SitesBLAST
Comparing WP_011781165.1 NCBI__GCF_000015305.1:WP_011781165.1 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)
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)
41% identity, 51% coverage: 507:1041/1043 of query aligns to 22:577/590 of Q4WR83
Sites not aligning to the query:
- 6:14 PTS2-type peroxisomal targeting signal
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)
36% identity, 48% coverage: 11:508/1043 of query aligns to 8:501/503 of P9WQ37
- R9 (≠ A12) mutation to A: Alteration of the strength of the membrane binding; when associated with A-9; A-195; A-197 and A-244.
- R17 (≠ H20) mutation to A: Alteration of the strength of the membrane binding; when associated with A-9; A-17; A-197 and A-244.
- K172 (= K171) mutation to A: Slight reduction of the fatty acyl-CoA ligase activity. Slight increase of susceptibility to proteolysis.
- R195 (= R194) mutation to A: Alteration of the strength of the membrane binding; when associated with A-9; A-17; A-197 and A-244.
- R197 (≠ D196) mutation to A: Alteration of the strength of the membrane binding; when associated with A-9; A-17; A-195 and A-244.
- V209 (≠ T209) 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 (≠ G211) mutation to G: Slight increase of the fatty acyl-CoA ligase activity. Reduced rate of proteolytic degradation.
- T214 (≠ G214) 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 (≠ Q246) mutation to A: Alteration of the strength of the membrane binding; when associated with A-17; A-195; A-195 and A-197.
- A302 (≠ G306) 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 (= W382) 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 (= D387) 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 (= R402) mutation to A: Reduction of binding affinity for fatty acids.
- S404 (= S409) mutation to A: Slight reduction of the fatty acyl-CoA ligase activity. Enhanced affinity towards palmitic acid binding.
- G406 (= G411) mutation to L: No effect on the formation of acyl-adenylate intermediate. However, it shows very poor catalytic efficiency to form acyl-CoA.
- K487 (= K494) 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)
35% identity, 48% coverage: 11:508/1043 of query aligns to 11:501/502 of 3r44A
Sites not aligning to the query:
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)
35% identity, 47% coverage: 11:502/1043 of query aligns to 8:478/485 of 5x8fB
- active site: T151 (= T163), S171 (≠ H183), H195 (= H208), T288 (= T308), E289 (= E309), I387 (= I408), N392 (= N413), K470 (= K494)
- binding magnesium ion: Y23 (≠ D26), E24 (≠ P27), H70 (≠ L73), N178 (≠ T190), L202 (≠ M215), L214 (≠ I227), T296 (≠ C315), L297 (= L316), S298 (≠ R318)
- binding o-succinylbenzoyl-N-coenzyme A: K85 (≠ R88), L191 (≠ A204), P192 (= P205), H195 (= H208), I196 (≠ T209), S197 (≠ A210), A237 (= A255), V238 (≠ Q256), L260 (≠ W278), G262 (= G280), G286 (= G306), M287 (≠ Q307), S292 (= S311), Q293 (≠ P312), S388 (= S409), G389 (= G410), G390 (= G411), E391 (= E412), K420 (= K441), W421 (= W442), K450 (≠ S474), Y451 (= Y475)
5gtdA O-succinylbenzoate coa synthetase (mene) from bacillus subtilis in complex with the acyl-adenylate intermediate osb-amp (see paper)
35% identity, 47% coverage: 11:502/1043 of query aligns to 8:478/484 of 5gtdA
- active site: T151 (= T163), S171 (≠ H183), H195 (= H208), T288 (= T308), E289 (= E309)
- binding adenosine-5'-monophosphate: G263 (≠ A281), G264 (≠ A282), Y285 (≠ F305), G286 (= G306), M287 (≠ Q307), T288 (= T308), D366 (= D387), V378 (= V399)
- binding magnesium ion: F314 (≠ L334), S315 (≠ N335)
- binding 2-succinylbenzoate: H195 (= H208), S197 (≠ A210), A237 (= A255), L260 (≠ W278), G262 (= G280), G263 (≠ A281), G286 (= G306), M287 (≠ Q307), S292 (= S311), Q293 (≠ P312)
5burA O-succinylbenzoate coenzyme a synthetase (mene) from bacillus subtilis, in complex with atp and magnesium ion (see paper)
34% identity, 47% coverage: 11:502/1043 of query aligns to 7:475/475 of 5burA
