SitesBLAST
Comparing WP_022669731.1 NCBI__GCF_000420385.1:WP_022669731.1 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)
61% identity, 99% coverage: 3:340/340 of query aligns to 1:338/338 of C1DFH7
- D190 (= D192) binding Mg(2+)
- E226 (= E228) binding Mg(2+)
- E230 (= E232) binding Mg(2+)
8upqB Campylobacter jejuni ketol-acid reductoisomerase in complex with 2,3- dihydroxy-3-isovalerate.
60% identity, 100% coverage: 2:340/340 of query aligns to 1:339/342 of 8upqB
7rduA Crystal structure of campylobacter jejuni keto said reductoisomerase in complex with magnesium and oxidixized and reduced NADPH
61% identity, 97% coverage: 2:330/340 of query aligns to 1:329/329 of 7rduA
- binding nadp nicotinamide-adenine-dinucleotide phosphate: G24 (= G25), G26 (= G27), S27 (= S28), Q28 (= Q29), R48 (= R49), S51 (= S52), S53 (= S54), A81 (= A82), P82 (= P83), D83 (= D84), I89 (= I90), A107 (≠ G108), H108 (= H109), P130 (= P131), K131 (= K132), A132 (≠ G133)
- binding nadph dihydro-nicotinamide-adenine-dinucleotide phosphate: G24 (= G25), F25 (≠ Y26), G26 (= G27), S27 (= S28), Q28 (= Q29), S51 (= S52), S53 (= S54), L80 (= L81), P82 (= P83), D83 (= D84), I89 (= I90), A107 (≠ G108), H108 (= H109)
8uppA Campylobacter jejuni ketol-acid reductoisomerase in complex with NADPH and hoe704
61% identity, 96% coverage: 3:329/340 of query aligns to 1:327/327 of 8uppA
- binding magnesium ion: D190 (= D192), E194 (= E196)
- binding nadph dihydro-nicotinamide-adenine-dinucleotide phosphate: F24 (≠ Y26), G25 (= G27), S26 (= S28), Q27 (= Q29), R47 (= R49), S50 (= S52), L79 (= L81), P81 (= P83), D82 (= D84), I84 (≠ L86), Q85 (= Q87), I88 (= I90), H107 (= H109), P132 (= P134), I250 (= I252), S251 (= S253)
- binding (2R)-(dimethylphosphoryl)(hydroxy)acetic acid: A131 (≠ G133), P132 (= P134), D190 (= D192), E194 (= E196), E230 (= E232), I250 (= I252), S251 (= S253), A254 (= A256)
8sxdA Campylobacter jejuni keto-acid reductoisomerase in complex with intermediate and NADP+
61% identity, 96% coverage: 3:329/340 of query aligns to 1:327/327 of 8sxdA
- binding magnesium ion: D190 (= D192), E194 (= E196)
- binding nadph dihydro-nicotinamide-adenine-dinucleotide phosphate: G23 (= G25), F24 (≠ Y26), G25 (= G27), S26 (= S28), Q27 (= Q29), S50 (= S52), S52 (= S54), L79 (= L81), A80 (= A82), P81 (= P83), D82 (= D84), P129 (= P131)
- binding 3-hydroxy-3-methyl-2-oxobutanoic acid: D190 (= D192), E194 (= E196)
4xiyA Crystal structure of ketol-acid reductoisomerase from azotobacter (see paper)
61% identity, 96% coverage: 3:329/340 of query aligns to 1:327/328 of 4xiyA
8swmA Crystal structure of campylobacter jejuni ketol-acid reductoisomerase in complex with 2-acetolactate
61% identity, 95% coverage: 6:328/340 of query aligns to 1:323/323 of 8swmA
8k32C The complex structure of slkari with nadh at 2.12-angstrom resolution
60% identity, 96% coverage: 4:330/340 of query aligns to 2:333/333 of 8k32C
- binding magnesium ion: D195 (= D192), E199 (= E196), E231 (= E228), E235 (= E232)
- binding 1,4-dihydronicotinamide adenine dinucleotide: Y24 (= Y26), G25 (= G27), S26 (= S28), Q27 (= Q29), R47 (= R49), E57 (≠ S54), L84 (= L81), V85 (≠ A82), P86 (= P83), D87 (= D84), V93 (≠ I90), S111 (≠ G108), H112 (= H109)
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)
59% identity, 99% coverage: 1:338/340 of query aligns to 1:336/337 of P9WKJ7
- M1 (= M1) modified: Initiator methionine, Removed
- D192 (= D192) binding Mg(2+); binding Mg(2+)
- E196 (= E196) binding Mg(2+)
- E228 (= E228) binding Mg(2+)
- E232 (= E232) binding Mg(2+)
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)
59% identity, 98% coverage: 5:337/340 of query aligns to 4:335/344 of C8WR67
- YGSQ 25:28 (= YGSQ 26:29) binding NADP(+)
- R48 (= R49) binding NADP(+); mutation to P: Inversion of the cofactor specificity from NADPH to NADH.
