SitesBLAST
Comparing 15820 FitnessBrowser__Keio:15820 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)
5wm6A Crystal structure of cahj in complex with benzoyl adenylate (see paper)
32% identity, 96% coverage: 15:539/548 of query aligns to 18:534/535 of 5wm6A
- active site: S193 (≠ T196), N213 (≠ S216), H237 (= H240), A336 (≠ T337), E337 (= E338), N437 (≠ V438), K442 (≠ N443), K524 (= K525)
- binding magnesium ion: S301 (= S303), L303 (= L305), G326 (= G327)
- binding 5'-O-[(R)-(benzoyloxy)(hydroxy)phosphoryl]adenosine: F239 (≠ T242), G310 (= G312), S311 (≠ T313), K312 (≠ T314), V332 (= V333), F333 (≠ Y334), G334 (= G335), M335 (≠ S336), A336 (≠ T337), D416 (= D417), K433 (= K434), K442 (≠ N443)
5wm3A Crystal structure of cahj in complex with salicyl adenylate (see paper)
32% identity, 96% coverage: 15:539/548 of query aligns to 18:534/537 of 5wm3A
- active site: S193 (≠ T196), N213 (≠ S216), H237 (= H240), A336 (≠ T337), E337 (= E338), N437 (≠ V438), K442 (≠ N443), K524 (= K525)
- binding 9-(5-O-{(S)-hydroxy[(2-hydroxybenzene-1-carbonyl)oxy]phosphoryl}-alpha-L-lyxofuranosyl)-9H-purin-6-amine: N238 (≠ A241), F239 (≠ T242), G310 (= G312), S311 (≠ T313), K312 (≠ T314), V332 (= V333), F333 (≠ Y334), G334 (= G335), M335 (≠ S336), A336 (≠ T337), D416 (= D417), K433 (= K434), K442 (≠ N443)
- binding magnesium ion: S301 (= S303), L303 (= L305), G326 (= G327)
5wm2A Crystal structure of cahj in complex with salicylic acid and amp (see paper)
32% identity, 96% coverage: 15:539/548 of query aligns to 18:534/536 of 5wm2A
- active site: S193 (≠ T196), N213 (≠ S216), H237 (= H240), A336 (≠ T337), E337 (= E338), N437 (≠ V438), K442 (≠ N443), K524 (= K525)
- binding adenosine monophosphate: G310 (= G312), S311 (≠ T313), K312 (≠ T314), V332 (= V333), F333 (≠ Y334), G334 (= G335), M335 (≠ S336), A336 (≠ T337), E337 (= E338), D416 (= D417), V428 (≠ I429), K433 (= K434), K442 (≠ N443)
5wm5A Crystal structure of cahj in complex with 5-methylsalicyl adenylate (see paper)
32% identity, 96% coverage: 15:539/548 of query aligns to 18:532/533 of 5wm5A
- active site: S193 (≠ T196), N213 (≠ S216), H237 (= H240), A336 (≠ T337), E337 (= E338), N437 (≠ V438), K442 (≠ N443), K522 (= K525)
- binding 9-(5-O-{(S)-hydroxy[(2-hydroxy-5-methylbenzene-1-carbonyl)oxy]phosphoryl}-alpha-L-lyxofuranosyl)-9H-purin-6-amine: H237 (= H240), N238 (≠ A241), F239 (≠ T242), G309 (= G311), G310 (= G312), S311 (≠ T313), K312 (≠ T314), V332 (= V333), F333 (≠ Y334), G334 (= G335), M335 (≠ S336), A336 (≠ T337), L340 (≠ P341), D416 (= D417), K433 (= K434), K442 (≠ N443)
5wm4A Crystal structure of cahj in complex with 6-methylsalicyl adenylate (see paper)
32% identity, 96% coverage: 15:539/548 of query aligns to 18:531/534 of 5wm4A
- active site: S193 (≠ T196), N213 (≠ S216), H237 (= H240), A336 (≠ T337), E337 (= E338), N437 (≠ V438), K442 (≠ N443), K521 (≠ T522)
- binding 9-(5-O-{(S)-hydroxy[(2-hydroxy-6-methylbenzene-1-carbonyl)oxy]phosphoryl}-alpha-L-lyxofuranosyl)-9H-purin-6-amine: N238 (≠ A241), F239 (≠ T242), C243 (vs. gap), G309 (= G311), G310 (= G312), S311 (≠ T313), K312 (≠ T314), V332 (= V333), F333 (≠ Y334), G334 (= G335), M335 (≠ S336), A336 (≠ T337), L340 (≠ P341), D416 (= D417), K433 (= K434), K442 (≠ N443)
- binding magnesium ion: M453 (≠ L454), H455 (= H456), V458 (≠ I459)
