SitesBLAST
Comparing WP_024850719.1 NCBI__GCF_000526715.1:WP_024850719.1 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)
P0A6C5 Amino-acid acetyltransferase; N-acetylglutamate synthase; AGS; NAGS; EC 2.3.1.1 from Escherichia coli (strain K12) (see paper)
39% identity, 100% coverage: 1:432/432 of query aligns to 2:442/443 of P0A6C5
- H15 (≠ Q14) mutation to Y: In EE17.
- Y19 (= Y18) mutation to C: In EE51.
- S54 (≠ N54) mutation to N: In PT2M217.
- R58 (≠ K58) mutation to H: In EE11.
- G287 (= G278) mutation to S: In PT2M216.
- Q432 (= Q422) mutation to R: In PT2M217.
4i49A Structure of ngnags bound with bisubstrate analog coa-NAG (see paper)
36% identity, 98% coverage: 8:432/432 of query aligns to 3:422/424 of 4i49A
- binding (2S)-2-({(3S,5R,9R)-1-[(2R,3S,4R,5R)-5-(6-amino-9H-purin-9-yl)-4-hydroxy-3-(phosphonooxy)tetrahydrofuran-2-yl]-3,5,9-trihydroxy-8,8-dimethyl-3,5-dioxido-10,14,20-trioxo-2,4,6-trioxa-18-thia-11,15-diaza-3lambda~5~,5lambda~5~-diphosphaicosan-20-yl}amino)pentanedioic acid (non-preferred name): I300 (= I312), L301 (= L313), L302 (≠ V314), R304 (= R316), A343 (= A354), C344 (= C355), L345 (= L356), A346 (= A357), V347 (= V358), Q352 (= Q363), D353 (≠ G364), G355 (≠ D366), G357 (= G368), E358 (≠ Q369), L379 (= L390), S380 (≠ T391), T383 (= T394), W386 (= W397), F387 (= F398), R413 (= R423), S415 (= S425)
3d2mA Crystal structure of n-acetylglutamate synthase from neisseria gonorrhoeae complexed with coenzyme a and l-glutamate (see paper)
36% identity, 98% coverage: 8:432/432 of query aligns to 3:422/424 of 3d2mA
- active site: I26 (≠ L31)
- binding coenzyme a: L345 (= L356), V347 (= V358), Q352 (= Q363), D353 (≠ G364), G355 (≠ D366), G357 (= G368), E358 (≠ Q369), S380 (≠ T391), T383 (= T394), W386 (= W397)
- binding glutamic acid: L302 (≠ V314), R304 (= R316), A343 (= A354), C344 (= C355), L379 (= L390), R413 (= R423), S415 (= S425)
3b8gA Crysta structure of n-acetylglutamate synthase from neisseria gonorrhoeae complexed with coenzyme a and n-acetyl-glutamate (see paper)
36% identity, 98% coverage: 8:432/432 of query aligns to 3:422/424 of 3b8gA
- active site: I26 (≠ L31)
- binding coenzyme a: I300 (= I312), L345 (= L356), V347 (= V358), Q352 (= Q363), D353 (≠ G364), G355 (≠ D366), Y356 (≠ L367), G357 (= G368), E358 (≠ Q369), S380 (≠ T391), T383 (= T394), E385 (≠ H396), W386 (= W397)
- binding n-acetyl-l-glutamate: L302 (≠ V314), R304 (= R316), A343 (= A354), C344 (= C355), L379 (= L390), R413 (= R423), S415 (= S425)
2r8vA Native structure of n-acetylglutamate synthase from neisseria gonorrhoeae (see paper)
36% identity, 98% coverage: 8:432/432 of query aligns to 3:422/424 of 2r8vA
- active site: I26 (≠ L31)
- binding acetyl coenzyme *a: I300 (= I312), L301 (= L313), L345 (= L356), V347 (= V358), Q352 (= Q363), D353 (≠ G364), G355 (≠ D366), G357 (= G368), E358 (≠ Q369), T383 (= T394), E385 (≠ H396), W386 (= W397), F387 (= F398)
3d2pA Crystal structure of n-acetylglutamate synthase from neisseria gonorrhoeae complexed with coenzyme a and l-arginine (see paper)
34% identity, 98% coverage: 8:432/432 of query aligns to 3:422/424 of 3d2pA
- active site: I26 (≠ L31)
- binding arginine: Y13 (= Y18), K197 (= K201), E216 (vs. gap), Q253 (≠ H257), E266 (= E270), L267 (= L271), T269 (≠ S273), R270 (= R274), N271 (≠ D275), G274 (= G278), S276 (≠ L280)
- binding coenzyme a: L303 (≠ M307), L349 (= L356), V351 (= V358), Q356 (= Q363), D357 (≠ G364), G359 (≠ D366), G361 (= G368), E362 (≠ Q369), E389 (≠ H396), W390 (= W397)
