SitesBLAST
Comparing WP_012674346.1 NCBI__GCF_000021545.1:WP_012674346.1 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)
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)
54% identity, 97% coverage: 3:500/516 of query aligns to 6:501/517 of Q9JZG1
- D16 (= D13) binding Mn(2+)
- H204 (= H201) binding Mn(2+)
- H206 (= H203) binding Mn(2+)
- N240 (= N237) binding Mn(2+)
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, 62% coverage: 3:320/516 of query aligns to 3:306/308 of 3rmjB
6e1jA Crystal structure of methylthioalkylmalate synthase (bjumam1.1) from brassica juncea (see paper)
49% identity, 73% coverage: 6:380/516 of query aligns to 20:407/409 of 6e1jA
- binding coenzyme a: Q30 (= Q16), F60 (= F46), S63 (≠ A49), I95 (≠ L72), R97 (= R74), F121 (= F98), K132 (= K109), L133 (= L110), S322 (≠ A297), G323 (= G298), I324 (= I299), D327 (≠ H302), K331 (≠ A306), L359 (≠ H331), R362 (= R334), H363 (= H335)
- binding 4-(methylsulfanyl)-2-oxobutanoic acid: P192 (= P168), T194 (= T170), H225 (= H201), H227 (= H203)
- binding manganese (ii) ion: D27 (= D13), V82 (vs. gap), E84 (vs. gap), H225 (= H201), H227 (= H203)
Q9FG67 Methylthioalkylmalate synthase 1, chloroplastic; 2-isopropylmalate synthase 3; EC 2.3.3.17 from Arabidopsis thaliana (Mouse-ear cress) (see paper)
48% identity, 73% coverage: 6:380/516 of query aligns to 87:474/506 of Q9FG67
- S102 (= S21) mutation to F: In gsm1-1; loss of conversion of C3 to C4 glucosinolates.
- A290 (≠ S199) mutation to T: In gsm1-2; loss of conversion of C3 to C4 glucosinolates.
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)
48% identity, 73% coverage: 6:381/516 of query aligns to 87:475/503 of Q9FN52
- G263 (= G172) 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, 74% coverage: 3:383/516 of query aligns to 21:388/399 of 6ktqA
- binding 2-oxoglutaric acid: R30 (= R12), R154 (≠ E136), T156 (≠ S138), E158 (= E140), S184 (≠ N166), T188 (= T170), H216 (= H201), H218 (= H203)
- binding coenzyme a: V67 (≠ A49), R96 (= R74), A97 (= A75), F116 (= F98), H128 (≠ L110), E158 (= E140)
- binding zinc ion: E31 (≠ D13), H216 (= H201), H218 (= H203)
Q8F3Q1 (R)-citramalate synthase CimA; LiCMS; EC 2.3.3.21 from Leptospira interrogans serogroup Icterohaemorrhagiae serovar Lai (strain 56601) (see 2 papers)
31% identity, 90% coverage: 3:466/516 of query aligns to 7:472/516 of Q8F3Q1
- R16 (= R12) mutation R->K,Q: Loss of activity.
- RD 16:17 (= RD 12:13) binding pyruvate
- D17 (= D13) 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 (= L76) 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 (vs. gap) mutation to A: 5-fold increase in Km for acetyl-CoA and 120-fold decrease in kcat.
- L104 (≠ F98) mutation to V: 1.8-fold increase in Km for pyruvate and 3.4-fold decrease in kcat.
- Y144 (≠ S138) binding pyruvate; 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 (= E140) mutation E->D,Q: Minor effects on the binding of acetyl-CoA, but causes a strong decrease in kcat.
- T179 (= T170) binding pyruvate; mutation to A: 16.4-fold increase in Km for pyruvate and 186-fold decrease in kcat.
- H302 (= H300) mutation H->A,N: Loss of activity.
- D304 (≠ H302) mutation to A: 5.2-fold increase in Km for acetyl-CoA and 16.6-fold decrease in kcat.
- N310 (≠ R308) mutation to A: 2.2-fold increase in Km for acetyl-CoA and 1.7-fold decrease in kcat.
- L311 (≠ E309) mutation to A: 8-fold increase in Km for acetyl-CoA and 6-fold decrease in kcat.
- Y312 (≠ T310) mutation to A: Loss of activity.
- Y430 (≠ I429) mutation to L: No change in Km for acetyl-CoA and 2.3-fold decrease in kcat. Severely impairs inhibition by isoleucine.
- D431 (= D430) mutation to A: 1.8-fold decrease in Km for acetyl-CoA and 5-fold decrease in kcat.
- L451 (= L446) mutation to V: 1.5-fold increase in Km for acetyl-CoA and 4.3 decrease in kcat.
- Y454 (= Y449) 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 (≠ S453) 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 (≠ G462) 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.
Sites not aligning to the query:
- 493 P→A: 1.5-fold decrease in Km for acetyl-CoA and 2.6-fold decrease in kcat.
- 495 Q→A: 1.6-fold decrease in Km for acetyl-CoA and 2.8-fold decrease in kcat.
4ov4A Isopropylmalate synthase binding with ketoisovalerate (see paper)
33% identity, 72% coverage: 6:379/516 of query aligns to 6:377/379 of 4ov4A
4ov9A Structure of isopropylmalate synthase binding with alpha- isopropylmalate (see paper)
32% identity, 72% coverage: 6:379/516 of query aligns to 6:379/380 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, 73% coverage: 6:382/516 of query aligns to 37:401/418 of Q9Y823
- R43 (= R12) binding 2-oxoglutarate; mutation R->A,K,Q: Abolishes the catalytic activity.
