SitesBLAST
Comparing Synpcc7942_1552 FitnessBrowser__SynE:Synpcc7942_1552 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)
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)
69% identity, 100% coverage: 1:326/327 of query aligns to 4:328/344 of C8WR67
- YGSQ 25:28 (= YGSQ 22:25) binding
- R48 (≠ Y45) binding ; mutation to P: Inversion of the cofactor specificity from NADPH to NADH.
- S52 (= S50) binding ; mutation to D: Inversion of the cofactor specificity from NADPH to NADH.
- DERQ 82:85 (≠ DEFQ 80:83) binding
- G133 (= G131) binding
- D190 (= D188) binding
- E194 (= E192) binding
- E226 (= E224) binding
4tskA Ketol-acid reductoisomerase from alicyclobacillus acidocaldarius (see paper)
69% identity, 100% coverage: 1:326/327 of query aligns to 3:327/333 of 4tskA
- active site: K129 (= K128), D189 (= D188), E193 (= E192)
- binding magnesium ion: D189 (= D188), D189 (= D188), E193 (= E192), E193 (= E192), R246 (= R245), Y247 (≠ D246), I249 (= I248), D251 (≠ N250), Q254 (≠ E253)
- binding nadph dihydro-nicotinamide-adenine-dinucleotide phosphate: Y24 (= Y22), G25 (= G23), S26 (= S24), Q27 (= Q25), L46 (= L44), R47 (≠ Y45), S51 (= S50), L78 (= L77), L79 (= L78), P80 (= P79), D81 (= D80), H106 (= H105), P131 (= P130)
7rduA Crystal structure of campylobacter jejuni keto said reductoisomerase in complex with magnesium and oxidixized and reduced NADPH
64% identity, 99% coverage: 1:325/327 of query aligns to 4:328/329 of 7rduA
- binding nadp nicotinamide-adenine-dinucleotide phosphate: G24 (= G21), G26 (= G23), S27 (= S24), Q28 (= Q25), R48 (≠ Y45), S51 (= S48), S53 (= S50), A81 (≠ L78), P82 (= P79), D83 (= D80), I89 (≠ V86), A107 (= A104), H108 (= H105), P130 (= P127), K131 (= K128), A132 (≠ S129)
- binding nadph dihydro-nicotinamide-adenine-dinucleotide phosphate: G24 (= G21), F25 (≠ Y22), G26 (= G23), S27 (= S24), Q28 (= Q25), S51 (= S48), S53 (= S50), L80 (= L77), P82 (= P79), D83 (= D80), I89 (≠ V86), A107 (= A104), H108 (= H105)
7latA Campylobacter jejuni keto-acid reductoisomerase in complex with mg2+
64% identity, 99% coverage: 1:325/327 of query aligns to 4:328/329 of 7latA
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: 1:325/327 of query aligns to 3:327/338 of C1DFH7
- D190 (= D188) binding
- E226 (= E224) binding
- E230 (= E228) binding
4xiyA Crystal structure of ketol-acid reductoisomerase from azotobacter (see paper)
61% identity, 99% coverage: 1:325/327 of query aligns to 3:327/328 of 4xiyA
8ep7C Crystal structure of the ketol-acid reductoisomerase from bacillus anthracis in complex with NADP
63% identity, 99% coverage: 2:325/327 of query aligns to 4:326/328 of 8ep7C
- binding nadp nicotinamide-adenine-dinucleotide phosphate: Y24 (= Y22), G25 (= G23), S26 (= S24), Q27 (= Q25), R47 (≠ Y45), S51 (= S50), L78 (= L77), L79 (= L78), P80 (= P79), D81 (= D80), Q83 (≠ F82), V87 (= V86), H106 (= H105)
8cy8A Apo form cryo-em structure of campylobacter jejune ketol-acid reductoisommerase crosslinked by glutaraldehyde
62% identity, 99% coverage: 1:325/327 of query aligns to 3:311/312 of 8cy8A
6bulB Crystal structure of staphylococcus aureus ketol-acid reductoisomerase with hydroxyoxamate inhibitor 2
