SitesBLAST
Comparing WP_011840694.1 NCBI__GCF_000015985.1:WP_011840694.1 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)
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)
32% identity, 85% coverage: 31:562/629 of query aligns to 3:495/512 of O74976
- S283 (= S343) modified: Phosphoserine
- S284 (≠ A344) modified: Phosphoserine
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, 87% coverage: 34:579/629 of query aligns to 31:561/561 of P69451
- Y213 (≠ H223) mutation to A: Loss of activity.
- T214 (= T224) mutation to A: 10% of wild-type activity.
- G216 (= G226) mutation to A: Decreases activity.
- T217 (= T227) mutation to A: Decreases activity.
- G219 (= G229) mutation to A: Decreases activity.
- K222 (= K232) mutation to A: Decreases activity.
- E361 (= E370) mutation to A: Loss of activity.
6qjzA Identificationand characterization of an oxalylfrom grass pea (lathyrus sativuscoa-synthetase l.) (see paper)
30% identity, 80% coverage: 60:563/629 of query aligns to 31:501/504 of 6qjzA
- active site: T169 (= T224), S189 (≠ M241), H213 (= H267), T314 (= T369), E315 (= E370), N414 (≠ I475), K419 (≠ N480)
- binding adenosine monophosphate: H213 (= H267), S288 (= S343), A289 (= A344), S290 (≠ P345), A312 (≠ G367), M313 (≠ L368), T314 (= T369), D393 (= D454), L405 (≠ I466), K410 (= K471), K419 (≠ N480)
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)
27% identity, 89% coverage: 27:583/629 of query aligns to 38:584/590 of Q4WR83
Sites not aligning to the query:
- 6:14 PTS2-type peroxisomal targeting signal
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, 85% coverage: 27:562/629 of query aligns to 5:501/514 of Q9SMT7
- TSGTT 170:174 (≠ TGGTT 224:228) binding ATP
- H214 (= H267) binding ATP; mutation to A: Abolished activity.
- S289 (= S343) binding oxalate; mutation to A: Abolished activity.
- SAS 289:291 (≠ SAP 343:345) binding ATP
- EA 310:311 (≠ EG 364:365) binding ATP
- M314 (≠ L368) binding oxalate
- T315 (= T369) binding ATP
- H319 (≠ C373) binding oxalate; mutation to A: Abolished activity.
- D394 (= D454) binding ATP
- R409 (= R469) binding ATP; mutation to A: Abolished activity.
- K500 (= K561) binding ATP; binding oxalate; mutation to A: Abolished 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, 81% coverage: 60:568/629 of query aligns to 30:494/503 of P9WQ37
- K172 (= K232) mutation to A: Slight reduction of the fatty acyl-CoA ligase activity. Slight increase of susceptibility to proteolysis.
- R195 (≠ Q254) mutation to A: Alteration of the strength of the membrane binding; when associated with A-9; A-17; A-197 and A-244.
- R197 (≠ T256) mutation to A: Alteration of the strength of the membrane binding; when associated with A-9; A-17; A-195 and A-244.
- V209 (= V268) 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 (= A270) mutation to G: Slight increase of the fatty acyl-CoA ligase activity. Reduced rate of proteolytic degradation.
- T214 (≠ P273) 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 (= R310) mutation to A: Alteration of the strength of the membrane binding; when associated with A-17; A-195; A-195 and A-197.
- A302 (≠ G367) 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 (≠ F449) 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 (= D454) 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 (= R469) mutation to A: Reduction of binding affinity for fatty acids.
- S404 (≠ R476) mutation to A: Slight reduction of the fatty acyl-CoA ligase activity. Enhanced affinity towards palmitic acid binding.
- G406 (= G478) mutation to L: No effect on the formation of acyl-adenylate intermediate. However, it shows very poor catalytic efficiency to form acyl-CoA.
- K487 (= K561) 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.
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)
25% identity, 83% coverage: 55:574/629 of query aligns to 53:543/546 of Q84P21
- K530 (= K561) mutation to N: Lossed enzymatic activity.