- S52 (= S54) binding NADP(+); mutation to D: Inversion of the cofactor specificity from NADPH to NADH.
- DERQ 82:85 (≠ DELQ 84:87) binding NADP(+)
- G133 (= G135) binding NADP(+)
- D190 (= D192) binding Mg(2+)
- E194 (= E196) binding Mg(2+)
- E226 (= E228) binding Mg(2+)
4ypoA Crystal structure of mycobacterium tuberculosis ketol-acid reductoisomerase in complex with mg2+ (see paper)
60% identity, 96% coverage: 5:329/340 of query aligns to 1:325/325 of 4ypoA
4tskA Ketol-acid reductoisomerase from alicyclobacillus acidocaldarius (see paper)
60% identity, 98% coverage: 5:336/340 of query aligns to 3:333/333 of 4tskA
- active site: K129 (= K132), D189 (= D192), E193 (= E196)
- binding magnesium ion: D189 (= D192), D189 (= D192), E193 (= E196), E193 (= E196), R246 (= R249), Y247 (= Y250), I249 (= I252), D251 (≠ N254), Q254 (≠ K257)
- binding nadph dihydro-nicotinamide-adenine-dinucleotide phosphate: Y24 (= Y26), G25 (= G27), S26 (= S28), Q27 (= Q29), L46 (= L48), R47 (= R49), S51 (= S54), L78 (= L81), L79 (≠ A82), P80 (= P83), D81 (= D84), H106 (= H109), P131 (= P134)
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)
57% identity, 97% coverage: 1:331/340 of query aligns to 10:340/342 of D0WGK0
- YGSQ 35:38 (= YGSQ 26:29) binding NADP(+)
- R58 (= R49) binding NADP(+)
- S61 (= 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-63.
- S63 (= S54) 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 (≠ DELQ 84:87) binding NADP(+)
- G144 (= G135) binding NADP(+)
- D201 (= D192) binding Mg(2+)
- E205 (= E196) binding Mg(2+)
- S262 (= S253) binding substrate
4kqxB Mutant slackia exigua kari ddv in complex with NAD and an inhibitor (see paper)
57% identity, 97% coverage: 1:331/340 of query aligns to 1:331/335 of 4kqxB
- active site: K132 (= K132), D192 (= D192), E196 (= E196)
- binding n-hydroxy-n-isopropyloxamic acid: P134 (= P134), D192 (= D192), E196 (= E196), E232 (= E232), I252 (= I252), S253 (= S253), A256 (= A256)
- binding magnesium ion: G27 (= G27), Q29 (= Q29), G30 (= G30), A72 (= A72), E73 (≠ A73), A75 (= A75), L81 (= L81), N103 (≠ D103), D192 (= D192), E196 (= E196), N249 (≠ R249), S251 (= S251), I252 (= I252), I252 (= I252), S253 (= S253), N254 (= N254), E257 (≠ K257)
- binding nicotinamide-adenine-dinucleotide: Y26 (= Y26), G27 (= G27), S28 (= S28), Q29 (= Q29), R49 (= R49), L81 (= L81), V82 (≠ A82), P83 (= P83), D84 (= D84), V90 (≠ I90), H109 (= H109), P134 (= P134), S251 (= S251), I252 (= I252), S253 (= S253)
Sites not aligning to the query:
4kqwA The structure of the slackia exigua kari in complex with NADP (see paper)
58% identity, 96% coverage: 4:329/340 of query aligns to 1:326/326 of 4kqwA
- active site: K129 (= K132), D189 (= D192), E193 (= E196)
