SitesBLAST
Comparing 17054 FitnessBrowser__Keio:17054 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)
P37330 Malate synthase G; MSG; EC 2.3.3.9 from Escherichia coli (strain K12) (see 2 papers)
100% identity, 100% coverage: 1:723/723 of query aligns to 1:723/723 of P37330
- M1 (= M1) modified: Initiator methionine, Removed
- R338 (= R338) mutation to K: Has a specific activity which is only 6.6% of the wild-type activity.
- C617 (= C617) 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 (= D631) mutation to N: Absence of malate synthase activity.
- C688 (= C688) modified: Cysteine sulfenic acid (-SOH)
1d8cA Malate synthase g complexed with magnesium and glyoxylate (see paper)
98% identity, 100% coverage: 3:722/723 of query aligns to 1:709/709 of 1d8cA
- active site: D268 (= D270), E270 (= E272), R325 (= R338), E414 (= E427), D442 (= D455), D618 (= D631)
- binding glyoxylic acid: M412 (= M425), E414 (= E427), G439 (= G452), L441 (= L454), D442 (= D455)
- binding magnesium ion: E414 (= E427), D442 (= D455)
- binding sorbitol: Q59 (= Q61), H449 (= H462), V688 (= V701), K689 (= K702), Q690 (= Q703), P691 (= P704)
1p7tA Structure of escherichia coli malate synthase g:pyruvate:acetyl- coenzyme a abortive ternary complex at 1.95 angstrom resolution (see paper)
98% identity, 99% coverage: 4:722/723 of query aligns to 1:706/706 of 1p7tA
- active site: D259 (= D270), E261 (= E272), R322 (= R338), E411 (= E427), D439 (= D455), D615 (= D631)
- binding acetyl coenzyme *a: V115 (= V118), V116 (= V119), P117 (= P120), R122 (= R125), Y123 (= Y126), N126 (= N129), A127 (= A130), S263 (= S274), R295 (= R311), R322 (= R338), M492 (= M508), P520 (= P536), P522 (= P538), C601 (= C617), M613 (= M629), D615 (= D631)
- binding magnesium ion: E411 (= E427), D439 (= D455)
- binding pyruvic acid: E411 (= E427), G436 (= G452), L438 (= L454), D439 (= D455), W518 (= W534)
5oasA Crystal structure of malate synthase g from pseudomonas aeruginosa in apo form. (see paper)
59% identity, 99% coverage: 1:716/723 of query aligns to 4:719/728 of 5oasA
5vfbA 1.36 angstrom resolution crystal structure of malate synthase g from pseudomonas aeruginosa in complex with glycolic acid.
60% identity, 97% coverage: 19:716/723 of query aligns to 18:715/724 of 5vfbA
P9WK16 Malate synthase G; EC 2.3.3.9 from Mycobacterium tuberculosis (strain CDC 1551 / Oshkosh) (see paper)
58% identity, 99% coverage: 1:716/723 of query aligns to 1:718/741 of P9WK16
- R339 (= R338) active site, Proton acceptor
- D633 (= D631) active site, Proton donor
2gq3A Mycobacterium tuberculosis malate synthase in complex with magnesium, malate, and coenzyme a (see paper)
58% identity, 98% coverage: 5:716/723 of query aligns to 4:711/720 of 2gq3A
- active site: D267 (= D270), E269 (= E272), R335 (= R338), E430 (= E427), D458 (= D455), D626 (= D631)
- binding coenzyme a: V114 (= V118), V115 (= V119), R121 (= R125), F122 (≠ Y126), N125 (= N129), A126 (= A130), K301 (= K304), R308 (= R311), P539 (= P536), P541 (= P538), C612 (= C617), M624 (= M629), D626 (= D631)
- binding magnesium ion: H370 (≠ Y373), K373 (= K376), N378 (vs. gap), G379 (vs. gap), L381 (vs. gap), E430 (= E427), D458 (= D455)
6dnpA Crystal structure of mycobacterium tuberculosis malate synthase in complex with 2-f-3-methyl-6-f-phenyldiketoacid (see paper)
58% identity, 98% coverage: 5:716/723 of query aligns to 4:703/712 of 6dnpA
- active site: D270 (= D270), E272 (= E272), R328 (= R338), E419 (= E427), D447 (= D455), D618 (= D631)
- binding (2Z)-4-(2,6-difluoro-3-methylphenyl)-2-hydroxy-4-oxobut-2-enoic acid: R328 (= R338), E419 (= E427), G444 (= G452), L446 (= L454), D447 (= D455), M500 (= M508), W526 (= W534), M616 (= M629), D618 (= D631)
