SitesBLAST
Comparing WP_011914321.1 NCBI__GCF_000013785.1:WP_011914321.1 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)
C1DFH7 Ketol-acid reductoisomerase (NADP(+)); KARI; Acetohydroxy-acid isomeroreductase; AHIR; Alpha-keto-beta-hydroxylacyl reductoisomerase; Ketol-acid reductoisomerase type 1; Ketol-acid reductoisomerase type I; EC 1.1.1.86 from Azotobacter vinelandii (strain DJ / ATCC BAA-1303) (see paper)
93% identity, 100% coverage: 1:338/338 of query aligns to 1:338/338 of C1DFH7
- D190 (= D190) binding Mg(2+)
- E226 (= E226) binding Mg(2+)
- E230 (= E230) binding Mg(2+)
4xiyA Crystal structure of ketol-acid reductoisomerase from azotobacter (see paper)
93% identity, 97% coverage: 1:328/338 of query aligns to 1:328/328 of 4xiyA
8upqB Campylobacter jejuni ketol-acid reductoisomerase in complex with 2,3- dihydroxy-3-isovalerate.
64% identity, 100% coverage: 1:338/338 of query aligns to 2:339/342 of 8upqB
7rduA Crystal structure of campylobacter jejuni keto said reductoisomerase in complex with magnesium and oxidixized and reduced NADPH
64% identity, 97% coverage: 1:328/338 of query aligns to 2:329/329 of 7rduA
- binding nadp nicotinamide-adenine-dinucleotide phosphate: G24 (= G23), G26 (= G25), S27 (= S26), Q28 (= Q27), R48 (= R47), S51 (= S50), S53 (= S52), A81 (≠ T80), P82 (= P81), D83 (= D82), I89 (≠ L88), A107 (= A106), H108 (= H107), P130 (= P129), K131 (= K130), A132 (= A131)
- binding nadph dihydro-nicotinamide-adenine-dinucleotide phosphate: G24 (= G23), F25 (≠ Y24), G26 (= G25), S27 (= S26), Q28 (= Q27), S51 (= S50), S53 (= S52), L80 (= L79), P82 (= P81), D83 (= D82), I89 (≠ L88), A107 (= A106), H108 (= H107)
8uppA Campylobacter jejuni ketol-acid reductoisomerase in complex with NADPH and hoe704
64% identity, 97% coverage: 1:327/338 of query aligns to 1:327/327 of 8uppA
- binding magnesium ion: D190 (= D190), E194 (= E194)
- binding nadph dihydro-nicotinamide-adenine-dinucleotide phosphate: F24 (≠ Y24), G25 (= G25), S26 (= S26), Q27 (= Q27), R47 (= R47), S50 (= S50), L79 (= L79), P81 (= P81), D82 (= D82), I84 (≠ F84), Q85 (= Q85), I88 (≠ L88), H107 (= H107), P132 (= P132), I250 (= I250), S251 (= S251)
- binding (2R)-(dimethylphosphoryl)(hydroxy)acetic acid: A131 (= A131), P132 (= P132), D190 (= D190), E194 (= E194), E230 (= E230), I250 (= I250), S251 (= S251), A254 (= A254)
8sxdA Campylobacter jejuni keto-acid reductoisomerase in complex with intermediate and NADP+
64% identity, 97% coverage: 1:327/338 of query aligns to 1:327/327 of 8sxdA
- binding magnesium ion: D190 (= D190), E194 (= E194)
- binding nadph dihydro-nicotinamide-adenine-dinucleotide phosphate: G23 (= G23), F24 (≠ Y24), G25 (= G25), S26 (= S26), Q27 (= Q27), S50 (= S50), S52 (= S52), L79 (= L79), A80 (≠ T80), P81 (= P81), D82 (= D82), P129 (= P129)
- binding 3-hydroxy-3-methyl-2-oxobutanoic acid: D190 (= D190), E194 (= E194)
8swmA Crystal structure of campylobacter jejuni ketol-acid reductoisomerase in complex with 2-acetolactate
65% identity, 95% coverage: 5:326/338 of query aligns to 2:323/323 of 8swmA
D0WGK0 Ketol-acid reductoisomerase (NADP(+)); KARI; Acetohydroxy-acid isomeroreductase; AHIR; Alpha-keto-beta-hydroxylacyl reductoisomerase; Ketol-acid reductoisomerase type 1; Ketol-acid reductoisomerase type I; EC 1.1.1.86 from Slackia exigua (strain ATCC 700122 / DSM 15923 / CIP 105133 / JCM 11022 / KCTC 5966 / S-7) (see paper)
59% identity, 97% coverage: 1:327/338 of query aligns to 12:338/342 of D0WGK0
- YGSQ 35:38 (= YGSQ 24:27) binding NADP(+)
- R58 (= R47) binding NADP(+)
- S61 (= S50) binding NADP(+); mutation to D: Inversion of cofactor specificity from NADPH to NADH. Strong decrease of the affinity for NADPH and 2.5-fold decrease of the affinity for NADH. 8-fold decrease of the catalytic efficiency for NADPH and 2-fold increase of the catalytic efficiency for NADH; when associated with D-63.