2btyA Acetylglutamate kinase from thermotoga maritima complexed with its inhibitor arginine (see paper)
27% identity, 64% coverage: 6:281/432 of query aligns to 3:277/282 of 2btyA
- active site: K27 (≠ Y30), G30 (= G33), G63 (≠ S66), D182 (≠ L187), K237 (≠ L242)
- binding arginine: Y15 (= Y18), F19 (≠ H22), K196 (= K201), S214 (= S219), E266 (= E270), I267 (≠ L271), R270 (= R274), K271 (≠ D275), G274 (= G278), M276 (≠ L280)
- binding n-acetyl-l-glutamate: G29 (≠ P32), G30 (= G33), G61 (= G64), G62 (≠ A65), N180 (= N185), D182 (≠ L187)
Q9X2A4 Acetylglutamate kinase; N-acetyl-L-glutamate 5-phosphotransferase; NAG kinase; NAGK; EC 2.7.2.8 from Thermotoga maritima (strain ATCC 43589 / DSM 3109 / JCM 10099 / NBRC 100826 / MSB8) (see paper)
27% identity, 64% coverage: 6:281/432 of query aligns to 3:277/282 of Q9X2A4
- N178 (= N183) binding substrate
- K196 (= K201) binding L-arginine
- S214 (= S219) binding L-arginine
- EIFS 266:269 (≠ ELFS 270:273) binding L-arginine
2v5hB Controlling the storage of nitrogen as arginine: the complex of pii and acetylglutamate kinase from synechococcus elongatus pcc 7942 (see paper)
23% identity, 65% coverage: 7:288/432 of query aligns to 5:288/289 of 2v5hB
2bufA Arginine feed-back inhibitable acetylglutamate kinase (see paper)
24% identity, 64% coverage: 12:287/432 of query aligns to 14:292/292 of 2bufA
Q9HTN2 Acetylglutamate kinase; N-acetyl-L-glutamate 5-phosphotransferase; NAG kinase; NAGK; EC 2.7.2.8 from Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1) (see 2 papers)
24% identity, 64% coverage: 12:287/432 of query aligns to 15:301/301 of Q9HTN2
- R90 (= R87) binding substrate
- N195 (= N183) binding substrate
Sites not aligning to the query:
- 1 modified: Initiator methionine, Removed
2bufC Arginine feed-back inhibitable acetylglutamate kinase (see paper)
24% identity, 63% coverage: 12:281/432 of query aligns to 14:294/298 of 2bufC
- active site: K32 (≠ Y30), G35 (= G33), G68 (≠ S66), D198 (≠ L187), K254 (≠ L242)
- binding adenosine-5'-diphosphate: N36 (≠ E34), N218 (≠ D207), L222 (≠ F211), M223 (vs. gap), T246 (≠ D234), I247 (≠ N235), Y248 (≠ Q236), G250 (≠ E238), M251 (≠ L239)
2bufK Arginine feed-back inhibitable acetylglutamate kinase (see paper)
24% identity, 63% coverage: 12:281/432 of query aligns to 14:271/273 of 2bufK
2rd5B Structural basis for the regulation of n-acetylglutamate kinase by pii in arabidopsis thaliana (see paper)
24% identity, 63% coverage: 12:281/432 of query aligns to 9:281/283 of 2rd5B
- active site: K27 (≠ Y30), G30 (= G33), G63 (≠ S66), D182 (≠ L187), K241 (≠ L242)
- binding adenosine-5'-diphosphate: A31 (≠ E34), T201 (≠ S206), D202 (= D207), L207 (vs. gap), K210 (= K212), A235 (≠ Q236), G237 (≠ E238), M238 (≠ L239), K241 (≠ L242)
- binding arginine: K196 (= K201), K218 (≠ S219), E270 (= E270), S273 (= S273), E275 (≠ D275), G278 (= G278), M280 (≠ L280)
- binding n-acetyl-l-glutamate: G61 (= G64), R84 (= R87), N178 (= N183), N180 (= N185), A181 (≠ T186)
4usjB N-acetylglutamate kinase from arabidopsis thaliana in complex with pii from chlamydomonas reinhardtii (see paper)
24% identity, 63% coverage: 12:281/432 of query aligns to 7:279/281 of 4usjB
- active site: K25 (≠ Y30), G28 (= G33), G61 (≠ S66), D180 (≠ L187), K239 (≠ L242)
- binding arginine: F17 (≠ H22), K194 (= K201), K216 (≠ S219), E268 (= E270), I269 (≠ L271), S271 (= S273), E273 (≠ D275), G274 (= G276), M278 (≠ L280)
