SitesBLAST
Comparing CA265_RS13115 FitnessBrowser__Pedo557:CA265_RS13115 to proteins with known functional sites using BLASTp with E ≤ 0.001.
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Found 11 hits to proteins with known functional sites (download)
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)
33% identity, 95% coverage: 7:277/286 of query aligns to 79:347/370 of Q8TB92
- R86 (= R13) mutation to Q: Abolishes catalytic activity.
- L237 (= L166) mutation to S: Abolishes catalytic activity.
- H278 (= H207) 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.
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)
32% identity, 95% coverage: 7:277/286 of query aligns to 34:302/325 of P35914
- E37 (= E10) to K: in HMGCLD; activity lower than 5% respect to the wild-type; mutation to D: Normal activity.
- R41 (= R13) to Q: in HMGCLD; loss of activity and of proton exchange; dbSNP:rs121964997; mutation to M: Reduced activity, and loss of proton exchange.
- D42 (= D14) 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 (≠ H20) to N: in HMGCLD; abolishes almost all enzymatic activity
- E72 (≠ D44) mutation to A: Loss of activity, and reduced affinity for metal cofactor and substrate.
- S142 (= S116) to F: in HMGCLD; activity lower than 5% respect to the wild-type
- C174 (≠ N148) to Y: in HMGCLD; activity lower than 5% respect to the wild-type; dbSNP:rs765475941
- F192 (≠ L166) to S: in HMGCLD; activity lower than 5% respect to the wild-type
- I200 (≠ L174) to F: in HMGCLD; activity lower than 5% respect to the wild-type
- G203 (≠ A177) to E: in HMGCLD; complete loss of activity; dbSNP:rs1553131940
- D204 (= D178) mutation to A: Reduced activity, and reduced affinity for metal cofactor and substrate.
- H233 (= H207) 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.
3mp3B Crystal structure of human lyase in complex with inhibitor hg-coa (see paper)
32% identity, 95% coverage: 7:277/286 of query aligns to 7:275/296 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 (= R13), D15 (= D14), Q18 (= Q17), F49 (= F48), V50 (= V49), S51 (= S50), W54 (≠ A53), P81 (≠ A81), N82 (= N82), K84 (≠ R84), G85 (= G85), N111 (= N112), R122 (≠ T123), Y140 (= Y141), S142 (= S143), T178 (= T179), H206 (= H207)
- binding magnesium ion: D15 (= D14), H206 (= H207), H208 (= H209)
2cw6A Crystal structure of human hmg-coa lyase: insights into catalysis and the molecular basis for hydroxymethylglutaric aciduria (see paper)
32% identity, 95% coverage: 7:277/286 of query aligns to 7:275/296 of 2cw6A
3mp5B Crystal structure of human lyase r41m in complex with hmg-coa (see paper)
31% identity, 95% coverage: 7:277/286 of query aligns to 7:275/296 of 3mp5B
- binding 3-hydroxy-3-methylglutaryl-coenzyme a: D15 (= D14), Q18 (= Q17), S51 (= S50), W54 (≠ A53), F100 (= F100), N111 (= N112), N113 (= N114), Y140 (= Y141), S142 (= S143), T178 (= T179), C239 (= C240)
- binding magnesium ion: D15 (= D14), H206 (= H207), H208 (= H209)
6ndsA Structure of an hmg-coa lyase from acenitobacter baumannii in complex with coenzyme a and 3-methylmalate
32% identity, 91% coverage: 12:272/286 of query aligns to 15:271/305 of 6ndsA
- binding coenzyme a: V52 (= V49), S53 (= S50), I57 (= I54), N84 (= N82), G87 (= G85), R90 (≠ D88), N113 (= N112), M114 (≠ T113), R115 (≠ N114)
- binding zinc ion: D17 (= D14), H207 (= H207), H209 (= H209)
1ydnA Crystal structure of the hmg-coa lyase from brucella melitensis, northeast structural genomics target lr35. (see paper)
28% identity, 93% coverage: 13:277/286 of query aligns to 12:273/283 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)
30% identity, 85% coverage: 12:255/286 of query aligns to 11:251/301 of P13703
- C237 (= C240) 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)
23% identity, 56% coverage: 79:238/286 of query aligns to 91:247/399 of 6ktqA
- binding 2-oxoglutaric acid: R154 (≠ G145), T156 (≠ G147), E158 (≠ P149), S184 (= S175), T188 (= T179), H216 (= H207), H218 (= H209)
- binding coenzyme a: R96 (= R84), A97 (≠ G85), F116 (≠ P101), H128 (≠ T113), E158 (≠ P149)
- binding zinc ion: H216 (= H207), H218 (= H209)
Sites not aligning to the query:
2nx9B Crystal structure of the carboxyltransferase domain of the oxaloacetate decarboxylase na+ pump from vibrio cholerae (see paper)
28% identity, 41% coverage: 159:276/286 of query aligns to 156:268/453 of 2nx9B
Sites not aligning to the query:
Q05920 Pyruvate carboxylase, mitochondrial; Pyruvic carboxylase; PCB; EC 6.4.1.1 from Mus musculus (Mouse) (see paper)
24% identity, 51% coverage: 94:239/286 of query aligns to 648:803/1178 of Q05920
- K717 (= K153) modified: N6-acetyllysine
- K748 (≠ T184) modified: N6-acetyllysine; mutation to Q: Reduced pyruvate carboxylase activity.
Sites not aligning to the query:
- 35 modified: N6-acetyllysine
- 39 modified: N6-acetyllysine
- 79 modified: N6-acetyllysine; alternate; mutation K->Q,R: Reduced pyruvate carboxylase activity.
- 148 modified: N6-acetyllysine
- 152 modified: N6-acetyllysine; mutation K->Q,R: Reduced pyruvate carboxylase activity.
- 241 modified: N6-acetyllysine
- 434 modified: N6-acetyllysine
- 589 modified: N6-acetyllysine
- 892 modified: N6-acetyllysine
- 969 modified: N6-acetyllysine
Query Sequence
>CA265_RS13115 FitnessBrowser__Pedo557:CA265_RS13115
MSQNNFKLVECPRDAMQGLHDFVPTKLKAEYLNLLLQVGFDTLDFGSFVSPKAIPQMADT
AEVLAQLDLSNTSTKLLAIVANLRGVEDAVKHQAVNYLGFPFSISETFQQRNTNSSIAQS
LNTVEEMLSLCAKNNKKAVVYLSMGFGNPYGDKWNYEIVEKWADVLVSRGVEILSLADTV
GISTPEKIENILPKLISRFSNTEIGIHLHSTPAERFEKIEAAYHSGVKRIDSALKGFGGC
PMAADDLTGNIATEDVITFLNMKGEKLNLNMDKWNEAMVLSGKIFG
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