 (≠ L268) mutation M->A,P: Affects the substrate specificity.
- K320 (≠ A295) mutation K->L,A: Affects the substrate specificity.
- E401 (= E372) mutation to Q: Slighlty reduces the substrate specificity.
- C403 (≠ W374) mutation to A: Significantly reduces the substrate specificity.
- R449 (= R419) mutation to Q: Drastically reduces the activity.
- K457 (≠ A427) mutation to S: Drastically reduces the activity.
- K540 (= K509) mutation to N: Abolishes the activity.
5wm3A Crystal structure of cahj in complex with salicyl adenylate (see paper)
33% identity, 96% coverage: 22:521/521 of query aligns to 29:536/537 of 5wm3A
- active site: S193 (≠ T182), N213 (≠ S202), H237 (= H226), A336 (≠ T325), E337 (= E326), N437 (= N425), K442 (= K430), K524 (= K509)
- binding 9-(5-O-{(S)-hydroxy[(2-hydroxybenzene-1-carbonyl)oxy]phosphoryl}-alpha-L-lyxofuranosyl)-9H-purin-6-amine: N238 (≠ M227), F239 (≠ T228), G310 (= G298), S311 (≠ A299), K312 (≠ P300), V332 (= V321), F333 (≠ Y322), G334 (= G323), M335 (≠ A324), A336 (≠ T325), D416 (= D404), K433 (= K421), K442 (= K430)
- binding magnesium ion: S301 (= S289), L303 (≠ W291), G326 (vs. gap)
5wm2A Crystal structure of cahj in complex with salicylic acid and amp (see paper)
33% identity, 96% coverage: 22:521/521 of query aligns to 29:536/536 of 5wm2A
- active site: S193 (≠ T182), N213 (≠ S202), H237 (= H226), A336 (≠ T325), E337 (= E326), N437 (= N425), K442 (= K430), K524 (= K509)
- binding adenosine monophosphate: G310 (= G298), S311 (≠ A299), K312 (≠ P300), V332 (= V321), F333 (≠ Y322), G334 (= G323), M335 (≠ A324), A336 (≠ T325), E337 (= E326), D416 (= D404), V428 (= V416), K433 (= K421), K442 (= K430)
5buqB Unliganded form of o-succinylbenzoate coenzyme a synthetase (mene) from bacillus subtilis, solved at 1.98 angstroms (see paper)
29% identity, 95% coverage: 28:521/521 of query aligns to 5:470/473 of 5buqB
6sq8B Structure of amide bond synthetase mcba from marinactinospora thermotolerans (see paper)
33% identity, 92% coverage: 37:516/521 of query aligns to 16:489/494 of 6sq8B
- active site: T160 (= T185), D200 (≠ H226), Q296 (≠ T325), E297 (= E326), I397 (≠ N425), N402 (≠ K430), K482 (= K509)
- binding adenosine monophosphate: G270 (= G298), Q291 (≠ F319), Q296 (≠ T325), D376 (= D404), R391 (= R419), R406 (≠ A434), K482 (= K509)
- binding 1-ethanoyl-9~{H}-pyrido[3,4-b]indole-3-carboxylic acid: L201 (≠ M227), G294 (= G323), T295 (≠ A324), A299 (≠ S328), F300 (≠ S329)
5wm6A Crystal structure of cahj in complex with benzoyl adenylate (see paper)
33% identity, 96% coverage: 22:520/521 of query aligns to 29:535/535 of 5wm6A
- active site: S193 (≠ T182), N213 (≠ S202), H237 (= H226), A336 (≠ T325), E337 (= E326), N437 (= N425), K442 (= K430), K524 (= K509)
- binding magnesium ion: S301 (= S289), L303 (≠ W291), G326 (vs. gap)
- binding 5'-O-[(R)-(benzoyloxy)(hydroxy)phosphoryl]adenosine: F239 (≠ T228), G310 (= G298), S311 (≠ A299), K312 (≠ P300), V332 (= V321), F333 (≠ Y322), G334 (= G323), M335 (≠ A324), A336 (≠ T325), D416 (= D404), K433 (= K421), K442 (= K430)
5wm5A Crystal structure of cahj in complex with 5-methylsalicyl adenylate (see paper)
33% identity, 96% coverage: 22:520/521 of query aligns to 29:533/533 of 5wm5A
- active site: S193 (≠ T182), N213 (≠ S202), H237 (= H226), A336 (≠ T325), E337 (= E326), N437 (= N425), K442 (= K430), K522 (= K509)
- binding 9-(5-O-{(S)-hydroxy[(2-hydroxy-5-methylbenzene-1-carbonyl)oxy]phosphoryl}-alpha-L-lyxofuranosyl)-9H-purin-6-amine: H237 (= H226), N238 (≠ M227), F239 (≠ T228), G309 (= G297), G310 (= G298), S311 (≠ A299), K312 (≠ P300), V332 (= V321), F333 (≠ Y322), G334 (= G323), M335 (≠ A324), A336 (≠ T325), L340 (≠ S329), D416 (= D404), K433 (= K421), K442 (= K430)
5wm4A Crystal structure of cahj in complex with 6-methylsalicyl adenylate (see paper)
33% identity, 96% coverage: 22:521/521 of query aligns to 29:533/534 of 5wm4A
- active site: S193 (≠ T182), N213 (≠ S202), H237 (= H226), A336 (≠ T325), E337 (= E326), N437 (= N425), K442 (= K430), K521 (= K509)
- binding 9-(5-O-{(S)-hydroxy[(2-hydroxy-6-methylbenzene-1-carbonyl)oxy]phosphoryl}-alpha-L-lyxofuranosyl)-9H-purin-6-amine: N238 (≠ M227), F239 (≠ T228), C243 (vs. gap), G309 (= G297), G310 (= G298), S311 (≠ A299), K312 (≠ P300), V332 (= V321), F333 (≠ Y322), G334 (= G323), M335 (≠ A324), A336 (≠ T325), L340 (≠ S329), D416 (= D404), K433 (= K421), K442 (= K430)
- binding magnesium ion: M453 (≠ V441), H455 (= H443), V458 (= V446)
Query Sequence
>WP_012116043.1 NCBI__GCF_000017645.1:WP_012116043.1
MIRHEVHFGRVVPCFIDRPPSVDALFRSWVARTPDALAVVGGERRVTYGALDAAVERLAD
GLFAHGVRKGARVATLVGNHLAVVELSLACARIGAIHVTLDIRQRRPEIAYILAQSGTML
LVHDAACASELPEAAEVPELRHRFAAGGSATGSEPYEELFAQPAPERAADVSEEDPFCIL
YTSGTTGKPKGAVLTNLGVIHSCLHYRYALGLEPGDRTVLAVPNAHMTGLVGVIHGTLAA
GACLILMGQFKARLFLELAARERLTAALMVPAMYNLCLLDPQFEQLDLSSWRIAAFGGAP
MPEASARRLKEKSPKLTLFNVYGATETSSPVAILPRDAPPERLDSVGRVMPCIDLKVMDE
DGREVPPGTAGELWIAGASIVPGYWRNPEADATAFVGGYWRSGDVGSIDAEGYLKVFDRK
KDMINRAGYKVYSAEVESVLVFHPDVSEAAVVGYPDPVLGERVEAFVVAGPDLSVDDLRR
FCAARLSDYKVPDRVTILPEGLPRNPNGKVMKNVLRERAAG
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