- active site: T150 (= T163), S170 (≠ H183), H194 (= H208), T287 (= T308), E288 (= E309)
- binding adenosine-5'-triphosphate: T150 (= T163), S151 (= S164), T153 (= T166), T154 (= T167), K158 (= K171), G263 (≠ A282), S283 (≠ A304), T287 (= T308), D365 (= D387), V377 (= V399), R380 (= R402)
5busA O-succinylbenzoate coenzyme a synthetase (mene) from bacillus subtilis, in complex with amp (see paper)
34% identity, 47% coverage: 11:502/1043 of query aligns to 7:475/481 of 5busA
- active site: T150 (= T163), S170 (≠ H183), H194 (= H208), T287 (= T308), E288 (= E309)
- binding adenosine monophosphate: H194 (= H208), G262 (≠ A281), G263 (≠ A282), S283 (≠ A304), M286 (≠ Q307), T287 (= T308), D365 (= D387), V377 (= V399), R380 (= R402), K467 (= K494)
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)
33% identity, 45% coverage: 31:504/1043 of query aligns to 48:534/541 of Q5SKN9
- T184 (= T163) binding Mg(2+)
- G302 (≠ A281) binding tetradecanoyl-AMP
- Q322 (≠ A303) binding tetradecanoyl-AMP
- G323 (≠ A304) binding tetradecanoyl-AMP
- T327 (= T308) binding tetradecanoyl-AMP
- E328 (= E309) binding Mg(2+)
- D418 (= D387) binding tetradecanoyl-AMP
- K435 (= K404) binding tetradecanoyl-AMP
- K439 (≠ I408) binding tetradecanoyl-AMP
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, 47% coverage: 540:1033/1043 of query aligns to 48:536/546 of Q84P21
- K530 (= K1027) mutation to N: Lossed enzymatic activity.
P0DX84 3-methylmercaptopropionyl-CoA ligase; MMPA-CoA ligase; EC 6.2.1.44 from Ruegeria lacuscaerulensis (strain DSM 11314 / KCTC 2953 / ITI-1157) (Silicibacter lacuscaerulensis) (see paper)
32% identity, 45% coverage: 31:503/1043 of query aligns to 40:532/539 of P0DX84
- H231 (= H208) mutation to A: Retains 74% of wild-type activity.
- W235 (≠ V212) mutation to A: Almost completely abolishes the activity.
- G302 (= G280) mutation to P: Almost completely abolishes the activity.
- G303 (≠ A281) mutation to P: Almost completely abolishes the activity.
- W326 (≠ F305) mutation to A: Retains 7.7% of wild-type activity.
- P333 (= P312) mutation to A: Retains 69% of wild-type activity.
- R432 (= R402) mutation to A: Retains 4.3% of wild-type activity.
- K434 (= K404) mutation to A: Retains 36% of wild-type activity.
- D435 (= D405) mutation to A: Retains 76% of wild-type activity.
- K438 (≠ I408) mutation to A: Retains 5.6% of wild-type activity.
- G440 (= G410) mutation to P: Retains 3.6% of wild-type activity.
- G441 (= G411) mutation to P: Retains 2.7% of wild-type activity.
- E442 (= E412) mutation to A: Retains 27% of wild-type activity.
- W443 (≠ N413) mutation to A: Retains 60% of wild-type activity.
- E474 (= E444) mutation to A: Retains 33% of wild-type activity.
- K523 (= K494) Plays an important role in catalysis; mutation to A: Retains 1.6% of wild-type activity.; mutation to E: Retains 1.4% of wild-type activity.; mutation to R: Retains 57% of wild-type activity.
- K526 (= K497) mutation to A: Retains 48% of wild-type activity.
6ijbB Structure of 3-methylmercaptopropionate coa ligase mutant k523a in complex with amp and mmpa (see paper)
31% identity, 45% coverage: 31:503/1043 of query aligns to 40:532/538 of 6ijbB
- active site: T185 (= T163), H205 (= H183), H231 (= H208), S329 (≠ T308), E330 (= E309), K438 (≠ I408), W443 (≠ N413), A523 (≠ K494)
- binding 3-(methylsulfanyl)propanoic acid: W235 (≠ V212), G303 (≠ A281), A325 (= A304), W326 (≠ F305), G327 (= G306), M328 (≠ Q307)
- binding adenosine monophosphate: G303 (≠ A281), A304 (= A282), A305 (≠ P283), H324 (≠ A303), W326 (≠ F305), G327 (= G306), M328 (≠ Q307), S329 (≠ T308), Q359 (≠ V329), D417 (= D387)
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, 49% coverage: 528:1035/1043 of query aligns to 43:548/556 of Q9S725
- K211 (= K702) mutation to S: Drastically reduces the activity.
- M293 (≠ Y781) mutation M->A,P: Affects the substrate specificity.
