SitesBLAST
Comparing 8501897 FitnessBrowser__Miya:8501897 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)
Q9FG67 Methylthioalkylmalate synthase 1, chloroplastic; 2-isopropylmalate synthase 3; EC 2.3.3.17 from Arabidopsis thaliana (Mouse-ear cress) (see paper)
30% identity, 81% coverage: 2:370/455 of query aligns to 87:470/506 of Q9FG67
- S102 (≠ Y17) mutation to F: In gsm1-1; loss of conversion of C3 to C4 glucosinolates.
- A290 (≠ G200) 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)
31% identity, 80% coverage: 2:363/455 of query aligns to 20:397/409 of 6e1jA
- binding coenzyme a: Q30 (= Q12), F60 (≠ W42), S63 (≠ A43), I95 (≠ W67), R97 (= R69), F121 (≠ G89), K132 (≠ R100), L133 (= L101), S322 (= S292), G323 (= G293), I324 (≠ L294), D327 (≠ H297), K331 (≠ R301), L359 (≠ K325), R362 (≠ V328), H363 (≠ A329)
- binding 4-(methylsulfanyl)-2-oxobutanoic acid: P192 (≠ S160), T194 (= T162), H225 (= H202), H227 (= H204)
- binding manganese (ii) ion: D27 (≠ E9), V82 (≠ L62), E84 (vs. gap), H225 (= H202), H227 (= H204)
6ktqA Crystal structure of catalytic domain of homocitrate synthase from sulfolobus acidocaldarius (sahcs(dram)) in complex with alpha- ketoglutarate/zn2+/coa (see paper)
29% identity, 83% coverage: 2:380/455 of query aligns to 24:397/399 of 6ktqA
- binding 2-oxoglutaric acid: R30 (= R8), R154 (≠ T128), T156 (≠ G130), E158 (= E132), S184 (≠ R158), T188 (= T162), H216 (= H202), H218 (= H204)
- binding coenzyme a: V67 (vs. gap), R96 (= R69), A97 (≠ C70), F116 (≠ G89), H128 (≠ L101), E158 (= E132)
- binding zinc ion: E31 (= E9), H216 (= H202), H218 (= H204)
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, 81% coverage: 2:370/455 of query aligns to 87:470/503 of Q9FN52
- G263 (= G164) mutation to E: In gsm2-1; loss of activity and lack of C6, C7 and C8 aliphatic glucosinolates.
Q9Y823 Homocitrate synthase, mitochondrial; HCS; EC 2.3.3.14 from Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast) (see 2 papers)
30% identity, 75% coverage: 2:340/455 of query aligns to 37:367/418 of Q9Y823
- R43 (= R8) binding ; mutation R->A,K,Q: Abolishes the catalytic activity.
- E44 (= E9) binding ; binding ; binding
- Q47 (= Q12) mutation to A: Abolishes the catalytic activity.
- E74 (= E39) 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 (≠ G61) binding ; mutation to A: Substantially impairs catalytic efficiency.
- D123 (≠ C87) binding ; mutation to N: Does not affect the catalytic activity but impairs L-lysine inhibition.
- R163 (≠ T128) binding ; mutation R->A,Q: Abolishes the catalytic activity.; mutation to K: Severely diminishes affinity for 2-oxoglutarate and substantially impairs catalytic efficiency.
- S165 (≠ G130) binding ; mutation to A: Results in a moderate decrease in catalytic efficiency.
- E167 (= E132) mutation E->A,Q: Abolishes the catalytic activity.
- T197 (= T162) 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 (≠ G200) mutation to Q: Does not affect the catalytic activity but impairs L-lysine inhibition.
- H224 (= H202) binding ; binding
- H226 (= H204) binding ; binding
- R288 (= R262) mutation to K: Does not affect the catalytic activity but impairs L-lysine inhibition.
- Y332 (≠ F306) mutation to A: Abolishes the catalytic activity.; mutation to F: Results in a decrease in catalytic efficiency.