6e97B Crystal structure of the aryl acid adenylating enzyme fscc from fuscachelin nrps in complex with dhb-adenylate
32% identity, 96% coverage: 15:539/548 of query aligns to 13:536/537 of 6e97B
- active site: S190 (≠ T196), S210 (= S216), H234 (= H240), A336 (≠ T337), E337 (= E338), N437 (≠ V438), K442 (≠ N443), K522 (= K525)
- binding 5'-O-[(S)-[(2,3-dihydroxybenzene-1-carbonyl)oxy](hydroxy)phosphoryl]adenosine: H234 (= H240), N235 (vs. gap), F236 (vs. gap), S240 (≠ A241), G310 (= G312), A311 (≠ T313), K312 (≠ T314), V332 (= V333), F333 (≠ Y334), G334 (= G335), M335 (≠ S336), A336 (≠ T337), D416 (= D417), K433 (= K434), K442 (≠ N443)
6e8oA Crystal structure of aryl acid adenylating enzyme fscc from fuscachelin nrps in complex with amp
32% identity, 96% coverage: 15:539/548 of query aligns to 13:535/536 of 6e8oA
- active site: S190 (≠ T196), S210 (= S216), H234 (= H240), A336 (≠ T337), E337 (= E338), N437 (≠ V438), K442 (≠ N443), K521 (= K525)
- binding adenosine monophosphate: H234 (= H240), G310 (= G312), A311 (≠ T313), K312 (≠ T314), V332 (= V333), F333 (≠ Y334), G334 (= G335), M335 (≠ S336), A336 (≠ T337), D416 (= D417), V428 (≠ I429), K442 (≠ N443)
P40871 2,3-dihydroxybenzoate-AMP ligase; Dihydroxybenzoic acid-activating enzyme; EC 6.2.1.71 from Bacillus subtilis (strain 168) (see paper)
30% identity, 96% coverage: 15:539/548 of query aligns to 16:533/539 of P40871
- G191 (≠ S197) binding
- HN 234:235 (≠ HA 240:241) binding
- S240 (≠ H246) binding
- G307 (= G312) binding
- V329 (= V333) binding
- D413 (= D417) binding
- R428 (= R432) binding
- K519 (= K525) binding ; binding
1md9A Crystal structure of dhbe in complex with dhb and amp (see paper)
30% identity, 96% coverage: 15:539/548 of query aligns to 16:533/536 of 1md9A
- active site: S190 (≠ T196), S210 (= S216), H234 (= H240), A333 (≠ T337), E334 (= E338), N434 (≠ V438), K439 (≠ N443), K519 (= K525)
- binding adenosine monophosphate: G191 (≠ S197), G307 (= G312), A308 (≠ T313), K309 (≠ T314), V329 (= V333), F330 (≠ Y334), G331 (= G335), M332 (≠ S336), D413 (= D417), V425 (≠ I429), R428 (= R432), K519 (= K525)
- binding 2,3-dihydroxy-benzoic acid: H234 (= H240), N235 (≠ A241), Y236 (≠ T242), S240 (≠ H246), G307 (= G312), V329 (= V333), G331 (= G335), M332 (≠ S336), K519 (= K525)
P10378 Enterobactin synthase component E; 2,3-dihydroxybenzoate-AMP ligase; DHB-AMP ligase; 2,3-dihydroxybenzoate-AMP synthase; Dihydroxybenzoic acid-activating enzyme; Enterochelin synthase E; EC 6.3.2.14; EC 6.2.1.71 from Escherichia coli (strain K12) (see 3 papers)
31% identity, 96% coverage: 15:538/548 of query aligns to 16:533/536 of P10378
- N235 (≠ A241) binding
- S240 (≠ H246) binding
- G309 (= G312) binding
- V331 (= V333) binding
- A335 (≠ T337) binding
- D415 (= D417) binding
- K432 (= K434) binding
- R437 (= R439) mutation to D: Catalyzes the adenylation reaction with 10% reduction of activity compared to the wild-type. 3% reduction of activity compared to the wild-type; when associated with D-473.
- GG 438:439 (= GG 440:441) Phosphopantetheine binding
- K441 (≠ N443) binding
- K473 (≠ R475) mutation to D: Catalyzes the adenylation reaction with same activity as the wild-type. 3% reduction of activity compared to the wild-type; when associated with D-437.
