SitesBLAST
Comparing Ac3H11_199 FitnessBrowser__acidovorax_3H11:Ac3H11_199 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)
6ndsA Structure of an hmg-coa lyase from acenitobacter baumannii in complex with coenzyme a and 3-methylmalate
42% identity, 81% coverage: 43:324/349 of query aligns to 10:288/305 of 6ndsA
- binding coenzyme a: V52 (= V85), S53 (≠ P86), I57 (≠ L90), N84 (= N117), G87 (= G120), R90 (= R123), N113 (= N146), M114 (≠ L147), R115 (= R148)
- binding zinc ion: D17 (= D50), H207 (= H243), H209 (= H245)
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)
36% identity, 81% coverage: 29:310/349 of query aligns to 21:300/325 of P35914
- E37 (= E45) to K: in HMGCLD; activity lower than 5% respect to the wild-type; mutation to D: Normal activity.
- R41 (= R49) to Q: in HMGCLD; loss of activity and of proton exchange; dbSNP:rs121964997; mutation to M: Reduced activity, and loss of proton exchange.
- D42 (= D50) 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 (≠ A56) to N: in HMGCLD; abolishes almost all enzymatic activity
- E72 (= E80) mutation to A: Loss of activity, and reduced affinity for metal cofactor and substrate.
- S142 (≠ T150) to F: in HMGCLD; activity lower than 5% respect to the wild-type
- C174 (= C184) to Y: in HMGCLD; activity lower than 5% respect to the wild-type; dbSNP:rs765475941
- F192 (≠ L202) to S: in HMGCLD; activity lower than 5% respect to the wild-type
- I200 (≠ V210) to F: in HMGCLD; activity lower than 5% respect to the wild-type
- G203 (≠ A213) to E: in HMGCLD; complete loss of activity; dbSNP:rs1553131940
- D204 (= D214) mutation to A: Reduced activity, and reduced affinity for metal cofactor and substrate.
- H233 (= H243) to R: in HMGCLD; loss of activity; dbSNP:rs727503963; mutation to A: Loss of activity, and reduced proton exchange rate.
- E279 (= E289) mutation to A: Reduced thermal stability, but normal activity.
- D280 (= D290) mutation to A: Normal activity.
Sites not aligning to the query:
- 323 modified: Interchain; C→S: Abolishes interchain homodimerization. Exhibits no DTT stimulated activity.
3mp3B Crystal structure of human lyase in complex with inhibitor hg-coa (see paper)
36% identity, 79% coverage: 36:310/349 of query aligns to 1:273/296 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 (= R49), D15 (= D50), Q18 (= Q53), F49 (= F84), V50 (= V85), S51 (≠ P86), W54 (≠ L89), P81 (= P116), N82 (= N117), K84 (= K119), G85 (= G120), N111 (= N146), R122 (≠ E157), Y140 (≠ G177), S142 (≠ G179), T178 (= T215), H206 (= H243)
- binding magnesium ion: D15 (= D50), H206 (= H243), H208 (= H245)
2cw6A Crystal structure of human hmg-coa lyase: insights into catalysis and the molecular basis for hydroxymethylglutaric aciduria (see paper)
36% identity, 79% coverage: 36:310/349 of query aligns to 1:273/296 of 2cw6A
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, 80% coverage: 32:310/349 of query aligns to 69:345/370 of Q8TB92
- R86 (= R49) mutation to Q: Abolishes catalytic activity.
- L237 (= L202) mutation to S: Abolishes catalytic activity.
- H278 (= H243) 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.
3mp5B Crystal structure of human lyase r41m in complex with hmg-coa (see paper)
36% identity, 79% coverage: 36:310/349 of query aligns to 1:273/296 of 3mp5B
- binding 3-hydroxy-3-methylglutaryl-coenzyme a: D15 (= D50), Q18 (= Q53), S51 (≠ P86), W54 (≠ L89), F100 (≠ P135), N111 (= N146), N113 (≠ R148), Y140 (≠ G177), S142 (≠ G179), T178 (= T215), C239 (= C276)
- binding magnesium ion: D15 (= D50), H206 (= H243), H208 (= H245)
P13703 Hydroxymethylglutaryl-CoA lyase; HL; HMG-CoA lyase; 3-hydroxy-3-methylglutarate-CoA lyase; EC 4.1.3.4 from Pseudomonas mevalonii (see paper)
39% identity, 80% coverage: 43:320/349 of query aligns to 6:281/301 of P13703
- C237 (= C276) active site
1ydnA Crystal structure of the hmg-coa lyase from brucella melitensis, northeast structural genomics target lr35. (see paper)
38% identity, 77% coverage: 43:309/349 of query aligns to 6:270/283 of 1ydnA
6ktqA Crystal structure of catalytic domain of homocitrate synthase from sulfolobus acidocaldarius (sahcs(dram)) in complex with alpha- ketoglutarate/zn2+/coa (see paper)
29% identity, 65% coverage: 48:274/349 of query aligns to 29:247/399 of 6ktqA
- binding 2-oxoglutaric acid: R30 (= R49), R154 (≠ A181), T156 (≠ G183), E158 (≠ T185), S184 (= S211), T188 (= T215), H216 (= H243), H218 (= H245)
- binding coenzyme a: V67 (≠ L89), R96 (≠ K119), A97 (≠ G120), F116 (≠ P135), H128 (≠ L147), E158 (≠ T185)
- binding zinc ion: E31 (≠ D50), H216 (= H243), H218 (= H245)
3mi3A Homocitrate synthase lys4 bound to lysine (see paper)
27% identity, 70% coverage: 30:274/349 of query aligns to 1:221/370 of 3mi3A
Q9Y823 Homocitrate synthase, mitochondrial; HCS; EC 2.3.3.14 from Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast) (see 2 papers)
27% identity, 73% coverage: 19:274/349 of query aligns to 13:255/418 of Q9Y823
- R43 (= R49) binding ; mutation R->A,K,Q: Abolishes the catalytic activity.