5ie2A Crystal structure of a plant enzyme (see paper)
28% identity, 85% coverage: 27:562/629 of query aligns to 5:496/506 of 5ie2A
- active site: T165 (= T224), S185 (≠ M241), H209 (= H267), T310 (= T369), E311 (= E370), N410 (≠ I475), K415 (≠ N480), K495 (= K561)
- binding adenosine-5'-triphosphate: T165 (= T224), S166 (≠ G225), G167 (= G226), T168 (= T227), T169 (= T228), S284 (= S343), A285 (= A344), S286 (≠ P345), Y307 (= Y366), A308 (≠ G367), M309 (≠ L368), T310 (= T369), D389 (= D454), L401 (≠ I466), R404 (= R469), K495 (= K561)
5ie3A Crystal structure of a plant enzyme (see paper)
28% identity, 85% coverage: 27:562/629 of query aligns to 5:494/504 of 5ie3A
- active site: T163 (= T224), S183 (≠ M241), H207 (= H267), T308 (= T369), E309 (= E370), N408 (≠ I475), K413 (≠ N480), K493 (= K561)
- binding adenosine monophosphate: S164 (≠ G225), S282 (= S343), A283 (= A344), S284 (≠ P345), Y305 (= Y366), A306 (≠ G367), M307 (≠ L368), T308 (= T369), D387 (= D454), L399 (≠ I466), R402 (= R469), K493 (= K561)
- binding oxalic acid: V208 (= V268), S282 (= S343), A306 (≠ G367), M307 (≠ L368), H312 (≠ C373), K493 (= K561)
5wm6A Crystal structure of cahj in complex with benzoyl adenylate (see paper)
29% identity, 89% coverage: 11:571/629 of query aligns to 16:535/535 of 5wm6A
- active site: S193 (≠ T224), N213 (= N244), H237 (= H267), A336 (≠ T369), E337 (= E370), N437 (≠ I475), K442 (≠ N480), K524 (= K561)
- binding magnesium ion: S301 (= S334), L303 (= L336), G326 (= G359)
- binding 5'-O-[(R)-(benzoyloxy)(hydroxy)phosphoryl]adenosine: F239 (= F269), G310 (≠ S343), S311 (≠ A344), K312 (≠ P345), V332 (≠ G365), F333 (≠ Y366), G334 (= G367), M335 (≠ L368), A336 (≠ T369), D416 (= D454), K433 (= K471), K442 (≠ N480)
5wm3A Crystal structure of cahj in complex with salicyl adenylate (see paper)
29% identity, 89% coverage: 11:571/629 of query aligns to 16:535/537 of 5wm3A
- active site: S193 (≠ T224), N213 (= N244), H237 (= H267), A336 (≠ T369), E337 (= E370), N437 (≠ I475), K442 (≠ N480), K524 (= K561)
- binding 9-(5-O-{(S)-hydroxy[(2-hydroxybenzene-1-carbonyl)oxy]phosphoryl}-alpha-L-lyxofuranosyl)-9H-purin-6-amine: N238 (≠ V268), F239 (= F269), G310 (≠ S343), S311 (≠ A344), K312 (≠ P345), V332 (≠ G365), F333 (≠ Y366), G334 (= G367), M335 (≠ L368), A336 (≠ T369), D416 (= D454), K433 (= K471), K442 (≠ N480)
- binding magnesium ion: S301 (= S334), L303 (= L336), G326 (= G359)
5wm2A Crystal structure of cahj in complex with salicylic acid and amp (see paper)
29% identity, 89% coverage: 11:571/629 of query aligns to 16:535/536 of 5wm2A
- active site: S193 (≠ T224), N213 (= N244), H237 (= H267), A336 (≠ T369), E337 (= E370), N437 (≠ I475), K442 (≠ N480), K524 (= K561)
- binding adenosine monophosphate: G310 (≠ S343), S311 (≠ A344), K312 (≠ P345), V332 (≠ G365), F333 (≠ Y366), G334 (= G367), M335 (≠ L368), A336 (≠ T369), E337 (= E370), D416 (= D454), V428 (≠ I466), K433 (= K471), K442 (≠ N480)