- R494 (≠ S499) mutation to D: Catalyzes the adenylation reaction with same activity as the wild-type.
3rg2C Structure of a two-domain nrps fusion protein containing the ente adenylation domain and entb aryl-carrier protein from enterobactin biosynthesis (see paper)
31% identity, 96% coverage: 15:538/548 of query aligns to 16:533/613 of 3rg2C
- active site: S190 (≠ T196), S210 (= S216), H234 (= H240), A335 (≠ T337), E336 (= E338), N436 (≠ V438), K441 (≠ N443), K520 (= K525)
- binding 4'-phosphopantetheine: P231 (= P237), V279 (≠ A284), G438 (= G440), G439 (= G441)
- binding 5'-deoxy-5'-({[2-(2-hydroxyphenyl)ethyl]sulfonyl}amino)adenosine: N235 (≠ A241), Y236 (≠ T242), G309 (= G312), A310 (≠ T313), R311 (≠ T314), V331 (= V333), F332 (≠ Y334), G333 (= G335), M334 (≠ S336), A335 (≠ T337), D415 (= D417), V427 (≠ I429)
4gxqA Crystal structure of atp bound rpmatb-bxbclm chimera b1 (see paper)
31% identity, 91% coverage: 38:537/548 of query aligns to 16:506/506 of 4gxqA
- active site: T163 (= T196), N183 (≠ S216), H207 (= H240), T303 (= T337), E304 (= E338), I403 (≠ V438), N408 (= N443), A491 (≠ K525)
- binding adenosine-5'-triphosphate: T163 (= T196), S164 (= S197), G165 (= G198), T166 (= T199), T167 (≠ E200), H207 (= H240), S277 (≠ G312), A278 (≠ T313), P279 (≠ T314), E298 (≠ S332), M302 (≠ S336), T303 (= T337), D382 (= D417), R397 (= R432)
- binding carbonate ion: H207 (= H240), S277 (≠ G312), R299 (≠ V333), G301 (= G335)
4iz6A Structure of ente and entb, an nrps adenylation-pcp fusion protein with pseudo translational symmetry (see paper)
31% identity, 96% coverage: 15:538/548 of query aligns to 15:531/609 of 4iz6A
- active site: S189 (≠ T196), S208 (= S216), H232 (= H240), A333 (≠ T337), E334 (= E338), N434 (≠ V438), K439 (≠ N443), K518 (= K525)
- binding 5'-deoxy-5'-({[2-(2,3-dihydroxyphenyl)ethyl]sulfonyl}amino)adenosine: Y234 (≠ T242), S238 (≠ H246), G307 (= G312), A308 (≠ T313), R309 (≠ T314), V329 (= V333), F330 (≠ Y334), G331 (= G335), M332 (≠ S336), D413 (= D417), K430 (= K434), K439 (≠ N443)
- binding 4'-phosphopantetheine: P229 (= P237), H232 (= H240), V277 (≠ A284), G436 (= G440)
7tz4A Salicylate adenylate pchd from pseudomonas aeruginosa containing 4- cyanosalicyl-ams (see paper)
30% identity, 95% coverage: 15:537/548 of query aligns to 13:529/530 of 7tz4A
- binding 5'-O-[(4-cyano-2-hydroxybenzoyl)sulfamoyl]adenosine: H232 (= H240), N233 (≠ A241), F234 (vs. gap), C238 (≠ L245), G305 (= G312), S306 (≠ T313), R307 (≠ T314), V327 (= V333), L328 (≠ Y334), G329 (= G335), M330 (≠ S336), A331 (≠ T337), I335 (≠ P341), D411 (= D417), V423 (≠ I429), K517 (= K525)
6iylA The structure of ente with 3-cyanobenzoyl adenylate analog (see paper)
31% identity, 94% coverage: 15:528/548 of query aligns to 14:521/521 of 6iylA
- active site: S188 (≠ T196), S208 (= S216), H232 (= H240), A333 (≠ T337), E334 (= E338), N434 (≠ V438), K439 (≠ N443)
- binding 5'-O-[(3-cyanobenzene-1-carbonyl)sulfamoyl]adenosine: H232 (= H240), Y234 (≠ T242), S238 (≠ H246), G307 (= G312), A308 (≠ T313), R309 (≠ T314), V329 (= V333), F330 (≠ Y334), G331 (= G335), M332 (≠ S336), A333 (≠ T337), D413 (= D417), V425 (≠ I429), K430 (= K434), K439 (≠ N443)
6iykA The structure of ente with 2-nitrobenzoyl adenylate analog (see paper)
31% identity, 94% coverage: 15:528/548 of query aligns to 14:521/521 of 6iykA
