SitesBLAST
Comparing BPHYT_RS06570 FitnessBrowser__BFirm:BPHYT_RS06570 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)
62% identity, 100% coverage: 2:514/515 of query aligns to 4:514/517 of Q9JZG1
- D16 (= D14) binding
- H204 (= H202) binding
- H206 (= H204) binding
- N240 (= N239) binding
Sites not aligning to the query:
- 366:517 Required for the condensation reaction. Not required to bind substrate
3rmjB Crystal structure of truncated alpha-isopropylmalate synthase from neisseria meningitidis (see paper)
63% identity, 63% coverage: 2:323/515 of query aligns to 1:308/308 of 3rmjB
Q9FG67 Methylthioalkylmalate synthase 1, chloroplastic; 2-isopropylmalate synthase 3; EC 2.3.3.17 from Arabidopsis thaliana (Mouse-ear cress) (see paper)
49% identity, 73% coverage: 7:382/515 of query aligns to 87:475/506 of Q9FG67
- S102 (= S22) mutation to F: In gsm1-1; loss of conversion of C3 to C4 glucosinolates.
- A290 (≠ S200) mutation to T: In gsm1-2; loss of conversion of C3 to C4 glucosinolates.
6e1jA Crystal structure of methylthioalkylmalate synthase (bjumam1.1) from brassica juncea (see paper)
48% identity, 73% coverage: 7:382/515 of query aligns to 20:408/409 of 6e1jA
- binding coenzyme a: Q30 (= Q17), F60 (= F47), S63 (= S50), I95 (≠ L73), R97 (= R75), F121 (= F99), K132 (= K110), L133 (= L111), S322 (= S298), G323 (= G299), I324 (= I300), D327 (= D303), K331 (= K307), L359 (= L332), R362 (= R335), H363 (≠ N336)
- binding 4-(methylsulfanyl)-2-oxobutanoic acid: P192 (≠ A169), T194 (= T171), H225 (= H202), H227 (= H204)
- binding manganese (ii) ion: D27 (= D14), V82 (vs. gap), E84 (vs. gap), H225 (= H202), H227 (= H204)
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)
45% identity, 76% coverage: 7:395/515 of query aligns to 87:488/503 of Q9FN52
- G263 (= G173) mutation to E: In gsm2-1; loss of activity and lack of C6, C7 and C8 aliphatic glucosinolates.
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: 4:363/515 of query aligns to 21:370/399 of 6ktqA
- binding 2-oxoglutaric acid: R30 (= R13), R154 (≠ E137), T156 (≠ S139), E158 (= E141), S184 (≠ N167), T188 (= T171), H216 (= H202), H218 (= H204)
- binding coenzyme a: V67 (≠ S50), R96 (= R75), A97 (= A76), F116 (= F99), H128 (≠ L111), E158 (= E141)
- binding zinc ion: E31 (≠ D14), H216 (= H202), H218 (= H204)
Q8F3Q1 (R)-citramalate synthase CimA; LiCMS; EC 2.3.3.21 from Leptospira interrogans serogroup Icterohaemorrhagiae serovar Lai (strain 56601) (see 2 papers)
30% identity, 97% coverage: 4:502/515 of query aligns to 7:510/516 of Q8F3Q1
- R16 (= R13) mutation R->K,Q: Loss of activity.
- RD 16:17 (= RD 13:14) binding
- D17 (= D14) 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 (≠ A76) 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 (≠ D78) mutation to A: 5-fold increase in Km for acetyl-CoA and 120-fold decrease in kcat.
- L104 (≠ F99) mutation to V: 1.8-fold increase in Km for pyruvate and 3.4-fold decrease in kcat.
- Y144 (≠ S139) 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 (= E141) mutation E->D,Q: Minor effects on the binding of acetyl-CoA, but causes a strong decrease in kcat.
- T179 (= T171) binding ; mutation to A: 16.4-fold increase in Km for pyruvate and 186-fold decrease in kcat.
- H302 (= H301) mutation H->A,N: Loss of activity.
- D304 (= D303) mutation to A: 5.2-fold increase in Km for acetyl-CoA and 16.6-fold decrease in kcat.
- N310 (≠ R309) mutation to A: 2.2-fold increase in Km for acetyl-CoA and 1.7-fold decrease in kcat.
- L311 (≠ D310) mutation to A: 8-fold increase in Km for acetyl-CoA and 6-fold decrease in kcat.
- Y312 (≠ T311) mutation to A: Loss of activity.
- Y430 (≠ V432) mutation to L: No change in Km for acetyl-CoA and 2.3-fold decrease in kcat. Severely impairs inhibition by isoleucine.
- D431 (= D433) mutation to A: 1.8-fold decrease in Km for acetyl-CoA and 5-fold decrease in kcat.
- L451 (= L449) mutation to V: 1.5-fold increase in Km for acetyl-CoA and 4.3 decrease in kcat.
- Y454 (= Y452) 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 (≠ A456) mutation to A: 1.3-fold decrease in Km for acetyl-CoA and 14-fold decrease in kcat. Abolishes inhibition by isoleucine.
- T464 (= T461) mutation to A: 1.8-fold decrease in Km for acetyl-CoA and 4.3-fold decrease in kcat.
- V468 (≠ G465) 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 (= P485) mutation to A: 1.5-fold decrease in Km for acetyl-CoA and 2.6-fold decrease in kcat.
- Q495 (≠ I487) mutation to A: 1.6-fold decrease in Km for acetyl-CoA and 2.8-fold decrease in kcat.
