SitesBLAST
Comparing CCNA_02483 FitnessBrowser__Caulo:CCNA_02483 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)
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)
35% identity, 98% coverage: 10:495/496 of query aligns to 11:503/503 of P9WQ37
- R17 (≠ G16) mutation to A: Alteration of the strength of the membrane binding; when associated with A-9; A-17; A-197 and A-244.
- K172 (= K157) mutation to A: Slight reduction of the fatty acyl-CoA ligase activity. Slight increase of susceptibility to proteolysis.
- R195 (≠ T180) mutation to A: Alteration of the strength of the membrane binding; when associated with A-9; A-17; A-197 and A-244.
- R197 (≠ E182) mutation to A: Alteration of the strength of the membrane binding; when associated with A-9; A-17; A-195 and A-244.
- V209 (≠ I194) 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 (≠ G196) mutation to G: Slight increase of the fatty acyl-CoA ligase activity. Reduced rate of proteolytic degradation.
- T214 (= T199) 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 (≠ T230) mutation to A: Alteration of the strength of the membrane binding; when associated with A-17; A-195; A-195 and A-197.
- A302 (≠ G290) 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 (= W368) 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 (= D373) 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 (= R388) mutation to A: Reduction of binding affinity for fatty acids.
- S404 (= S395) mutation to A: Slight reduction of the fatty acyl-CoA ligase activity. Enhanced affinity towards palmitic acid binding.
- G406 (= G397) mutation to L: No effect on the formation of acyl-adenylate intermediate. However, it shows very poor catalytic efficiency to form acyl-CoA.
- K487 (= K479) 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.
4gxqA Crystal structure of atp bound rpmatb-bxbclm chimera b1 (see paper)
34% identity, 94% coverage: 20:487/496 of query aligns to 20:499/506 of 4gxqA
- active site: T163 (= T149), N183 (≠ T169), H207 (= H193), T303 (≠ S292), E304 (= E293), I403 (= I394), N408 (= N399), A491 (≠ K479)
- binding adenosine-5'-triphosphate: T163 (= T149), S164 (= S150), G165 (= G151), T166 (= T152), T167 (≠ S153), H207 (= H193), S277 (≠ G267), A278 (= A268), P279 (= P269), E298 (≠ D287), M302 (= M291), T303 (≠ S292), D382 (= D373), R397 (= R388)
- binding carbonate ion: H207 (= H193), S277 (≠ G267), R299 (≠ G288), G301 (= G290)
3r44A Mycobacterium tuberculosis fatty acyl coa synthetase (see paper)
34% identity, 98% coverage: 10:494/496 of query aligns to 14:502/502 of 3r44A
Sites not aligning to the query:
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)
30% identity, 93% coverage: 25:487/496 of query aligns to 61:571/590 of Q4WR83
Sites not aligning to the query:
- 6:14 PTS2-type peroxisomal targeting signal
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, 96% coverage: 10:487/496 of query aligns to 11:478/485 of 5x8fB
- active site: T151 (= T149), S171 (≠ T169), H195 (= H193), T288 (≠ S292), E289 (= E293), I387 (= I394), N392 (= N399), K470 (= K479)
- binding magnesium ion: Y23 (≠ A24), E24 (≠ N25), H70 (≠ L71), N178 (≠ L176), L202 (≠ S200), L214 (≠ V213), T296 (≠ G299), L297 (≠ M300), S298 (≠ P301)
- binding o-succinylbenzoyl-N-coenzyme A: K85 (≠ R86), L191 (≠ A189), P192 (= P190), H195 (= H193), I196 (= I194), S197 (≠ I195), A237 (≠ C238), V238 (= V239), L260 (≠ F264), G262 (= G266), G286 (= G290), M287 (= M291), S292 (≠ G295), Q293 (≠ T296), S388 (= S395), G389 (= G396), G390 (= G397), E391 (= E398), K420 (≠ R427), W421 (= W428), K450 (≠ R459), Y451 (= Y460)
5gtdA O-succinylbenzoate coa synthetase (mene) from bacillus subtilis in complex with the acyl-adenylate intermediate osb-amp (see paper)
29% identity, 96% coverage: 10:487/496 of query aligns to 11:478/484 of 5gtdA
- active site: T151 (= T149), S171 (≠ T169), H195 (= H193), T288 (≠ S292), E289 (= E293)
- binding adenosine-5'-monophosphate: G263 (= G267), G264 (≠ A268), Y285 (= Y289), G286 (= G290), M287 (= M291), T288 (≠ S292), D366 (= D373), V378 (≠ L385)
