SitesBLAST
Comparing CCNA_01610 FitnessBrowser__Caulo:CCNA_01610 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)
55% identity, 95% coverage: 9:507/524 of query aligns to 1:502/517 of Q9JZG1
- D16 (= D24) binding
- H204 (= H212) binding
- H206 (= H214) binding
- N240 (= N248) binding
Sites not aligning to the query:
- 366:517 Required for the condensation reaction. Not required to bind substrate
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)
49% identity, 74% coverage: 12:400/524 of query aligns to 82:485/503 of Q9FN52
- G263 (= G183) 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)
49% identity, 72% coverage: 12:389/524 of query aligns to 15:407/409 of 6e1jA
- binding coenzyme a: Q30 (= Q27), F60 (= F57), S63 (≠ A60), I95 (≠ L83), R97 (= R85), F121 (= F109), K132 (= K120), L133 (= L121), S322 (= S307), G323 (= G308), I324 (= I309), D327 (= D312), K331 (= K316), L359 (≠ H341), R362 (= R344), H363 (= H345)
- binding 4-(methylsulfanyl)-2-oxobutanoic acid: P192 (= P179), T194 (= T181), H225 (= H212), H227 (= H214)
- binding manganese (ii) ion: D27 (= D24), V82 (≠ T79), E84 (vs. gap), H225 (= H212), H227 (= H214)
3rmjB Crystal structure of truncated alpha-isopropylmalate synthase from neisseria meningitidis (see paper)
58% identity, 61% coverage: 13:330/524 of query aligns to 2:306/308 of 3rmjB
Q9FG67 Methylthioalkylmalate synthase 1, chloroplastic; 2-isopropylmalate synthase 3; EC 2.3.3.17 from Arabidopsis thaliana (Mouse-ear cress) (see paper)
48% identity, 72% coverage: 15:389/524 of query aligns to 85:474/506 of Q9FG67
- S102 (= S32) mutation to F: In gsm1-1; loss of conversion of C3 to C4 glucosinolates.
- A290 (≠ S210) mutation to T: In gsm1-2; loss of conversion of C3 to C4 glucosinolates.
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, 70% coverage: 4:371/524 of query aligns to 13:370/399 of 6ktqA
- binding 2-oxoglutaric acid: R30 (= R23), R154 (≠ E147), T156 (≠ S149), E158 (= E151), S184 (≠ N177), T188 (= T181), H216 (= H212), H218 (= H214)
- binding coenzyme a: V67 (≠ A60), R96 (= R85), A97 (= A86), F116 (= F109), H128 (≠ L121), E158 (= E151)
- binding zinc ion: E31 (≠ D24), H216 (= H212), H218 (= H214)
4ov9A Structure of isopropylmalate synthase binding with alpha- isopropylmalate (see paper)
32% identity, 71% coverage: 19:388/524 of query aligns to 8:379/380 of 4ov9A
4ov4A Isopropylmalate synthase binding with ketoisovalerate (see paper)
32% identity, 71% coverage: 19:388/524 of query aligns to 8:377/379 of 4ov4A
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, 82% coverage: 17:447/524 of query aligns to 10:440/516 of Q8F3Q1
- R16 (= R23) mutation R->K,Q: Loss of activity.
- RD 16:17 (= RD 23:24) binding
- D17 (= D24) 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 (≠ A86) 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 (≠ A88) mutation to A: 5-fold increase in Km for acetyl-CoA and 120-fold decrease in kcat.
- L104 (≠ F109) mutation to V: 1.8-fold increase in Km for pyruvate and 3.4-fold decrease in kcat.
- Y144 (vs. gap) 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 (vs. gap) mutation E->D,Q: Minor effects on the binding of acetyl-CoA, but causes a strong decrease in kcat.
- T179 (= T181) binding ; mutation to A: 16.4-fold increase in Km for pyruvate and 186-fold decrease in kcat.
- H302 (= H310) mutation H->A,N: Loss of activity.
- D304 (= D312) mutation to A: 5.2-fold increase in Km for acetyl-CoA and 16.6-fold decrease in kcat.
- N310 (≠ A318) mutation to A: 2.2-fold increase in Km for acetyl-CoA and 1.7-fold decrease in kcat.
- L311 (≠ E319) mutation to A: 8-fold increase in Km for acetyl-CoA and 6-fold decrease in kcat.
- Y312 (≠ T320) mutation to A: Loss of activity.
- Y430 (≠ V437) mutation to L: No change in Km for acetyl-CoA and 2.3-fold decrease in kcat. Severely impairs inhibition by isoleucine.
- D431 (= D438) mutation to A: 1.8-fold decrease in Km for acetyl-CoA and 5-fold decrease in kcat.
Sites not aligning to the query:
- 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.
Q9Y823 Homocitrate synthase, mitochondrial; HCS; EC 2.3.3.14 from Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast) (see 2 papers)
29% identity, 72% coverage: 5:383/524 of query aligns to 25:394/418 of Q9Y823
- R43 (= R23) binding ; mutation R->A,K,Q: Abolishes the catalytic activity.
- E44 (≠ D24) binding ; binding ; binding
- Q47 (= Q27) mutation to A: Abolishes the catalytic activity.
- E74 (= E54) 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 (≠ A86) binding ; mutation to A: Substantially impairs catalytic efficiency.
