SitesBLAST
Comparing PfGW456L13_4854 FitnessBrowser__pseudo13_GW456_L13:PfGW456L13_4854 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, 97% coverage: 7:550/559 of query aligns to 42:642/644 of P9WQB3
- 51:368 (vs. 16:329, 60% identical) N-terminal domain
- R80 (= R41) binding
- T254 (= T215) binding
- H285 (= H246) binding
- H287 (= H248) binding
- 369:424 (vs. 330:375, 61% identical) Subdomain I
- 425:433 (vs. 376:384, 100% identical) Linker
- 434:490 (vs. 385:438, 44% identical) Subdomain II
- N532 (= N480) binding
- A536 (≠ E484) binding
- D563 (≠ T508) binding
- A565 (= A510) binding
- P625 (≠ E533) binding
- I627 (= I535) binding
Sites not aligning to the query:
- 426:644 Required for the condensation reaction. Not required to bind substrate
- 491:644 Regulatory domain
3hpzB Crystal structure of mycobacterium tuberculosis leua complexed with bromopyruvate
53% identity, 97% coverage: 7:550/559 of query aligns to 25:575/576 of 3hpzB
3hq1A Crystal structure of mycobacterium tuberculosis leua complexed with citrate and mn2+
53% identity, 97% coverage: 7:550/559 of query aligns to 25:572/573 of 3hq1A
1sr9A Crystal structure of leua from mycobacterium tuberculosis (see paper)
53% identity, 97% coverage: 7:550/559 of query aligns to 25:572/573 of 1sr9A
3figB Crystal structure of leucine-bound leua from mycobacterium tuberculosis (see paper)
53% identity, 97% coverage: 7:550/559 of query aligns to 25:575/577 of 3figB
3hpsA Crystal structure of mycobacterium tuberculosis leua complexed with ketoisocaproate (kic)
53% identity, 97% coverage: 7:550/559 of query aligns to 25:574/575 of 3hpsA
- binding 2-oxo-4-methylpentanoic acid: R63 (= R41), H150 (= H128), Y152 (= Y130), P235 (= P213), T237 (= T215), H268 (= H246), H270 (= H248)
- binding leucine: G500 (= G481), P501 (≠ A482), L502 (= L483), A503 (≠ E484), D530 (≠ T508), A532 (= A510), Q533 (≠ K511), P557 (≠ E533), I559 (= I535)
- binding zinc ion: D64 (= D42), H268 (= H246), H270 (= H248)
4ov9A Structure of isopropylmalate synthase binding with alpha- isopropylmalate (see paper)
28% identity, 70% coverage: 40:431/559 of query aligns to 11:379/380 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)
26% identity, 94% coverage: 34:559/559 of query aligns to 8:514/517 of Q9JZG1
- D16 (= D42) binding
- H204 (= H246) binding
- H206 (= H248) binding
- N240 (= N282) binding
Sites not aligning to the query:
- 366:517 Required for the condensation reaction. Not required to bind substrate
4ov4A Isopropylmalate synthase binding with ketoisovalerate (see paper)
28% identity, 70% coverage: 40:431/559 of query aligns to 11:377/379 of 4ov4A
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, 64% coverage: 40:399/559 of query aligns to 92:444/503 of Q9FN52
- G263 (≠ E217) 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)
27% identity, 65% coverage: 38:399/559 of query aligns to 23:377/409 of 6e1jA
- binding coenzyme a: Q30 (= Q45), F60 (= F75), S63 (≠ A78), I95 (≠ L104), R97 (≠ Q106), F121 (≠ Y130), K132 (≠ V141), L133 (≠ F142), S322 (= S337), G323 (= G338), I324 (≠ S339), D327 (= D342), K331 (= K346), L359 (≠ Q382), R362 (≠ K385), H363 (≠ G386)
- binding 4-(methylsulfanyl)-2-oxobutanoic acid: P192 (= P213), T194 (= T215), H225 (= H246), H227 (= H248)
- binding manganese (ii) ion: D27 (= D42), V82 (≠ I95), E84 (≠ D97), H225 (= H246), H227 (= H248)
Q9FG67 Methylthioalkylmalate synthase 1, chloroplastic; 2-isopropylmalate synthase 3; EC 2.3.3.17 from Arabidopsis thaliana (Mouse-ear cress) (see paper)
25% identity, 60% coverage: 38:370/559 of query aligns to 90:412/506 of Q9FG67
- S102 (≠ P50) mutation to F: In gsm1-1; loss of conversion of C3 to C4 glucosinolates.
- A290 (≠ S244) mutation to T: In gsm1-2; loss of conversion of C3 to C4 glucosinolates.
