SitesBLAST
Comparing 17826 FitnessBrowser__Keio:17826 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)
P05793 Ketol-acid reductoisomerase (NADP(+)); KARI; Acetohydroxy-acid isomeroreductase; AHIR; Alpha-keto-beta-hydroxylacyl reductoisomerase; Ketol-acid reductoisomerase type 2; Ketol-acid reductoisomerase type II; EC 1.1.1.86 from Escherichia coli (strain K12) (see 5 papers)
100% identity, 100% coverage: 1:491/491 of query aligns to 1:491/491 of P05793
- M1 (= M1) modified: Initiator methionine, Removed
- CGAQ 45:48 (= CGAQ 45:48) binding
- R68 (= R68) mutation to D: Inversion of cofactor specificity from NADPH to NADH; when associated with L-69, V-75 and D-76.; mutation to Q: 18-fold decrease of the catalytic efficiency and 3-fold decrease of the affinity for NADPH.
- K69 (= K69) mutation to L: Does not significantly alter the affinity for NADPH. Slight increase of the catalytic efficiency. Inversion of cofactor specificity from NADPH to NADH; when associated with D-68, V-75 and D-76.
- A71 (= A71) mutation to S: 7- and 2.5-fold increase of the reductoisomerase activity with NADH and NADPH, respectively.
- K75 (= K75) mutation to Q: 13-fold decrease of the catalytic efficiency and 3-fold increase of the affinity for NADPH.; mutation to V: Inversion of cofactor specificity from NADPH to NADH; when associated with D-68, L-69 and D-76.
- R76 (= R76) binding ; mutation to D: 3-fold increase of the reductoisomerase activity with NADH and slight decrease of the reductoisomerase activity with NADPH.; mutation to D: Strong increase of catalytic efficiency and 2.5-fold increase of the affinity for NADH. 4-fold decrease of the catalytic efficiency and strong decrease of the affinity for NADPH. Inversion of cofactor specificity from NADPH to NADH; when associated with D-68, L-69 and V-75.; mutation to Q: 20-fold decrease of the catalytic efficiency and 5-fold decrease of the affinity for NADPH.
- S78 (= S78) binding ; mutation to D: 12-fold increase of the reductoisomerase activity with NADH and slight decrease of the reductoisomerase activity with NADPH.
- DKQ 108:110 (= DKQ 108:110) binding
- Q110 (= Q110) mutation Q->V,A: 12- and 2-fold increase of the reductoisomerase activity with NADH and NADPH, respectively.
- H132 (= H132) mutation to K: Loss of reductoisomerase activity.; mutation to Q: Loss of reductoisomerase activity. The reductase activity with 3-hydroxypyruvate and HMKB is nearly normal, and the isomerase activity decreases 24-fold.
- K155 (= K155) mutation K->E,Q: Loss of reductoisomerase activity.; mutation to R: Loss of reductoisomerase activity. The reductase activity with 3-hydroxypyruvate and HMKB is nearly normal, and the isomerase activity decreases 40-fold.
- E213 (= E213) mutation to D: Loss of reductoisomerase activity. 1.5-fold decrease of the reductase activity with 3-hydroxypyruvate and the isomerase activity decreases 48-fold.
- D217 (= D217) binding ; binding ; mutation D->E,N: Loss of reductoisomerase activity.
- E221 (= E221) mutation E->D,Q: Loss of reductoisomerase activity.
- E389 (= E389) binding ; mutation to D: Loss of reductoisomerase activity. 1.5-fold decrease of the reductase activity with 3-hydroxypyruvate and the isomerase activity decreases 4-fold.; mutation to Q: Loss of reductoisomerase activity.
- E393 (= E393) binding ; mutation to D: Loss of reductoisomerase activity. The reductase activity with HMKB is nearly normal.
- S414 (= S414) mutation to A: Loss of reductoisomerase activity. The isomerase activity decreases 15-fold.; mutation to T: Loss of reductoisomerase activity. The isomerase activity decreases 24-fold.