- E44 (≠ D13) binding 2-oxoglutarate; binding L-lysine; binding Zn(2+)
- Q47 (= Q16) mutation to A: Abolishes the catalytic activity.
- E74 (= E43) 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 (≠ A75) binding 2-oxoglutarate; mutation to A: Substantially impairs catalytic efficiency.
- D123 (≠ H96) binding L-lysine; mutation to N: Does not affect the catalytic activity but impairs L-lysine inhibition.
- R163 (≠ E136) 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 (= S138) binding 2-oxoglutarate; mutation to A: Results in a moderate decrease in catalytic efficiency.
- E167 (= E140) mutation E->A,Q: Abolishes the catalytic activity.
- T197 (= T170) 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 (≠ S199) mutation to Q: Does not affect the catalytic activity but impairs L-lysine inhibition.
- H224 (= H201) binding 2-oxoglutarate; binding Zn(2+)
- H226 (= H203) binding 2-oxoglutarate; binding Zn(2+)
- R288 (≠ K264) mutation to K: Does not affect the catalytic activity but impairs L-lysine inhibition.
- Y332 (= Y311) mutation to A: Abolishes the catalytic activity.; mutation to F: Results in a decrease in catalytic efficiency.
- Q364 (≠ E343) 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, 73% coverage: 6:382/516 of query aligns to 32:396/400 of 3ivtB
3mi3A Homocitrate synthase lys4 bound to lysine (see paper)
31% identity, 72% coverage: 6:374/516 of query aligns to 14:360/370 of 3mi3A
3bliA Crystal structure of the catalytic domain of licms in complexed with pyruvate and acetyl-coa (see paper)
32% identity, 59% coverage: 3:308/516 of query aligns to 1:306/311 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: 1:374/516 of query aligns to 1:365/376 of O87198
- R12 (= R12) binding 2-oxoglutarate
- E13 (≠ D13) binding Mg(2+)
- H72 (≠ A75) binding 2-oxoglutarate; 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 (≠ H96) binding L-lysine
- R133 (vs. gap) binding 2-oxoglutarate
- S135 (= S138) binding L-lysine
- T166 (= T170) binding 2-oxoglutarate; binding L-lysine
- H195 (= H201) binding Mg(2+)
- H197 (= H203) binding Mg(2+)
3ivsA Homocitrate synthase lys4 (see paper)
30% identity, 72% coverage: 6:375/516 of query aligns to 14:356/364 of 3ivsA
2ztjA Crystal structure of homocitrate synthase from thermus thermophilus complexed with alpha-ketoglutarate (see paper)
30% identity, 63% coverage: 1:327/516 of query aligns to 1:311/312 of 2ztjA
2zyfA Crystal structure of homocitrate synthase from thermus thermophilus complexed with magnesuim ion and alpha-ketoglutarate (see paper)
31% identity, 63% coverage: 1:327/516 of query aligns to 1:313/314 of 2zyfA
3a9iA Crystal structure of homocitrate synthase from thermus thermophilus complexed with lys (see paper)
31% identity, 61% coverage: 6:321/516 of query aligns to 5:306/347 of 3a9iA
3hpsA Crystal structure of mycobacterium tuberculosis leua complexed with ketoisocaproate (kic)
25% identity, 95% coverage: 11:500/516 of query aligns to 62:573/575 of 3hpsA
- binding 2-oxo-4-methylpentanoic acid: R63 (= R12), H150 (= H96), Y152 (≠ F98), P235 (= P168), T237 (= T170), H268 (= H201), H270 (= H203)
- binding leucine: G500 (= G427), P501 (= P428), L502 (≠ I429), A503 (≠ D430), D530 (≠ K458), A532 (= A460), Q533 (≠ M461), P557 (≠ T484), I559 (= I486)
- binding zinc ion: D64 (= D13), H268 (= H201), H270 (= H203)
3figB Crystal structure of leucine-bound leua from mycobacterium tuberculosis (see paper)
25% identity, 95% coverage: 11:500/516 of query aligns to 62:574/577 of 3figB
Query Sequence
>WP_012674346.1 NCBI__GCF_000021545.1:WP_012674346.1
MEKLIIFDTTLRDGEQAPGFSMTVEEKVKMALQLEKLGVDVIEAGFAAASEGDFEAVKRV
AEEVKNAIVCSLARALQSDIDKAGEALLAAENRRIHTFIATSPIHMQYKLKMTPDEVVER
AVAAVKYALKYTDDVEFSAEDAFRSEREFLYRVFEAVIKAGAKTINVPDTVGYAIPEEFG
QLIKDIKNNVPNIDKAVISVHCHNDLGLAVANSLAAVKNGARQVHATVNGIGERAGNAAV
EEVVMAIKVRHDYFKGIYTTINTKEIYKTSRLLCRITGSFVQPNKAIVGDNAFAHEAGIH
QHGILAHRETYEIMRAEDVGVPKSKIVLGKHSGRHAFKTRLQELGYTNLSDAEIDSLFLK
FKKLADKKKEVFDEDIEALILEEFSFFENEVKVSYFHVVSGDNVIPSATVKIEKDGEEII
STASGDGPIDSVINAVEKAIGIKGKLLDYTIRSLSSGKDAMGEVRVLVKFDDTDYVASGK
GTSTDIIEASLKAYVDAYNKYTARKAFLEKRISEGV
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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