SitesBLAST
Comparing WP_011737275.1 NCBI__GCF_000015045.1:WP_011737275.1 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)
6ktqA Crystal structure of catalytic domain of homocitrate synthase from sulfolobus acidocaldarius (sahcs(dram)) in complex with alpha- ketoglutarate/zn2+/coa (see paper)
34% identity, 88% coverage: 12:355/389 of query aligns to 24:370/399 of 6ktqA
- binding 2-oxoglutaric acid: R30 (= R18), R154 (≠ S138), T156 (≠ G140), E158 (= E142), S184 (≠ R168), T188 (= T172), H216 (= H200), H218 (= H202)
- binding coenzyme a: V67 (≠ M55), R96 (= R80), A97 (= A81), F116 (≠ S100), H128 (≠ I112), E158 (= E142)
- binding zinc ion: E31 (≠ D19), H216 (= H200), H218 (= H202)
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)
34% identity, 96% coverage: 14:386/389 of query aligns to 89:485/503 of Q9FN52
- G263 (= G174) 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)
33% identity, 93% coverage: 14:373/389 of query aligns to 22:406/409 of 6e1jA
- binding coenzyme a: Q30 (= Q22), F60 (≠ I52), S63 (≠ M55), I95 (≠ W78), R97 (= R80), F121 (≠ S100), K132 (= K111), L133 (≠ I112), S322 (= S292), G323 (= G293), I324 (≠ L294), D327 (= D297), K331 (= K301), L359 (≠ H325), R362 (≠ S328), H363 (≠ S329)
- binding 4-(methylsulfanyl)-2-oxobutanoic acid: P192 (≠ C170), T194 (= T172), H225 (= H200), H227 (= H202)
- binding manganese (ii) ion: D27 (= D19), V82 (vs. gap), E84 (vs. gap), H225 (= H200), H227 (= H202)
Q9FG67 Methylthioalkylmalate synthase 1, chloroplastic; 2-isopropylmalate synthase 3; EC 2.3.3.17 from Arabidopsis thaliana (Mouse-ear cress) (see paper)
33% identity, 90% coverage: 14:363/389 of query aligns to 89:464/506 of Q9FG67
- S102 (≠ V27) mutation to F: In gsm1-1; loss of conversion of C3 to C4 glucosinolates.
- A290 (≠ E198) mutation to T: In gsm1-2; loss of conversion of C3 to C4 glucosinolates.
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)
32% identity, 97% coverage: 10:386/389 of query aligns to 7:394/517 of Q9JZG1
- D16 (= D19) binding Mn(2+)
- H204 (= H200) binding Mn(2+)
- H206 (= H202) binding Mn(2+)
- N240 (= N236) binding Mn(2+)
Sites not aligning to the query:
- 366:517 Required for the condensation reaction. Not required to bind substrate
3ivtB Homocitrate synthase lys4 bound to 2-og (see paper)
31% identity, 94% coverage: 9:374/389 of query aligns to 29:397/400 of 3ivtB
Q9Y823 Homocitrate synthase, mitochondrial; HCS; EC 2.3.3.14 from Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast) (see 2 papers)
31% identity, 94% coverage: 9:374/389 of query aligns to 34:402/418 of Q9Y823
- R43 (= R18) binding 2-oxoglutarate; mutation R->A,K,Q: Abolishes the catalytic activity.
- E44 (≠ D19) binding 2-oxoglutarate; binding L-lysine; binding Zn(2+)
- Q47 (= Q22) mutation to A: Abolishes the catalytic activity.
- E74 (= E49) 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 (≠ W78) binding 2-oxoglutarate; mutation to A: Substantially impairs catalytic efficiency.
- D123 (= D98) binding L-lysine; mutation to N: Does not affect the catalytic activity but impairs L-lysine inhibition.
- R163 (≠ S138) 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 (≠ G140) binding 2-oxoglutarate; mutation to A: Results in a moderate decrease in catalytic efficiency.
- E167 (= E142) mutation E->A,Q: Abolishes the catalytic activity.