- binding magnesium ion: D189 (= D192), E193 (= E196)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: Y23 (= Y26), G24 (= G27), S25 (= S28), Q26 (= Q29), R46 (= R49), S49 (= S52), S51 (= S54), L78 (= L81), V79 (≠ A82), P80 (= P83), D81 (= D84), I83 (≠ L86), Q84 (= Q87), H106 (= H109), P131 (= P134), I249 (= I252), S250 (= S253)
8cy8A Apo form cryo-em structure of campylobacter jejune ketol-acid reductoisommerase crosslinked by glutaraldehyde
59% identity, 96% coverage: 3:330/340 of query aligns to 1:312/312 of 8cy8A
8ep7C Crystal structure of the ketol-acid reductoisomerase from bacillus anthracis in complex with NADP
56% identity, 96% coverage: 3:330/340 of query aligns to 1:327/328 of 8ep7C
- binding nadp nicotinamide-adenine-dinucleotide phosphate: Y24 (= Y26), G25 (= G27), S26 (= S28), Q27 (= Q29), R47 (= R49), S51 (= S54), L78 (= L81), L79 (≠ A82), P80 (= P83), D81 (= D84), Q83 (≠ L86), V87 (≠ I90), H106 (= H109)
7q03A Ketol-acid reductoisomerase from methanothermococcus thermolithotrophicus in the close state with NADP and mg2+ (see paper)
57% identity, 95% coverage: 3:325/340 of query aligns to 1:323/328 of 7q03A
- binding magnesium ion: D190 (= D192), E194 (= E196)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: Y24 (= Y26), G25 (= G27), S26 (= S28), Q27 (= Q29), R47 (= R49), S52 (= S54), L79 (= L81), I80 (≠ A82), P81 (= P83), D82 (= D84), I84 (≠ L86), H107 (= H109), P132 (= P134)
6jx2B Crystal structure of ketol-acid reductoisomerase from corynebacterium glutamicum (see paper)
59% identity, 96% coverage: 3:329/340 of query aligns to 1:327/327 of 6jx2B
6bulB Crystal structure of staphylococcus aureus ketol-acid reductoisomerase with hydroxyoxamate inhibitor 2
58% identity, 96% coverage: 5:330/340 of query aligns to 3:327/327 of 6bulB
- active site: K129 (= K132), D189 (= D192), E193 (= E196)
- binding {hydroxy[(1S)-1-phenylethyl]amino}(oxo)acetic acid: P131 (= P134), D189 (= D192), E193 (= E196), E229 (= E232), I233 (= I236), I249 (= I252), S250 (= S253), A253 (= A256)
- binding oxo{[(1S)-1-phenylethyl]amino}acetic acid: P131 (= P134), D189 (= D192), E193 (= E196), E229 (= E232), I233 (= I236), I249 (= I252), S250 (= S253), A253 (= A256)
- binding magnesium ion: D189 (= D192), E193 (= E196)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: Y24 (= Y26), G25 (= G27), S26 (= S28), Q27 (= Q29), I46 (≠ L48), R47 (= R49), S51 (= S54), L78 (= L81), L79 (≠ A82), P80 (= P83), D81 (= D84), H106 (= H109), P131 (= P134), S248 (= S251), I249 (= I252), S250 (= S253)
Query Sequence
>WP_022669731.1 NCBI__GCF_000420385.1:WP_022669731.1
MALNVYYEKDADLSLIKSKKIAVIGYGSQGYAHSNNLKDSGCDVVVGLRKGSKSWKKAED
AGLKVLETAEAAAWADVIMILAPDELQPEIYKESIEPNLKEGDTIAFGHGFNIHFKQIVP
PETVNVMMIAPKGPGHLVRREYELGRGVPMLIAIANDYSGNTKELALSYAAAIGGARAGV
IETTFKDETETDLFGEQTVLCGGITSLVKAGFETLVEAGYPEEMAYFETFHELKLIVDLM
YESGIWGMRYSISNTAKYGDVTRGPRVIDESVKERMKEILKEIQSGEFAREWVLENKSGR
TVFNALINKDKEHQIEKVGERLRKMMPWIQENKAIDESKN
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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