SitesBLAST
Comparing Ac3H11_4530 FitnessBrowser__acidovorax_3H11:Ac3H11_4530 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
43% identity, 92% coverage: 6:285/306 of query aligns to 8:284/305 of 6ndsA
- binding coenzyme a: V52 (= V50), S53 (≠ P51), I57 (≠ L55), N84 (= N82), G87 (= G85), R90 (≠ A88), N113 (= N111), M114 (≠ V112), R115 (= R113)
- binding zinc ion: D17 (= D15), H207 (= H208), H209 (= H210)
3mp3B Crystal structure of human lyase in complex with inhibitor hg-coa (see paper)
40% identity, 90% coverage: 3:277/306 of query aligns to 3:275/296 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 (= R14), D15 (= D15), Q18 (= Q18), F49 (= F49), V50 (= V50), S51 (≠ P51), W54 (≠ L54), P81 (= P81), N82 (= N82), K84 (≠ R84), G85 (= G85), N111 (= N111), R122 (≠ E122), Y140 (≠ G142), S142 (= S144), T178 (= T180), H206 (= H208)
- binding magnesium ion: D15 (= D15), H206 (= H208), H208 (= H210)
2cw6A Crystal structure of human hmg-coa lyase: insights into catalysis and the molecular basis for hydroxymethylglutaric aciduria (see paper)
40% identity, 90% coverage: 3:277/306 of query aligns to 3:275/296 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)
40% identity, 90% coverage: 3:277/306 of query aligns to 30:302/325 of P35914
- E37 (= E10) to K: in HMGCLD; activity lower than 5% respect to the wild-type; mutation to D: Normal activity.
- R41 (= R14) to Q: in HMGCLD; loss of activity and of proton exchange; dbSNP:rs121964997; mutation to M: Reduced activity, and loss of proton exchange.
- D42 (= D15) 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 (≠ Q21) to N: in HMGCLD; abolishes almost all enzymatic activity
- E72 (= E45) mutation to A: Loss of activity, and reduced affinity for metal cofactor and substrate.
- S142 (≠ T115) to F: in HMGCLD; activity lower than 5% respect to the wild-type
- C174 (= C149) to Y: in HMGCLD; activity lower than 5% respect to the wild-type; dbSNP:rs765475941
- F192 (≠ C167) to S: in HMGCLD; activity lower than 5% respect to the wild-type
- I200 (≠ V175) to F: in HMGCLD; activity lower than 5% respect to the wild-type
- G203 (≠ S178) to E: in HMGCLD; complete loss of activity; dbSNP:rs1553131940
- D204 (= D179) mutation to A: Reduced activity, and reduced affinity for metal cofactor and substrate.
- H233 (= H208) to R: in HMGCLD; loss of activity; dbSNP:rs727503963; mutation to A: Loss of activity, and reduced proton exchange rate.
- E279 (= E254) mutation to A: Reduced thermal stability, but normal activity.
- D280 (= D255) mutation to A: Normal activity.
Sites not aligning to the query:
- 323 modified: Interchain; C→S: Abolishes interchain homodimerization. Exhibits no DTT stimulated activity.
3mp5B Crystal structure of human lyase r41m in complex with hmg-coa (see paper)
40% identity, 90% coverage: 3:277/306 of query aligns to 3:275/296 of 3mp5B
- binding 3-hydroxy-3-methylglutaryl-coenzyme a: D15 (= D15), Q18 (= Q18), S51 (≠ P51), W54 (≠ L54), F100 (≠ P100), N111 (= N111), N113 (≠ R113), Y140 (≠ G142), S142 (= S144), T178 (= T180), C239 (= C241)
- binding magnesium ion: D15 (= D15), H206 (= H208), H208 (= H210)
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)
39% identity, 90% coverage: 3:277/306 of query aligns to 75:347/370 of Q8TB92
- R86 (= R14) mutation to Q: Abolishes catalytic activity.
- L237 (≠ C167) mutation to S: Abolishes catalytic activity.
- H278 (= H208) 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.
P13703 Hydroxymethylglutaryl-CoA lyase; HL; HMG-CoA lyase; 3-hydroxy-3-methylglutarate-CoA lyase; EC 4.1.3.4 from Pseudomonas mevalonii (see paper)
42% identity, 87% coverage: 6:272/306 of query aligns to 4:268/301 of P13703
- C237 (= C241) active site
1ydnA Crystal structure of the hmg-coa lyase from brucella melitensis, northeast structural genomics target lr35. (see paper)
37% identity, 91% coverage: 5:283/306 of query aligns to 3:279/283 of 1ydnA
3rmjB Crystal structure of truncated alpha-isopropylmalate synthase from neisseria meningitidis (see paper)
26% identity, 93% coverage: 6:290/306 of query aligns to 4:280/308 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)
26% identity, 93% coverage: 6:290/306 of query aligns to 7:283/517 of Q9JZG1
- D16 (= D15) binding
- H204 (= H208) binding
- H206 (= H210) binding
- N240 (= N250) binding
Sites not aligning to the query:
- 366:517 Required for the condensation reaction. Not required to bind substrate
Q9FG67 Methylthioalkylmalate synthase 1, chloroplastic; 2-isopropylmalate synthase 3; EC 2.3.3.17 from Arabidopsis thaliana (Mouse-ear cress) (see paper)
27% identity, 64% coverage: 87:282/306 of query aligns to 175:366/506 of Q9FG67
- A290 (= A206) 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.