5jrhA Crystal structure of salmonella enterica acetyl-coa synthetase (acs) in complex with camp and coenzyme a (see paper)
27% identity, 92% coverage: 19:597/629 of query aligns to 65:639/640 of 5jrhA
- active site: T260 (= T224), T412 (= T369), E413 (= E370), N517 (≠ I475), R522 (≠ N480), K605 (= K561)
- binding (r,r)-2,3-butanediol: W93 (≠ F47), E140 (= E96), G169 (≠ A124), K266 (≠ M230), P267 (= P231)
- binding adenosine-3',5'-cyclic-monophosphate: G383 (≠ S343), E384 (≠ A344), P385 (= P345), T408 (≠ G365), W409 (≠ Y366), W410 (≠ G367), Q411 (≠ L368), T412 (= T369), D496 (= D454), I508 (= I466), N517 (≠ I475), R522 (≠ N480)
- binding coenzyme a: F159 (≠ N114), G160 (≠ P115), G161 (≠ L116), R187 (= R138), S519 (≠ G477), R580 (≠ H539), P585 (vs. gap)
- binding magnesium ion: V533 (≠ M491), H535 (= H493), I538 (≠ V496)
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)
32% identity, 56% coverage: 214:568/629 of query aligns to 141:477/485 of 5x8fB
- active site: T151 (= T224), S171 (≠ N244), H195 (= H267), T288 (= T369), E289 (= E370), I387 (= I475), N392 (= N480), K470 (= K561)
- binding magnesium ion: N178 (≠ R250), L202 (≠ I274), L214 (≠ F287), T296 (≠ S376), L297 (≠ V377), S298 (≠ N378)
- binding o-succinylbenzoyl-N-coenzyme A: L191 (= L263), P192 (= P264), H195 (= H267), I196 (≠ V268), S197 (≠ F269), A237 (≠ T316), V238 (= V317), L260 (≠ F340), G262 (= G342), G286 (= G367), M287 (≠ L368), S292 (≠ T372), Q293 (≠ C373), S388 (≠ R476), G389 (= G477), G390 (= G478), E391 (≠ H479), K420 (≠ F508), W421 (≠ A509), K450 (≠ R541), Y451 (≠ A542)
Sites not aligning to the query:
5gtdA O-succinylbenzoate coa synthetase (mene) from bacillus subtilis in complex with the acyl-adenylate intermediate osb-amp (see paper)
32% identity, 56% coverage: 214:568/629 of query aligns to 141:477/484 of 5gtdA
- active site: T151 (= T224), S171 (≠ N244), H195 (= H267), T288 (= T369), E289 (= E370)
- binding adenosine-5'-monophosphate: G263 (≠ S343), G264 (≠ A344), Y285 (= Y366), G286 (= G367), M287 (≠ L368), T288 (= T369), D366 (= D454), V378 (≠ I466)
- binding magnesium ion: F314 (≠ P394), S315 (≠ H395)
- binding 2-succinylbenzoate: H195 (= H267), S197 (≠ F269), A237 (≠ T316), L260 (≠ F340), G262 (= G342), G263 (≠ S343), G286 (= G367), M287 (≠ L368), S292 (≠ T372), Q293 (≠ C373)
1pg3A Acetyl coa synthetase, acetylated on lys609 (see paper)
27% identity, 89% coverage: 19:577/629 of query aligns to 65:621/634 of 1pg3A
- active site: T260 (= T224), T412 (= T369), E413 (= E370), N517 (≠ I475), R522 (≠ N480), K605 (= K561)
- binding coenzyme a: F159 (≠ N114), G160 (≠ P115), R187 (= R138), R190 (≠ P141), A301 (≠ L263), T307 (≠ F269), P330 (vs. gap), A356 (= A320), S519 (≠ G477), R580 (≠ H539), P585 (vs. gap)
- binding magnesium ion: V533 (≠ M491), H535 (= H493), I538 (≠ V496)
