SitesBLAST
Comparing N515DRAFT_0574 FitnessBrowser__Dyella79:N515DRAFT_0574 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)
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)
49% identity, 96% coverage: 20:533/535 of query aligns to 5:514/517 of Q9JZG1
- D16 (= D31) binding
- H204 (= H219) binding
- H206 (= H221) binding
- N240 (= N255) binding
Sites not aligning to the query:
- 366:517 Required for the condensation reaction. Not required to bind substrate
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)
46% identity, 71% coverage: 20:397/535 of query aligns to 83:475/503 of Q9FN52
- G263 (= G190) mutation to E: In gsm2-1; loss of activity and lack of C6, C7 and C8 aliphatic glucosinolates.
6e1jA Crystal structure of methylthioalkylmalate synthase (bjumam1.1) from brassica juncea (see paper)
45% identity, 70% coverage: 20:396/535 of query aligns to 16:407/409 of 6e1jA
- binding coenzyme a: Q30 (= Q34), F60 (= F64), S63 (≠ A67), I95 (≠ L90), R97 (= R92), F121 (= F116), K132 (= K127), L133 (= L128), S322 (= S314), G323 (= G315), I324 (= I316), D327 (≠ H319), K331 (= K323), L359 (≠ H348), R362 (= R351), H363 (= H352)
- binding 4-(methylsulfanyl)-2-oxobutanoic acid: P192 (= P186), T194 (= T188), H225 (= H219), H227 (= H221)
- binding manganese (ii) ion: D27 (= D31), V82 (≠ T86), E84 (vs. gap), H225 (= H219), H227 (= H221)
Q9FG67 Methylthioalkylmalate synthase 1, chloroplastic; 2-isopropylmalate synthase 3; EC 2.3.3.17 from Arabidopsis thaliana (Mouse-ear cress) (see paper)
45% identity, 71% coverage: 20:400/535 of query aligns to 83:478/506 of Q9FG67
- S102 (≠ G39) mutation to F: In gsm1-1; loss of conversion of C3 to C4 glucosinolates.
- A290 (≠ S217) mutation to T: In gsm1-2; loss of conversion of C3 to C4 glucosinolates.
3rmjB Crystal structure of truncated alpha-isopropylmalate synthase from neisseria meningitidis (see paper)
54% identity, 59% coverage: 20:337/535 of query aligns to 2:306/308 of 3rmjB
6ktqA Crystal structure of catalytic domain of homocitrate synthase from sulfolobus acidocaldarius (sahcs(dram)) in complex with alpha- ketoglutarate/zn2+/coa (see paper)
36% identity, 70% coverage: 21:396/535 of query aligns to 21:387/399 of 6ktqA
- binding 2-oxoglutaric acid: R30 (= R30), R154 (≠ E154), T156 (≠ S156), E158 (= E158), S184 (≠ N184), T188 (= T188), H216 (= H219), H218 (= H221)
- binding coenzyme a: V67 (≠ A67), R96 (= R92), A97 (≠ C93), F116 (= F116), H128 (≠ L128), E158 (= E158)
- binding zinc ion: E31 (≠ D31), H216 (= H219), H218 (= H221)
4ov4A Isopropylmalate synthase binding with ketoisovalerate (see paper)
31% identity, 70% coverage: 22:396/535 of query aligns to 4:378/379 of 4ov4A
4ov9A Structure of isopropylmalate synthase binding with alpha- isopropylmalate (see paper)
31% identity, 70% coverage: 22:396/535 of query aligns to 4:380/380 of 4ov9A
Q9Y823 Homocitrate synthase, mitochondrial; HCS; EC 2.3.3.14 from Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast) (see 2 papers)
30% identity, 67% coverage: 24:382/535 of query aligns to 37:386/418 of Q9Y823
- R43 (= R30) binding ; mutation R->A,K,Q: Abolishes the catalytic activity.
- E44 (≠ D31) binding ; binding ; binding
- Q47 (= Q34) mutation to A: Abolishes the catalytic activity.
- E74 (= E61) 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 (≠ L90) binding ; mutation to A: Substantially impairs catalytic efficiency.
- D123 (≠ H114) binding ; mutation to N: Does not affect the catalytic activity but impairs L-lysine inhibition.
- R163 (≠ E154) binding ; mutation R->A,Q: Abolishes the catalytic activity.; mutation to K: Severely diminishes affinity for 2-oxoglutarate and substantially impairs catalytic efficiency.
