SitesBLAST
Comparing Ac3H11_5000 FitnessBrowser__acidovorax_3H11:Ac3H11_5000 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)
51% identity, 93% coverage: 5:529/566 of query aligns to 42:589/644 of P9WQB3
- 51:368 (vs. 14:327, 56% identical) N-terminal domain
- R80 (= R39) binding
- T254 (= T213) binding
- H285 (= H244) binding
- H287 (= H246) binding
- 369:424 (vs. 328:373, 57% identical) Subdomain I
- 425:433 (vs. 374:382, 100% identical) Linker
- 434:490 (vs. 383:437, 38% identical) Subdomain II
- N532 (= N475) binding
- A536 (= A479) binding
- D563 (≠ A503) binding
- A565 (= A505) binding
Sites not aligning to the query:
- 426:644 Required for the condensation reaction. Not required to bind substrate
- 491:644 Regulatory domain
- 625 binding
- 627 binding
3figB Crystal structure of leucine-bound leua from mycobacterium tuberculosis (see paper)
51% identity, 96% coverage: 5:545/566 of query aligns to 25:574/577 of 3figB
3hpzB Crystal structure of mycobacterium tuberculosis leua complexed with bromopyruvate
51% identity, 96% coverage: 5:545/566 of query aligns to 25:574/576 of 3hpzB
3hq1A Crystal structure of mycobacterium tuberculosis leua complexed with citrate and mn2+
50% identity, 96% coverage: 5:545/566 of query aligns to 25:571/573 of 3hq1A
1sr9A Crystal structure of leua from mycobacterium tuberculosis (see paper)
50% identity, 96% coverage: 5:545/566 of query aligns to 25:571/573 of 1sr9A
3hpsA Crystal structure of mycobacterium tuberculosis leua complexed with ketoisocaproate (kic)
50% identity, 96% coverage: 5:545/566 of query aligns to 25:573/575 of 3hpsA
- binding 2-oxo-4-methylpentanoic acid: R63 (= R39), H150 (= H126), Y152 (= Y128), P235 (= P211), T237 (= T213), H268 (= H244), H270 (= H246)
- binding leucine: G500 (= G476), P501 (= P477), L502 (≠ I478), A503 (= A479), D530 (≠ A503), A532 (= A505), Q533 (= Q506), P557 (≠ H529), I559 (= I531)
- binding zinc ion: D64 (= D40), H268 (= H244), H270 (= H246)
4ov4A Isopropylmalate synthase binding with ketoisovalerate (see paper)
28% identity, 70% coverage: 38:431/566 of query aligns to 11:379/379 of 4ov4A
4ov9A Structure of isopropylmalate synthase binding with alpha- isopropylmalate (see paper)
29% identity, 63% coverage: 38:392/566 of query aligns to 11:342/380 of 4ov9A
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, 55% coverage: 34:344/566 of query aligns to 10:308/517 of Q9JZG1
- D16 (= D40) binding
- H204 (= H244) binding
- H206 (= H246) binding
- N240 (= N280) 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)
26% identity, 62% coverage: 32:383/566 of query aligns to 86:429/503 of Q9FN52
- G263 (≠ E215) 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)
24% identity, 72% coverage: 21:429/566 of query aligns to 3:406/409 of 6e1jA
- binding coenzyme a: Q30 (= Q43), F60 (= F73), S63 (≠ A76), I95 (≠ M102), R97 (≠ Q104), F121 (≠ Y128), K132 (≠ V139), L133 (≠ F140), S322 (= S335), G323 (= G336), I324 (≠ S337), D327 (= D340), K331 (= K344), L359 (≠ Q380), R362 (≠ K383), H363 (≠ G384)
- binding 4-(methylsulfanyl)-2-oxobutanoic acid: P192 (= P211), T194 (= T213), H225 (= H244), H227 (= H246)
- binding manganese (ii) ion: D27 (= D40), V82 (≠ I88), E84 (= E90), H225 (= H244), H227 (= H246)
3rmjB Crystal structure of truncated alpha-isopropylmalate synthase from neisseria meningitidis (see paper)
28% identity, 53% coverage: 34:332/566 of query aligns to 7:293/308 of 3rmjB
Q9FG67 Methylthioalkylmalate synthase 1, chloroplastic; 2-isopropylmalate synthase 3; EC 2.3.3.17 from Arabidopsis thaliana (Mouse-ear cress) (see paper)
23% identity, 64% coverage: 6:368/566 of query aligns to 58:412/506 of Q9FG67
- S102 (≠ P48) mutation to F: In gsm1-1; loss of conversion of C3 to C4 glucosinolates.
- A290 (≠ S242) 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)
23% identity, 63% coverage: 34:392/566 of query aligns to 25:352/399 of 6ktqA
- binding 2-oxoglutaric acid: R30 (= R39), R154 (≠ Q173), T156 (≠ S175), E158 (= E177), S184 (≠ N209), T188 (= T213), H216 (= H244), H218 (= H246)
- binding coenzyme a: V67 (≠ A76), R96 (≠ M102), A97 (≠ T103), F116 (≠ Y128), H128 (≠ F140), E158 (= E177)
- binding zinc ion: E31 (≠ D40), H216 (= H244), H218 (= H246)
O87198 Homocitrate synthase; HCS; EC 2.3.3.14 from Thermus thermophilus (strain ATCC BAA-163 / DSM 7039 / HB27) (see paper)
25% identity, 57% coverage: 29:351/566 of query aligns to 2:305/376 of O87198
- R12 (= R39) binding
- E13 (≠ D40) binding
- H72 (≠ L99) 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 (≠ Q173) binding
- S135 (= S175) binding
- T166 (= T213) binding ; binding
- H195 (= H244) binding
- H197 (= H246) binding
Q8F3Q1 (R)-citramalate synthase CimA; LiCMS; EC 2.3.3.21 from Leptospira interrogans serogroup Icterohaemorrhagiae serovar Lai (strain 56601) (see 2 papers)
28% identity, 27% coverage: 208:361/566 of query aligns to 174:318/516 of Q8F3Q1
- T179 (= T213) binding ; mutation to A: 16.4-fold increase in Km for pyruvate and 186-fold decrease in kcat.