- binding magnesium ion: E419 (= E427), D447 (= D455)
6axeA Crystal structure of a malate synthase g from mycobacterium marinum bound to acetyl coa
58% identity, 99% coverage: 1:716/723 of query aligns to 2:721/729 of 6axeA
- active site: D272 (= D270), E274 (= E272), R338 (= R338), E437 (= E427), D465 (= D455), D636 (= D631)
- binding acetyl coenzyme *a: V119 (= V118), V120 (= V119), R126 (= R125), F127 (≠ Y126), N130 (= N129), A131 (= A130), R311 (= R311), R338 (= R338), M518 (= M508), W544 (= W534), P546 (= P536), P548 (= P538), C622 (= C617), K624 (= K619), M634 (= M629), D636 (= D631)
- binding magnesium ion: E437 (= E427), D465 (= D455)
5e9xA Crystal structure of mycobacterium tuberculosis malate synthase in complex with 2-chloro-6h-thieno[2,3-b]pyrrole-5-carboxylic acid (see paper)
58% identity, 98% coverage: 5:716/723 of query aligns to 4:706/715 of 5e9xA
- active site: D267 (= D270), E269 (= E272), R327 (= R338), E422 (= E427), D450 (= D455), D621 (= D631)
- binding 2-chloranyl-6~{H}-thieno[2,3-b]pyrrole-5-carboxylic acid: V114 (= V118), S271 (= S274), M503 (= M508), M619 (= M629), E620 (= E630), D621 (= D631)
- binding magnesium ion: E422 (= E427), D450 (= D455)
5cahA Crystal structure of mycobacterium tuberculosis malate synthase in complex with 6h-thieno[2,3-b]pyrrole-5-carboxylic acid (see paper)
58% identity, 98% coverage: 5:716/723 of query aligns to 4:697/706 of 5cahA
- active site: D266 (= D270), E268 (= E272), R324 (= R338), E413 (= E427), D441 (= D455), D612 (= D631)
- binding 6H-thieno[2,3-b]pyrrole-5-carboxylic acid: S270 (= S274), M494 (= M508), M610 (= M629), E611 (= E630), D612 (= D631)
- binding magnesium ion: E413 (= E427), D441 (= D455)
5c9rA Crystal structure of mycobacterium tuberculosis malate synthase in complex with 3-((4-chlorophenyl)thio)propanoic acid (see paper)
58% identity, 98% coverage: 5:716/723 of query aligns to 4:708/717 of 5c9rA
- active site: D270 (= D270), E272 (= E272), R331 (= R338), E424 (= E427), D452 (= D455), D623 (= D631)
- binding 3-[(4-chlorophenyl)sulfanyl]propanoic acid: V117 (= V118), E424 (= E427), D452 (= D455), M505 (= M508), W531 (= W534), M621 (= M629), D623 (= D631)
- binding magnesium ion: E424 (= E427), D452 (= D455)
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)
58% identity, 98% coverage: 5:716/723 of query aligns to 4:707/716 of 5drcA
- active site: D270 (= D270), E272 (= E272), R330 (= R338), E423 (= E427), D451 (= D455), D622 (= D631)
- binding (2Z)-2-hydroxy-4-(1H-indol-3-yl)-4-oxobut-2-enoic acid: R330 (= R338), E423 (= E427), G448 (= G452), L450 (= L454), D451 (= D455), M504 (= M508), W530 (= W534), M620 (= M629), D622 (= D631)
- binding magnesium ion: E423 (= E427), D451 (= D455), R468 (= R472), T471 (≠ Q475)
5c9wA Crystal structure of mycobacterium tuberculosis malate synthase in complex with (z)-n-(2-bromophenyl)-2-(hydroxyimino)acetamide (see paper)
58% identity, 98% coverage: 5:716/723 of query aligns to 4:704/713 of 5c9wA
- active site: D269 (= D270), E271 (= E272), R327 (= R338), E420 (= E427), D448 (= D455), D619 (= D631)
- binding (2E)-N-(2-bromophenyl)-2-(hydroxyimino)acetamide: V116 (= V118), R327 (= R338), M501 (= M508), W527 (= W534), M617 (= M629), D619 (= D631)
- binding magnesium ion: E420 (= E427), D448 (= D455), V464 (≠ L471), R465 (= R472), T468 (≠ Q475)
5cjmA Crystal structure of mycobacterium tuberculosis malate synthase in complex with 4h-thieno[3,2-b]pyrrole-5-carboxylic acid (see paper)
58% identity, 98% coverage: 5:716/723 of query aligns to 4:702/711 of 5cjmA
- active site: D270 (= D270), E272 (= E272), R328 (= R338), E418 (= E427), D446 (= D455), D617 (= D631)
- binding 4h-thieno[3,2-b]pyrole-5-carboxylic acid: V117 (= V118), S274 (= S274), M499 (= M508), E616 (= E630), D617 (= D631)