- S63 (= S52) binding NADP(+); mutation to D: Inversion of cofactor specificity from NADPH to NADH. Strong decrease of the affinity for NADPH and 2.5-fold decrease of the affinity for NADH. 8-fold decrease of the catalytic efficiency for NADPH and 2-fold increase of the catalytic efficiency for NADH; when associated with D-61.
- DEIQ 93:96 (≠ DEFQ 82:85) binding NADP(+)
- G144 (= G133) binding NADP(+)
- D201 (= D190) binding Mg(2+)
- E205 (= E194) binding Mg(2+)
- S262 (= S251) binding substrate
8cy8A Apo form cryo-em structure of campylobacter jejune ketol-acid reductoisommerase crosslinked by glutaraldehyde
61% identity, 97% coverage: 1:328/338 of query aligns to 1:312/312 of 8cy8A
4kqwA The structure of the slackia exigua kari in complex with NADP (see paper)
60% identity, 96% coverage: 3:327/338 of query aligns to 2:326/326 of 4kqwA
- active site: K129 (= K130), D189 (= D190), E193 (= E194)
- binding magnesium ion: D189 (= D190), E193 (= E194)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: Y23 (= Y24), G24 (= G25), S25 (= S26), Q26 (= Q27), R46 (= R47), S49 (= S50), S51 (= S52), L78 (= L79), V79 (≠ T80), P80 (= P81), D81 (= D82), I83 (≠ F84), Q84 (= Q85), H106 (= H107), P131 (= P132), I249 (= I250), S250 (= S251)
4kqxB Mutant slackia exigua kari ddv in complex with NAD and an inhibitor (see paper)
59% identity, 97% coverage: 1:327/338 of query aligns to 3:329/335 of 4kqxB
- active site: K132 (= K130), D192 (= D190), E196 (= E194)
- binding n-hydroxy-n-isopropyloxamic acid: P134 (= P132), D192 (= D190), E196 (= E194), E232 (= E230), I252 (= I250), S253 (= S251), A256 (= A254)
- binding magnesium ion: G27 (= G25), Q29 (= Q27), G30 (= G28), A72 (≠ V70), E73 (≠ A71), A75 (= A73), L81 (= L79), N103 (≠ A101), D192 (= D190), E196 (= E194), N249 (= N247), S251 (= S249), I252 (= I250), I252 (= I250), S253 (= S251), N254 (= N252), E257 (= E255)
- binding nicotinamide-adenine-dinucleotide: Y26 (= Y24), G27 (= G25), S28 (= S26), Q29 (= Q27), R49 (= R47), L81 (= L79), V82 (≠ T80), P83 (= P81), D84 (= D82), V90 (≠ L88), H109 (= H107), P134 (= P132), S251 (= S249), I252 (= I250), S253 (= S251)
Sites not aligning to the query:
C8WR67 Ketol-acid reductoisomerase (NADP(+)); KARI; Acetohydroxy-acid isomeroreductase; AHIR; Alpha-keto-beta-hydroxylacyl reductoisomerase; Ketol-acid reductoisomerase type 1; Ketol-acid reductoisomerase type I; EC 1.1.1.86 from Alicyclobacillus acidocaldarius subsp. acidocaldarius (strain ATCC 27009 / DSM 446 / BCRC 14685 / JCM 5260 / KCTC 1825 / NBRC 15652 / NCIMB 11725 / NRRL B-14509 / 104-IA) (Bacillus acidocaldarius) (see paper)
58% identity, 98% coverage: 2:331/338 of query aligns to 3:331/344 of C8WR67
- YGSQ 25:28 (= YGSQ 24:27) binding NADP(+)
- R48 (= R47) binding NADP(+); mutation to P: Inversion of the cofactor specificity from NADPH to NADH.