- H302 (= H338) mutation H->A,N: Loss of activity.
- D304 (= D340) mutation to A: 5.2-fold increase in Km for acetyl-CoA and 16.6-fold decrease in kcat.
- N310 (≠ A353) mutation to A: 2.2-fold increase in Km for acetyl-CoA and 1.7-fold decrease in kcat.
- L311 (= L354) mutation to A: 8-fold increase in Km for acetyl-CoA and 6-fold decrease in kcat.
- Y312 (≠ W355) mutation to A: Loss of activity.
Sites not aligning to the query:
- 16 mutation R->K,Q: Loss of activity.
- 16:17 binding
- 17 D→A: 34-fold increase in Km for pyruvate and 315-fold decrease in kcat.; D→N: 4.4-fold increase in Km for pyruvate and 480-fold decrease in kcat.
- 81 L→A: 4.7-fold increase in Km for pyruvate and 15.7-fold decrease in kcat.; L→V: 3.3-fold increase in Km for pyruvate and 10.1-fold decrease in kcat.
- 83 F→A: 5-fold increase in Km for acetyl-CoA and 120-fold decrease in kcat.
- 104 L→V: 1.8-fold increase in Km for pyruvate and 3.4-fold decrease in kcat.
- 144 binding ; Y→L: 259-fold increase in Km for pyruvate and 76-fold decrease in kcat.; Y→V: 114-fold increase in Km for pyruvate and 5.3-fold decrease in kcat.
- 146 mutation E->D,Q: Minor effects on the binding of acetyl-CoA, but causes a strong decrease in kcat.
- 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.
2zyfA Crystal structure of homocitrate synthase from thermus thermophilus complexed with magnesuim ion and alpha-ketoglutarate (see paper)
24% identity, 57% coverage: 32:351/566 of query aligns to 5:299/314 of 2zyfA
2ztjA Crystal structure of homocitrate synthase from thermus thermophilus complexed with alpha-ketoglutarate (see paper)
24% identity, 57% coverage: 32:351/566 of query aligns to 5:297/312 of 2ztjA
3a9iA Crystal structure of homocitrate synthase from thermus thermophilus complexed with lys (see paper)
24% identity, 57% coverage: 29:351/566 of query aligns to 1:298/347 of 3a9iA
Q9Y823 Homocitrate synthase, mitochondrial; HCS; EC 2.3.3.14 from Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast) (see 2 papers)
22% identity, 60% coverage: 4:342/566 of query aligns to 13:325/418 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 (≠ P121) binding ; mutation to N: Does not affect the catalytic activity but impairs L-lysine inhibition.
- R163 (≠ Q173) binding ; mutation R->A,Q: Abolishes the catalytic activity.; mutation to K: Severely diminishes affinity for 2-oxoglutarate and substantially impairs catalytic efficiency.
- S165 (= S175) binding ; mutation to A: Results in a moderate decrease in catalytic efficiency.
- E167 (= E177) mutation E->A,Q: Abolishes the catalytic activity.
- T197 (= T213) 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 (≠ S242) mutation to Q: Does not affect the catalytic activity but impairs L-lysine inhibition.
- H224 (= H244) binding ; binding
- H226 (= H246) binding ; binding
- R288 (≠ T305) mutation to K: Does not affect the catalytic activity but impairs L-lysine inhibition.
Sites not aligning to the query:
- 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
>Ac3H11_5000 FitnessBrowser__acidovorax_3H11:Ac3H11_5000
MIAKPATKYQPIAPIALADRQWPSRSITRAPRWLSTDLRDGNQALFEPMNGERKMKLFAE
LVRIGFKEIEVGFPAASQTDFDFVRRLIDENLIPDDVTLMVMTQSREDLIARTVEAVQGA
PRAIVHLYNATAPAWRRIVFGMNVTQVMQLIAHHVGYLKQLTDTQPETQWTLQYSPETFS
ATELSVSLKACQTAIAAWNAGPGRPIIINLPTTVENATPNVFADQIEWMDRHLAPREHIV
LSVHPHNDRGTGVAAAELAMMAGADRVEGCLFGNGERCGNVDIVTLALNLYTQGVHPNLD
FSDITSVARIAEECTSLPVHPRHPYAGDLVFTAFSGSHQDAIKKGFAAQDPNALWEVPYL
PIDPADLGRTYDSVIRVNSQSGKGGIAFLLEREHGVVMPRRMQVEFSAVVQRQTDASEGE
MTGDALWSLFQATYLRAPAQAAITCHSHKLDEDGQGIELDVTIDGTRQTLRGQGNGPIAA
TVDALGLPLRVDHYEERATGTGANAQALAIVEAAMEGVAGATFGAGASHNIVTASVLAIV
GVANRLMARRPQATAGATAAPMAHVD
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