SitesBLAST
Comparing Ga0059261_2979 FitnessBrowser__Korea:Ga0059261_2979 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)
5oasA Crystal structure of malate synthase g from pseudomonas aeruginosa in apo form. (see paper)
61% identity, 100% coverage: 1:699/700 of query aligns to 4:725/728 of 5oasA
5vfbA 1.36 angstrom resolution crystal structure of malate synthase g from pseudomonas aeruginosa in complex with glycolic acid.
61% identity, 100% coverage: 2:699/700 of query aligns to 1:721/724 of 5vfbA
6axeA Crystal structure of a malate synthase g from mycobacterium marinum bound to acetyl coa
59% identity, 100% coverage: 1:699/700 of query aligns to 2:727/729 of 6axeA
- active site: D272 (= D249), E274 (= E251), R338 (= R317), E437 (= E408), D465 (= D436), D636 (= D608)
- binding acetyl coenzyme *a: V119 (= V118), V120 (= V119), R126 (= R125), F127 (= F126), N130 (= N129), A131 (= A130), R311 (= R290), R338 (= R317), M518 (= M489), W544 (= W515), P546 (= P517), P548 (= P519), C622 (= C594), K624 (= K596), M634 (= M606), D636 (= D608)
- binding magnesium ion: E437 (= E408), D465 (= D436)
4ex4B The structure of glcb from mycobacterium leprae
58% identity, 99% coverage: 5:699/700 of query aligns to 3:721/721 of 4ex4B
- active site: D266 (= D249), E268 (= E251), R334 (= R317), E431 (= E408), D459 (= D436), D630 (= D608)
- binding magnesium ion: N290 (≠ M273), K291 (≠ R274), H371 (= H351), N379 (≠ L356), L382 (≠ H359), T383 (≠ R360), N384 (= N361), E431 (= E408), D459 (= D436)
P9WK16 Malate synthase G; EC 2.3.3.9 from Mycobacterium tuberculosis (strain CDC 1551 / Oshkosh) (see paper)
58% identity, 100% coverage: 1:699/700 of query aligns to 1:724/741 of P9WK16
- R339 (= R317) active site, Proton acceptor
- D633 (= D608) active site, Proton donor
P37330 Malate synthase G; MSG; EC 2.3.3.9 from Escherichia coli (strain K12) (see 2 papers)
56% identity, 100% coverage: 1:697/700 of query aligns to 1:720/723 of P37330
- M1 (= M1) modified: Initiator methionine, Removed
- R338 (= R317) mutation to K: Has a specific activity which is only 6.6% of the wild-type activity.
- C617 (= C594) modified: Cysteine sulfenic acid (-SOH); mutation to S: Affinity binding for acetyl-CoA is more than five times greater than that of wild-type, although its specific activity is comparable.
- D631 (= D608) mutation to N: Absence of malate synthase activity.
- C688 (≠ L665) modified: Cysteine sulfenic acid (-SOH)
2gq3A Mycobacterium tuberculosis malate synthase in complex with magnesium, malate, and coenzyme a (see paper)
58% identity, 100% coverage: 2:699/700 of query aligns to 1:717/720 of 2gq3A
- active site: D267 (= D249), E269 (= E251), R335 (= R317), E430 (= E408), D458 (= D436), D626 (= D608)
- binding coenzyme a: V114 (= V118), V115 (= V119), R121 (= R125), F122 (= F126), N125 (= N129), A126 (= A130), K301 (= K283), R308 (= R290), P539 (= P517), P541 (= P519), C612 (= C594), M624 (= M606), D626 (= D608)
- binding magnesium ion: H370 (= H351), K373 (= K354), N378 (vs. gap), G379 (= G357), L381 (≠ H359), E430 (= E408), D458 (= D436)
6dkoA Crystal structure of mycobacterium tuberculosis malate synthase in complex with 2,6-f-phenyldiketoacid (see paper)
57% identity, 100% coverage: 2:699/700 of query aligns to 1:713/716 of 6dkoA
- active site: D270 (= D249), E272 (= E251), R332 (= R317), E424 (= E408), D452 (= D436), D622 (= D608)
- binding 4-(2,6-difluorophenyl)-2,4-dioxobutanoic acid: R332 (= R317), G449 (= G433), L451 (= L435), D452 (= D436), M505 (= M489), W531 (= W515), M620 (= M606), D622 (= D608)
- binding magnesium ion: E424 (= E408), D452 (= D436)
6bu1A Crystal structure of mycobacterium tuberculosis malate synthase in complex with 2-br-3-oh-phenyldiketoacid (see paper)
