SitesBLAST
Comparing GFF1364 FitnessBrowser__WCS417:GFF1364 to proteins with known functional sites using BLASTp with E ≤ 0.001.
Or try Sites on a Tree, PaperBLAST, Conserved Domains, or compare to all protein structures
Found 20 (the maximum) hits to proteins with known functional sites (download)
6ndsA Structure of an hmg-coa lyase from acenitobacter baumannii in complex with coenzyme a and 3-methylmalate
70% identity, 98% coverage: 2:307/313 of query aligns to 1:305/305 of 6ndsA
- binding coenzyme a: Q20 (= Q21), F51 (= F52), V52 (= V53), S53 (= S54), P54 (= P55), A56 (= A57), I57 (= I58), L81 (= L82), P83 (= P84), N84 (= N85), K86 (= K87), G87 (= G88), R90 (= R91), N113 (= N114), M114 (= M115), R115 (= R116), C240 (= C242)
- binding zinc ion: D17 (= D18), H207 (= H209), H209 (= H211)
3mp3B Crystal structure of human lyase in complex with inhibitor hg-coa (see paper)
39% identity, 92% coverage: 11:297/313 of query aligns to 8:294/296 of 3mp3B
- binding (3R,5S,9R,21S)-1-[(2R,3S,4R,5R)-5-(6-amino-9H-purin-9-yl)-4-hydroxy-3-(phosphonooxy)tetrahydrofuran-2-yl]-3,5,9,21-tetrahydroxy-8,8-dimethyl-10,14,19-trioxo-2,4,6-trioxa-18-thia-11,15-diaza-3,5-diphosphatricosan-23-oic acid 3,5-dioxide: R14 (= R17), D15 (= D18), Q18 (= Q21), F49 (= F52), V50 (= V53), S51 (= S54), P52 (= P55), K53 (= K56), W54 (≠ A57), H61 (≠ G64), L79 (= L82), P81 (= P84), N82 (= N85), K84 (= K87), G85 (= G88), F100 (≠ V103), N111 (= N114), I112 (≠ M115), N113 (≠ R116), R122 (≠ A125), Y140 (≠ S143), S142 (≠ A145), T178 (= T181), H206 (= H209), H208 (= H211)
- binding magnesium ion: D15 (= D18), H206 (= H209), H208 (= H211)
2cw6A Crystal structure of human hmg-coa lyase: insights into catalysis and the molecular basis for hydroxymethylglutaric aciduria (see paper)
39% identity, 92% coverage: 11:297/313 of query aligns to 8:294/296 of 2cw6A
P35914 Hydroxymethylglutaryl-CoA lyase, mitochondrial; HL; HMG-CoA lyase; 3-hydroxy-3-methylglutarate-CoA lyase; EC 4.1.3.4 from Homo sapiens (Human) (see 11 papers)
39% identity, 94% coverage: 11:303/313 of query aligns to 35:325/325 of P35914
- E37 (= E13) to K: in HMGCLD; activity lower than 5% respect to the wild-type; mutation to D: Normal activity.
- R41 (= R17) to Q: in HMGCLD; loss of activity and of proton exchange; dbSNP:rs121964997; mutation to M: Reduced activity, and loss of proton exchange.
- D42 (= D18) to E: in HMGCLD; reduced activity; to G: in HMGCLD; loss of activity; dbSNP:rs1467902610; to H: in HMGCLD; loss of activity; mutation D->A,N: Loss of activity, and reduced proton exchange rate.
- K48 (≠ P24) to N: in HMGCLD; abolishes almost all enzymatic activity
- E72 (= E48) mutation to A: Loss of activity, and reduced affinity for metal cofactor and substrate.
