SitesBLAST
Comparing WP_011461751.1 NCBI__GCF_000021925.1:WP_011461751.1 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)
P9WQB3 2-isopropylmalate synthase; Alpha-IPM synthase; Alpha-isopropylmalate synthase; EC 2.3.3.13 from Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv) (see 2 papers)
45% identity, 96% coverage: 16:552/557 of query aligns to 58:644/644 of P9WQB3
- R80 (= R39) binding
- T254 (= T212) binding
- H285 (= H243) binding
- H287 (= H245) binding
- 369:424 (vs. 327:374, 48% identical) Subdomain I
- 425:433 (vs. 376:384, 89% identical) Linker
- 426:644 (vs. 377:552, 30% identical) Required for the condensation reaction. Not required to bind substrate
- 434:490 (vs. 385:438, 28% identical) Subdomain II
- 491:644 (vs. 439:552, 27% identical) Regulatory domain
- N532 (≠ D476) binding
- A536 (≠ D480) binding
- D563 (≠ S508) binding
- A565 (≠ S510) binding
- P625 (≠ T533) binding
- I627 (= I535) binding
Sites not aligning to the query:
3hpzB Crystal structure of mycobacterium tuberculosis leua complexed with bromopyruvate
48% identity, 96% coverage: 16:548/557 of query aligns to 41:573/576 of 3hpzB
3figB Crystal structure of leucine-bound leua from mycobacterium tuberculosis (see paper)
48% identity, 96% coverage: 16:548/557 of query aligns to 41:573/577 of 3figB
3hq1A Crystal structure of mycobacterium tuberculosis leua complexed with citrate and mn2+
47% identity, 96% coverage: 16:548/557 of query aligns to 41:570/573 of 3hq1A
1sr9A Crystal structure of leua from mycobacterium tuberculosis (see paper)
47% identity, 96% coverage: 16:548/557 of query aligns to 41:570/573 of 1sr9A
3hpsA Crystal structure of mycobacterium tuberculosis leua complexed with ketoisocaproate (kic)
47% identity, 96% coverage: 16:548/557 of query aligns to 41:572/575 of 3hpsA
- binding 2-oxo-4-methylpentanoic acid: R63 (= R39), H150 (= H126), Y152 (= Y128), P235 (= P210), T237 (= T212), H268 (= H243), H270 (= H245)
- binding leucine: G500 (= G477), P501 (≠ R478), L502 (= L479), A503 (≠ D480), D530 (≠ S508), A532 (≠ S510), Q533 (= Q511), P557 (≠ T533), I559 (= I535)
- binding zinc ion: D64 (= D40), H268 (= H243), H270 (= H245)
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)
26% identity, 92% coverage: 38:550/557 of query aligns to 14:502/517 of Q9JZG1
- D16 (= D40) binding
- H204 (= H243) binding
- H206 (= H245) binding
- N240 (= N279) binding
Sites not aligning to the query:
- 366:517 Required for the condensation reaction. Not required to bind substrate
4ov9A Structure of isopropylmalate synthase binding with alpha- isopropylmalate (see paper)
28% identity, 64% coverage: 36:394/557 of query aligns to 9:342/380 of 4ov9A
4ov4A Isopropylmalate synthase binding with ketoisovalerate (see paper)
28% identity, 64% coverage: 36:394/557 of query aligns to 9:340/379 of 4ov4A
6e1jA Crystal structure of methylthioalkylmalate synthase (bjumam1.1) from brassica juncea (see paper)
28% identity, 60% coverage: 38:369/557 of query aligns to 25:345/409 of 6e1jA
- binding coenzyme a: Q30 (= Q43), F60 (= F73), S63 (≠ A76), I95 (≠ L102), R97 (≠ Q104), F121 (≠ Y128), K132 (≠ V139), L133 (≠ F140), S322 (= S334), G323 (= G335), I324 (≠ S336), D327 (= D339), K331 (= K343)
- binding 4-(methylsulfanyl)-2-oxobutanoic acid: P192 (= P210), T194 (= T212), H225 (= H243), H227 (= H245)
- binding manganese (ii) ion: D27 (= D40), V82 (≠ I93), E84 (= E95), H225 (= H243), H227 (= H245)
Sites not aligning to the query:
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)
28% identity, 65% coverage: 8:369/557 of query aligns to 70:412/503 of Q9FN52
- G263 (≠ S214) mutation to E: In gsm2-1; loss of activity and lack of C6, C7 and C8 aliphatic glucosinolates.
