SitesBLAST
Comparing PP_3458 FitnessBrowser__Putida:PP_3458 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)
42% identity, 98% coverage: 5:555/562 of query aligns to 24:578/590 of Q4WR83
Sites not aligning to the query:
- 6:14 PTS2-type peroxisomal targeting signal
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)
32% identity, 96% coverage: 10:548/562 of query aligns to 15:551/561 of P69451
- Y213 (= Y208) mutation to A: Loss of activity.
- T214 (= T209) mutation to A: 10% of wild-type activity.
- G216 (= G211) mutation to A: Decreases activity.
- T217 (= T212) mutation to A: Decreases activity.
- G219 (= G214) mutation to A: Decreases activity.
- K222 (= K217) mutation to A: Decreases activity.
- E361 (= E354) mutation to A: Loss of activity.
4gxqA Crystal structure of atp bound rpmatb-bxbclm chimera b1 (see paper)
32% identity, 90% coverage: 45:548/562 of query aligns to 28:499/506 of 4gxqA
- active site: T163 (= T209), N183 (= N229), H207 (= H253), T303 (= T353), E304 (= E354), I403 (= I455), N408 (= N460), A491 (≠ K540)
- binding adenosine-5'-triphosphate: T163 (= T209), S164 (= S210), G165 (= G211), T166 (= T212), T167 (= T213), H207 (= H253), S277 (≠ G326), A278 (= A327), P279 (≠ T328), E298 (≠ Q347), M302 (= M352), T303 (= T353), D382 (= D434), R397 (= R449)
- binding carbonate ion: H207 (= H253), S277 (≠ G326), R299 (≠ A349), G301 (= G351)
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)
30% identity, 93% coverage: 26:548/562 of query aligns to 12:495/503 of P9WQ37
- R17 (≠ D33) mutation to A: Alteration of the strength of the membrane binding; when associated with A-9; A-17; A-197 and A-244.
- K172 (= K217) mutation to A: Slight reduction of the fatty acyl-CoA ligase activity. Slight increase of susceptibility to proteolysis.
- R195 (≠ T240) mutation to A: Alteration of the strength of the membrane binding; when associated with A-9; A-17; A-197 and A-244.
- R197 (≠ H242) mutation to A: Alteration of the strength of the membrane binding; when associated with A-9; A-17; A-195 and A-244.
- V209 (≠ C254) 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 (≠ G256) mutation to G: Slight increase of the fatty acyl-CoA ligase activity. Reduced rate of proteolytic degradation.
- T214 (≠ M259) 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 (≠ K291) mutation to A: Alteration of the strength of the membrane binding; when associated with A-17; A-195; A-195 and A-197.
- A302 (≠ G351) 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 (= W429) 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 (= D434) 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 (= R449) mutation to A: Reduction of binding affinity for fatty acids.
- S404 (≠ R456) mutation to A: Slight reduction of the fatty acyl-CoA ligase activity. Enhanced affinity towards palmitic acid binding.
- G406 (= G458) mutation to L: No effect on the formation of acyl-adenylate intermediate. However, it shows very poor catalytic efficiency to form acyl-CoA.
- K487 (= K540) 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.
3r44A Mycobacterium tuberculosis fatty acyl coa synthetase (see paper)
30% identity, 93% coverage: 26:548/562 of query aligns to 15:495/502 of 3r44A
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)
27% identity, 93% coverage: 34:555/562 of query aligns to 46:545/546 of Q84P21
- K530 (= K540) mutation to N: Lossed enzymatic activity.