3rmjB Crystal structure of truncated alpha-isopropylmalate synthase from neisseria meningitidis (see paper)
30% identity, 52% coverage: 38:329/559 of query aligns to 9:288/308 of 3rmjB
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, 71% coverage: 36:432/559 of query aligns to 25:366/399 of 6ktqA
- binding 2-oxoglutaric acid: R30 (= R41), R154 (≠ K162), T156 (≠ A164), E158 (≠ Q167), S184 (≠ C193), T188 (≠ V196), H216 (= H246), H218 (= H248)
- binding coenzyme a: V67 (≠ A78), R96 (≠ D110), A97 (≠ L111), F116 (≠ Y130), H128 (≠ F142), E158 (≠ Q167)
- binding zinc ion: E31 (≠ D42), H216 (= H246), H218 (= H248)
3ivtB Homocitrate synthase lys4 bound to 2-og (see paper)
23% identity, 55% coverage: 38:344/559 of query aligns to 35:320/400 of 3ivtB
Q9Y823 Homocitrate synthase, mitochondrial; HCS; EC 2.3.3.14 from Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast) (see 2 papers)
23% identity, 55% coverage: 38:344/559 of query aligns to 40:325/418 of Q9Y823
- R43 (= R41) binding ; mutation R->A,K,Q: Abolishes the catalytic activity.
- E44 (≠ D42) binding ; binding ; binding
- Q47 (= Q45) mutation to A: Abolishes the catalytic activity.
- E74 (= E72) 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 (= H128) binding ; mutation to A: Substantially impairs catalytic efficiency.
- D123 (≠ K150) binding ; mutation to N: Does not affect the catalytic activity but impairs L-lysine inhibition.
- R163 (vs. gap) binding ; mutation R->A,Q: Abolishes the catalytic activity.; mutation to K: Severely diminishes affinity for 2-oxoglutarate and substantially impairs catalytic efficiency.
- S165 (≠ A183) binding ; mutation to A: Results in a moderate decrease in catalytic efficiency.
- E167 (= E185) mutation E->A,Q: Abolishes the catalytic activity.
- T197 (= T215) 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 (≠ S244) mutation to Q: Does not affect the catalytic activity but impairs L-lysine inhibition.
- H224 (= H246) binding ; binding
- H226 (= H248) binding ; binding
- R288 (≠ D307) 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.
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)
35% identity, 14% coverage: 243:323/559 of query aligns to 198:279/347 of Q53WI0
Sites not aligning to the query:
- 324 A→G: Increases the channeling efficiency of propanaldehyde from 57% to 94%.
3mi3A Homocitrate synthase lys4 bound to lysine (see paper)
23% identity, 55% coverage: 38:344/559 of query aligns to 17:291/370 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)
25% identity, 29% coverage: 203:363/559 of query aligns to 167:318/516 of Q8F3Q1
- T179 (= T215) binding ; mutation to A: 16.4-fold increase in Km for pyruvate and 186-fold decrease in kcat.
- H302 (= H340) mutation H->A,N: Loss of activity.
- D304 (= D342) mutation to A: 5.2-fold increase in Km for acetyl-CoA and 16.6-fold decrease in kcat.
- N310 (≠ A355) mutation to A: 2.2-fold increase in Km for acetyl-CoA and 1.7-fold decrease in kcat.
- L311 (= L356) mutation to A: 8-fold increase in Km for acetyl-CoA and 6-fold decrease in kcat.
- Y312 (≠ W357) 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.
3ivsA Homocitrate synthase lys4 (see paper)
23% identity, 55% coverage: 38:344/559 of query aligns to 17:289/364 of 3ivsA
Query Sequence
>PfGW456L13_4854 FitnessBrowser__pseudo13_GW456_L13:PfGW456L13_4854
MSMLKDPSSKYRAFPTIDIPDRTWPSKTITAAPIWCSSDLRDGNQSLIEPMDAVKKLRFW
KTLVQVGVKEIEASFPAASQTDFDFVRTLIEGNHIPDDTTIQVLTQGREDLIERTFESLR
GAKKAIVHLYNATSPSFRRIVFNQDKDGVKAIAVNAAKLFVKYAAMQPDTEWTFEYSPET
FSATEMEFAKEVCDAVIEVWNPTPEHKMILNLPATVECATPNIYADQIEWFGRHINRRDS
VIISLHTHNDRGTGVAATELGLMAGADRVEGCLFGNGERTGNVDLVTVALNLYTQGVNPE
LDFSDIDGVRKVVEECNQIQVHPRHPYVGDLVHTAFSGSHQDAIRKGFAQQKPDALWEVP
YLPIDPADIGRSYEAVIRVNSQSGKGGIAYLLEQEYGISLPRRMQIEFSQVVQRETDRLG
LEMTAQQIHALLHSEYLQANTPYALVSHRLQEENGHSAVEVEVASQGQGETNLHWRGKGN
GALEALVAGLPVPVEIMDYNEHAIGAGTNAKAAAYIELRVNGERAVHGVGIDENITTASF
KALFSALNRSLSQPEAKAA
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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