SitesBLAST
Comparing 207383 MicrobesOnline__882:207383 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)
Q9FG67 Methylthioalkylmalate synthase 1, chloroplastic; 2-isopropylmalate synthase 3; EC 2.3.3.17 from Arabidopsis thaliana (Mouse-ear cress) (see paper)
30% identity, 66% coverage: 5:357/538 of query aligns to 85:447/506 of Q9FG67
- S102 (≠ N22) mutation to F: In gsm1-1; loss of conversion of C3 to C4 glucosinolates.
- A290 (≠ G205) 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)
29% identity, 66% coverage: 2:357/538 of query aligns to 15:380/409 of 6e1jA
- binding coenzyme a: Q30 (= Q17), F60 (≠ W47), S63 (= S50), I95 (≠ P80), R97 (≠ H82), F121 (= F104), K132 (≠ A115), L133 (= L116), S322 (≠ G303), G323 (= G304), I324 (≠ V305), D327 (≠ S308), K331 (≠ R312), L359 (= L336), R362 (= R339), H363 (≠ S340)
- binding 4-(methylsulfanyl)-2-oxobutanoic acid: P192 (≠ C177), T194 (= T179), H225 (= H207), H227 (= H209)
- binding manganese (ii) ion: D27 (= D14), V82 (≠ K67), E84 (≠ A69), H225 (= H207), H227 (= H209)
6ktqA Crystal structure of catalytic domain of homocitrate synthase from sulfolobus acidocaldarius (sahcs(dram)) in complex with alpha- ketoglutarate/zn2+/coa (see paper)
28% identity, 66% coverage: 1:357/538 of query aligns to 18:361/399 of 6ktqA
- binding 2-oxoglutaric acid: R30 (= R13), R154 (≠ F142), T156 (≠ D144), E158 (= E146), S184 (≠ V175), T188 (= T179), H216 (= H207), H218 (= H209)
- binding coenzyme a: V67 (≠ S50), R96 (≠ A84), A97 (≠ E85), F116 (= F104), H128 (≠ L116), E158 (= E146)
- binding zinc ion: E31 (≠ D14), H216 (= H207), H218 (= H209)
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, 66% coverage: 2:357/538 of query aligns to 82:447/503 of Q9FN52
- G263 (= G181) mutation to E: In gsm2-1; loss of activity and lack of C6, C7 and C8 aliphatic 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)
26% identity, 90% coverage: 4:485/538 of query aligns to 6:468/517 of Q9JZG1
- D16 (= D14) binding
- H204 (= H207) binding
- H206 (= H209) binding
- N240 (= N243) binding
Sites not aligning to the query:
- 366:517 Required for the condensation reaction. Not required to bind substrate
O87198 Homocitrate synthase; HCS; EC 2.3.3.14 from Thermus thermophilus (strain ATCC BAA-163 / DSM 7039 / HB27) (see paper)
30% identity, 66% coverage: 3:357/538 of query aligns to 2:344/376 of O87198
- R12 (= R13) binding
- E13 (≠ D14) binding
- H72 (= H78) 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 (≠ A101) binding
- R133 (≠ F142) binding
- S135 (≠ D144) binding
- T166 (= T179) binding ; binding
- H195 (= H207) binding
- H197 (= H209) binding
4ov9A Structure of isopropylmalate synthase binding with alpha- isopropylmalate (see paper)
27% identity, 66% coverage: 3:356/538 of query aligns to 2:350/380 of 4ov9A
4ov4A Isopropylmalate synthase binding with ketoisovalerate (see paper)
27% identity, 66% coverage: 3:356/538 of query aligns to 2:348/379 of 4ov4A
2zyfA Crystal structure of homocitrate synthase from thermus thermophilus complexed with magnesuim ion and alpha-ketoglutarate (see paper)
30% identity, 62% coverage: 3:333/538 of query aligns to 2:313/314 of 2zyfA
3rmjB Crystal structure of truncated alpha-isopropylmalate synthase from neisseria meningitidis (see paper)
27% identity, 60% coverage: 4:326/538 of query aligns to 3:306/308 of 3rmjB
3a9iA Crystal structure of homocitrate synthase from thermus thermophilus complexed with lys (see paper)
30% identity, 60% coverage: 3:326/538 of query aligns to 1:305/347 of 3a9iA
2ztjA Crystal structure of homocitrate synthase from thermus thermophilus complexed with alpha-ketoglutarate (see paper)
30% identity, 62% coverage: 3:333/538 of query aligns to 2:311/312 of 2ztjA
3ivtB Homocitrate synthase lys4 bound to 2-og (see paper)
27% identity, 68% coverage: 7:373/538 of query aligns to 32:382/400 of 3ivtB
3ivsA Homocitrate synthase lys4 (see paper)
26% identity, 66% coverage: 7:361/538 of query aligns to 14:341/364 of 3ivsA
Q9Y823 Homocitrate synthase, mitochondrial; HCS; EC 2.3.3.14 from Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast) (see 2 papers)
27% identity, 64% coverage: 7:353/538 of query aligns to 37:369/418 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 (= H78) binding ; mutation to A: Substantially impairs catalytic efficiency.