- active site: S188 (≠ T196), S208 (= S216), H232 (= H240), A333 (≠ T337), E334 (= E338), N434 (≠ V438), K439 (≠ N443)
- binding 5'-O-[(2-nitrobenzene-1-carbonyl)sulfamoyl]adenosine: H232 (= H240), G233 (≠ A241), Y234 (≠ T242), G307 (= G312), A308 (≠ T313), R309 (≠ T314), V329 (= V333), F330 (≠ Y334), G331 (= G335), M332 (≠ S336), A333 (≠ T337), D413 (= D417), V425 (≠ I429), K439 (≠ N443)
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, 89% coverage: 48:533/548 of query aligns to 62:571/590 of Q4WR83
Sites not aligning to the query:
- 6:14 PTS2-type peroxisomal targeting signal
7tybA Salicylate adenylate pchd from pseudomonas aeruginosa containing salicyl-ams (see paper)
31% identity, 96% coverage: 15:539/548 of query aligns to 12:522/523 of 7tybA
- binding 5'-O-[(2-hydroxybenzoyl)sulfamoyl]adenosine: H227 (= H240), N228 (≠ A241), F229 (vs. gap), C233 (≠ L245), G300 (= G312), S301 (≠ T313), R302 (≠ T314), V322 (= V333), L323 (≠ Y334), G324 (= G335), M325 (≠ S336), A326 (≠ T337), Q346 (≠ D358), D406 (= D417), V418 (≠ I429), R421 (= R432), K512 (= K525)
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, 88% coverage: 52:533/548 of query aligns to 31:495/503 of P9WQ37
- K172 (= K204) mutation to A: Slight reduction of the fatty acyl-CoA ligase activity. Slight increase of susceptibility to proteolysis.
- R195 (≠ T227) mutation to A: Alteration of the strength of the membrane binding; when associated with A-9; A-17; A-197 and A-244.
- R197 (≠ Q229) mutation to A: Alteration of the strength of the membrane binding; when associated with A-9; A-17; A-195 and A-244.
- V209 (≠ A241) 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 (≠ G243) mutation to G: Slight increase of the fatty acyl-CoA ligase activity. Reduced rate of proteolytic degradation.
- T214 (≠ G247) 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 (= R277) mutation to A: Alteration of the strength of the membrane binding; when associated with A-17; A-195; A-195 and A-197.
- A302 (≠ G335) 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 (= W412) 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 (= D417) 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 (= R432) mutation to A: Reduction of binding affinity for fatty acids.
- S404 (≠ R439) mutation to A: Slight reduction of the fatty acyl-CoA ligase activity. Enhanced affinity towards palmitic acid binding.
- G406 (= G441) mutation to L: No effect on the formation of acyl-adenylate intermediate. However, it shows very poor catalytic efficiency to form acyl-CoA.
- K487 (= K525) 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)
27% identity, 88% coverage: 52:533/548 of query aligns to 34:495/502 of 3r44A
Sites not aligning to the query:
Query Sequence
>15820 FitnessBrowser__Keio:15820
MKVTLTFNEQRRAAYRQQGLWGDASLADYWQQTARAMPDKIAVVDNHGASYTYSALDHAA
SCLANWMLAKGIESGDRIAFQLPGWCEFTVIYLACLKIGAVSVPLLPSWREAELVWVLNK
CQAKMFFAPTLFKQTRPVDLILPLQNQLPQLQQIVGVDKLAPATSSLSLSQIIADNTSLT
TAITTHGDELAAVLFTSGTEGLPKGVMLTHNNILASERAYCARLNLTWQDVFMMPAPLGH
ATGFLHGVTAPFLIGARSVLLDIFTPDACLALLEQQRCTCMLGATPFVYDLLNVLEKQPA
DLSALRFFLCGGTTIPKKVARECQQRGIKLLSVYGSTESSPHAVVNLDDPLSRFMHTDGY
AAAGVEIKVVDDARKTLPPGCEGEEASRGPNVFMGYFDEPELTARALDEEGWYYSGDLCR
MDEAGYIKITGRKKDIIVRGGENISSREVEDILLQHPKIHDACVVAMSDERLGERSCAYV
VLKAPHHSLSLEEVVAFFSRKRVAKYKYPEHIVVIEKLPRTTSGKIQKFLLRKDIMRRLT
QDVCEEIE
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