- T197 (= T172) 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 (= E198) mutation to Q: Does not affect the catalytic activity but impairs L-lysine inhibition.
- H224 (= H200) binding 2-oxoglutarate; binding Zn(2+)
- H226 (= H202) binding 2-oxoglutarate; binding Zn(2+)
- R288 (= R262) mutation to K: Does not affect the catalytic activity but impairs L-lysine inhibition.
- Y332 (= Y306) mutation to A: Abolishes the catalytic activity.; mutation to F: Results in a decrease in catalytic efficiency.
- Q364 (≠ A337) mutation to R: Does not affect the catalytic activity but impairs L-lysine inhibition.
3mi3A Homocitrate synthase lys4 bound to lysine (see paper)
31% identity, 94% coverage: 9:374/389 of query aligns to 11:368/370 of 3mi3A
3ivsA Homocitrate synthase lys4 (see paper)
30% identity, 94% coverage: 9:374/389 of query aligns to 11:362/364 of 3ivsA
3rmjB Crystal structure of truncated alpha-isopropylmalate synthase from neisseria meningitidis (see paper)
33% identity, 73% coverage: 10:292/389 of query aligns to 4:296/308 of 3rmjB
O87198 Homocitrate synthase; HCS; EC 2.3.3.14 from Thermus thermophilus (strain ATCC BAA-163 / DSM 7039 / HB27) (see paper)
27% identity, 93% coverage: 12:373/389 of query aligns to 6:369/376 of O87198
- R12 (= R18) binding 2-oxoglutarate
- E13 (≠ D19) binding Mg(2+)
- H72 (≠ W78) 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 (= D98) binding L-lysine
- R133 (vs. gap) binding 2-oxoglutarate
- S135 (≠ G140) binding L-lysine
- T166 (= T172) binding 2-oxoglutarate; binding L-lysine
- H195 (= H200) binding Mg(2+)
- H197 (= H202) binding Mg(2+)
2zyfA Crystal structure of homocitrate synthase from thermus thermophilus complexed with magnesuim ion and alpha-ketoglutarate (see paper)
29% identity, 80% coverage: 12:323/389 of query aligns to 6:314/314 of 2zyfA
2ztjA Crystal structure of homocitrate synthase from thermus thermophilus complexed with alpha-ketoglutarate (see paper)
28% identity, 80% coverage: 12:323/389 of query aligns to 6:312/312 of 2ztjA
Q8F3Q1 (R)-citramalate synthase CimA; LiCMS; EC 2.3.3.21 from Leptospira interrogans serogroup Icterohaemorrhagiae serovar Lai (strain 56601) (see 2 papers)
27% identity, 91% coverage: 8:362/389 of query aligns to 6:369/516 of Q8F3Q1
- R16 (= R18) mutation R->K,Q: Loss of activity.
- RD 16:17 (= RD 18:19) binding pyruvate
- D17 (= D19) 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 (= L82) 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 (≠ V83) mutation to A: 5-fold increase in Km for acetyl-CoA and 120-fold decrease in kcat.
- L104 (≠ S100) mutation to V: 1.8-fold increase in Km for pyruvate and 3.4-fold decrease in kcat.
- Y144 (≠ G140) 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 (= E142) mutation E->D,Q: Minor effects on the binding of acetyl-CoA, but causes a strong decrease in kcat.
- T179 (= T172) binding pyruvate; mutation to A: 16.4-fold increase in Km for pyruvate and 186-fold decrease in kcat.
- H302 (= H295) mutation H->A,N: Loss of activity.
- D304 (= D297) mutation to A: 5.2-fold increase in Km for acetyl-CoA and 16.6-fold decrease in kcat.
- N310 (≠ P303) mutation to A: 2.2-fold increase in Km for acetyl-CoA and 1.7-fold decrease in kcat.
- L311 (≠ S304) mutation to A: 8-fold increase in Km for acetyl-CoA and 6-fold decrease in kcat.
- Y312 (≠ N305) mutation to A: Loss of activity.
