SitesBLAST
Comparing WP_057508571.1 NCBI__GCF_001431535.1:WP_057508571.1 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)
6ndsA Structure of an hmg-coa lyase from acenitobacter baumannii in complex with coenzyme a and 3-methylmalate
65% identity, 96% coverage: 7:304/310 of query aligns to 8:305/305 of 6ndsA
- binding coenzyme a: V52 (= V51), S53 (= S52), I57 (≠ V56), N84 (= N83), G87 (= G86), R90 (= R89), N113 (= N112), M114 (= M113), R115 (= R114)
- binding zinc ion: D17 (= D16), H207 (= H206), H209 (= H208)
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)
41% identity, 92% coverage: 9:294/310 of query aligns to 35:321/325 of P35914
- E37 (= E11) to K: in HMGCLD; activity lower than 5% respect to the wild-type; mutation to D: Normal activity.
- R41 (= R15) to Q: in HMGCLD; loss of activity and of proton exchange; dbSNP:rs121964997; mutation to M: Reduced activity, and loss of proton exchange.
- D42 (= D16) 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 (≠ P22) to N: in HMGCLD; abolishes almost all enzymatic activity
- E72 (= E46) mutation to A: Loss of activity, and reduced affinity for metal cofactor and substrate.
- S142 (≠ T116) to F: in HMGCLD; activity lower than 5% respect to the wild-type
- C174 (= C147) to Y: in HMGCLD; activity lower than 5% respect to the wild-type; dbSNP:rs765475941
- F192 (≠ Y165) to S: in HMGCLD; activity lower than 5% respect to the wild-type
- I200 (= I173) to F: in HMGCLD; activity lower than 5% respect to the wild-type
- G203 (≠ A176) to E: in HMGCLD; complete loss of activity; dbSNP:rs1553131940
- D204 (= D177) mutation to A: Reduced activity, and reduced affinity for metal cofactor and substrate.
- H233 (= H206) to R: in HMGCLD; loss of activity; dbSNP:rs727503963; mutation to A: Loss of activity, and reduced proton exchange rate.
- E279 (= E252) mutation to A: Reduced thermal stability, but normal activity.
- D280 (= D253) 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)
41% identity, 92% coverage: 9:294/310 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 (= R15), D15 (= D16), Q18 (= Q19), F49 (= F50), V50 (= V51), S51 (= S52), W54 (≠ A55), P81 (= P82), N82 (= N83), K84 (= K85), G85 (= G86), N111 (= N112), R122 (≠ G123), Y140 (≠ S140), S142 (≠ A142), T178 (= T178), H206 (= H206)
- binding magnesium ion: D15 (= D16), H206 (= H206), H208 (= H208)
2cw6A Crystal structure of human hmg-coa lyase: insights into catalysis and the molecular basis for hydroxymethylglutaric aciduria (see paper)
41% identity, 92% coverage: 9:294/310 of query aligns to 8:294/296 of 2cw6A
3mp5B Crystal structure of human lyase r41m in complex with hmg-coa (see paper)
41% identity, 92% coverage: 9:294/310 of query aligns to 8:294/296 of 3mp5B
- binding 3-hydroxy-3-methylglutaryl-coenzyme a: D15 (= D16), Q18 (= Q19), S51 (= S52), W54 (≠ A55), F100 (≠ V101), N111 (= N112), N113 (≠ R114), Y140 (≠ S140), S142 (≠ A142), T178 (= T178), C239 (= C239)
- binding magnesium ion: D15 (= D16), H206 (= H206), H208 (= H208)
1ydnA Crystal structure of the hmg-coa lyase from brucella melitensis, northeast structural genomics target lr35. (see paper)
45% identity, 85% coverage: 9:272/310 of query aligns to 6:270/283 of 1ydnA
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)
38% identity, 92% coverage: 9:294/310 of query aligns to 80:366/370 of Q8TB92
- R86 (= R15) mutation to Q: Abolishes catalytic activity.
- L237 (≠ Y165) mutation to S: Abolishes catalytic activity.