3ulkA E. Coli ketol-acid reductoisomerase in complex with NADPH and mg2+ (see paper)
100% identity, 100% coverage: 1:489/491 of query aligns to 1:489/489 of 3ulkA
- active site: K155 (= K155), D217 (= D217), E221 (= E221)
- binding magnesium ion: D217 (= D217), E389 (= E389), E393 (= E393)
- binding nadph dihydro-nicotinamide-adenine-dinucleotide phosphate: G46 (= G46), A47 (= A47), Q48 (= Q48), R68 (= R68), R76 (= R76), S78 (= S78), L105 (= L105), T106 (= T106), P107 (= P107), D108 (= D108), Q110 (= Q110), V114 (= V114)
5e4rA Crystal structure of domain-duplicated synthetic class ii ketol-acid reductoisomerase 2ia_kari-dd (see paper)
31% identity, 91% coverage: 35:481/491 of query aligns to 14:462/466 of 5e4rA
- active site: K130 (= K155), D190 (= D217), E194 (= E221)
- binding oxo(propan-2-ylamino)acetic acid: P132 (= P157), D190 (= D217), E194 (= E221), V388 (≠ I413), S389 (= S414), A392 (= A417)
- binding magnesium ion: D190 (= D217), E194 (= E221)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: G25 (= G46), S26 (≠ A47), Q27 (= Q48), S52 (= S78), L79 (= L105), V80 (≠ T106), P81 (= P107), D82 (= D108), V84 (vs. gap), A106 (≠ S131), H107 (= H132), P132 (= P157), A387 (≠ V412), V388 (≠ I413), S389 (= S414)
7rduA Crystal structure of campylobacter jejuni keto said reductoisomerase in complex with magnesium and oxidixized and reduced NADPH
35% identity, 57% coverage: 35:312/491 of query aligns to 15:291/329 of 7rduA
- binding nadp nicotinamide-adenine-dinucleotide phosphate: G24 (= G44), G26 (= G46), S27 (≠ A47), Q28 (= Q48), R48 (= R68), S51 (≠ R76), S53 (= S78), A81 (≠ T106), P82 (= P107), D83 (= D108), I89 (≠ V114), A107 (≠ S131), H108 (= H132), P130 (= P154), K131 (= K155), A132 (≠ C156)
- binding nadph dihydro-nicotinamide-adenine-dinucleotide phosphate: G24 (= G44), F25 (≠ C45), G26 (= G46), S27 (≠ A47), Q28 (= Q48), S51 (≠ R76), S53 (= S78), L80 (= L105), P82 (= P107), D83 (= D108), I89 (≠ V114), A107 (≠ S131), H108 (= H132)
7latA Campylobacter jejuni keto-acid reductoisomerase in complex with mg2+
35% identity, 57% coverage: 35:312/491 of query aligns to 15:291/329 of 7latA
4xiyA Crystal structure of ketol-acid reductoisomerase from azotobacter (see paper)
34% identity, 63% coverage: 33:341/491 of query aligns to 12:315/328 of 4xiyA
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)
34% identity, 63% coverage: 33:341/491 of query aligns to 12:315/338 of C1DFH7
- D190 (= D217) binding
- E226 (= E251) binding
- E230 (≠ Q255) binding
7q03A Ketol-acid reductoisomerase from methanothermococcus thermolithotrophicus in the close state with NADP and mg2+ (see paper)
37% identity, 58% coverage: 35:321/491 of query aligns to 14:291/328 of 7q03A
- binding magnesium ion: D190 (= D217), E194 (= E221)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: Y24 (≠ C45), G25 (= G46), S26 (≠ A47), Q27 (= Q48), R47 (= R68), S52 (= S78), L79 (= L105), I80 (≠ T106), P81 (= P107), D82 (= D108), I84 (≠ Q110), H107 (= H132), P132 (= P157)
4xdyA Structure of nadh-preferring ketol-acid reductoisomerase from an uncultured archean (see paper)
35% identity, 65% coverage: 25:341/491 of query aligns to 5:320/331 of 4xdyA
- active site: K135 (= K155), D195 (= D217), E199 (= E221)
- binding n-hydroxy-n-isopropyloxamic acid: P137 (= P157), D195 (= D217), E199 (= E221), E235 (≠ Q255), I239 (= I261), I255 (≠ L277), S256 (= S278), A259 (= A281)
- binding magnesium ion: D195 (= D217), E199 (= E221)
- binding 1,4-dihydronicotinamide adenine dinucleotide: G25 (= G46), A26 (= A47), Q27 (= Q48), E46 (≠ L67), L50 (≠ A71), N55 (≠ R76), S57 (= S78), L84 (= L105), L85 (≠ T106), P86 (= P107), D87 (= D108), I93 (≠ V114), H112 (= H132), P137 (= P157)
Q64BR7 Ketol-acid reductoisomerase (NAD(+)); KARI; Acetohydroxy-acid isomeroreductase; AHIR; Alpha-keto-beta-hydroxylacyl reductoisomerase; Ketol-acid reductoisomerase type 1; Ketol-acid reductoisomerase type I; EC 1.1.1.382 from Uncultured archaeon GZfos26G2 (see paper)
35% identity, 65% coverage: 25:341/491 of query aligns to 5:320/332 of Q64BR7
6l2iB Ilvc, a ketol-acid reductoisomerase, from streptococcus pneumoniae_wt
34% identity, 62% coverage: 35:340/491 of query aligns to 14:313/323 of 6l2iB
- binding magnesium ion: D189 (= D217), D189 (= D217), E193 (= E221), E193 (= E221)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: Y24 (≠ C45), G25 (= G46), S26 (≠ A47), Q27 (= Q48), V46 (≠ L67), R47 (= R68), S51 (= S78), P80 (= P107), D81 (= D108), I83 (≠ Q110), L87 (≠ V114), H106 (= H132), P131 (= P157)
6l2iA Ilvc, a ketol-acid reductoisomerase, from streptococcus pneumoniae_wt
34% identity, 62% coverage: 35:340/491 of query aligns to 14:313/324 of 6l2iA
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)
34% identity, 65% coverage: 23:341/491 of query aligns to 5:317/337 of P9WKJ7
- D192 (= D217) binding ; binding
- E196 (= E221) binding
- E228 (= E251) binding
- E232 (≠ Q255) binding
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)
34% identity, 65% coverage: 23:341/491 of query aligns to 1:313/325 of 4ypoA
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)
35% identity, 61% coverage: 33:332/491 of query aligns to 14:307/340 of Q02138
- V48 (≠ L67) 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 (= R68) 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 (≠ A77) 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 (= S78) 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.