- K320 (≠ I808) mutation K->L,A: Affects the substrate specificity.
- E401 (= E887) mutation to Q: Slighlty reduces the substrate specificity.
- C403 (= C889) mutation to A: Significantly reduces the substrate specificity.
- R449 (= R935) mutation to Q: Drastically reduces the activity.
- K457 (≠ G943) mutation to S: Drastically reduces the activity.
- K540 (= K1027) mutation to N: Abolishes the activity.
5upsA Acyl-coa synthetase ptma2 from streptomyces platensis in complex with sbnp663 ligand (see paper)
34% identity, 47% coverage: 6:493/1043 of query aligns to 3:494/520 of 5upsA
- active site: T169 (= T163), M189 (≠ H183), H213 (= H208), T312 (= T308), E313 (= E309), K410 (≠ I408), N415 (= N413)
- binding 5'-O-[(R)-hydroxy{[(7beta,8alpha,9beta,10alpha,11beta,13alpha)-7-hydroxy-19-oxo-11,16-epoxykauran-19-yl]oxy}phosphoryl]adenosine: Y309 (≠ F305), G310 (= G306), Q311 (= Q307), T312 (= T308), G316 (vs. gap), F317 (vs. gap), D389 (= D387), F401 (≠ V399), K410 (≠ I408), N415 (= N413)
Sites not aligning to the query:
5uptA Acyl-coa synthetase ptma2 from streptomyces platensis in complex with sbnp468 ligand (see paper)
34% identity, 47% coverage: 6:493/1043 of query aligns to 7:498/515 of 5uptA
- active site: T173 (= T163), M193 (≠ H183), H217 (= H208), T316 (= T308), E317 (= E309), K414 (≠ I408), N419 (= N413)
- binding (7alpha,8alpha,10alpha,13alpha)-7,16-dihydroxykauran-18-oic acid: Y87 (≠ N86), R89 (= R88), R89 (= R88), P214 (= P205), F216 (= F207), H217 (= H208), V241 (≠ F233), G314 (= G306)
Sites not aligning to the query:
4gxqA Crystal structure of atp bound rpmatb-bxbclm chimera b1 (see paper)
31% identity, 49% coverage: 528:1034/1043 of query aligns to 6:498/506 of 4gxqA
- active site: T163 (= T694), N183 (= N714), H207 (= H738), T303 (= T838), E304 (= E839), I403 (= I941), N408 (= N946), A491 (≠ K1027)
- binding adenosine-5'-triphosphate: T163 (= T694), S164 (= S695), G165 (= G696), T166 (= T697), T167 (= T698), H207 (= H738), S277 (≠ G811), A278 (≠ S812), P279 (= P813), E298 (≠ I833), M302 (= M837), T303 (= T838), D382 (= D920), R397 (= R935)
- binding carbonate ion: H207 (= H738), S277 (≠ G811), R299 (≠ A834), G301 (= G836)
4wv3B Crystal structure of the anthranilate coa ligase auaeii in complex with anthranoyl-amp (see paper)
32% identity, 47% coverage: 9:502/1043 of query aligns to 14:510/518 of 4wv3B
- active site: S175 (≠ T163), T320 (= T308), E321 (= E309), K418 (≠ I408), W423 (≠ N413), K502 (= K494)
- binding 5'-O-[(S)-[(2-aminobenzoyl)oxy](hydroxy)phosphoryl]adenosine: F220 (≠ H208), T221 (= T209), F222 (≠ A210), A293 (= A281), S294 (≠ A282), E295 (≠ P283), A296 (= A284), G316 (≠ A304), I317 (≠ F305), G318 (= G306), C319 (≠ Q307), T320 (= T308), D397 (= D387), H409 (≠ V399), R412 (= R402), K502 (= K494)
5upqA Acyl-coa synthetase ptma2 from streptomyces platensis in complex with sbnp465 ligand (see paper)
34% identity, 47% coverage: 6:493/1043 of query aligns to 6:495/512 of 5upqA