62% identity, 100% coverage: 1:326/327 of query aligns to 3:327/327 of 6bulB
- active site: K129 (= K128), D189 (= D188), E193 (= E192)
- binding {hydroxy[(1S)-1-phenylethyl]amino}(oxo)acetic acid: P131 (= P130), D189 (= D188), E193 (= E192), E229 (= E228), I233 (= I232), I249 (= I248), S250 (= S249), A253 (= A252)
- binding oxo{[(1S)-1-phenylethyl]amino}acetic acid: P131 (= P130), D189 (= D188), E193 (= E192), E229 (= E228), I233 (= I232), I249 (= I248), S250 (= S249), A253 (= A252)
- binding magnesium ion: D189 (= D188), E193 (= E192)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: Y24 (= Y22), G25 (= G23), S26 (= S24), Q27 (= Q25), I46 (≠ L44), R47 (≠ Y45), S51 (= S50), L78 (= L77), L79 (= L78), P80 (= P79), D81 (= D80), H106 (= H105), P131 (= P130), S248 (= S247), I249 (= I248), S250 (= S249)
6vo2A Crystal structure of staphylococcus aureus ketol-acid reductoisomerase in complex with mg, NADPH and inhibitor. (see paper)
62% identity, 99% coverage: 1:325/327 of query aligns to 3:326/326 of 6vo2A
- binding magnesium ion: D189 (= D188), E193 (= E192)
- binding nadph dihydro-nicotinamide-adenine-dinucleotide phosphate: Y24 (= Y22), G25 (= G23), S26 (= S24), Q27 (= Q25), I46 (≠ L44), R47 (≠ Y45), S51 (= S50), L78 (= L77), L79 (= L78), P80 (= P79), D81 (= D80), H106 (= H105), P131 (= P130), I249 (= I248), S250 (= S249)
- binding 3-(methylsulfonyl)-2-oxopropanoic acid: G130 (≠ S129), P131 (= P130), D189 (= D188), E193 (= E192), E229 (= E228), I249 (= I248), S250 (= S249), A253 (= A252)
6c5nA Crystal structure of staphylococcus aureus ketol-acid reductoisomerase with hydroxyoxamate inhibitor 1
62% identity, 99% coverage: 1:325/327 of query aligns to 3:326/326 of 6c5nA
- active site: K129 (= K128), D189 (= D188), E193 (= E192)
- binding (cyclopentylamino)(oxo)acetic acid: P131 (= P130), D189 (= D188), E193 (= E192), C198 (= C197), E229 (= E228), I233 (= I232), I249 (= I248), S250 (= S249), A253 (= A252)
- binding [cyclopentyl(hydroxy)amino](oxo)acetic acid: P131 (= P130), D189 (= D188), E193 (= E192), C198 (= C197), E229 (= E228), I249 (= I248), S250 (= S249), A253 (= A252)
- binding magnesium ion: D189 (= D188), E193 (= E192)
- binding nadph dihydro-nicotinamide-adenine-dinucleotide phosphate: Y24 (= Y22), G25 (= G23), S26 (= S24), Q27 (= Q25), I46 (≠ L44), R47 (≠ Y45), S51 (= S50), L78 (= L77), L79 (= L78), P80 (= P79), D81 (= D80), H106 (= H105), P131 (= P130), S248 (= S247), I249 (= I248), S250 (= S249)
6c55A Crystal structure of staphylococcus aureus ketol-acid reductosimerrase with hydroxyoxamate inhibitor 3
62% identity, 99% coverage: 1:325/327 of query aligns to 3:326/326 of 6c55A
- active site: K129 (= K128), D189 (= D188), E193 (= E192)
- binding [cyclohexyl(hydroxy)amino](oxo)acetic acid: P131 (= P130), D189 (= D188), E193 (= E192), C198 (= C197)
- binding (cyclohexylamino)(oxo)acetic acid: P131 (= P130), D189 (= D188), E193 (= E192), C198 (= C197), I249 (= I248), S250 (= S249), A253 (= A252)
- binding magnesium ion: D189 (= D188), E193 (= E192)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: G25 (= G23), S26 (= S24), Q27 (= Q25), I46 (≠ L44), R47 (≠ Y45), S51 (= S50), L79 (= L78), P80 (= P79), D81 (= D80), I83 (≠ F82), H106 (= H105), S248 (= S247), S250 (= S249)