4ov9A Structure of isopropylmalate synthase binding with alpha- isopropylmalate (see paper)
31% identity, 73% coverage: 7:380/515 of query aligns to 6:379/380 of 4ov9A
4ov4A Isopropylmalate synthase binding with ketoisovalerate (see paper)
31% identity, 73% coverage: 7:380/515 of query aligns to 6:377/379 of 4ov4A
Q9Y823 Homocitrate synthase, mitochondrial; HCS; EC 2.3.3.14 from Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast) (see 2 papers)
30% identity, 72% coverage: 7:375/515 of query aligns to 37:394/418 of Q9Y823
- R43 (= R13) binding ; mutation R->A,K,Q: Abolishes the catalytic activity.
- E44 (≠ D14) binding ; binding ; binding
- 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 (≠ L73) binding ; mutation to A: Substantially impairs catalytic efficiency.
- D123 (≠ H97) binding ; mutation to N: Does not affect the catalytic activity but impairs L-lysine inhibition.
- R163 (≠ E137) binding ; mutation R->A,Q: Abolishes the catalytic activity.; mutation to K: Severely diminishes affinity for 2-oxoglutarate and substantially impairs catalytic efficiency.
- S165 (= S139) binding ; mutation to A: Results in a moderate decrease in catalytic efficiency.
- E167 (= E141) mutation E->A,Q: Abolishes the catalytic activity.
- T197 (= T171) 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 (≠ S200) mutation to Q: Does not affect the catalytic activity but impairs L-lysine inhibition.
- H224 (= H202) binding ; binding
- H226 (= H204) binding ; binding
- R288 (≠ V268) mutation to K: Does not affect the catalytic activity but impairs L-lysine inhibition.
- Y332 (= Y312) mutation to A: Abolishes the catalytic activity.; mutation to F: Results in a decrease in catalytic efficiency.
- Q364 (≠ E344) 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, 72% coverage: 7:375/515 of query aligns to 32:389/400 of 3ivtB
3mi3A Homocitrate synthase lys4 bound to lysine (see paper)
31% identity, 72% coverage: 7:375/515 of query aligns to 14:360/370 of 3mi3A
3ivsA Homocitrate synthase lys4 (see paper)
30% identity, 72% coverage: 7:376/515 of query aligns to 14:356/364 of 3ivsA
3bliA Crystal structure of the catalytic domain of licms in complexed with pyruvate and acetyl-coa (see paper)
30% identity, 58% coverage: 4:301/515 of query aligns to 1:296/311 of 3bliA
O87198 Homocitrate synthase; HCS; EC 2.3.3.14 from Thermus thermophilus (strain ATCC BAA-163 / DSM 7039 / HB27) (see paper)
31% identity, 72% coverage: 7:375/515 of query aligns to 6:365/376 of O87198
- R12 (= R13) binding
- E13 (≠ D14) binding
- H72 (≠ D80) 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 (vs. gap) binding
- R133 (vs. gap) binding
- S135 (= S139) binding
- T166 (= T171) binding ; binding
- H195 (= H202) binding
- H197 (= H204) binding
3hpzB Crystal structure of mycobacterium tuberculosis leua complexed with bromopyruvate
25% identity, 95% coverage: 12:501/515 of query aligns to 62:574/576 of 3hpzB
3hq1A Crystal structure of mycobacterium tuberculosis leua complexed with citrate and mn2+
25% identity, 95% coverage: 12:501/515 of query aligns to 62:571/573 of 3hq1A
1sr9A Crystal structure of leua from mycobacterium tuberculosis (see paper)
25% identity, 95% coverage: 12:501/515 of query aligns to 62:571/573 of 1sr9A
3figB Crystal structure of leucine-bound leua from mycobacterium tuberculosis (see paper)
25% identity, 95% coverage: 12:501/515 of query aligns to 62:574/577 of 3figB
3hpsA Crystal structure of mycobacterium tuberculosis leua complexed with ketoisocaproate (kic)
25% identity, 95% coverage: 12:501/515 of query aligns to 62:573/575 of 3hpsA
- binding 2-oxo-4-methylpentanoic acid: R63 (= R13), H150 (= H97), Y152 (≠ F99), P235 (≠ A169), T237 (= T171), H268 (= H202), H270 (= H204)
- binding leucine: G500 (= G430), P501 (= P431), L502 (≠ V432), A503 (≠ D433), D530 (≠ T461), A532 (= A463), Q533 (= Q464), P557 (= P485), I559 (= I487)
- binding zinc ion: D64 (= D14), H268 (= H202), H270 (= H204)
Query Sequence
>BPHYT_RS06570 FitnessBrowser__BFirm:BPHYT_RS06570
MSDKLIIFDTTLRDGEQSPGASMTKEEKIRIAKQLERMKVDVIEAGFAASSNGDFDSIHT
IAGLIKDSTVCSLARANDKDIQRAADALKPADHFRIHTFIATSPLHMEKKLRMTPDQVFE
QAKLAVRFARKFTNDVEFSPEDGSRSDMDFLCRVLEAVIAEGATTINIADTVGYGVPELY
GQLVKTLRERIPNSDKAVFSVHCHNDLGMAVANSLAGVQIGGARQVECTINGLGERAGNT
SLEEIVMAVKTRKDYFGLDIGLDTTQIVPASKLVSQITGFVVQPNKAVVGANAFAHASGI
HQDGVLKARDTYEIMRAEDVGWSANKIVLGKLSGRNAFKQRLQELGIALDSEAELNTAFA
RFKELADRKSEIFDEDIIAIVTEESAEAQEREHYKFLSLSQHSETGEQPHARIVFSVEGK
EITGEARGNGPVDATLNAIETEVGSGSELLLYSVNAITTGTQAQGEVTVRLSKSGRIVNG
VGTDPDIVAASAKAYISALNKLYSNADKLNPQRSE
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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