- E44 (≠ D50) binding ; binding ; binding
- Q47 (= Q53) mutation to A: Abolishes the catalytic activity.
- E74 (= E80) 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 (≠ P116) binding ; mutation to A: Substantially impairs catalytic efficiency.
- D123 (≠ V133) binding ; mutation to N: Does not affect the catalytic activity but impairs L-lysine inhibition.
- R163 (= R162) binding ; mutation R->A,Q: Abolishes the catalytic activity.; mutation to K: Severely diminishes affinity for 2-oxoglutarate and substantially impairs catalytic efficiency.
- S165 (≠ L164) binding ; mutation to A: Results in a moderate decrease in catalytic efficiency.
- E167 (≠ D166) mutation E->A,Q: Abolishes the catalytic activity.
- T197 (= T215) binding ; binding ; 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 (≠ A240) mutation to Q: Does not affect the catalytic activity but impairs L-lysine inhibition.
- H224 (= H243) binding ; binding
- H226 (= H245) binding ; binding
Sites not aligning to the query:
- 288 R→K: Does not affect the catalytic activity but impairs L-lysine inhibition.
- 332 Y→A: Abolishes the catalytic activity.; Y→F: Results in a decrease in catalytic efficiency.
- 364 Q→R: Does not affect the catalytic activity but impairs L-lysine inhibition.
3ivtB Homocitrate synthase lys4 bound to 2-og (see paper)
27% identity, 70% coverage: 30:274/349 of query aligns to 19:250/400 of 3ivtB
O87198 Homocitrate synthase; HCS; EC 2.3.3.14 from Thermus thermophilus (strain ATCC BAA-163 / DSM 7039 / HB27) (see paper)
30% identity, 65% coverage: 48:274/349 of query aligns to 11:226/376 of O87198
- R12 (= R49) binding
- E13 (≠ D50) binding
- H72 (≠ V113) 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 (= D130) binding
- R133 (≠ A181) binding
- S135 (≠ G183) binding
- T166 (= T215) binding ; binding
- H195 (= H243) binding
- H197 (= H245) binding
3ivsA Homocitrate synthase lys4 (see paper)
27% identity, 70% coverage: 30:274/349 of query aligns to 1:219/364 of 3ivsA
2zyfA Crystal structure of homocitrate synthase from thermus thermophilus complexed with magnesuim ion and alpha-ketoglutarate (see paper)
29% identity, 65% coverage: 48:274/349 of query aligns to 11:220/314 of 2zyfA
3a9iA Crystal structure of homocitrate synthase from thermus thermophilus complexed with lys (see paper)
29% identity, 65% coverage: 48:274/349 of query aligns to 10:219/347 of 3a9iA
3rmjB Crystal structure of truncated alpha-isopropylmalate synthase from neisseria meningitidis (see paper)
25% identity, 78% coverage: 40:310/349 of query aligns to 3:266/308 of 3rmjB
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)
25% identity, 79% coverage: 36:310/349 of query aligns to 2:269/517 of Q9JZG1
- D16 (= D50) binding
- H204 (= H243) binding
- H206 (= H245) binding
- N240 (= N285) binding
Sites not aligning to the query:
- 366:517 Required for the condensation reaction. Not required to bind substrate
2ztjA Crystal structure of homocitrate synthase from thermus thermophilus complexed with alpha-ketoglutarate (see paper)
29% identity, 65% coverage: 48:274/349 of query aligns to 11:218/312 of 2ztjA
Q9FG67 Methylthioalkylmalate synthase 1, chloroplastic; 2-isopropylmalate synthase 3; EC 2.3.3.17 from Arabidopsis thaliana (Mouse-ear cress) (see paper)
26% identity, 54% coverage: 132:319/349 of query aligns to 185:368/506 of Q9FG67
- A290 (≠ C241) mutation to T: In gsm1-2; loss of conversion of C3 to C4 glucosinolates.
Sites not aligning to the query:
- 102 S→F: In gsm1-1; loss of conversion of C3 to C4 glucosinolates.
Query Sequence
>Ac3H11_199 FitnessBrowser__acidovorax_3H11:Ac3H11_199
MASKMYFLILLGISKIDGRTPPAGDDTVLTPSTASTTPARATVREVGLRDGLQSIATVVS
TAQKIEWLNAAYAAGQREIEVGSFVPARLLPQLADTADVLAHAKTLPGLVASVLVPNVKG
AERALECGADLMVVPLSASHAHSLANLRKTPDEVVAEVARIRALRDASGRSTLIEGGVGT
AFGCTLQGEVAESEVLRLMQALLDAGADHVSLADTVGFADPASVARLFDKARALVGDRLA
CAHFHDTRGMGLANVYAAWQTGITRFDACLAGIGGCPHAPGASGNVTTEDLVFMLERMGV
ATGIDVSALLALRQRVAGWLAGETLHGTLWQAGLPQNAAPAALREAATA
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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