SitesBLAST
Comparing WP_078427294.1 NCBI__GCF_002019605.1:WP_078427294.1 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)
Q9JZG1 2-isopropylmalate synthase; Alpha-IPM synthase; Alpha-isopropylmalate synthase; EC 2.3.3.13 from Neisseria meningitidis serogroup B (strain MC58) (see 2 papers)
45% identity, 96% coverage: 2:501/520 of query aligns to 3:502/517 of Q9JZG1
- D16 (= D15) binding Mn(2+)
- H204 (= H203) binding Mn(2+)
- H206 (= H205) binding Mn(2+)
- N240 (= N239) binding Mn(2+)
Sites not aligning to the query:
- 366:517 Required for the condensation reaction. Not required to bind substrate
Q9FN52 Methylthioalkylmalate synthase 3, chloroplastic; 2-isopropylmalate synthase 2; Methylthioalkylmalate synthase-like; EC 2.3.3.17 from Arabidopsis thaliana (Mouse-ear cress) (see paper)
44% identity, 73% coverage: 3:380/520 of query aligns to 82:474/503 of Q9FN52
- G263 (= G174) mutation to E: In gsm2-1; loss of activity and lack of C6, C7 and C8 aliphatic glucosinolates.
6e1jA Crystal structure of methylthioalkylmalate synthase (bjumam1.1) from brassica juncea (see paper)
44% identity, 73% coverage: 3:380/520 of query aligns to 15:407/409 of 6e1jA
- binding coenzyme a: Q30 (= Q18), F60 (= F48), S63 (≠ A51), I95 (≠ L74), R97 (= R76), F121 (= F100), K132 (= K111), L133 (= L112), S322 (= S298), G323 (= G299), I324 (= I300), D327 (= D303), K331 (= K307), L359 (= L332), R362 (= R335), H363 (= H336)
- binding 4-(methylsulfanyl)-2-oxobutanoic acid: P192 (= P170), T194 (= T172), H225 (= H203), H227 (= H205)
- binding manganese (ii) ion: D27 (= D15), V82 (vs. gap), E84 (vs. gap), H225 (= H203), H227 (= H205)
Q9FG67 Methylthioalkylmalate synthase 1, chloroplastic; 2-isopropylmalate synthase 3; EC 2.3.3.17 from Arabidopsis thaliana (Mouse-ear cress) (see paper)
44% identity, 73% coverage: 6:382/520 of query aligns to 85:476/506 of Q9FG67
- S102 (≠ N23) mutation to F: In gsm1-1; loss of conversion of C3 to C4 glucosinolates.
- A290 (≠ S201) mutation to T: In gsm1-2; loss of conversion of C3 to C4 glucosinolates.
3rmjB Crystal structure of truncated alpha-isopropylmalate synthase from neisseria meningitidis (see paper)
48% identity, 62% coverage: 4:323/520 of query aligns to 2:308/308 of 3rmjB
6ktqA Crystal structure of catalytic domain of homocitrate synthase from sulfolobus acidocaldarius (sahcs(dram)) in complex with alpha- ketoglutarate/zn2+/coa (see paper)
35% identity, 73% coverage: 5:382/520 of query aligns to 21:389/399 of 6ktqA
- binding 2-oxoglutaric acid: R30 (= R14), R154 (≠ E138), T156 (≠ S140), E158 (= E142), S184 (≠ N168), T188 (= T172), H216 (= H203), H218 (= H205)
- binding coenzyme a: V67 (≠ A51), R96 (= R76), A97 (≠ T77), F116 (= F100), H128 (≠ L112), E158 (= E142)
- binding zinc ion: E31 (≠ D15), H216 (= H203), H218 (= H205)
3ivtB Homocitrate synthase lys4 bound to 2-og (see paper)
31% identity, 71% coverage: 8:374/520 of query aligns to 32:389/400 of 3ivtB
Q9Y823 Homocitrate synthase, mitochondrial; HCS; EC 2.3.3.14 from Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast) (see 2 papers)
31% identity, 71% coverage: 8:374/520 of query aligns to 37:394/418 of Q9Y823
- R43 (= R14) binding 2-oxoglutarate; mutation R->A,K,Q: Abolishes the catalytic activity.