Sites not aligning to the query:
- 430 Y→L: No change in Km for acetyl-CoA and 2.3-fold decrease in kcat. Severely impairs inhibition by isoleucine.
- 431 D→A: 1.8-fold decrease in Km for acetyl-CoA and 5-fold decrease in kcat.
- 451 L→V: 1.5-fold increase in Km for acetyl-CoA and 4.3 decrease in kcat.
- 454 Y→A: 1.4 decrease in Km for acetyl-CoA and 17-fold decrease in kcat. Still inhibited by isoleucine and weakly inhibited by leucine.
- 458 I→A: 1.3-fold decrease in Km for acetyl-CoA and 14-fold decrease in kcat. Abolishes inhibition by isoleucine.
- 464 T→A: 1.8-fold decrease in Km for acetyl-CoA and 4.3-fold decrease in kcat.
- 468 V→A: No change in Km for acetyl-CoA and 2-fold decrease in kcat. Increases inhibition by isoleucine and leucine becomes an effective inhibitor.
- 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.
3a9iA Crystal structure of homocitrate synthase from thermus thermophilus complexed with lys (see paper)
29% identity, 82% coverage: 12:331/389 of query aligns to 5:316/347 of 3a9iA
4ov9A Structure of isopropylmalate synthase binding with alpha- isopropylmalate (see paper)
27% identity, 94% coverage: 10:373/389 of query aligns to 4:379/380 of 4ov9A
4ov4A Isopropylmalate synthase binding with ketoisovalerate (see paper)
27% identity, 94% coverage: 10:373/389 of query aligns to 4:377/379 of 4ov4A
3bliA Crystal structure of the catalytic domain of licms in complexed with pyruvate and acetyl-coa (see paper)
28% identity, 73% coverage: 12:295/389 of query aligns to 4:296/311 of 3bliA
Q53WI0 4-hydroxy-2-oxovalerate aldolase; HOA; 4-hydroxy-2-keto-pentanoic acid aldolase; 4-hydroxy-2-oxohexanoate aldolase; 4-hydroxy-2-oxopentanoate aldolase; EC 4.1.3.39; EC 4.1.3.43 from Thermus thermophilus (strain ATCC 27634 / DSM 579 / HB8) (see paper)
28% identity, 66% coverage: 11:268/389 of query aligns to 12:268/347 of Q53WI0
Sites not aligning to the query:
- 324 A→G: Increases the channeling efficiency of propanaldehyde from 57% to 94%.
3mp3B Crystal structure of human lyase in complex with inhibitor hg-coa (see paper)
26% identity, 66% coverage: 18:274/389 of query aligns to 14:285/296 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 (= R18), D15 (= D19), Q18 (= Q22), F49 (vs. gap), V50 (vs. gap), S51 (vs. gap), W54 (vs. gap), P81 (≠ W78), N82 (= N79), K84 (≠ P84), G85 (≠ D85), N111 (≠ K111), R122 (≠ Q122), Y140 (= Y136), S142 (= S138), T178 (= T172), H206 (= H200)
- binding magnesium ion: D15 (= D19), H206 (= H200), H208 (= H202)
Query Sequence
>WP_011737275.1 NCBI__GCF_000015045.1:WP_011737275.1
MREQAGSTNIIIDDTTLRDGEQTAGVVFSKRDKIAIARMLDSIGVQELECGIPAMGREER
EGIRALVDLGLNARLIAWNRALVPDIQASIDCGISAVDISLPVSDIMIRNKIRKSRSWVR
EQLKTALGFAKQHGLYVSVGGEDASRADHAFLVELMRITLQMGGDRFRFCDTLGILDPFG
MYDRIRALREAVPELAIEVHTHNDFGMATANTIAGIRAGATFANTTVNGLGERAGNAALE
EVVMGLRHACAMDTGIASHRFRELSLFVSRASRRPLPPWKAVVGESVFAHESGLHTDGVL
KNPSNYEGFDPAEVGLSRSIVVGKHSGSSGLIDRYRAMGIAVSRSEATRLVERVRRVAQR
TRRPLTNEQLLRLYDGRGAEIPANSFCVC
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