Q9FG67 Methylthioalkylmalate synthase 1, chloroplastic; 2-isopropylmalate synthase 3; EC 2.3.3.17 from Arabidopsis thaliana (Mouse-ear cress) (see paper)
27% identity, 60% coverage: 38:369/557 of query aligns to 92:412/506 of Q9FG67
- S102 (≠ P48) mutation to F: In gsm1-1; loss of conversion of C3 to C4 glucosinolates.
- A290 (≠ S241) 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)
28% identity, 53% coverage: 38:331/557 of query aligns to 11:293/308 of 3rmjB
Q8F3Q1 (R)-citramalate synthase CimA; LiCMS; EC 2.3.3.21 from Leptospira interrogans serogroup Icterohaemorrhagiae serovar Lai (strain 56601) (see 2 papers)
22% identity, 93% coverage: 34:552/557 of query aligns to 11:512/516 of Q8F3Q1
- R16 (= R39) mutation R->K,Q: Loss of activity.
- RD 16:17 (= RD 39:40) binding
- D17 (= D40) 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 (= L102) 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 (≠ V120) mutation to V: 1.8-fold increase in Km for pyruvate and 3.4-fold decrease in kcat.
- Y144 (= Y161) 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 (≠ A163) mutation E->D,Q: Minor effects on the binding of acetyl-CoA, but causes a strong decrease in kcat.
- T179 (= T212) binding ; mutation to A: 16.4-fold increase in Km for pyruvate and 186-fold decrease in kcat.
- H302 (= H337) mutation H->A,N: Loss of activity.
- D304 (= D339) mutation to A: 5.2-fold increase in Km for acetyl-CoA and 16.6-fold decrease in kcat.
- N310 (≠ H354) mutation to A: 2.2-fold increase in Km for acetyl-CoA and 1.7-fold decrease in kcat.
- L311 (≠ Y355) mutation to A: 8-fold increase in Km for acetyl-CoA and 6-fold decrease in kcat.
- Y312 (≠ W356) mutation to A: Loss of activity.
- Y430 (≠ L479) mutation to L: No change in Km for acetyl-CoA and 2.3-fold decrease in kcat. Severely impairs inhibition by isoleucine.
- D431 (= D480) mutation to A: 1.8-fold decrease in Km for acetyl-CoA and 5-fold decrease in kcat.
- L451 (= L497) mutation to V: 1.5-fold increase in Km for acetyl-CoA and 4.3 decrease in kcat.
- Y454 (≠ K500) 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 (≠ L504) mutation to A: 1.3-fold decrease in Km for acetyl-CoA and 14-fold decrease in kcat. Abolishes inhibition by isoleucine.
- T464 (≠ S510) mutation to A: 1.8-fold decrease in Km for acetyl-CoA and 4.3-fold decrease in kcat.
- V468 (≠ S514) 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 (≠ T533) mutation to A: 1.5-fold decrease in Km for acetyl-CoA and 2.6-fold decrease in kcat.
- Q495 (≠ I535) mutation to A: 1.6-fold decrease in Km for acetyl-CoA and 2.8-fold decrease in kcat.