- binding n-acetyl-l-glutamyl 5-phosphate: G59 (= G64), G60 (≠ A65), G61 (≠ S66), R82 (= R87), N176 (= N183), A179 (≠ T186)
Q9SCL7 Acetylglutamate kinase, chloroplastic; N-acetyl-L-glutamate 5-phosphotransferase; NAG kinase; AtNAGK; EC 2.7.2.8 from Arabidopsis thaliana (Mouse-ear cress) (see 3 papers)
24% identity, 63% coverage: 12:281/432 of query aligns to 73:345/347 of Q9SCL7
- GA 94:95 (≠ GE 33:34) binding ATP
- G126 (≠ A65) binding N-acetyl-L-glutamate
- R148 (= R87) binding N-acetyl-L-glutamate
- NINA 242:245 (≠ NLNT 183:186) binding N-acetyl-L-glutamate
- K260 (= K201) binding L-arginine
- TD 265:266 (≠ SD 206:207) binding ATP
- L271 (vs. gap) binding ATP
- K282 (≠ S219) binding L-arginine
- 297:305 (vs. 234:242, 0% identical) binding ATP
- EIMS 334:337 (≠ ELFS 270:273) binding L-arginine
- G342 (= G278) binding L-arginine
Sites not aligning to the query:
- 1:50 modified: transit peptide, Chloroplast
5ygeA Arga complexed with acecoa and glutamate (see paper)
29% identity, 27% coverage: 289:403/432 of query aligns to 7:122/169 of 5ygeA
- binding acetyl coenzyme *a: Y25 (≠ M307), I73 (≠ L353), V76 (≠ L356), A77 (= A357), V78 (= V358), T83 (≠ Q363), G84 (= G364), H85 (≠ D365), G86 (≠ D366), G88 (= G368), H89 (≠ Q369), T111 (= T391), E113 (≠ H393), F117 (= F398)
- binding glutamic acid: K33 (≠ R316), E44 (≠ N327), H64 (≠ Y344), R74 (≠ A354)
Sites not aligning to the query:
6addA The crystal structure of rv2747 from mycobacterium tuberculosis in complex with coa and nlq (see paper)
29% identity, 27% coverage: 289:403/432 of query aligns to 6:121/168 of 6addA
- binding coenzyme a: Y24 (≠ M307), I28 (= I312), V75 (≠ L356), A76 (= A357), V77 (= V358), T82 (≠ Q363), G83 (= G364), H84 (≠ D365), G85 (≠ D366), G87 (= G368), H88 (≠ Q369), T110 (= T391), E112 (≠ H393), F115 (≠ W397)
- binding n~2~-acetyl-l-glutamine: K27 (≠ E310), I28 (= I312), L30 (≠ V314), T74 (≠ C355), L109 (= L390)
Sites not aligning to the query:
5yo2A The crystal structure of rv2747 from mycobacterium tuberculosis in complex with acetyl coa and l-arginine (see paper)
29% identity, 27% coverage: 289:403/432 of query aligns to 6:121/168 of 5yo2A
- binding acetyl coenzyme *a: Y24 (≠ M307), I28 (= I312), I72 (≠ L353), R73 (≠ A354), T74 (≠ C355), V75 (≠ L356), V77 (= V358), T82 (≠ Q363), G83 (= G364), H84 (≠ D365), G85 (≠ D366), G87 (= G368), H88 (≠ Q369), T110 (= T391), E112 (≠ H393), F115 (≠ W397), F116 (= F398)
- binding arginine: G26 (≠ E309), L29 (= L313), L30 (≠ V314), R73 (≠ A354), L109 (= L390)
Sites not aligning to the query:
7nlwA Crystal structure of mycobacterium tuberculosis argb in complex with 2-(5-methoxy-1h-indol-3-yl)acetonitrile
25% identity, 62% coverage: 12:279/432 of query aligns to 13:286/290 of 7nlwA
Query Sequence
>WP_024850719.1 NCBI__GCF_000526715.1:WP_024850719.1
MQQSELDFINNLRQSSPYIAAHRGKTLVIYLPGEMLQHPGTLLQFAKDIVLLNNLGIKVV
LTLGASVQINDALIEQKFSWETSQHCRITLPEHIVTIQKTIGWVRSQLEAAFSQACAEQH
SPLSLVSGNWVIAKPKGVINGVDFQHTGSLRKINSEAIHASLQSNQVCLLTPLAYSLTGE
VFNLNTLDQAFAVSQAIHADKLIIYSDIDSFKALPKAMSLLDAQHHLDLIQKDDNQQELH
TLLKLSLDAASSVKRIHIISQQEPSAMLFELFSRDGMGTLIYADRYHQLRPATVDDVAGI
LKLIEPMEEEGILVKRSREVLELEIDNFIIAEVDQQIIGCAALYPMENHQGELACLAVDP
SYQGDDLGQEILNHIEVMAKQQTIQQLFLLTTHTDHWFQEQGFERSSLEILPEKRQSLYN
FQRQSKVLIKTL
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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