- S52 (= S51) binding NADP(+); mutation to D: Inversion of the cofactor specificity from NADPH to NADH.
- DERQ 82:85 (≠ DEFQ 82:85) binding NADP(+)
- G133 (= G133) binding NADP(+)
- D190 (= D190) binding Mg(2+)
- E194 (= E194) binding Mg(2+)
- E226 (= E226) binding Mg(2+)
4tskA Ketol-acid reductoisomerase from alicyclobacillus acidocaldarius (see paper)
58% identity, 98% coverage: 2:331/338 of query aligns to 2:330/333 of 4tskA
- active site: K129 (= K130), D189 (= D190), E193 (= E194)
- binding magnesium ion: D189 (= D190), D189 (= D190), E193 (= E194), E193 (= E194), R246 (≠ N247), Y247 (= Y248), I249 (= I250), D251 (≠ N252), Q254 (≠ E255)
- binding nadph dihydro-nicotinamide-adenine-dinucleotide phosphate: Y24 (= Y24), G25 (= G25), S26 (= S26), Q27 (= Q27), L46 (= L46), R47 (= R47), S51 (= S51), L78 (= L79), L79 (≠ T80), P80 (= P81), D81 (= D82), H106 (= H107), P131 (= P132)
P9WKJ7 Ketol-acid reductoisomerase (NADP(+)); KARI; Acetohydroxy-acid isomeroreductase; AHIR; Alpha-keto-beta-hydroxylacyl reductoisomerase; Ketol-acid reductoisomerase type 1; Ketol-acid reductoisomerase type I; EC 1.1.1.86 from Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv) (see 2 papers)
56% identity, 97% coverage: 1:327/338 of query aligns to 3:329/337 of P9WKJ7
- D192 (= D190) binding Mg(2+); binding Mg(2+)
- E196 (= E194) binding Mg(2+)
- E228 (= E226) binding Mg(2+)
- E232 (= E230) binding Mg(2+)
Sites not aligning to the query:
- 1 modified: Initiator methionine, Removed
4ypoA Crystal structure of mycobacterium tuberculosis ketol-acid reductoisomerase in complex with mg2+ (see paper)
57% identity, 96% coverage: 5:327/338 of query aligns to 3:325/325 of 4ypoA
6vo2A Crystal structure of staphylococcus aureus ketol-acid reductoisomerase in complex with mg, NADPH and inhibitor. (see paper)
57% identity, 96% coverage: 3:327/338 of query aligns to 3:326/326 of 6vo2A
- binding magnesium ion: D189 (= D190), E193 (= E194)
- binding nadph dihydro-nicotinamide-adenine-dinucleotide phosphate: Y24 (= Y24), G25 (= G25), S26 (= S26), Q27 (= Q27), I46 (≠ L46), R47 (= R47), S51 (= S51), L78 (= L79), L79 (≠ T80), P80 (= P81), D81 (= D82), H106 (= H107), P131 (= P132), I249 (= I250), S250 (= S251)
- binding 3-(methylsulfonyl)-2-oxopropanoic acid: G130 (≠ A131), P131 (= P132), D189 (= D190), E193 (= E194), E229 (= E230), I249 (= I250), S250 (= S251), A253 (= A254)
6c5nA Crystal structure of staphylococcus aureus ketol-acid reductoisomerase with hydroxyoxamate inhibitor 1
57% identity, 96% coverage: 3:327/338 of query aligns to 3:326/326 of 6c5nA
- active site: K129 (= K130), D189 (= D190), E193 (= E194)
- binding (cyclopentylamino)(oxo)acetic acid: P131 (= P132), D189 (= D190), E193 (= E194), C198 (= C199), E229 (= E230), I233 (= I234), I249 (= I250), S250 (= S251), A253 (= A254)
- binding [cyclopentyl(hydroxy)amino](oxo)acetic acid: P131 (= P132), D189 (= D190), E193 (= E194), C198 (= C199), E229 (= E230), I249 (= I250), S250 (= S251), A253 (= A254)
- binding magnesium ion: D189 (= D190), E193 (= E194)