6ktqA Crystal structure of catalytic domain of homocitrate synthase from sulfolobus acidocaldarius (sahcs(dram)) in complex with alpha- ketoglutarate/zn2+/coa (see paper)
22% identity, 54% coverage: 38:337/557 of query aligns to 29:310/399 of 6ktqA
- binding 2-oxoglutaric acid: R30 (= R39), R154 (≠ E172), T156 (≠ S174), E158 (= E176), S184 (≠ N208), T188 (= T212), H216 (= H243), H218 (= H245)
- binding coenzyme a: V67 (≠ A76), R96 (= R106), A97 (≠ I109), F116 (≠ Y128), H128 (≠ F140), E158 (= E176)
- binding zinc ion: E31 (≠ D40), H216 (= H243), H218 (= H245)
2zyfA Crystal structure of homocitrate synthase from thermus thermophilus complexed with magnesuim ion and alpha-ketoglutarate (see paper)
25% identity, 44% coverage: 33:278/557 of query aligns to 4:224/314 of 2zyfA
3a9iA Crystal structure of homocitrate synthase from thermus thermophilus complexed with lys (see paper)
25% identity, 44% coverage: 33:278/557 of query aligns to 3:223/347 of 3a9iA
2ztjA Crystal structure of homocitrate synthase from thermus thermophilus complexed with alpha-ketoglutarate (see paper)
26% identity, 44% coverage: 33:278/557 of query aligns to 4:222/312 of 2ztjA
O87198 Homocitrate synthase; HCS; EC 2.3.3.14 from Thermus thermophilus (strain ATCC BAA-163 / DSM 7039 / HB27) (see paper)
25% identity, 44% coverage: 33:278/557 of query aligns to 4:230/376 of O87198
- R12 (= R39) binding
- E13 (≠ D40) binding
- H72 (= H108) 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 (≠ H126) binding
- R133 (≠ E172) binding
- S135 (= S174) binding
- T166 (= T212) binding ; binding
- H195 (= H243) binding
- H197 (= H245) binding
Q9Y823 Homocitrate synthase, mitochondrial; HCS; EC 2.3.3.14 from Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast) (see 2 papers)
23% identity, 43% coverage: 38:278/557 of query aligns to 42:259/418 of Q9Y823
- R43 (= R39) binding ; mutation R->A,K,Q: Abolishes the catalytic activity.
- E44 (≠ D40) binding ; binding ; binding
- Q47 (= Q43) mutation to A: Abolishes the catalytic activity.
- E74 (= E70) 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 (≠ Q104) binding ; mutation to A: Substantially impairs catalytic efficiency.
- D123 (≠ E149) binding ; mutation to N: Does not affect the catalytic activity but impairs L-lysine inhibition.
- R163 (≠ E184) binding ; mutation R->A,Q: Abolishes the catalytic activity.; mutation to K: Severely diminishes affinity for 2-oxoglutarate and substantially impairs catalytic efficiency.
- S165 (≠ A186) binding ; mutation to A: Results in a moderate decrease in catalytic efficiency.
- E167 (= E188) mutation E->A,Q: Abolishes the catalytic activity.
- T197 (= T212) 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 (≠ S241) mutation to Q: Does not affect the catalytic activity but impairs L-lysine inhibition.
- H224 (= H243) binding ; binding
- H226 (= H245) binding ; binding
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.
Query Sequence
>WP_011461751.1 NCBI__GCF_000021925.1:WP_011461751.1
MKNVDNYRRGYFMPPVKSLKWAEKEYITTPPTWCSVDLRDGNQALVVPMSLEEKLEYYHM
LLKIGFKEIEVGFPAASETEYAFLRTLIEQNLIPEDVTIQVLTQSRDHIIEKTFKALVGV
KKAVVHLYNSTSVAQREQVFKMSREEIVEIAVSGARLLKKYAAETEGNFQFEYSPESFTG
TEMEFALEICNQVLDVFEPTPENKVIINLPATVSLSMPHVYASQIEYMSEHLKYRDNVIL
SLHPHNDRGTAVADAELGLLAGGQRIEGTLFGNGERTGNVDIVTLALNLFSHGVDPGLNF
ASMLEITAKYEALTRMKVHDRQPYGGKLVFAAFSGSHQDAITKGIKWREEHECHYWNVPY
LLIDPQDIGREYEGDVIRINSQSGKGGIAYMLEQHYALDLPAKMREAFGYKVKNVSDNLH
KELMPEEIKDIFFKEYVNIENPIKFLNFHFLNHDDFQTTVTLEFKGEIQELSGEGDGRLD
AISNALQARLGLSYSNLIYKEHALELGSKSQAVSYVGVTGPDGVIHWGCGIHTDIFTSSV
KALISAINTMIKDSAAV
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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