- S165 (= S156) binding ; mutation to A: Results in a moderate decrease in catalytic efficiency.
- E167 (= E158) mutation E->A,Q: Abolishes the catalytic activity.
- T197 (= T188) 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 (≠ S217) mutation to Q: Does not affect the catalytic activity but impairs L-lysine inhibition.
- H224 (= H219) binding ; binding
- H226 (= H221) binding ; binding
- R288 (≠ V284) mutation to K: Does not affect the catalytic activity but impairs L-lysine inhibition.
- Y332 (= Y328) mutation to A: Abolishes the catalytic activity.; mutation to F: Results in a decrease in catalytic efficiency.
- Q364 (≠ A360) mutation to R: Does not affect the catalytic activity but impairs L-lysine inhibition.
3ivtB Homocitrate synthase lys4 bound to 2-og (see paper)
30% identity, 67% coverage: 24:382/535 of query aligns to 32:381/400 of 3ivtB
3mi3A Homocitrate synthase lys4 bound to lysine (see paper)
30% identity, 67% coverage: 24:382/535 of query aligns to 14:352/370 of 3mi3A
O87198 Homocitrate synthase; HCS; EC 2.3.3.14 from Thermus thermophilus (strain ATCC BAA-163 / DSM 7039 / HB27) (see paper)
30% identity, 67% coverage: 23:383/535 of query aligns to 5:358/376 of O87198
- R12 (= R30) binding
- E13 (≠ D31) binding
- H72 (≠ L90) 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 (≠ I113) binding
- R133 (≠ E154) binding
- S135 (= S156) binding
- T166 (= T188) binding ; binding
- H195 (= H219) binding
- H197 (= H221) binding
Q8F3Q1 (R)-citramalate synthase CimA; LiCMS; EC 2.3.3.21 from Leptospira interrogans serogroup Icterohaemorrhagiae serovar Lai (strain 56601) (see 2 papers)
25% identity, 93% coverage: 18:516/535 of query aligns to 4:510/516 of Q8F3Q1
- R16 (= R30) mutation R->K,Q: Loss of activity.
- RD 16:17 (= RD 30:31) binding
- D17 (= D31) mutation to A: 34-fold increase in Km for pyruvate and 315-fold decrease in kcat.; mutation to N: 4.4-fold increase in Km for pyruvate and 480-fold decrease in kcat.
- L81 (≠ A96) mutation to A: 4.7-fold increase in Km for pyruvate and 15.7-fold decrease in kcat.; mutation to V: 3.3-fold increase in Km for pyruvate and 10.1-fold decrease in kcat.
- F83 (≠ I98) mutation to A: 5-fold increase in Km for acetyl-CoA and 120-fold decrease in kcat.
- L104 (= L117) mutation to V: 1.8-fold increase in Km for pyruvate and 3.4-fold decrease in kcat.
- Y144 (≠ S156) binding ; mutation to L: 259-fold increase in Km for pyruvate and 76-fold decrease in kcat.; mutation to V: 114-fold increase in Km for pyruvate and 5.3-fold decrease in kcat.
- E146 (= E158) mutation E->D,Q: Minor effects on the binding of acetyl-CoA, but causes a strong decrease in kcat.
- T179 (= T188) binding ; mutation to A: 16.4-fold increase in Km for pyruvate and 186-fold decrease in kcat.
- H302 (= H317) mutation H->A,N: Loss of activity.
- D304 (≠ H319) mutation to A: 5.2-fold increase in Km for acetyl-CoA and 16.6-fold decrease in kcat.
- N310 (≠ R325) mutation to A: 2.2-fold increase in Km for acetyl-CoA and 1.7-fold decrease in kcat.
- L311 (≠ G326) mutation to A: 8-fold increase in Km for acetyl-CoA and 6-fold decrease in kcat.
- Y312 (≠ T327) mutation to A: Loss of activity.
- Y430 (≠ V446) mutation to L: No change in Km for acetyl-CoA and 2.3-fold decrease in kcat. Severely impairs inhibition by isoleucine.
- D431 (= D447) mutation to A: 1.8-fold decrease in Km for acetyl-CoA and 5-fold decrease in kcat.
- L451 (= L463) mutation to V: 1.5-fold increase in Km for acetyl-CoA and 4.3 decrease in kcat.