O87198 Homocitrate synthase; HCS; EC 2.3.3.14 from Thermus thermophilus (strain ATCC BAA-163 / DSM 7039 / HB27) (see paper)
30% identity, 74% coverage: 14:239/306 of query aligns to 12:226/376 of O87198
- R12 (= R14) binding
- E13 (≠ D15) binding
- H72 (≠ A78) 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 (≠ T98) binding
- R133 (≠ E140) binding
- S135 (≠ G142) binding
- T166 (= T180) binding ; binding
- H195 (= H208) binding
- H197 (= H210) binding
2zyfA Crystal structure of homocitrate synthase from thermus thermophilus complexed with magnesuim ion and alpha-ketoglutarate (see paper)
29% identity, 74% coverage: 14:239/306 of query aligns to 12:220/314 of 2zyfA
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)
27% identity, 67% coverage: 87:292/306 of query aligns to 175:381/503 of Q9FN52
- G263 (= G182) mutation to E: In gsm2-1; loss of activity and lack of C6, C7 and C8 aliphatic glucosinolates.
3a9iA Crystal structure of homocitrate synthase from thermus thermophilus complexed with lys (see paper)
29% identity, 74% coverage: 14:239/306 of query aligns to 11:219/347 of 3a9iA
2ztjA Crystal structure of homocitrate synthase from thermus thermophilus complexed with alpha-ketoglutarate (see paper)
29% identity, 74% coverage: 14:239/306 of query aligns to 12:218/312 of 2ztjA
6e1jA Crystal structure of methylthioalkylmalate synthase (bjumam1.1) from brassica juncea (see paper)
25% identity, 91% coverage: 14:292/306 of query aligns to 26:314/409 of 6e1jA
- binding coenzyme a: Q30 (= Q18), F60 (≠ S48), S63 (≠ P51), I95 (≠ M77), R97 (≠ L79), F121 (≠ P100), K132 (≠ N111), L133 (≠ V112)
- binding 4-(methylsulfanyl)-2-oxobutanoic acid: P192 (≠ S178), T194 (= T180), H225 (= H208), H227 (= H210)
- binding manganese (ii) ion: D27 (= D15), V82 (≠ L69), E84 (≠ H71), H225 (= H208), H227 (= H210)
Sites not aligning to the query:
6ktqA Crystal structure of catalytic domain of homocitrate synthase from sulfolobus acidocaldarius (sahcs(dram)) in complex with alpha- ketoglutarate/zn2+/coa (see paper)
25% identity, 74% coverage: 14:239/306 of query aligns to 30:247/399 of 6ktqA
- binding 2-oxoglutaric acid: R30 (= R14), R154 (≠ E140), T156 (≠ G142), E158 (≠ S144), S184 (≠ G176), T188 (= T180), H216 (= H208), H218 (= H210)
- binding coenzyme a: V67 (≠ M58), R96 (= R84), A97 (≠ G85), F116 (≠ P100), H128 (≠ V112), E158 (≠ S144)
- binding zinc ion: E31 (≠ D15), H216 (= H208), H218 (= H210)
3ivtB Homocitrate synthase lys4 bound to 2-og (see paper)
25% identity, 76% coverage: 8:239/306 of query aligns to 32:250/400 of 3ivtB
Q9Y823 Homocitrate synthase, mitochondrial; HCS; EC 2.3.3.14 from Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast) (see 2 papers)
25% identity, 76% coverage: 8:239/306 of query aligns to 37:255/418 of Q9Y823
- R43 (= R14) binding ; mutation R->A,K,Q: Abolishes the catalytic activity.
- E44 (≠ D15) binding ; binding ; binding
- 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 (≠ A78) binding ; mutation to A: Substantially impairs catalytic efficiency.
- D123 (≠ T98) binding ; mutation to N: Does not affect the catalytic activity but impairs L-lysine inhibition.
- R163 (≠ E140) binding ; mutation R->A,Q: Abolishes the catalytic activity.; mutation to K: Severely diminishes affinity for 2-oxoglutarate and substantially impairs catalytic efficiency.
- S165 (≠ G142) binding ; mutation to A: Results in a moderate decrease in catalytic efficiency.
- E167 (≠ S144) mutation E->A,Q: Abolishes the catalytic activity.
- T197 (= T180) 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 (≠ A206) mutation to Q: Does not affect the catalytic activity but impairs L-lysine inhibition.
- H224 (= H208) binding ; binding
- H226 (= H210) 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.
Query Sequence
>Ac3H11_4530 FitnessBrowser__acidovorax_3H11:Ac3H11_4530
MTPPEILISEVGPRDGLQSVQATMPTADKLRWIDALVAAGLREIEVGSFVPARLLPQMAD
VAEVVRHALTHPGITVMALAPNLRGAEAALAAGVHKVTLPVSASAAHSLANVRKTREAMV
EEVRAVAQLRDAQAPGTLVEVGLSTAFGCTLQGAVPEDDVLWLAGLCAEAGADEVGLSDT
TGMANPAQVRRLFTRLRAELGAKAGAAHMHNTRGLGLANCLAAYDVGVRTFDASLGGLGG
CPYAPGASGNVVTEDLVFMFEAMGITTGVDLERLMAARAPLQAGLPGEPVYGMTPEAGLP
KGWVQR
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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