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, 90% coverage: 36:543/562 of query aligns to 18:497/512 of O74976
- S283 (≠ T328) modified: Phosphoserine
- S284 (≠ C329) modified: Phosphoserine
4wv3B Crystal structure of the anthranilate coa ligase auaeii in complex with anthranoyl-amp (see paper)
30% identity, 92% coverage: 32:547/562 of query aligns to 32:509/518 of 4wv3B
- active site: S175 (≠ T209), T320 (= T353), E321 (= E354), K418 (≠ I455), W423 (≠ N460), K502 (= K540)
- binding 5'-O-[(S)-[(2-aminobenzoyl)oxy](hydroxy)phosphoryl]adenosine: F220 (≠ H253), T221 (≠ C254), F222 (= F255), A293 (= A325), S294 (≠ G326), E295 (≠ A327), A296 (≠ T328), G316 (≠ A349), I317 (≠ Y350), G318 (= G351), C319 (≠ M352), T320 (= T353), D397 (= D434), H409 (≠ I446), R412 (= R449), K502 (= K540)
O24146 4-coumarate--CoA ligase 2; 4CL 2; Nt4CL-19; Nt4CL-2; 4-coumaroyl-CoA synthase 2; Caffeate--CoA ligase; Cinnamate--CoA ligase; Ferulate--CoA ligase; EC 6.2.1.12; EC 6.2.1.-; EC 6.2.1.-; EC 6.2.1.34 from Nicotiana tabacum (Common tobacco) (see paper)
28% identity, 95% coverage: 14:547/562 of query aligns to 26:533/542 of O24146
- S189 (≠ T209) binding
- S190 (= S210) binding
- G191 (= G211) binding
- T192 (= T212) binding
- T193 (= T213) binding ; mutation to A: Reduced activity against 4-coumarate.
- K197 (= K217) binding ; mutation to A: Reduced activity against 4-coumarate.
- H237 (= H253) mutation to A: Strongly reduced activity against 4-coumarate.
- Y239 (≠ F255) binding ; binding ; binding ; mutation to A: Strongly reduced activity against 4-coumarate.; mutation to F: Reduced activity against 4-coumarate.
- S243 (≠ M259) binding ; binding ; binding
- K260 (≠ A277) binding
- A309 (≠ G326) binding ; binding ; binding
- Q331 (≠ I348) binding
- G332 (≠ A349) binding ; binding ; binding ; binding ; binding
- T336 (= T353) binding ; binding ; binding ; binding ; binding ; mutation to A: Strongly reduced activity against 4-coumarate.
- V341 (= V358) mutation to G: Reduced activity against 4-coumarate.; mutation Missing: Reduced activity against 4-coumarate, but acquired ability to use sinapate as substrate.
- M344 (≠ Q361) binding ; binding ; binding ; mutation to A: Reduced activity against 4-coumarate.
- D420 (= D434) binding ; binding ; binding ; binding ; binding
- R435 (= R449) binding ; binding ; binding ; binding ; mutation to A: Strongly reduced activity against 4-coumarate.
- K437 (= K451) binding ; binding ; binding ; binding
- K441 (≠ I455) binding ; binding ; binding ; binding ; mutation to A: Abolished activity against 4-coumarate.
- K443 (≠ G457) binding ; mutation to A: Normal activity against 4-coumarate.
- G444 (= G458) binding
- Q446 (≠ N460) binding
- K526 (= K540) binding ; mutation to A: Abolished activity against 4-coumarate.
5bsmA Crystal structure of 4-coumarate:coa ligase complexed with magnesium and adenosine triphosphate (see paper)
28% identity, 95% coverage: 14:547/562 of query aligns to 19:526/530 of 5bsmA
- active site: S182 (≠ T209), S202 (≠ N229), H230 (= H253), T329 (= T353), E330 (= E354), K434 (≠ I455), Q439 (≠ N460), K519 (= K540)
- binding adenosine-5'-triphosphate: S182 (≠ T209), S183 (= S210), G184 (= G211), T185 (= T212), T186 (= T213), K190 (= K217), H230 (= H253), A302 (≠ G326), A303 (= A327), P304 (≠ T328), Y326 (= Y350), G327 (= G351), M328 (= M352), T329 (= T353), D413 (= D434), I425 (= I446), R428 (= R449), K519 (= K540)
5bsvA Crystal structure of 4-coumarate:coa ligase complexed with feruloyl adenylate (see paper)
