SitesBLAST
Comparing WP_079649896.1 NCBI__GCF_900167915.1:WP_079649896.1 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
42% identity, 95% coverage: 1:286/302 of query aligns to 4:281/305 of 6ndsA
- binding coenzyme a: V52 (= V49), S53 (= S50), I57 (≠ A54), N84 (= N81), G87 (= G84), R90 (≠ L87), N113 (= N110), M114 (≠ V111), R115 (= R112)
- binding zinc ion: D17 (= D14), H207 (= H208), H209 (= 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, 91% coverage: 1:275/302 of query aligns to 74:345/370 of Q8TB92
- R86 (= R13) mutation to Q: Abolishes catalytic activity.
- L237 (= L167) 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.
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)
38% identity, 90% coverage: 5:275/302 of query aligns to 33:300/325 of P35914
- E37 (= E9) 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 (≠ A20) to N: in HMGCLD; abolishes almost all enzymatic activity
- E72 (= E44) mutation to A: Loss of activity, and reduced affinity for metal cofactor and substrate.
- S142 (≠ T114) 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 (≠ L167) to S: in HMGCLD; activity lower than 5% respect to the wild-type
- I200 (= I175) to F: in HMGCLD; activity lower than 5% respect to the wild-type
- G203 (≠ A178) 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 (≠ G255) 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)
38% identity, 90% coverage: 5:275/302 of query aligns to 6:273/296 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 (= R13), D15 (= D14), Q18 (= Q17), F49 (= F48), V50 (= V49), S51 (= S50), W54 (≠ L53), P81 (= P80), N82 (= N81), K84 (= K83), G85 (= G84), N111 (= N110), R122 (≠ E121), Y140 (≠ G142), S142 (≠ A144), T178 (= T180), H206 (= H208)
- binding magnesium ion: D15 (= D14), H206 (= H208), H208 (= H210)
2cw6A Crystal structure of human hmg-coa lyase: insights into catalysis and the molecular basis for hydroxymethylglutaric aciduria (see paper)
38% identity, 90% coverage: 5:275/302 of query aligns to 6:273/296 of 2cw6A
3mp5B Crystal structure of human lyase r41m in complex with hmg-coa (see paper)
38% identity, 90% coverage: 5:275/302 of query aligns to 6:273/296 of 3mp5B
- binding 3-hydroxy-3-methylglutaryl-coenzyme a: D15 (= D14), Q18 (= Q17), S51 (= S50), W54 (≠ L53), F100 (≠ V99), N111 (= N110), N113 (≠ R112), Y140 (≠ G142), S142 (≠ A144), T178 (= T180), C239 (= C241)
- binding magnesium ion: D15 (= D14), H206 (= H208), H208 (= H210)
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, 90% coverage: 3:274/302 of query aligns to 2:270/301 of P13703
- C237 (= C241) active site
1ydnA Crystal structure of the hmg-coa lyase from brucella melitensis, northeast structural genomics target lr35. (see paper)
36% identity, 92% coverage: 2:280/302 of query aligns to 1:283/283 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)
26% identity, 75% coverage: 13:239/302 of query aligns to 30:247/399 of 6ktqA
- binding 2-oxoglutaric acid: R30 (= R13), R154 (≠ A146), T156 (≠ G148), E158 (≠ T150), S184 (≠ N176), T188 (= T180), H216 (= H208), H218 (= H210)
- binding coenzyme a: V67 (≠ L53), R96 (≠ K83), A97 (≠ G84), F116 (≠ V99), H128 (≠ V111), E158 (≠ T150)
- binding zinc ion: E31 (≠ D14), H216 (= H208), H218 (= H210)
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)
26% identity, 89% coverage: 13:282/302 of query aligns to 93:366/503 of Q9FN52
- G263 (= G182) mutation to E: In gsm2-1; loss of activity and lack of C6, C7 and C8 aliphatic glucosinolates.
P0DO78 Methylthioalkylmalate synthase 1-2, chloroplastic; EjMAM1-2; EC 2.3.3.17 from Eutrema japonicum (Wasabi plant) (Eutrema wasabi) (see paper)
24% identity, 90% coverage: 13:284/302 of query aligns to 93:368/503 of P0DO78
- R93 (= R13) mutation to A: Lost catalytic activity.
- D94 (= D14) mutation to A: Lost catalytic activity.
- H292 (= H208) mutation to A: Lost catalytic activity.
- H294 (= H210) mutation to A: Lost catalytic activity.
Sites not aligning to the query:
- 392 H→A: Lost catalytic activity.
3ivtB Homocitrate synthase lys4 bound to 2-og (see paper)
22% identity, 75% coverage: 13:239/302 of query aligns to 38:250/400 of 3ivtB
Q9Y823 Homocitrate synthase, mitochondrial; HCS; EC 2.3.3.14 from Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast) (see 2 papers)
22% identity, 75% coverage: 13:239/302 of query aligns to 43:255/418 of Q9Y823
- R43 (= R13) binding 2-oxoglutarate; mutation R->A,K,Q: Abolishes the catalytic activity.