- S142 (≠ R118) to F: in HMGCLD; activity lower than 5% respect to the wild-type
- C174 (= C150) to Y: in HMGCLD; activity lower than 5% respect to the wild-type; dbSNP:rs765475941
- F192 (≠ Y168) to S: in HMGCLD; activity lower than 5% respect to the wild-type
- I200 (= I176) to F: in HMGCLD; activity lower than 5% respect to the wild-type
- G203 (≠ A179) to E: in HMGCLD; complete loss of activity; dbSNP:rs1553131940
- D204 (= D180) mutation to A: Reduced activity, and reduced affinity for metal cofactor and substrate.
- H233 (= H209) to R: in HMGCLD; loss of activity; dbSNP:rs727503963; mutation to A: Loss of activity, and reduced proton exchange rate.
- E279 (= E255) mutation to A: Reduced thermal stability, but normal activity.
- D280 (= D256) mutation to A: Normal activity.
- C323 (= C301) modified: Interchain; mutation to S: Abolishes interchain homodimerization. Exhibits no DTT stimulated activity.
3mp5B Crystal structure of human lyase r41m in complex with hmg-coa (see paper)
39% identity, 92% coverage: 11:297/313 of query aligns to 8:294/296 of 3mp5B
- binding 3-hydroxy-3-methylglutaryl-coenzyme a: D15 (= D18), Q18 (= Q21), S51 (= S54), P52 (= P55), K53 (= K56), W54 (≠ A57), H61 (≠ G64), L79 (= L82), F100 (≠ V103), N111 (= N114), I112 (≠ M115), N113 (≠ R116), R122 (≠ A125), Y140 (≠ S143), S142 (≠ A145), G176 (≠ A179), T178 (= T181), H206 (= H209), H208 (= H211), C239 (= C242)
- binding magnesium ion: D15 (= D18), H206 (= H209), H208 (= H211)
Q8TB92 3-hydroxy-3-methylglutaryl-CoA lyase, cytoplasmic; 3-hydroxy-3-methylglutaryl-CoA lyase-like protein 1; HMGCL-like 1; Endoplasmic reticulum 3-hydroxy-3-methylglutaryl-CoA lyase; er-cHL; EC 4.1.3.4 from Homo sapiens (Human) (see 2 papers)
35% identity, 93% coverage: 11:300/313 of query aligns to 80:369/370 of Q8TB92
- R86 (= R17) mutation to Q: Abolishes catalytic activity.
- L237 (≠ Y168) mutation to S: Abolishes catalytic activity.
- H278 (= H209) mutation to R: Abolishes catalytic activity.
Sites not aligning to the query:
- 2 modified: N-myristoyl glycine; G→A: Abolishes myristoylation and induces a subcellular location change.
1ydnA Crystal structure of the hmg-coa lyase from brucella melitensis, northeast structural genomics target lr35. (see paper)
41% identity, 85% coverage: 11:275/313 of query aligns to 6:270/283 of 1ydnA
P13703 Hydroxymethylglutaryl-CoA lyase; HL; HMG-CoA lyase; 3-hydroxy-3-methylglutarate-CoA lyase; EC 4.1.3.4 from Pseudomonas mevalonii (see paper)
35% identity, 90% coverage: 7:287/313 of query aligns to 2:282/301 of P13703
- C237 (= C242) active site
6ktqA Crystal structure of catalytic domain of homocitrate synthase from sulfolobus acidocaldarius (sahcs(dram)) in complex with alpha- ketoglutarate/zn2+/coa (see paper)
28% identity, 72% coverage: 17:240/313 of query aligns to 30:247/399 of 6ktqA
- binding 2-oxoglutaric acid: R30 (= R17), E31 (≠ D18), H94 (≠ N85), R154 (= R139), T156 (≠ N141), E158 (≠ S143), S184 (= S177), A186 (= A179), T188 (= T181), H216 (= H209), H218 (= H211), H240 (≠ D233)