- H278 (= H206) 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)
38% identity, 95% coverage: 9:301/310 of query aligns to 6:301/301 of P13703
- C237 (= C239) active site
2zyfA Crystal structure of homocitrate synthase from thermus thermophilus complexed with magnesuim ion and alpha-ketoglutarate (see paper)
30% identity, 75% coverage: 4:237/310 of query aligns to 1:220/314 of 2zyfA
2ztjA Crystal structure of homocitrate synthase from thermus thermophilus complexed with alpha-ketoglutarate (see paper)
30% identity, 75% coverage: 4:237/310 of query aligns to 1:218/312 of 2ztjA
3a9iA Crystal structure of homocitrate synthase from thermus thermophilus complexed with lys (see paper)
30% identity, 75% coverage: 5:237/310 of query aligns to 1:219/347 of 3a9iA
O87198 Homocitrate synthase; HCS; EC 2.3.3.14 from Thermus thermophilus (strain ATCC BAA-163 / DSM 7039 / HB27) (see paper)
30% identity, 75% coverage: 4:237/310 of query aligns to 1:226/376 of O87198
- R12 (= R15) binding
- E13 (≠ D16) binding
- H72 (≠ A79) 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 (≠ N99) binding
- R133 (≠ N138) binding
- S135 (= S140) binding
- T166 (= T178) binding ; binding
- H195 (= H206) binding
- H197 (= H208) binding
Q9Y823 Homocitrate synthase, mitochondrial; HCS; EC 2.3.3.14 from Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast) (see 2 papers)
24% identity, 76% coverage: 1:237/310 of query aligns to 29:255/418 of Q9Y823
- R43 (= R15) binding ; mutation R->A,K,Q: Abolishes the catalytic activity.
- E44 (≠ D16) binding ; binding ; binding
- Q47 (= Q19) mutation to A: Abolishes the catalytic activity.
- E74 (= E46) 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 (≠ A79) binding ; mutation to A: Substantially impairs catalytic efficiency.
- D123 (≠ N99) binding ; mutation to N: Does not affect the catalytic activity but impairs L-lysine inhibition.
- R163 (≠ A144) binding ; mutation R->A,Q: Abolishes the catalytic activity.; mutation to K: Severely diminishes affinity for 2-oxoglutarate and substantially impairs catalytic efficiency.
- S165 (≠ G146) binding ; mutation to A: Results in a moderate decrease in catalytic efficiency.
- E167 (≠ P148) mutation E->A,Q: Abolishes the catalytic activity.
- T197 (= T178) 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 (≠ T204) mutation to Q: Does not affect the catalytic activity but impairs L-lysine inhibition.
- H224 (= H206) binding ; binding
- H226 (= H208) 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)
24% identity, 76% coverage: 1:237/310 of query aligns to 24:250/400 of 3ivtB
3mi3A Homocitrate synthase lys4 bound to lysine (see paper)
24% identity, 76% coverage: 1:237/310 of query aligns to 6:221/370 of 3mi3A
6ktqA Crystal structure of catalytic domain of homocitrate synthase from sulfolobus acidocaldarius (sahcs(dram)) in complex with alpha- ketoglutarate/zn2+/coa (see paper)
23% identity, 73% coverage: 13:237/310 of query aligns to 28:247/399 of 6ktqA
- binding 2-oxoglutaric acid: R30 (= R15), R154 (≠ A144), T156 (≠ G146), E158 (≠ P148), S184 (≠ T174), T188 (= T178), H216 (= H206), H218 (= H208)
- binding coenzyme a: V67 (≠ A55), R96 (≠ K85), A97 (≠ G86), F116 (≠ V101), H128 (≠ M113), E158 (≠ P148)
- binding zinc ion: E31 (≠ D16), H216 (= H206), H218 (= H208)
3ivsA Homocitrate synthase lys4 (see paper)
24% identity, 76% coverage: 1:237/310 of query aligns to 6:219/364 of 3ivsA
3rmjB Crystal structure of truncated alpha-isopropylmalate synthase from neisseria meningitidis (see paper)
22% identity, 90% coverage: 7:285/310 of query aligns to 4:278/308 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)
21% identity, 92% coverage: 1:285/310 of query aligns to 1:281/517 of Q9JZG1
- D16 (= D16) binding
- H204 (= H206) binding
- H206 (= H208) binding
- N240 (= N248) binding
Sites not aligning to the query:
- 366:517 Required for the condensation reaction. Not required to bind substrate
2nx9B Crystal structure of the carboxyltransferase domain of the oxaloacetate decarboxylase na+ pump from vibrio cholerae (see paper)
32% identity, 37% coverage: 159:272/310 of query aligns to 160:266/453 of 2nx9B
Sites not aligning to the query:
Query Sequence
>WP_057508571.1 NCBI__GCF_001431535.1:WP_057508571.1
MNTVRPLIVQEVCLRDGLQIEPVFVATADKIRLADAFSALGFARIEVSSFVSPKAVPALA
DAAEVFAGMQRAPGTVYVALVPNLKGAERALAAGAGELNLVMSAGQTHNLANMRMTTDES
FEGFARIAALPRGNVLLNGSVATAFGCPFEGAQPVAKVLDLVRRYLDLGCTGITLADTTG
MANPRQVAALVEQALPLVGADALTLHFHNTRGLGLANVVAAYDAGAQRFDAALGGLGGCP
FAPGASGNICTEDLVAMCEEMGIPTGLDLPALIALSRGLPALVGHETAGQVAKAGRVADL
HPAPPGLRAA
Or try a new SitesBLAST search
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