- E44 (≠ D14) binding 2-oxoglutarate; binding L-lysine; binding Zn(2+)
- Q47 (= Q17) mutation to A: Abolishes the catalytic activity.
- E74 (= E44) 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 (≠ G72) binding 2-oxoglutarate; mutation to A: Substantially impairs catalytic efficiency.
- D123 (≠ Y97) binding L-lysine; mutation to N: Does not affect the catalytic activity but impairs L-lysine inhibition.
- R163 (≠ A146) binding 2-oxoglutarate; mutation R->A,Q: Abolishes the catalytic activity.; mutation to K: Severely diminishes affinity for 2-oxoglutarate and substantially impairs catalytic efficiency.
- S165 (≠ G148) binding 2-oxoglutarate; mutation to A: Results in a moderate decrease in catalytic efficiency.
- E167 (≠ T150) mutation E->A,Q: Abolishes the catalytic activity.
- T197 (= T180) binding 2-oxoglutarate; binding L-lysine; 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 2-oxoglutarate; binding Zn(2+)
- H226 (= H210) binding 2-oxoglutarate; binding Zn(2+)
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.
4mfeA Structure of the carboxyl transferase domain from rhizobium etli pyruvate carboxylase with 3-hydroxypyruvate (see paper)
38% identity, 29% coverage: 158:245/302 of query aligns to 228:314/597 of 4mfeA
Sites not aligning to the query:
- active site: 79, 185, 412
- binding 3-hydroxypyruvic acid: 78, 82, 116, 149, 151, 411, 412
- binding biotin: 9, 19, 596
- binding magnesium ion: 64, 65, 67
- binding zinc ion: 79
4mfdA Structure of the carboxyl transferase domain from rhizobium etli pyruvate carboxylase with oxalate (see paper)
38% identity, 29% coverage: 158:245/302 of query aligns to 228:314/597 of 4mfdA
Sites not aligning to the query:
4m6vA Structure of the carboxyl transferase domain from rhizobium etli pyruvate carboxylase with pyruvate and biocytin (see paper)
38% identity, 29% coverage: 158:245/302 of query aligns to 228:314/597 of 4m6vA
Sites not aligning to the query:
- active site: 79, 185, 412
- binding Biocytin: 9, 12, 17, 18, 19, 20, 24, 124, 354, 376, 531, 596
- binding magnesium ion: 64, 65, 67
- binding pyruvic acid: 82, 149, 151, 412
- binding zinc ion: 79
4jx5A Structure of the carboxyl transferase domain from rhizobium etli pyruvate carboxylase with pyruvate (see paper)
38% identity, 29% coverage: 158:245/302 of query aligns to 228:314/597 of 4jx5A
Sites not aligning to the query:
4mimA Structure of the carboxyl transferase domain from rhizobium etli pyruvate carboxylase with 3-bromopyruvate (see paper)
38% identity, 29% coverage: 158:245/302 of query aligns to 228:314/595 of 4mimA
Sites not aligning to the query:
4locA Structure of the carboxyl transferase domain from rhizobium etli pyruvate carboxylase with oxamate and biotin (see paper)
38% identity, 29% coverage: 158:245/302 of query aligns to 228:314/595 of 4locA
Sites not aligning to the query:
2qf7B Crystal structure of a complete multifunctional pyruvate carboxylase from rhizobium etli (see paper)
38% identity, 29% coverage: 158:245/302 of query aligns to 647:733/1017 of 2qf7B
Sites not aligning to the query:
- active site: 123, 150, 169, 195, 234, 236, 250, 252, 254, 258, 306, 498, 604, 831
- binding phosphothiophosphoric acid-adenylate ester: 148, 150, 153, 161, 164, 169, 193, 236, 238, 249, 250, 407
- binding magnesium ion: 236, 250, 483, 484, 486
- binding zinc ion: 498
Query Sequence
>WP_079649896.1 NCBI__GCF_900167915.1:WP_079649896.1
MSETVQLREVGPRDGLQMTATILSTEQKLEWCRREVAAGLVDIEVTSFVSPKLAPQFADA
ADVARRAILIEGCRPAALVPNLKGAQLALEAGLTSLYFVMSASEAHNRANVRRTTEESLD
EFRRIIEHRDTMPGKKAWIGSGIATAFGCTIQGEVPERRVVEIAARLAEAGADGINVADT
VGYGDPAQVRRLVKAVMDEVAPLPVACHFHDTRGLGLANILAAVDVGVRSFDASLAGIGG
CPFAPSASGNVDTEGTAFLLERLGLDTGIDLEALMALRQEVERWLPGEQFARGVGVAGLP
RR
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