- D123 (≠ A101) binding ; mutation to N: Does not affect the catalytic activity but impairs L-lysine inhibition.
- R163 (≠ F142) binding ; mutation R->A,Q: Abolishes the catalytic activity.; mutation to K: Severely diminishes affinity for 2-oxoglutarate and substantially impairs catalytic efficiency.
- S165 (≠ D144) binding ; mutation to A: Results in a moderate decrease in catalytic efficiency.
- E167 (= E146) mutation E->A,Q: Abolishes the catalytic activity.
- T197 (= T179) 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 (≠ G205) mutation to Q: Does not affect the catalytic activity but impairs L-lysine inhibition.
- H224 (= H207) binding ; binding
- H226 (= H209) binding ; binding
- R288 (≠ T273) mutation to K: Does not affect the catalytic activity but impairs L-lysine inhibition.
- Y332 (= Y317) mutation to A: Abolishes the catalytic activity.; mutation to F: Results in a decrease in catalytic efficiency.
- Q364 (≠ R348) mutation to R: Does not affect the catalytic activity but impairs L-lysine inhibition.
3mi3A Homocitrate synthase lys4 bound to lysine (see paper)
26% identity, 68% coverage: 7:373/538 of query aligns to 14:353/370 of 3mi3A
Q8F3Q1 (R)-citramalate synthase CimA; LiCMS; EC 2.3.3.21 from Leptospira interrogans serogroup Icterohaemorrhagiae serovar Lai (strain 56601) (see 2 papers)
23% identity, 89% coverage: 4:481/538 of query aligns to 7:465/516 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 (vs. gap) 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 (≠ F104) mutation to V: 1.8-fold increase in Km for pyruvate and 3.4-fold decrease in kcat.
- Y144 (≠ D144) 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 (= E146) mutation E->D,Q: Minor effects on the binding of acetyl-CoA, but causes a strong decrease in kcat.
- T179 (= T179) binding ; mutation to A: 16.4-fold increase in Km for pyruvate and 186-fold decrease in kcat.
- H302 (= H306) mutation H->A,N: Loss of activity.
- D304 (≠ S308) mutation to A: 5.2-fold increase in Km for acetyl-CoA and 16.6-fold decrease in kcat.
- N310 (≠ T315) mutation to A: 2.2-fold increase in Km for acetyl-CoA and 1.7-fold decrease in kcat.
- L311 (= L316) mutation to A: 8-fold increase in Km for acetyl-CoA and 6-fold decrease in kcat.
- Y312 (= Y317) mutation to A: Loss of activity.
- Y430 (≠ V444) mutation to L: No change in Km for acetyl-CoA and 2.3-fold decrease in kcat. Severely impairs inhibition by isoleucine.
- D431 (≠ N445) mutation to A: 1.8-fold decrease in Km for acetyl-CoA and 5-fold decrease in kcat.
- L451 (= L467) mutation to V: 1.5-fold increase in Km for acetyl-CoA and 4.3 decrease in kcat.
- Y454 (≠ F470) 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 (≠ V474) mutation to A: 1.3-fold decrease in Km for acetyl-CoA and 14-fold decrease in kcat. Abolishes inhibition by isoleucine.