- Y454 (≠ F466) mutation to A: 1.4 decrease in Km for acetyl-CoA and 17-fold decrease in kcat. Still inhibited by isoleucine and weakly inhibited by leucine.
- I458 (≠ V471) mutation to A: 1.3-fold decrease in Km for acetyl-CoA and 14-fold decrease in kcat. Abolishes inhibition by isoleucine.
- T464 (vs. gap) mutation to A: 1.8-fold decrease in Km for acetyl-CoA and 4.3-fold decrease in kcat.
- V468 (≠ G479) mutation to A: No change in Km for acetyl-CoA and 2-fold decrease in kcat. Increases inhibition by isoleucine and leucine becomes an effective inhibitor.
- P493 (≠ T499) mutation to A: 1.5-fold decrease in Km for acetyl-CoA and 2.6-fold decrease in kcat.
- Q495 (≠ I501) mutation to A: 1.6-fold decrease in Km for acetyl-CoA and 2.8-fold decrease in kcat.
3ivsA Homocitrate synthase lys4 (see paper)
29% identity, 63% coverage: 24:362/535 of query aligns to 14:330/364 of 3ivsA
3a9iA Crystal structure of homocitrate synthase from thermus thermophilus complexed with lys (see paper)
30% identity, 62% coverage: 23:354/535 of query aligns to 4:316/347 of 3a9iA
2zyfA Crystal structure of homocitrate synthase from thermus thermophilus complexed with magnesuim ion and alpha-ketoglutarate (see paper)
30% identity, 60% coverage: 23:345/535 of query aligns to 5:313/314 of 2zyfA
2ztjA Crystal structure of homocitrate synthase from thermus thermophilus complexed with alpha-ketoglutarate (see paper)
30% identity, 60% coverage: 23:345/535 of query aligns to 5:311/312 of 2ztjA
3bliA Crystal structure of the catalytic domain of licms in complexed with pyruvate and acetyl-coa (see paper)
26% identity, 56% coverage: 21:319/535 of query aligns to 1:298/311 of 3bliA
3hpsA Crystal structure of mycobacterium tuberculosis leua complexed with ketoisocaproate (kic)
27% identity, 91% coverage: 29:515/535 of query aligns to 62:573/575 of 3hpsA
- binding 2-oxo-4-methylpentanoic acid: R63 (= R30), H150 (= H114), Y152 (≠ F116), P235 (= P186), T237 (= T188), H268 (= H219), H270 (= H221)
- binding leucine: G500 (= G444), P501 (= P445), L502 (≠ V446), A503 (≠ D447), D530 (≠ G475), A532 (= A477), Q533 (= Q478), P557 (≠ T499), I559 (= I501)
- binding zinc ion: D64 (= D31), H268 (= H219), H270 (= H221)
3hq1A Crystal structure of mycobacterium tuberculosis leua complexed with citrate and mn2+
27% identity, 91% coverage: 29:515/535 of query aligns to 62:571/573 of 3hq1A
Query Sequence
>N515DRAFT_0574 FitnessBrowser__Dyella79:N515DRAFT_0574
MNHETQHSNDSSEDGVVADDRVRIFDTTLRDGEQAPGFGMDRRAKLRMAHALEALGVDVM
EAGFPQASPDDFAAVADIAKAVRHSTVCALARCQAADIDTAGRALEAAQHSRIHVFLSTS
PLHREHKLGMSKQQVIDTAIAAVERARALCHEVEFSAEDAMRTEPDYLAEVFSAAIAAGA
TTVNAPDTVGYVTPAEIAERFAYLRKHVKGAERVVFSSHCHDDLGMAVANSLAAVSAGAR
QIECTINGIGERAGNASLEEVVMALRVRGPYFGVDSRIDARRLVQTSRLLTQLTGQAVPR
NKAIVGDNAFAHESGIHQHGMLKHRGTYEIMRPQDVGMGETKLVLGKHSGRHALRSRLQA
LGHTPEEAAMDDIFARFKALADKKREIHDEDLEALALGQDPDAAGPWRIVQLNSSSHLGG
SASASVRLAHDDGREIGEAAIGDGPVDAVLRAMERATGTDLELTQFQVRAVSEGGDAQGQ
AQLTARHAARNWRGNGVSTDIVEATALAALSIVNRIERQAAPSAAAQPQVQGATA
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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