- E44 (≠ D15) binding 2-oxoglutarate; binding L-lysine; binding Zn(2+)
- Q47 (= Q18) mutation to A: Abolishes the catalytic activity.
- E74 (= E45) mutation to A: Abolishes the catalytic activity.; mutation to Q: Results in a moderate decrease in the turnover number and a slight increase in the Km value for each substrate.
- H103 (≠ L74) binding 2-oxoglutarate; mutation to A: Substantially impairs catalytic efficiency.
- D123 (≠ H98) binding L-lysine; mutation to N: Does not affect the catalytic activity but impairs L-lysine inhibition.
- R163 (≠ E138) binding 2-oxoglutarate; mutation R->A,Q: Abolishes the catalytic activity.; mutation to K: Severely diminishes affinity for 2-oxoglutarate and substantially impairs catalytic efficiency.
- S165 (= S140) binding 2-oxoglutarate; mutation to A: Results in a moderate decrease in catalytic efficiency.
- E167 (= E142) mutation E->A,Q: Abolishes the catalytic activity.
- T197 (= T172) binding 2-oxoglutarate; binding L-lysine; mutation to A: Exhibits a 25-fold decrease in catalytic efficiency.; mutation to S: Results in a modest decrease in catalytic efficiency.; mutation to V: Abolishes the catalytic activity.
- E222 (≠ S201) mutation to Q: Does not affect the catalytic activity but impairs L-lysine inhibition.
- H224 (= H203) binding 2-oxoglutarate; binding Zn(2+)
- H226 (= H205) binding 2-oxoglutarate; binding Zn(2+)
- R288 (≠ A268) mutation to K: Does not affect the catalytic activity but impairs L-lysine inhibition.
- Y332 (= Y312) mutation to A: Abolishes the catalytic activity.; mutation to F: Results in a decrease in catalytic efficiency.
- Q364 (≠ E344) mutation to R: Does not affect the catalytic activity but impairs L-lysine inhibition.
3mi3A Homocitrate synthase lys4 bound to lysine (see paper)
31% identity, 71% coverage: 8:374/520 of query aligns to 14:360/370 of 3mi3A
O87198 Homocitrate synthase; HCS; EC 2.3.3.14 from Thermus thermophilus (strain ATCC BAA-163 / DSM 7039 / HB27) (see paper)
32% identity, 71% coverage: 1:367/520 of query aligns to 1:358/376 of O87198
- R12 (= R14) binding 2-oxoglutarate
- E13 (≠ D15) binding Mg(2+)
- H72 (≠ L74) binding 2-oxoglutarate; mutation to L: Significant decrease in sensitivity to lysine inhibition. Large decrease in affinity for 2-oxoglutarate. Almost no effect on affinity for acetyl-CoA and on turnover number.
- D92 (≠ H98) binding L-lysine
- R133 (vs. gap) binding 2-oxoglutarate
- S135 (= S140) binding L-lysine
- T166 (= T172) binding 2-oxoglutarate; binding L-lysine
- H195 (= H203) binding Mg(2+)
- H197 (= H205) binding Mg(2+)
3ivsA Homocitrate synthase lys4 (see paper)
31% identity, 71% coverage: 8:375/520 of query aligns to 14:356/364 of 3ivsA
Q8F3Q1 (R)-citramalate synthase CimA; LiCMS; EC 2.3.3.21 from Leptospira interrogans serogroup Icterohaemorrhagiae serovar Lai (strain 56601) (see 2 papers)
27% identity, 95% coverage: 8:502/520 of query aligns to 10:511/516 of Q8F3Q1