6aqjA Crystal structures of staphylococcus aureus ketol-acid reductoisomerase in complex with two transition state analogs that have biocidal activity. (see paper)
62% identity, 99% coverage: 1:325/327 of query aligns to 3:326/326 of 6aqjA
- active site: K129 (= K128), D189 (= D188), E193 (= E192)
- binding oxo(propan-2-ylamino)acetic acid: P131 (= P130), D189 (= D188), E193 (= E192), E229 (= E228), I233 (= I232), I249 (= I248), S250 (= S249), A253 (= A252)
- binding n-hydroxy-n-isopropyloxamic acid: P131 (= P130), D189 (= D188), E193 (= E192), E229 (= E228), I249 (= I248), S250 (= S249), A253 (= A252)
- binding magnesium ion: D189 (= D188), E193 (= E192)
- binding nadph dihydro-nicotinamide-adenine-dinucleotide phosphate: Y24 (= Y22), G25 (= G23), S26 (= S24), Q27 (= Q25), I46 (≠ L44), R47 (≠ Y45), S51 (= S50), L78 (= L77), L79 (= L78), P80 (= P79), D81 (= D80), H106 (= H105), P131 (= P130), I249 (= I248), S250 (= S249)
5w3kA Crystal structure of staphylococcus aureus ketol-acid reductoisomerase in complex NADPH, mg2+ and cpd (see paper)
62% identity, 99% coverage: 1:325/327 of query aligns to 3:326/326 of 5w3kA
- active site: K129 (= K128), D189 (= D188), E193 (= E192)
- binding cyclopropane-1,1-dicarboxylic acid: D189 (= D188), E193 (= E192), E229 (= E228), I249 (= I248), S250 (= S249), A253 (= A252)
- binding magnesium ion: V69 (≠ A68), K70 (≠ Q69), A72 (= A71), N100 (≠ K99), D189 (= D188), E193 (= E192)
- binding nadph dihydro-nicotinamide-adenine-dinucleotide phosphate: Y24 (= Y22), G25 (= G23), S26 (= S24), Q27 (= Q25), I46 (≠ L44), R47 (≠ Y45), S51 (= S50), L78 (= L77), L79 (= L78), P80 (= P79), D81 (= D80), H106 (= H105), P131 (= P130), G132 (= G131), I249 (= I248), S250 (= S249)
6l2iB Ilvc, a ketol-acid reductoisomerase, from streptococcus pneumoniae_wt
64% identity, 98% coverage: 1:319/327 of query aligns to 3:320/323 of 6l2iB
- binding magnesium ion: D189 (= D188), D189 (= D188), E193 (= E192), E193 (= E192)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: Y24 (= Y22), G25 (= G23), S26 (= S24), Q27 (= Q25), V46 (≠ L44), R47 (≠ Y45), S51 (= S50), P80 (= P79), D81 (= D80), I83 (≠ F82), L87 (≠ V86), H106 (= H105), P131 (= P130)
6l2iA Ilvc, a ketol-acid reductoisomerase, from streptococcus pneumoniae_wt
64% identity, 98% coverage: 1:319/327 of query aligns to 3:320/324 of 6l2iA
Q02138 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 Lactococcus lactis subsp. lactis (strain IL1403) (Streptococcus lactis) (see paper)
62% identity, 98% coverage: 1:319/327 of query aligns to 5:322/340 of Q02138
- V48 (≠ L44) mutation to L: Inversion of cofactor specificity from NADPH to NADH. Strong decrease of the affinity for NADPH and 2.5-fold increase of the affinity for NADH. 8-fold decrease of the catalytic efficiency for NADPH and 4-fold increase of the catalytic efficiency for NADH; when associated with P-49, L-52 and D-53.
- R49 (≠ Y45) mutation to P: Inversion of cofactor specificity from NADPH to NADH. Strong decrease of the affinity for NADPH and 2.5-fold increase of the affinity for NADH. 8-fold decrease of the catalytic efficiency for NADPH and 4-fold increase of the catalytic efficiency for NADH; when associated with L-48, L-52 and D-53.