- Q364 (≠ E337) 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, 75% coverage: 2:340/455 of query aligns to 32:362/400 of 3ivtB
3ivsA Homocitrate synthase lys4 (see paper)
30% identity, 78% coverage: 2:358/455 of query aligns to 14:351/364 of 3ivsA
3mi3A Homocitrate synthase lys4 bound to lysine (see paper)
30% identity, 75% coverage: 2:340/455 of query aligns to 14:333/370 of 3mi3A
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)
29% identity, 81% coverage: 1:370/455 of query aligns to 8:378/517 of Q9JZG1
- D16 (≠ E9) binding
- H204 (= H202) binding
- H206 (= H204) binding
- N240 (≠ V238) 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, 81% coverage: 2:370/455 of query aligns to 6:366/376 of O87198
- R12 (= R8) binding
- E13 (= E9) binding
- H72 (≠ G61) 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 (≠ C87) binding
- R133 (≠ G130) binding
- S135 (vs. gap) binding
- T166 (= T162) binding ; binding
- H195 (= H202) binding
- H197 (= H204) binding
4ov4A Isopropylmalate synthase binding with ketoisovalerate (see paper)
26% identity, 81% coverage: 2:370/455 of query aligns to 6:374/379 of 4ov4A
4ov9A Structure of isopropylmalate synthase binding with alpha- isopropylmalate (see paper)
25% identity, 81% coverage: 2:370/455 of query aligns to 6:376/380 of 4ov9A
2zyfA Crystal structure of homocitrate synthase from thermus thermophilus complexed with magnesuim ion and alpha-ketoglutarate (see paper)
29% identity, 70% coverage: 2:320/455 of query aligns to 6:311/314 of 2zyfA
2ztjA Crystal structure of homocitrate synthase from thermus thermophilus complexed with alpha-ketoglutarate (see paper)
29% identity, 70% coverage: 2:320/455 of query aligns to 6:309/312 of 2ztjA
3a9iA Crystal structure of homocitrate synthase from thermus thermophilus complexed with lys (see paper)
30% identity, 69% coverage: 2:315/455 of query aligns to 5:305/347 of 3a9iA
Q8F3Q1 (R)-citramalate synthase CimA; LiCMS; EC 2.3.3.21 from Leptospira interrogans serogroup Icterohaemorrhagiae serovar Lai (strain 56601) (see 2 papers)
24% identity, 82% coverage: 2:375/455 of query aligns to 10:385/516 of Q8F3Q1
- R16 (= R8) mutation R->K,Q: Loss of activity.
- RD 16:17 (≠ RE 8:9) binding
- D17 (≠ E9) 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 (≠ S55) 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 (≠ R57) mutation to A: 5-fold increase in Km for acetyl-CoA and 120-fold decrease in kcat.
- L104 (≠ G89) mutation to V: 1.8-fold increase in Km for pyruvate and 3.4-fold decrease in kcat.
- Y144 (≠ G130) 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 (= E132) mutation E->D,Q: Minor effects on the binding of acetyl-CoA, but causes a strong decrease in kcat.
- T179 (= T162) binding ; 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 (≠ H297) 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 (≠ L305) 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.
3rmjB Crystal structure of truncated alpha-isopropylmalate synthase from neisseria meningitidis (see paper)
31% identity, 55% coverage: 1:251/455 of query aligns to 5:250/308 of 3rmjB
3bliA Crystal structure of the catalytic domain of licms in complexed with pyruvate and acetyl-coa (see paper)
23% identity, 70% coverage: 2:318/455 of query aligns to 4:311/311 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)
37% identity, 21% coverage: 152:248/455 of query aligns to 163:247/347 of Q53WI0
Sites not aligning to the query:
- 324 A→G: Increases the channeling efficiency of propanaldehyde from 57% to 94%.
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)
23% identity, 65% coverage: 7:301/455 of query aligns to 79:385/644 of P9WQB3
- R80 (= R8) binding
- T254 (≠ E181) binding
- H285 (= H202) binding
- H287 (= H204) binding
Sites not aligning to the query:
- 51:368 N-terminal domain
- 369:424 Subdomain I
- 425:433 Linker
- 426:644 Required for the condensation reaction. Not required to bind substrate
- 434:490 Subdomain II
- 491:644 Regulatory domain
- 532 binding
- 536 binding
- 563 binding
- 565 binding
- 625 binding
- 627 binding
Query Sequence
>8501897 FitnessBrowser__Miya:8501897
MLLDTTLREGEQSFGTYLSMADRERVLRGLAAVGVPEAEVGWAGREDLTDMLALSARVAP
GLAAAAWCRCRPGDLRAAVACGASRVCVGVPVSDAHLARRLGLGRAALLDLLAATLAEAR
MLGIEHVTVGMEDASRADRAFVFAVACHAAAHGAHRVRLSDTVGLYTPLEVADVVRALRA
ELEGARQDDTAPRARRVSIGTHFHNDCGMATANALTALECGADCADVSVLGLGERAGVAR
LEELAAALVVRGRARFELAPLRALCGQVAQAASLSVPRHWPVAGRDIFAVESGLHAHGVR
RDPSLFEPFPPELVGDSRRMGVGRKSGVAAVAAALAELSILPPPDELPAIVEAVRDLSAT
LRRPLTPAELAEVAGLGKHHAPPMQTDIPGHAPTARPTARPVPANGIPPQSGPESAPVVS
GMPATDRAATGPHRHPDHTGAHRRGPVPTASGREA
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