- binding nadph dihydro-nicotinamide-adenine-dinucleotide phosphate: Y24 (= Y24), G25 (= G25), S26 (= S26), Q27 (= Q27), I46 (≠ L46), R47 (= R47), S51 (= S51), L78 (= L79), L79 (≠ T80), P80 (= P81), D81 (= D82), H106 (= H107), P131 (= P132), S248 (= S249), I249 (= I250), S250 (= S251)
6c55A Crystal structure of staphylococcus aureus ketol-acid reductosimerrase with hydroxyoxamate inhibitor 3
57% identity, 96% coverage: 3:327/338 of query aligns to 3:326/326 of 6c55A
- active site: K129 (= K130), D189 (= D190), E193 (= E194)
- binding [cyclohexyl(hydroxy)amino](oxo)acetic acid: P131 (= P132), D189 (= D190), E193 (= E194), C198 (= C199)
- binding (cyclohexylamino)(oxo)acetic acid: P131 (= P132), D189 (= D190), E193 (= E194), C198 (= C199), I249 (= I250), S250 (= S251), A253 (= A254)
- binding magnesium ion: D189 (= D190), E193 (= E194)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: G25 (= G25), S26 (= S26), Q27 (= Q27), I46 (≠ L46), R47 (= R47), S51 (= S51), L79 (≠ T80), P80 (= P81), D81 (= D82), I83 (≠ F84), H106 (= H107), S248 (= S249), S250 (= S251)
6aqjA Crystal structures of staphylococcus aureus ketol-acid reductoisomerase in complex with two transition state analogs that have biocidal activity. (see paper)
57% identity, 96% coverage: 3:327/338 of query aligns to 3:326/326 of 6aqjA
- active site: K129 (= K130), D189 (= D190), E193 (= E194)
- binding oxo(propan-2-ylamino)acetic acid: P131 (= P132), D189 (= D190), E193 (= E194), E229 (= E230), I233 (= I234), I249 (= I250), S250 (= S251), A253 (= A254)
- binding n-hydroxy-n-isopropyloxamic acid: P131 (= P132), D189 (= D190), E193 (= E194), E229 (= E230), I249 (= I250), S250 (= S251), A253 (= A254)
- binding magnesium ion: D189 (= D190), E193 (= E194)
- binding nadph dihydro-nicotinamide-adenine-dinucleotide phosphate: Y24 (= Y24), G25 (= G25), S26 (= S26), Q27 (= Q27), I46 (≠ L46), R47 (= R47), S51 (= S51), L78 (= L79), L79 (≠ T80), P80 (= P81), D81 (= D82), H106 (= H107), P131 (= P132), I249 (= I250), S250 (= S251)
5w3kA Crystal structure of staphylococcus aureus ketol-acid reductoisomerase in complex NADPH, mg2+ and cpd (see paper)
57% identity, 96% coverage: 3:327/338 of query aligns to 3:326/326 of 5w3kA
- active site: K129 (= K130), D189 (= D190), E193 (= E194)
- binding cyclopropane-1,1-dicarboxylic acid: D189 (= D190), E193 (= E194), E229 (= E230), I249 (= I250), S250 (= S251), A253 (= A254)
- binding magnesium ion: V69 (= V70), K70 (≠ A71), A72 (= A73), N100 (≠ A101), D189 (= D190), E193 (= E194)
- binding nadph dihydro-nicotinamide-adenine-dinucleotide phosphate: Y24 (= Y24), G25 (= G25), S26 (= S26), Q27 (= Q27), I46 (≠ L46), R47 (= R47), S51 (= S51), L78 (= L79), L79 (≠ T80), P80 (= P81), D81 (= D82), H106 (= H107), P131 (= P132), G132 (= G133), I249 (= I250), S250 (= S251)
Query Sequence
>WP_011914321.1 NCBI__GCF_000013785.1:WP_011914321.1
MKVSYDKDCDLSIIQGKKVAIIGYGSQGHAHACNLKDSGVDVTVGLRPGSSSIAKAEAHG
LKVSDVPAAVAAADLVMILTPDEFQGRLYKDEVEPNLKQGATLAFAHGFSIHYNQVVPRA
DLDVIMIAPKAPGHTVRSEFVKGGGIPDLIAIYQDASGNARNVALSYACGVGGGRTGIIE
TTFKDETETDLFGEQAVLCGGCVELVKAGFETLVEAGYAPEMAYFECLHELKLIVDLMFE
GGIANMNYSISNNAEYGEYVTGPEVINAESRAAMRNALKRIQDGEYAKMFITEGAANYPS
MTAYRRNNAAHGIEVVGEKLRAMMPWIAANKIVDKSKN
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