- binding adenosine-5'-monophosphate-propyl ester: G383 (≠ S343), E384 (≠ A344), P385 (= P345), T408 (≠ G365), W409 (≠ Y366), W410 (≠ G367), Q411 (≠ L368), T412 (= T369), D496 (= D454), R511 (= R469), R522 (≠ N480)
7kydA Drosophila melanogaster long-chain fatty-acyl-coa synthetase cg6178 (see paper)
26% identity, 81% coverage: 61:570/629 of query aligns to 53:532/534 of 7kydA
- binding 5'-O-[(S)-hydroxy(octanoyloxy)phosphoryl]adenosine: H240 (= H267), F242 (= F269), A311 (≠ S343), A312 (= A344), P313 (= P345), G334 (= G365), Y335 (= Y366), G336 (= G367), L337 (= L368), S338 (≠ T369), S343 (≠ L374), D416 (= D454), I428 (= I466)
P38137 Oxalate--CoA ligase; Acyl-activating enzyme 3; Oxalyl-CoA synthetase; Peroxisomal-coenzyme A synthetase; EC 6.2.1.8 from Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) (see paper)
27% identity, 79% coverage: 80:576/629 of query aligns to 58:533/543 of P38137
Sites not aligning to the query:
- 541:543 C-terminal peroxisome targeting signal (PTS1)
2p2fA Acetyl-coa synthetase, wild-type with acetate, amp, and coa bound (see paper)
27% identity, 92% coverage: 19:597/629 of query aligns to 64:636/637 of 2p2fA
- active site: T259 (= T224), T411 (= T369), E412 (= E370), N516 (≠ I475), R521 (≠ N480), K604 (= K561)
- binding adenosine monophosphate: G382 (≠ S343), E383 (≠ A344), P384 (= P345), T407 (≠ G365), W408 (≠ Y366), W409 (≠ G367), Q410 (≠ L368), T411 (= T369), D495 (= D454), I507 (= I466), R510 (= R469), N516 (≠ I475), R521 (≠ N480)
- binding coenzyme a: F158 (≠ N114), R186 (= R138), W304 (≠ H267), T306 (≠ F269), P329 (vs. gap), A352 (≠ V317), A355 (= A320), S518 (≠ G477), R579 (≠ H539), P584 (vs. gap)
2p20A Acetyl-coa synthetase, r584a mutation (see paper)
27% identity, 92% coverage: 19:597/629 of query aligns to 65:640/641 of 2p20A
- active site: T260 (= T224), T412 (= T369), E413 (= E370), N517 (≠ I475), R522 (≠ N480), K605 (= K561)
- binding adenosine-5'-monophosphate-propyl ester: G383 (≠ S343), E384 (≠ A344), P385 (= P345), T408 (≠ G365), W409 (≠ Y366), W410 (≠ G367), Q411 (≠ L368), T412 (= T369), D496 (= D454), I508 (= I466), R511 (= R469), R522 (≠ N480)
Query Sequence
>WP_011840694.1 NCBI__GCF_000015985.1:WP_011840694.1
MGSFACAADLRAIEAEGAWADLGTPRTMHRFLGRAAAEHGDRPAVSFQLLSAPKSRAETL
SWSQLHRRVTQAANLFRSLGVGERDVVAFVLPNCTETAVTLLGGAVAGIVNPINPLLEAN
QIAAILRETKARVVVTLRAFPKTDVAQKVAEAVRHAPEVRTVLEVDLLRYLGPPKSLIVP
LIRPKLKPAHHARVLSFNAELDRQPATLAFPDPETDRVAAYFHTGGTTGMPKVAQHKVSG
MIYNGWCGQRLLFQPTDTVMCPLPLFHVFAAYPILMSMIASGAHVVFPTPAGYRGEGVFD
NLWKLIERWRCTYLVTVPTALAALMQRPIDADVSSLRGAFSGSAPLPVELFNRFEKATGV
QIVEGYGLTECTCLVSVNPPEGAKKIGSVGLPFPHTHVRILHSNGSGHVLKECGVDEVGE
ICVANPGVYEGSTYTELDKNHGLFAEDRFLRTGDLGRLDAEGYLFITGRAKDLIIRGGHN
IDPAGIEAALMSHPAVSFVGAIGQPDAFAGELPCAYVELVQGAEVETAALFDHARAHIHE
RAAVPKHIEILPELPKTAVGKVFKPDLRRLAIARVYDAALASAGLPVRVAEVVEDRKRGL
VARLERAGEVDEERLAHVLGEYTRPWEWA
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