28% identity, 95% coverage: 14:547/562 of query aligns to 19:526/529 of 5bsvA
- active site: S182 (≠ T209), S202 (≠ N229), H230 (= H253), T329 (= T353), E330 (= E354), K434 (≠ I455), Q439 (≠ N460), K519 (= K540)
- binding 5'-O-[(R)-hydroxy{[(2E)-3-(5-methoxy-4-oxocyclohexa-1,5-dien-1-yl)prop-2-enoyl]oxy}phosphoryl]adenosine: H230 (= H253), Y232 (≠ F255), S236 (≠ M259), A302 (≠ G326), A303 (= A327), P304 (≠ T328), G325 (≠ A349), G327 (= G351), M328 (= M352), T329 (= T353), P333 (= P357), V334 (= V358), D413 (= D434), K430 (= K451), K434 (≠ I455), Q439 (≠ N460)
5bsuA Crystal structure of 4-coumarate:coa ligase complexed with caffeoyl adenylate (see paper)
28% identity, 95% coverage: 14:547/562 of query aligns to 19:526/529 of 5bsuA
- active site: S182 (≠ T209), S202 (≠ N229), H230 (= H253), T329 (= T353), E330 (= E354), K434 (≠ I455), Q439 (≠ N460), K519 (= K540)
- binding 5'-O-[(R)-{[(2E)-3-(3,4-dioxocyclohexa-1,5-dien-1-yl)prop-2-enoyl]oxy}(hydroxy)phosphoryl]adenosine: H230 (= H253), Y232 (≠ F255), S236 (≠ M259), M299 (≠ I323), A302 (≠ G326), A303 (= A327), P304 (≠ T328), G325 (≠ A349), G327 (= G351), M328 (= M352), T329 (= T353), P333 (= P357), D413 (= D434), K430 (= K451), K434 (≠ I455), Q439 (≠ N460)
5bstA Crystal structure of 4-coumarate:coa ligase complexed with coumaroyl adenylate (see paper)
28% identity, 95% coverage: 14:547/562 of query aligns to 19:526/529 of 5bstA
- active site: S182 (≠ T209), S202 (≠ N229), H230 (= H253), T329 (= T353), E330 (= E354), K434 (≠ I455), Q439 (≠ N460), K519 (= K540)
- binding 5'-O-[(R)-hydroxy{[(2E)-3-(4-oxocyclohexa-1,5-dien-1-yl)prop-2-enoyl]oxy}phosphoryl]adenosine: H230 (= H253), Y232 (≠ F255), S236 (≠ M259), A302 (≠ G326), A303 (= A327), P304 (≠ T328), G325 (≠ A349), Y326 (= Y350), G327 (= G351), M328 (= M352), T329 (= T353), P333 (= P357), V334 (= V358), D413 (= D434), K430 (= K451), K434 (≠ I455), Q439 (≠ N460)
5bsrA Crystal structure of 4-coumarate:coa ligase complexed with adenosine monophosphate and coenzyme a (see paper)
28% identity, 95% coverage: 14:547/562 of query aligns to 18:525/528 of 5bsrA
- active site: S181 (≠ T209), S201 (≠ N229), H229 (= H253), T328 (= T353), E329 (= E354), K433 (≠ I455), Q438 (≠ N460), K518 (= K540)
- binding adenosine monophosphate: A301 (≠ G326), G326 (= G351), T328 (= T353), D412 (= D434), K429 (= K451), K433 (≠ I455), Q438 (≠ N460)
- binding coenzyme a: L102 (≠ A103), P226 (= P250), H229 (= H253), Y231 (≠ F255), F253 (= F278), K435 (≠ G457), G436 (= G458), F437 (≠ E459), F498 (≠ H520)
5u95B Structure of the open conformation of 4-coumarate-coa ligase from nicotiana tabacum
28% identity, 95% coverage: 14:547/562 of query aligns to 18:522/527 of 5u95B
6k4dA Ancestral luciferase anclamp in complex with atp and d-luciferin (see paper)
28% identity, 93% coverage: 29:549/562 of query aligns to 32:536/539 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 (= H253), F245 (= F255), T249 (≠ A260), G314 (= G326), A315 (= A327), P316 (≠ T328), G337 (≠ A349), Y338 (= Y350), G339 (= G351), L340 (≠ M352), T341 (= T353), S345 (≠ P357), A346 (≠ V358), D420 (= D434), I432 (= I446), K527 (= K540)
- binding (4S)-2-(6-hydroxy-1,3-benzothiazol-2-yl)-4,5-dihydro-1,3-thiazole-4-carboxylic acid: F245 (= F255), R335 (≠ Q347), G337 (≠ A349), G339 (= G351), L340 (≠ M352), A346 (≠ V358)
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)
26% identity, 93% coverage: 27:547/562 of query aligns to 45:547/556 of Q9S725
- K211 (= K217) mutation to S: Drastically reduces the activity.