- active site: T172 (= T163), M190 (≠ H183), H214 (= H208), T313 (= T308), E314 (= E309), K411 (≠ I408)
- binding 5'-O-[(R)-{[(7beta,8alpha,9beta,10alpha,13alpha,16beta)-7,16-dihydroxy-18-oxokauran-18-yl]oxy}(hydroxy)phosphoryl]adenosine: H214 (= H208), F256 (≠ W251), G309 (≠ A304), Y310 (≠ F305), G311 (= G306), Q312 (= Q307), T313 (= T308), G317 (vs. gap), F318 (vs. gap), D390 (= D387), F402 (≠ V399)
Sites not aligning to the query:
6ihkB Structure of mmpa coa ligase in complex with adp (see paper)
31% identity, 45% coverage: 31:503/1043 of query aligns to 40:529/533 of 6ihkB
- active site: T185 (= T163), H202 (= H183), H228 (= H208), S326 (≠ T308), E327 (= E309), K435 (≠ I408), W440 (≠ N413), K520 (= K494)
- binding adenosine-5'-diphosphate: H228 (= H208), G300 (≠ A281), A301 (= A282), A302 (≠ P283), H321 (≠ A303), A322 (= A304), W323 (≠ F305), G324 (= G306), M325 (≠ Q307), S326 (≠ T308), Q356 (≠ V329), D414 (= D387), R429 (= R402), K520 (= K494)
5buqB Unliganded form of o-succinylbenzoate coenzyme a synthetase (mene) from bacillus subtilis, solved at 1.98 angstroms (see paper)
33% identity, 47% coverage: 11:502/1043 of query aligns to 7:466/473 of 5buqB
6e97B Crystal structure of the aryl acid adenylating enzyme fscc from fuscachelin nrps in complex with dhb-adenylate
31% identity, 50% coverage: 522:1041/1043 of query aligns to 22:536/537 of 6e97B
- active site: S190 (≠ T694), S210 (≠ N714), H234 (= H738), A336 (≠ T838), E337 (= E839), N437 (≠ I941), K442 (≠ N946), K522 (= K1027)
- binding 5'-O-[(S)-[(2,3-dihydroxybenzene-1-carbonyl)oxy](hydroxy)phosphoryl]adenosine: H234 (= H738), N235 (≠ C739), F236 (= F740), S240 (≠ M744), G310 (= G811), A311 (≠ S812), K312 (≠ P813), V332 (≠ A834), F333 (≠ Y835), G334 (= G836), M335 (= M837), A336 (≠ T838), D416 (= D920), K433 (= K937), K442 (≠ N946)
Query Sequence
>WP_011781165.1 NCBI__GCF_000015305.1:WP_011781165.1
MITGITLSDALARHAAVRPHACALADPRRHTTFGELDERVTRLASALAARGVRSGDRVAV
LGLNSIELVESWLAAHRLGAIAVPVNFRLAAGEIGYVLSDSAATAIVVDVALESMVVQVR
QQVPALHTVVTIGGNLEQTIAAADPDLPQCAVADDAPAFIMYTSGTTGFPKGAVLTHRNL
YLHAFSSIATLGHRSDDDCWMAVAPLFHTAGVSGMLPMFLTGGKTVIPPSGGFDPDATIA
AVVDEQVTSCWMTPAQWQSVCALPGLAAHDLSRLRRVWWGAAPASTTLLRTMIDTFTGAE
IIAAFGQTECSPITCLLRGEDAIAKIGSVGTPMLNVEVRVVDDEMNDVDRGEVGEIVYLG
PLVMKEYWNKAAETAEAFRGGWFHSGDLVRQDADGYFYVVDRKKDMIISGGENIYSAEVE
NVVATHPLVAEVAVIGVPHPKWGETPVAVIVPREPTDPPTDAEIEAHCRAQLASYKRPKY
VTLVDVLPRNAAGKVLKGRLRDEHATLISYSAGPTDAALLDETIGTNFERTVSRYPDNEA
LVDVPSGRRWTYAELNAEIDSLARALMAIGIEKGDRVGIWAPNCPEWTMLQYATAKIGAI
LVTINPAYRTHELAYVLRHSAVRLLVSATEFKTSDYRAMVAEVRPELPGLAEVLFLATED
WARLGERADLVSEDELRCRVRSLTPGDAINIQYTSGTTGSPKGATLSHRNILNNGYFVTD
LIDFGPGDRLCIPVPFYHCFGMVMGNLGCTTHGATMVIPAAGFDPAATLAAIEKEHCTAV
YGVPTMFIAMLGHPDLADCDVTSLRTGIMAGSPCPVEVMKRCVNELKMSEVGIAYGMTET
SPVSCQTRIEDDLDRRTATVGRAHPHVEIKIVDPDTGEIVKRGTAGEFCTRGYSVMLGYW
GDEDRTREAVDADGWMHTGDLAVMRDDGYCMIVGRIKDMVIRGGENVYPREIEEFLHTHP
DIDDVQVIGVPDERYGEEICAWIKVRAGAAPLDAHAVREFAAGKLAHYKIPRYVHMTDDF
PMTVTGKVRKIDMRAETVRILGL
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