57% identity, 99% coverage: 5:699/700 of query aligns to 3:709/712 of 6bu1A
- active site: D269 (= D249), E271 (= E251), R327 (= R317), E419 (= E408), D447 (= D436), D618 (= D608)
- binding (2Z)-4-(2-bromo-3-hydroxyphenyl)-2-hydroxy-4-oxobut-2-enoic acid: V116 (= V118), R327 (= R317), E419 (= E408), G444 (= G433), L446 (= L435), D447 (= D436), M500 (= M489), W526 (= W515), M616 (= M606), D618 (= D608)
- binding magnesium ion: E419 (= E408), D447 (= D436), V463 (≠ I452), R464 (≠ P453)
6dnpA Crystal structure of mycobacterium tuberculosis malate synthase in complex with 2-f-3-methyl-6-f-phenyldiketoacid (see paper)
57% identity, 100% coverage: 2:699/700 of query aligns to 1:709/712 of 6dnpA
- active site: D270 (= D249), E272 (= E251), R328 (= R317), E419 (= E408), D447 (= D436), D618 (= D608)
- binding (2Z)-4-(2,6-difluoro-3-methylphenyl)-2-hydroxy-4-oxobut-2-enoic acid: R328 (= R317), E419 (= E408), G444 (= G433), L446 (= L435), D447 (= D436), M500 (= M489), W526 (= W515), M616 (= M606), D618 (= D608)
- binding magnesium ion: E419 (= E408), D447 (= D436)
5cbiA Crystal structure of mycobacterium tuberculosis malate synthase in complex with 5-chloro-2-hydroxybenzonitrile (see paper)
57% identity, 100% coverage: 2:699/700 of query aligns to 1:716/719 of 5cbiA
- active site: D270 (= D249), E272 (= E251), R331 (= R317), E426 (= E408), D454 (= D436), D625 (= D608)
- binding 5-chloro-2-hydroxybenzonitrile: L53 (= L54), N54 (≠ D55), D57 (= D58), F125 (= F126), Y138 (= Y139), D139 (= D140), Y142 (= Y143), M507 (= M489), W533 (= W515), P535 (= P517), A611 (≠ C594), M623 (= M606), M623 (= M606), E624 (= E607), D625 (= D608)
- binding magnesium ion: E426 (= E408), D454 (= D436)
6c8pA Crystal structure of mycobacterium tuberculosis malate synthase in complex with 2-f-phenyldiketoacid (see paper)
57% identity, 100% coverage: 2:699/700 of query aligns to 1:713/716 of 6c8pA
- active site: D270 (= D249), E272 (= E251), R329 (= R317), E423 (= E408), D451 (= D436), D622 (= D608)
- binding (2Z)-4-(2-fluorophenyl)-2-hydroxy-4-oxobut-2-enoic acid: R329 (= R317), E423 (= E408), G448 (= G433), L450 (= L435), D451 (= D436), M504 (= M489), W530 (= W515), M620 (= M606), D622 (= D608)
- binding magnesium ion: E423 (= E408), D451 (= D436)
5c9rA Crystal structure of mycobacterium tuberculosis malate synthase in complex with 3-((4-chlorophenyl)thio)propanoic acid (see paper)
57% identity, 100% coverage: 2:699/700 of query aligns to 1:714/717 of 5c9rA
- active site: D270 (= D249), E272 (= E251), R331 (= R317), E424 (= E408), D452 (= D436), D623 (= D608)
- binding 3-[(4-chlorophenyl)sulfanyl]propanoic acid: V117 (= V118), E424 (= E408), D452 (= D436), M505 (= M489), W531 (= W515), M621 (= M606), D623 (= D608)
- binding magnesium ion: E424 (= E408), D452 (= D436)
5cc3A Crystal structure of mycobacterium tuberculosis malate synthase in complex with 6-bromo-1h-indole-2-carboxylic acid
57% identity, 100% coverage: 2:699/700 of query aligns to 1:712/715 of 5cc3A
- active site: D270 (= D249), E272 (= E251), R328 (= R317), E422 (= E408), D450 (= D436), D621 (= D608)
- binding 6-bromanyl-1H-indole-2-carboxylic acid: V117 (= V118), M503 (= M489), M619 (= M606), D621 (= D608)
- binding magnesium ion: E422 (= E408), D450 (= D436), V466 (≠ I452), R467 (≠ P453), T470 (≠ E456)
5cahA Crystal structure of mycobacterium tuberculosis malate synthase in complex with 6h-thieno[2,3-b]pyrrole-5-carboxylic acid (see paper)
57% identity, 100% coverage: 2:699/700 of query aligns to 1:703/706 of 5cahA
- active site: D266 (= D249), E268 (= E251), R324 (= R317), E413 (= E408), D441 (= D436), D612 (= D608)
- binding 6H-thieno[2,3-b]pyrrole-5-carboxylic acid: S270 (= S253), M494 (= M489), M610 (= M606), E611 (= E607), D612 (= D608)
- binding magnesium ion: E413 (= E408), D441 (= D436)