- binding coenzyme a: H64 (≠ S51), V67 (≠ A57), R96 (≠ K87), A97 (≠ G88), V98 (≠ A89), F116 (≠ V103), Y117 (≠ M104), K127 (≠ N114), H128 (≠ M115), E158 (≠ S143)
- binding zinc ion: E31 (≠ D18), H216 (= H209), H218 (= H211)
3ivtB Homocitrate synthase lys4 bound to 2-og (see paper)
27% identity, 73% coverage: 13:240/313 of query aligns to 34:250/400 of 3ivtB
- active site: Q42 (= Q21)
- binding 2-oxoglutaric acid: R38 (= R17), E39 (≠ D18), H98 (≠ A81), V120 (= V103), R158 (≠ N141), S160 (= S143), A190 (= A179), T192 (= T181), H219 (= H209), H221 (= H211)
- binding zinc ion: E39 (≠ D18), H219 (= H209), H221 (= H211)
3mi3A Homocitrate synthase lys4 bound to lysine (see paper)
27% identity, 73% coverage: 13:240/313 of query aligns to 16:221/370 of 3mi3A
- active site: Q24 (= Q21)
- binding lysine: R20 (= R17), E21 (≠ D18), D100 (≠ N101), S131 (= S143), A161 (= A179), T163 (= T181), E188 (≠ T207), H190 (= H209), H192 (= H211)
- binding zinc ion: E21 (≠ D18), H190 (= H209), H192 (= H211)
2zyfA Crystal structure of homocitrate synthase from thermus thermophilus complexed with magnesuim ion and alpha-ketoglutarate (see paper)
29% identity, 72% coverage: 17:240/313 of query aligns to 12:220/314 of 2zyfA
- active site: Q16 (= Q21)
- binding 2-oxoglutaric acid: R12 (= R17), H72 (≠ A81), L94 (≠ V103), R127 (= R139), S129 (≠ N141), A158 (= A179), T160 (= T181), H189 (= H209), H191 (= H211)
- binding magnesium ion: E13 (≠ D18), H189 (= H209), H191 (= H211)
3ivsA Homocitrate synthase lys4 (see paper)
26% identity, 73% coverage: 13:240/313 of query aligns to 16:219/364 of 3ivsA
3a9iA Crystal structure of homocitrate synthase from thermus thermophilus complexed with lys (see paper)
29% identity, 72% coverage: 17:240/313 of query aligns to 11:219/347 of 3a9iA
- binding cobalt (ii) ion: E12 (≠ D18), H188 (= H209), H190 (= H211)
- binding lysine: R11 (= R17), E12 (≠ D18), D91 (≠ N101), L93 (≠ V103), S128 (≠ N141), A157 (= A179), T159 (= T181), H188 (= H209), H190 (= H211)
O87198 Homocitrate synthase; HCS; EC 2.3.3.14 from Thermus thermophilus (strain ATCC BAA-163 / DSM 7039 / HB27) (see paper)
30% identity, 72% coverage: 17:240/313 of query aligns to 12:226/376 of O87198
- R12 (= R17) binding
- E13 (≠ D18) binding
- H72 (≠ A81) binding ; 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 (≠ N101) binding
- R133 (= R139) binding
- S135 (≠ N141) binding
- T166 (= T181) binding ; binding
- H195 (= H209) binding
- H197 (= H211) binding
2ztjA Crystal structure of homocitrate synthase from thermus thermophilus complexed with alpha-ketoglutarate (see paper)
29% identity, 72% coverage: 17:240/313 of query aligns to 12:218/312 of 2ztjA
- active site: Q16 (= Q21)
- binding 2-oxoglutaric acid: R12 (= R17), E13 (≠ D18), H72 (≠ A81), L94 (≠ V103), R125 (= R139), S127 (≠ N141), A156 (= A179), T158 (= T181), H187 (= H209), H189 (= H211)
- binding copper (ii) ion: E13 (≠ D18), H187 (= H209), H189 (= H211)
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)
23% identity, 94% coverage: 11:304/313 of query aligns to 87:387/503 of Q9FN52