- T464 (= T480) mutation to A: 1.8-fold decrease in Km for acetyl-CoA and 4.3-fold decrease in kcat.
Sites not aligning to the query:
- 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.
3bliA Crystal structure of the catalytic domain of licms in complexed with pyruvate and acetyl-coa (see paper)
23% identity, 57% coverage: 4:309/538 of query aligns to 1:299/311 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)
27% identity, 46% coverage: 9:254/538 of query aligns to 15:248/347 of Q53WI0
Sites not aligning to the query:
- 324 A→G: Increases the channeling efficiency of propanaldehyde from 57% to 94%.
P35914 Hydroxymethylglutaryl-CoA lyase, mitochondrial; HL; HMG-CoA lyase; 3-hydroxy-3-methylglutarate-CoA lyase; EC 4.1.3.4 from Homo sapiens (Human) (see 11 papers)
25% identity, 44% coverage: 1:238/538 of query aligns to 29:264/325 of P35914
- E37 (≠ D9) to K: in HMGCLD; activity lower than 5% respect to the wild-type; mutation to D: Normal activity.
- R41 (= R13) to Q: in HMGCLD; loss of activity and of proton exchange; dbSNP:rs121964997; mutation to M: Reduced activity, and loss of proton exchange.
- D42 (= D14) to E: in HMGCLD; reduced activity; to G: in HMGCLD; loss of activity; dbSNP:rs1467902610; to H: in HMGCLD; loss of activity; mutation D->A,N: Loss of activity, and reduced proton exchange rate.
- K48 (≠ D20) to N: in HMGCLD; abolishes almost all enzymatic activity
- E72 (= E44) mutation to A: Loss of activity, and reduced affinity for metal cofactor and substrate.
- S142 (vs. gap) to F: in HMGCLD; activity lower than 5% respect to the wild-type
- C174 (≠ H147) to Y: in HMGCLD; activity lower than 5% respect to the wild-type; dbSNP:rs765475941
- F192 (≠ A166) to S: in HMGCLD; activity lower than 5% respect to the wild-type
- I200 (≠ L174) to F: in HMGCLD; activity lower than 5% respect to the wild-type
- G203 (≠ C177) to E: in HMGCLD; complete loss of activity; dbSNP:rs1553131940
- D204 (= D178) mutation to A: Reduced activity, and reduced affinity for metal cofactor and substrate.
- H233 (= H207) to R: in HMGCLD; loss of activity; dbSNP:rs727503963; mutation to A: Loss of activity, and reduced proton exchange rate.
Sites not aligning to the query:
- 279 E→A: Reduced thermal stability, but normal activity.
- 280 D→A: Normal activity.
- 323 modified: Interchain; C→S: Abolishes interchain homodimerization. Exhibits no DTT stimulated activity.
Query Sequence
>207383 MicrobesOnline__882:207383
MRRQIHLYDTTLRDGSQSEDINLNTPDKLKIALRLDELGIAYIEGGWPGSNPVDVAFFKE
IRNYNLKQAKISAFGSTHHPSHTAENDPNLKAIAAARTDAAAIFGKSCERHAREALRLDG
RRNLDIIHDSIAFLKKQVAEVFFDAEHFFDGYRHNAAYALEVLRRAHEAGGDVLVLCDTN
GGTLPHEVHDIVTAVREQLPEAKLGIHAHNDCEVAVANSIAAVQAGAVQVQGTMNGVGER
CGNANLSSVIPILELKSAGAYACLPEGRLQQLTAVSSYVSEVTNLPPFSRQPFVGRSAFA
HKGGVHVSAVNRNATLYEHITPESVGNHQRVLITELAGRSNIVSLARRFGFHLDKDEPVV
KGLMNELKKKASLGYDYAAAEASVELLLLRKLARRGVREFFKLIQFRVLESKQENDLEPM
SEASVMVEVEGIIEHTAATGRGPVNALDNALRKALSSFYPRIREMRLLDFKVRVLTGTET
DGGTASTVRVLIESGDADSRWVTVGVSYNIIEASWQALADSMTYKLYKDEHVQRGMTD
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