- M293 (≠ Y296) mutation M->A,P: Affects the substrate specificity.
- K320 (≠ I323) mutation K->L,A: Affects the substrate specificity.
- E401 (= E401) mutation to Q: Slighlty reduces the substrate specificity.
- C403 (= C403) mutation to A: Significantly reduces the substrate specificity.
- R449 (= R449) mutation to Q: Drastically reduces the activity.
- K457 (≠ G457) mutation to S: Drastically reduces the activity.
- K540 (= K540) mutation to N: Abolishes the activity.
6k4cA Ancestral luciferase anclamp in complex with dlsa (see paper)
28% identity, 93% coverage: 29:549/562 of query aligns to 32:536/538 of 6k4cA
- binding 5'-o-[n-(dehydroluciferyl)-sulfamoyl] adenosine: H243 (= H253), F245 (= F255), T249 (≠ A260), G314 (= G326), A315 (= A327), P316 (≠ T328), G337 (≠ A349), Y338 (= Y350), G339 (= G351), L340 (≠ M352), T341 (= T353), A346 (≠ V358), D420 (= D434), I432 (= I446), K527 (= K540)
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)
30% identity, 91% coverage: 30:543/562 of query aligns to 16:503/514 of Q9SMT7
- TSGTT 170:174 (= TSGTT 209:213) binding
- H214 (= H253) binding ; mutation to A: Abolished activity.
- S289 (≠ G326) binding ; mutation to A: Abolished activity.
- SAS 289:291 (≠ GAT 326:328) binding
- EA 310:311 (≠ IA 348:349) binding
- M314 (= M352) binding
- T315 (= T353) binding
- H319 (≠ P357) binding ; mutation to A: Abolished activity.
- D394 (= D434) binding
- R409 (= R449) binding ; mutation to A: Abolished activity.
- K500 (= K540) binding ; binding ; mutation to A: Abolished activity.
2d1sA Crystal structure of the thermostable japanese firefly luciferase complexed with high-energy intermediate analogue (see paper)
29% identity, 90% coverage: 46:549/562 of query aligns to 47:534/539 of 2d1sA
- active site: S194 (≠ T209), R214 (≠ N229), H241 (= H253), T339 (= T353), E340 (= E354), K439 (≠ I455), Q444 (≠ N460), K525 (= K540)
- binding 5'-o-[n-(dehydroluciferyl)-sulfamoyl] adenosine: S194 (≠ T209), S195 (= S210), H241 (= H253), F243 (= F255), T247 (≠ A260), I282 (≠ Y296), G312 (= G326), A313 (= A327), P314 (≠ T328), Q334 (≠ I348), G335 (≠ A349), Y336 (= Y350), G337 (= G351), L338 (≠ M352), T339 (= T353), S343 (≠ P357), A344 (≠ V358), D418 (= D434), R433 (= R449), K525 (= K540)
Query Sequence
>PP_3458 FitnessBrowser__Putida:PP_3458
MPQPSYTQGTQDKPLLTQCIGDAFDATVARFPDREALVVHHQALRYTWRQLADAVDQHAR
ALMALGVQPGDRLGIWAPNCAEWCITQFASAKVGAILVNINPAYRSSELDYALGQSGCRW
VICADAFKTSDYHAMLQGLLPGLASSQPGALICERFPELRGVVSLALSPPPGFLAWHALQ
ARAEVVSGEALAARQAQLRCDDPINIQYTSGTTGFPKGATLSHSNILNNGYMVGESLGLT
EHDRLVVPVPLYHCFGMVMANLGCMTHGSALIYPSDAFDPLATLRAVAQEKATALYGVPT
MFIAELDHPQRGEFDLSSLRTGIMAGATCPIEVMRRVIGEMHMAEVQIAYGMTETSPVSL
QTGAADDLERRVTSVGRTQPRLESKVVDAEGNTVPRGEIGELCTRGYSVMLGYWNNPKAT
AESIDAEGWMHTGDLAVMDEQGYVRIVGRSKDMIIRGGENIYPRELEEFFFTHPAVADVQ
VIGVPCSKYGEEIVAWVRLHPGHAVSEVELREWARARIAHFKVPRYFRFVDEFPMTVTGK
VQKFRMREISVEELKATALPKI
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