5drcA Crystal structure of mycobacterium tuberculosis malate synthase in complex with 2-hydroxy-4-(1h-indol-3-yl)-4-oxobut-2-enoic acid (see paper)
57% identity, 100% coverage: 2:699/700 of query aligns to 1:713/716 of 5drcA
- active site: D270 (= D249), E272 (= E251), R330 (= R317), E423 (= E408), D451 (= D436), D622 (= D608)
- binding (2Z)-2-hydroxy-4-(1H-indol-3-yl)-4-oxobut-2-enoic acid: R330 (= R317), E423 (= E408), G448 (= G433), L450 (= L435), D451 (= D436), M504 (= M489), W530 (= W515), M620 (= M606), D622 (= D608)
- binding magnesium ion: E423 (= E408), D451 (= D436), R468 (≠ P453), T471 (≠ E456)
5cjmA Crystal structure of mycobacterium tuberculosis malate synthase in complex with 4h-thieno[3,2-b]pyrrole-5-carboxylic acid (see paper)
57% identity, 100% coverage: 2:699/700 of query aligns to 1:708/711 of 5cjmA
- active site: D270 (= D249), E272 (= E251), R328 (= R317), E418 (= E408), D446 (= D436), D617 (= D608)
- binding 4h-thieno[3,2-b]pyrole-5-carboxylic acid: V117 (= V118), S274 (= S253), M499 (= M489), E616 (= E607), D617 (= D608)
- binding magnesium ion: E418 (= E408), D446 (= D436)
5t8gA Crystal structure of mycobacterium tuberculosis malate synthase in complex with 2-oxo-4-((thiophene-2-carbonyl)oxy)butanoic acid (see paper)
57% identity, 100% coverage: 2:699/700 of query aligns to 1:711/714 of 5t8gA
- active site: D270 (= D249), E272 (= E251), R328 (= R317), E421 (= E408), D449 (= D436), D620 (= D608)
- binding (3E)-2-oxo-4-[(thiophen-2-ylcarbonyl)oxy]but-3-enoic acid: V117 (= V118), R328 (= R317), E421 (= E408), G446 (= G433), L448 (= L435), D449 (= D436), M502 (= M489), W528 (= W515), E619 (= E607), D620 (= D608)
- binding magnesium ion: E421 (= E408), D449 (= D436), R466 (≠ P453), T469 (≠ E456)
5dx7A Crystal structure of mycobacterium tuberculosis malate synthase in complex with 5-(5-chlorothiophen-2-yl)isoxazole-3-carboxylic acid (see paper)
57% identity, 100% coverage: 2:699/700 of query aligns to 1:711/714 of 5dx7A
- active site: D270 (= D249), E272 (= E251), R328 (= R317), E421 (= E408), D449 (= D436), D620 (= D608)
- binding 5-(5-chlorothiophen-2-yl)-1,2-oxazole-3-carboxylic acid: V117 (= V118), M502 (= M489), M618 (= M606), D620 (= D608)
- binding magnesium ion: E421 (= E408), D449 (= D436)
5c9uA Crystal structure of mycobacterium tuberculosis malate synthase in complex with 2-(2-(2,4-dichlorophenyl)hydrazinyl)-2-oxoacetic acid (see paper)
57% identity, 100% coverage: 2:699/700 of query aligns to 1:711/714 of 5c9uA
- active site: D270 (= D249), E272 (= E251), R328 (= R317), E421 (= E408), D449 (= D436), D620 (= D608)
- binding [2-(2,4-dichlorophenyl)hydrazinyl](oxo)acetic acid: E421 (= E408), G446 (= G433), L448 (= L435), D449 (= D436), M502 (= M489), W528 (= W515), M618 (= M606), E619 (= E607), D620 (= D608)
- binding magnesium ion: E421 (= E408), D449 (= D436)
Query Sequence
>Ga0059261_2979 FitnessBrowser__Korea:Ga0059261_2979
MTAYVTRAGLSVAEPLARFVEERVLPGPGIDADVFWSGAAAIFARFAPRNRALLDTRDSL
QAQIDAWCAEDPARAADPAAQEAFLRGIGYLVDQPGAFTVTTADVDAEIATMAGPQLVVP
ALNARFVLNAANARWGSLYDAFYGTDALPGAARAGGYDAERGAQVIAAAKAFLDEAVPLA
GMKWVDFAGGDLPLADPGQLVGTRGDSLLFRHNGLHIEVVIDRDSTIGRTDPAGIADVLL
EAALTTIVDLEDSIAAVDADDKVAAYSNWLGLMRGDLVETFDKGGKTLTRRLAEDRVYQR
PFASDLVLPGRSLLFVRNVGHLMTNPAVLIDGDEAPEGILDAIVTSTIALHDLKGLGTHR
NSRTGSVYIVKPKMHGPDEAAFTNDLFDAVEDLLGLDRHTIKVGVMDEERRTSANLAACI
HAVKGRIAFINTGFLDRTGDEIHSSMRAGPMIPKAEMKASSWIKAYEDRNVRIGLAHGLS
GRAQIGKGMWAAPDRMAEMLEVKVGHPQSGANTAWVPSPTAATLHAMHYHTVDVFARQRE
IAGETVPGLAPLLTIPVAAPGRNWTPEDVARELDNNAQGILGYVVRWIDQGVGCSKVPDI
NDIGLMEDRATLRISSQHMANWLLHGVATAADVDAALVRMAAKVDAQNAGDPLYRPMAGN
EAASLAFQAARALVFDGVAQPNGYTEPLLHRFRAEAKARG
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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