- K52 (= K49) mutation to L: Inversion of cofactor specificity from NADPH to NADH. Strong decrease of the affinity for NADPH and 2.5-fold increase of the affinity for NADH. 8-fold decrease of the catalytic efficiency for NADPH and 4-fold increase of the catalytic efficiency for NADH; when associated with L-48, P-49 and D-53.
- S53 (= S50) mutation to D: Inversion of cofactor specificity from NADPH to NADH. Strong decrease of the affinity for NADPH and 2.5-fold increase of the affinity for NADH. 8-fold decrease of the catalytic efficiency for NADPH and 4-fold increase of the catalytic efficiency for NADH; when associated with L-48, P-49 and L-52.
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, 99% coverage: 3:327/327 of query aligns to 16:340/342 of D0WGK0
- YGSQ 35:38 (= YGSQ 22:25) binding
- R58 (≠ Y45) binding
- S61 (= S48) binding ; 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 (= S50) binding ; 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 80:83) binding
- G144 (= G131) binding
- D201 (= D188) binding
- E205 (= E192) binding
- S262 (= S249) binding
4kqxB Mutant slackia exigua kari ddv in complex with NAD and an inhibitor (see paper)
56% identity, 99% coverage: 3:327/327 of query aligns to 7:331/335 of 4kqxB
- active site: K132 (= K128), D192 (= D188), E196 (= E192)
- binding n-hydroxy-n-isopropyloxamic acid: P134 (= P130), D192 (= D188), E196 (= E192), E232 (= E228), I252 (= I248), S253 (= S249), A256 (= A252)
- binding magnesium ion: G27 (= G23), Q29 (= Q25), G30 (= G26), A72 (= A68), E73 (≠ Q69), A75 (= A71), L81 (= L77), N103 (≠ K99), D192 (= D188), E196 (= E192), N249 (≠ R245), S251 (= S247), I252 (= I248), I252 (= I248), S253 (= S249), N254 (= N250), E257 (= E253)
- binding nicotinamide-adenine-dinucleotide: Y26 (= Y22), G27 (= G23), S28 (= S24), Q29 (= Q25), R49 (≠ Y45), L81 (= L77), V82 (≠ L78), P83 (= P79), D84 (= D80), V90 (= V86), H109 (= H105), P134 (= P130), S251 (= S247), I252 (= I248), S253 (= S249)
Sites not aligning to the query:
4kqwA The structure of the slackia exigua kari in complex with NADP (see paper)
56% identity, 99% coverage: 3:325/327 of query aligns to 4:326/326 of 4kqwA
- active site: K129 (= K128), D189 (= D188), E193 (= E192)
- binding magnesium ion: D189 (= D188), E193 (= E192)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: Y23 (= Y22), G24 (= G23), S25 (= S24), Q26 (= Q25), R46 (≠ Y45), S49 (= S48), S51 (= S50), L78 (= L77), V79 (≠ L78), P80 (= P79), D81 (= D80), I83 (≠ F82), Q84 (= Q83), H106 (= H105), P131 (= P130), I249 (= I248), S250 (= S249)
Query Sequence
>Synpcc7942_1552 FitnessBrowser__SynE:Synpcc7942_1552
MYYDADANLDLLNGKTVAIIGYGSQGHAHALNLRDSGVNVVVGLYPGSKSAAKAEAEGLK
VLPVAEAAQAADWIMILLPDEFQKSVFENEIRPALSAGKVLAFAHGFNIHFAQIVPPADV
DVVMIAPKSPGHLVRRTYEQGQGVPCLFAIYQDASGQARDRAMAYAKGIGGTRAGILETS
FREETETDLFGEQAVLCGGLSALIKAGFETLVEAGYQPELAYFECLHEVKLIVDLIVEGG
LAAMRDSISNTAEYGDYVTGPRLITEETKAEMKRVLADIQQGRFALDFVQECGAGKPVMT
ATRRLEAEHPIESVGKDLRAMFSWLKK
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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