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)
37% identity, 59% coverage: 35:322/491 of query aligns to 15:297/344 of C8WR67
- YGSQ 25:28 (≠ CGAQ 45:48) binding
- R48 (= R68) binding ; mutation to P: Inversion of the cofactor specificity from NADPH to NADH.
- S52 (= S78) binding ; mutation to D: Inversion of the cofactor specificity from NADPH to NADH.
- DERQ 82:85 (≠ DKQH 108:111) binding
- G133 (= G158) binding
- D190 (= D217) binding
- E194 (= E221) binding
- E226 (= E251) binding
4tskA Ketol-acid reductoisomerase from alicyclobacillus acidocaldarius (see paper)
37% identity, 59% coverage: 35:322/491 of query aligns to 14:296/333 of 4tskA
- active site: K129 (= K155), D189 (= D217), E193 (= E221)
- binding magnesium ion: D189 (= D217), D189 (= D217), E193 (= E221), E193 (= E221), R246 (≠ M274), Y247 (≠ D275), I249 (≠ L277), D251 (≠ N279), Q254 (≠ K282)
- binding nadph dihydro-nicotinamide-adenine-dinucleotide phosphate: Y24 (≠ C45), G25 (= G46), S26 (≠ A47), Q27 (= Q48), L46 (= L67), R47 (= R68), S51 (= S78), L78 (= L105), L79 (≠ T106), P80 (= P107), D81 (= D108), H106 (= H132), P131 (= P157)
4kqwA The structure of the slackia exigua kari in complex with NADP (see paper)
33% identity, 63% coverage: 35:341/491 of query aligns to 13:314/326 of 4kqwA
- active site: K129 (= K155), D189 (= D217), E193 (= E221)
- binding magnesium ion: D189 (= D217), E193 (= E221)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: Y23 (≠ C45), G24 (= G46), S25 (≠ A47), Q26 (= Q48), R46 (= R68), S49 (≠ R76), S51 (= S78), L78 (= L105), V79 (≠ T106), P80 (= P107), D81 (= D108), I83 (≠ Q110), Q84 (≠ H111), H106 (= H132), P131 (= P157), I249 (≠ L277), S250 (= S278)
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)
33% identity, 63% coverage: 35:341/491 of query aligns to 25:326/342 of D0WGK0
- YGSQ 35:38 (≠ CGAQ 45:48) binding
- R58 (= R68) binding
- S61 (≠ R76) 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 (= S78) 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 (≠ DKQH 108:111) binding
- G144 (= G158) binding
- D201 (= D217) binding
- E205 (= E221) binding
- S262 (= S278) binding
E0SRA9 Ketol-acid reductoisomerase (NAD(P)(+)); KARI; Acetohydroxy-acid isomeroreductase; AHIR; Alpha-keto-beta-hydroxylacyl reductoisomerase; Ketol-acid reductoisomerase type 1; Ketol-acid reductoisomerase type I; EC 1.1.1.383 from Ignisphaera aggregans (strain DSM 17230 / JCM 13409 / AQ1.S1) (see paper)
36% identity, 57% coverage: 35:313/491 of query aligns to 15:288/335 of E0SRA9
Query Sequence
>17826 FitnessBrowser__Keio:17826
MANYFNTLNLRQQLAQLGKCRFMGRDEFADGASYLQGKKVVIVGCGAQGLNQGLNMRDSG
LDISYALRKEAIAEKRASWRKATENGFKVGTYEELIPQADLVINLTPDKQHSDVVRTVQP
LMKDGAALGYSHGFNIVEVGEQIRKDITVVMVAPKCPGTEVREEYKRGFGVPTLIAVHPE
NDPKGEGMAIAKAWAAATGGHRAGVLESSFVAEVKSDLMGEQTILCGMLQAGSLLCFDKL
VEEGTDPAYAEKLIQFGWETITEALKQGGITLMMDRLSNPAKLRAYALSEQLKEIMAPLF
QKHMDDIISGEFSSGMMADWANDDKKLLTWREETGKTAFETAPQYEGKIGEQEYFDKGVL
MIAMVKAGVELAFETMVDSGIIEESAYYESLHELPLIANTIARKRLYEMNVVISDTAEYG
NYLFSYACVPLLKPFMAELQPGDLGKAIPEGAVDNGQLRDVNEAIRSHAIEQVGKKLRGY
MTDMKRIAVAG
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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