- binding magnesium ion: F314 (= F322), S315 (≠ T323)
- binding 2-succinylbenzoate: H195 (= H193), S197 (≠ I195), A237 (≠ C238), L260 (≠ F264), G262 (= G266), G263 (= G267), G286 (= G290), M287 (= M291), S292 (≠ G295), Q293 (≠ T296)
5upsA Acyl-coa synthetase ptma2 from streptomyces platensis in complex with sbnp663 ligand (see paper)
32% identity, 94% coverage: 12:478/496 of query aligns to 13:494/520 of 5upsA
- active site: T169 (= T149), M189 (≠ T169), H213 (= H193), T312 (≠ S292), E313 (= E293), K410 (≠ I394), N415 (= N399)
- binding 5'-O-[(R)-hydroxy{[(7beta,8alpha,9beta,10alpha,11beta,13alpha)-7-hydroxy-19-oxo-11,16-epoxykauran-19-yl]oxy}phosphoryl]adenosine: Y309 (= Y289), G310 (= G290), Q311 (≠ M291), T312 (≠ S292), G316 (= G299), F317 (≠ M300), D389 (= D373), F401 (≠ L385), K410 (≠ I394), N415 (= N399)
Sites not aligning to the query:
5uptA Acyl-coa synthetase ptma2 from streptomyces platensis in complex with sbnp468 ligand (see paper)
32% identity, 94% coverage: 12:478/496 of query aligns to 17:498/515 of 5uptA
- active site: T173 (= T149), M193 (≠ T169), H217 (= H193), T316 (≠ S292), E317 (= E293), K414 (≠ I394), N419 (= N399)
- binding (7alpha,8alpha,10alpha,13alpha)-7,16-dihydroxykauran-18-oic acid: Y87 (≠ N84), R89 (= R86), R89 (= R86), P214 (= P190), F216 (= F192), H217 (= H193), V241 (≠ F217), G314 (= G290)
Sites not aligning to the query:
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, 94% coverage: 16:480/496 of query aligns to 45:531/546 of Q84P21
- K530 (= K479) mutation to N: Lossed enzymatic activity.
5upqA Acyl-coa synthetase ptma2 from streptomyces platensis in complex with sbnp465 ligand (see paper)
32% identity, 94% coverage: 12:478/496 of query aligns to 16:495/512 of 5upqA
- active site: T172 (= T149), M190 (≠ T169), H214 (= H193), T313 (≠ S292), E314 (= E293), K411 (≠ I394)
- binding 5'-O-[(R)-{[(7beta,8alpha,9beta,10alpha,13alpha,16beta)-7,16-dihydroxy-18-oxokauran-18-yl]oxy}(hydroxy)phosphoryl]adenosine: H214 (= H193), F256 (= F237), G309 (= G288), Y310 (= Y289), G311 (= G290), Q312 (≠ M291), T313 (≠ S292), G317 (= G299), F318 (≠ M300), D390 (= D373), F402 (≠ L385)
Sites not aligning to the query:
5busA O-succinylbenzoate coenzyme a synthetase (mene) from bacillus subtilis, in complex with amp (see paper)
29% identity, 96% coverage: 10:487/496 of query aligns to 10:475/481 of 5busA
- active site: T150 (= T149), S170 (≠ T169), H194 (= H193), T287 (≠ S292), E288 (= E293)
- binding adenosine monophosphate: H194 (= H193), G262 (= G267), G263 (≠ A268), S283 (≠ G288), M286 (= M291), T287 (≠ S292), D365 (= D373), V377 (≠ L385), R380 (= R388), K467 (= K479)
5burA O-succinylbenzoate coenzyme a synthetase (mene) from bacillus subtilis, in complex with atp and magnesium ion (see paper)
29% identity, 96% coverage: 10:487/496 of query aligns to 10:475/475 of 5burA
- active site: T150 (= T149), S170 (≠ T169), H194 (= H193), T287 (≠ S292), E288 (= E293)
- binding adenosine-5'-triphosphate: T150 (= T149), S151 (= S150), T153 (= T152), T154 (≠ S153), K158 (= K157), G263 (≠ A268), S283 (≠ G288), T287 (≠ S292), D365 (= D373), V377 (≠ L385), R380 (= R388)
6qjzA Identificationand characterization of an oxalylfrom grass pea (lathyrus sativuscoa-synthetase l.) (see paper)
29% identity, 92% coverage: 21:474/496 of query aligns to 23:494/504 of 6qjzA
- active site: T169 (= T149), S189 (≠ T169), H213 (= H193), T314 (≠ S292), E315 (= E293), N414 (≠ I394), K419 (≠ N399)
- binding adenosine monophosphate: H213 (= H193), S288 (≠ G267), A289 (= A268), S290 (≠ P269), A312 (≠ G290), M313 (= M291), T314 (≠ S292), D393 (= D373), L405 (= L385), K410 (= K390), K419 (≠ N399)
Q4G176 Malonate--CoA ligase ACSF3, mitochondrial; Acyl-CoA synthetase family member 3; EC 6.2.1.76 from Homo sapiens (Human) (see 2 papers)
29% identity, 92% coverage: 28:485/496 of query aligns to 65:569/576 of Q4G176
- R354 (≠ G288) mutation to A: Impairs malonyl-CoA synthase activity.; mutation to L: Impairs malonyl-CoA synthase activity.