- D123 (≠ H107) binding ; mutation to N: Does not affect the catalytic activity but impairs L-lysine inhibition.
- R163 (≠ E147) binding ; mutation R->A,Q: Abolishes the catalytic activity.; mutation to K: Severely diminishes affinity for 2-oxoglutarate and substantially impairs catalytic efficiency.
- S165 (= S149) binding ; mutation to A: Results in a moderate decrease in catalytic efficiency.
- E167 (= E151) mutation E->A,Q: Abolishes the catalytic activity.
- T197 (= T181) 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 (≠ S210) mutation to Q: Does not affect the catalytic activity but impairs L-lysine inhibition.
- H224 (= H212) binding ; binding
- H226 (= H214) binding ; binding
- R288 (≠ T277) mutation to K: Does not affect the catalytic activity but impairs L-lysine inhibition.
- Y332 (= Y321) mutation to A: Abolishes the catalytic activity.; mutation to F: Results in a decrease in catalytic efficiency.
- Q364 (≠ A353) mutation to R: Does not affect the catalytic activity but impairs L-lysine inhibition.
3ivtB Homocitrate synthase lys4 bound to 2-og (see paper)
29% identity, 72% coverage: 5:383/524 of query aligns to 20:389/400 of 3ivtB
3mi3A Homocitrate synthase lys4 bound to lysine (see paper)
29% identity, 72% coverage: 5:383/524 of query aligns to 2:360/370 of 3mi3A
O87198 Homocitrate synthase; HCS; EC 2.3.3.14 from Thermus thermophilus (strain ATCC BAA-163 / DSM 7039 / HB27) (see paper)
30% identity, 70% coverage: 17:383/524 of query aligns to 6:365/376 of O87198
- R12 (= R23) binding
- E13 (≠ D24) binding
- H72 (≠ L83) 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 (≠ H107) binding
- R133 (vs. gap) binding
- S135 (= S149) binding
- T166 (= T181) binding ; binding
- H195 (= H212) binding
- H197 (= H214) binding
3ivsA Homocitrate synthase lys4 (see paper)
28% identity, 71% coverage: 5:374/524 of query aligns to 2:346/364 of 3ivsA
3bliA Crystal structure of the catalytic domain of licms in complexed with pyruvate and acetyl-coa (see paper)
31% identity, 56% coverage: 17:310/524 of query aligns to 4:296/311 of 3bliA
3a9iA Crystal structure of homocitrate synthase from thermus thermophilus complexed with lys (see paper)
31% identity, 67% coverage: 17:365/524 of query aligns to 5:336/347 of 3a9iA
2zyfA Crystal structure of homocitrate synthase from thermus thermophilus complexed with magnesuim ion and alpha-ketoglutarate (see paper)
31% identity, 60% coverage: 17:330/524 of query aligns to 6:306/314 of 2zyfA
3hpsA Crystal structure of mycobacterium tuberculosis leua complexed with ketoisocaproate (kic)
27% identity, 92% coverage: 22:505/524 of query aligns to 62:572/575 of 3hpsA
- binding 2-oxo-4-methylpentanoic acid: R63 (= R23), H150 (= H107), Y152 (≠ F109), P235 (= P179), T237 (= T181), H268 (= H212), H270 (= H214)
- binding leucine: G500 (= G435), P501 (= P436), L502 (≠ V437), A503 (≠ D438), D530 (≠ T466), A532 (= A468), Q533 (= Q469), P557 (≠ T490), I559 (≠ T492)
- binding zinc ion: D64 (= D24), H268 (= H212), H270 (= H214)
3hq1A Crystal structure of mycobacterium tuberculosis leua complexed with citrate and mn2+
27% identity, 92% coverage: 22:505/524 of query aligns to 62:570/573 of 3hq1A
1sr9A Crystal structure of leua from mycobacterium tuberculosis (see paper)
27% identity, 92% coverage: 22:505/524 of query aligns to 62:570/573 of 1sr9A
Query Sequence
>CCNA_01610 FitnessBrowser__Caulo:CCNA_01610
MTSVPAGAISKRDNVVVFDTTMRDGEQSPGASMSLEEKLELAKILEEMGVDVIEAGFPIA
SNGDFEAVRQIAELITESTVCGLARAAAGDIDRCAEAVRRAKRGRIHTFISTSPVHMKYK
LQMEPDAVLEAITRSVSHARNLVGDVEWSAEDATRTERDFLKRCVEAAIKAGATTINLPD
TVGYSYPSEYGELFRDVITSVPGADKAIFSAHCHNDLGLAVANSIAAIEGGARQVEVAIN
GIGERAGNAALEEIVMALRVRGDHLPYGTSVDPVHITRASRYVSAITGFPVQFNKAIVGK
NAFAHESGIHQDGMLKNAETYEIMKPEDVGQGATNLVMGKHSGRHAFREKLKALGYELGQ
NALNDAFGRFKELADKKKHVFDDDIVALVDDALARGSEKIRVSRLRVVAGTDGQSAELTL
DIDGVASTAEATGDGPVDAVFNAIHKIVPHSAALRLFQVHAVTEGTDAQAQVSVRLEEDG
RIATGAAADTDTLTASAKAYVNALNNLFARKEKSRPEAAIASGF
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