- V372 (≠ L306) 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)
31% identity, 95% coverage: 20:490/496 of query aligns to 22:511/514 of Q9SMT7
- TSGTT 170:174 (≠ TSGTS 149:153) binding
- H214 (= H193) binding ; mutation to A: Abolished activity.
- S289 (≠ G267) binding ; mutation to A: Abolished activity.
- SAS 289:291 (≠ GAP 267:269) binding
- EA 310:311 (≠ DG 287:288) binding
- M314 (= M291) binding
- T315 (≠ S292) binding
- H319 (≠ T296) binding ; mutation to A: Abolished activity.
- D394 (= D373) binding
- R409 (= R388) binding ; mutation to A: Abolished activity.
- K500 (= K479) binding ; binding ; mutation to A: Abolished activity.
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)
33% identity, 70% coverage: 144:488/496 of query aligns to 209:552/561 of P69451
- Y213 (= Y148) mutation to A: Loss of activity.
- T214 (= T149) mutation to A: 10% of wild-type activity.
- G216 (= G151) mutation to A: Decreases activity.
- T217 (= T152) mutation to A: Decreases activity.
- G219 (= G154) mutation to A: Decreases activity.
- K222 (= K157) mutation to A: Decreases activity.
- E361 (= E293) mutation to A: Loss of activity.
5ie2A Crystal structure of a plant enzyme (see paper)
31% identity, 95% coverage: 20:490/496 of query aligns to 22:506/506 of 5ie2A
- active site: T165 (= T149), S185 (≠ T169), H209 (= H193), T310 (≠ S292), E311 (= E293), N410 (≠ I394), K415 (≠ N399), K495 (= K479)
- binding adenosine-5'-triphosphate: T165 (= T149), S166 (= S150), G167 (= G151), T168 (= T152), T169 (≠ S153), S284 (≠ G267), A285 (= A268), S286 (≠ P269), Y307 (= Y289), A308 (≠ G290), M309 (= M291), T310 (≠ S292), D389 (= D373), L401 (= L385), R404 (= R388), K495 (= K479)
5ie3A Crystal structure of a plant enzyme (see paper)
31% identity, 95% coverage: 20:490/496 of query aligns to 22:504/504 of 5ie3A
- active site: T163 (= T149), S183 (≠ T169), H207 (= H193), T308 (≠ S292), E309 (= E293), N408 (≠ I394), K413 (≠ N399), K493 (= K479)
- binding adenosine monophosphate: S164 (= S150), S282 (≠ G267), A283 (= A268), S284 (≠ P269), Y305 (= Y289), A306 (≠ G290), M307 (= M291), T308 (≠ S292), D387 (= D373), L399 (= L385), R402 (= R388), K493 (= K479)
- binding oxalic acid: V208 (≠ I194), S282 (≠ G267), A306 (≠ G290), M307 (= M291), H312 (≠ T296), K493 (= K479)
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)
28% identity, 91% coverage: 37:485/496 of query aligns to 39:500/512 of O74976
- S283 (≠ G267) modified: Phosphoserine
- S284 (≠ A268) modified: Phosphoserine
5buqB Unliganded form of o-succinylbenzoate coenzyme a synthetase (mene) from bacillus subtilis, solved at 1.98 angstroms (see paper)
29% identity, 96% coverage: 10:487/496 of query aligns to 10:466/473 of 5buqB
Query Sequence
>CCNA_02483 FitnessBrowser__Caulo:CCNA_02483
MTPIDHVAFQARLQPGGLAAVELANGRRWTYAELDADIARAVGVLRRRGVGEGDRLAVLA
KNQVLLVILHLACARLGAMFAPLNWRLSASELHALIEDADPAMIVGDDQLAAAGLDGVDL
DVLRAEIDCADPDTRARADRERPSLILYTSGTSGRPKGALLSERNLDQTAINFGRLGKVT
HESVFLVDAPMFHIIGLITSIRPVLMHGGAILVSDGFEPARTLGRLGDPTLGITHYFCVP
QMAAMLRRQPAFDASALRRLTAIFTGGAPHPAPDIRAWLAEGIPMVDGYGMSEAGTVFGM
PADATLIDARAGSAGLCMPPVFTRIVDEQDRDCPPGVPGELLLKGDNVFRGYWRRPEDTA
RAFTEDGWFRTGDIALADAEGYHWLVDRKKDMFISGGENVYPAEIEAALADHPAILECAV
VGVPDPRWGEVGHLVVTCREGAVLDLALILSHLEDRLARYKLPKALTLVAALPRTASGKI
QKTVLRERLLAGDPRT
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