- binding magnesium ion: E418 (= E427), D446 (= D455)
5cbiA Crystal structure of mycobacterium tuberculosis malate synthase in complex with 5-chloro-2-hydroxybenzonitrile (see paper)
57% identity, 98% coverage: 5:716/723 of query aligns to 4:710/719 of 5cbiA
- active site: D270 (= D270), E272 (= E272), R331 (= R338), E426 (= E427), D454 (= D455), D625 (= D631)
- binding 5-chloro-2-hydroxybenzonitrile: L53 (= L54), N54 (≠ A55), D57 (= D58), F125 (≠ Y126), Y138 (= Y139), D139 (= D140), Y142 (= Y143), M507 (= M508), W533 (= W534), P535 (= P536), A611 (≠ C617), M623 (= M629), M623 (= M629), E624 (= E630), D625 (= D631)
- binding magnesium ion: E426 (= E427), D454 (= D455)
6c2xA Crystal structure of mycobacterium tuberculosis malate synthase in complex with 2-br-6-me-phenyldiketoacid (see paper)
58% identity, 98% coverage: 5:716/723 of query aligns to 4:702/711 of 6c2xA
- active site: D268 (= D270), E270 (= E272), R328 (= R338), E418 (= E427), D446 (= D455), D617 (= D631)
- binding (2S)-4-(2-bromo-6-methylphenyl)-2-hydroxy-4-oxobutanoic acid: V115 (= V118), R328 (= R338), E418 (= E427), G443 (= G452), L445 (= L454), D446 (= D455), M499 (= M508), W525 (= W534), M615 (= M629), D617 (= D631)
- binding magnesium ion: E418 (= E427), D446 (= D455)
6dkoA Crystal structure of mycobacterium tuberculosis malate synthase in complex with 2,6-f-phenyldiketoacid (see paper)
58% identity, 98% coverage: 5:716/723 of query aligns to 4:707/716 of 6dkoA
- active site: D270 (= D270), E272 (= E272), R332 (= R338), E424 (= E427), D452 (= D455), D622 (= D631)
- binding 4-(2,6-difluorophenyl)-2,4-dioxobutanoic acid: R332 (= R338), G449 (= G452), L451 (= L454), D452 (= D455), M505 (= M508), W531 (= W534), M620 (= M629), D622 (= D631)
- binding magnesium ion: E424 (= E427), D452 (= D455)
5cczA Crystal structure of mycobacterium tuberculosis malate synthase in complex with 3-(4-fluorophenyl)-4-methyl-1h-pyrazol-5-amine (see paper)
58% identity, 98% coverage: 5:716/723 of query aligns to 4:704/713 of 5cczA
- active site: D267 (= D270), E269 (= E272), R325 (= R338), E420 (= E427), D448 (= D455), D619 (= D631)
- binding 3-(4-fluorophenyl)-4-methyl-1H-pyrazol-5-amine: V114 (= V118), S271 (= S274), M501 (= M508), W527 (= W534), P529 (= P536), M617 (= M629), E618 (= E630), D619 (= D631)
- binding magnesium ion: E420 (= E427), D448 (= D455)
5cbjA Crystal structure of mycobacterium tuberculosis malate synthase in complex with 3-(phenylthio)acrylic acid (see paper)
58% identity, 98% coverage: 5:716/723 of query aligns to 4:700/709 of 5cbjA
- active site: D265 (= D270), E267 (= E272), R323 (= R338), E416 (= E427), D444 (= D455), D615 (= D631)
- binding (2E)-3-(phenylsulfanyl)prop-2-enoic acid: V112 (= V118), M497 (= M508), W523 (= W534), P525 (= P536), M613 (= M629), E614 (= E630), D615 (= D631)
- binding magnesium ion: E416 (= E427), D444 (= D455)
Query Sequence
>17054 FitnessBrowser__Keio:17054
MSQTITQSRLRIDANFKRFVDEEVLPGTGLDAAAFWRNFDEIVHDLAPENRQLLAERDRI
QAALDEWHRSNPGPVKDKAAYKSFLRELGYLVPQPERVTVETTGIDSEITSQAGPQLVVP
AMNARYALNAANARWGSLYDALYGSDIIPQEGAMVSGYDPQRGEQVIAWVRRFLDESLPL
ENGSYQDVVAFKVVDKQLRIQLKNGKETTLRTPAQFVGYRGDAAAPTCILLKNNGLHIEL
QIDANGRIGKDDPAHINDVIVEAAISTILDCEDSVAAVDAEDKILLYRNLLGLMQGTLQE
KMEKNGRQIVRKLNDDRHYTAADGSEISLHGRSLLFIRNVGHLMTIPVIWDSEGNEIPEG
ILDGVMTGAIALYDLKVQKNSRTGSVYIVKPKMHGPQEVAFANKLFTRIETMLGMAPNTL
KMGIMDEERRTSLNLRSCIAQARNRVAFINTGFLDRTGDEMHSVMEAGPMLRKNQMKSTP
WIKAYERNNVLSGLFCGLRGKAQIGKGMWAMPDLMADMYSQKGDQLRAGANTAWVPSPTA
ATLHALHYHQTNVQSVQANIAQTEFNAEFEPLLDDLLTIPVAENANWSAQEIQQELDNNV
QGILGYVVRWVEQGIGCSKVPDIHNVALMEDRATLRISSQHIANWLRHGILTKEQVQASL
ENMAKVVDQQNAGDPAYRPMAGNFANSCAFKAASDLIFLGVKQPNGYTEPLLHAWRLREK
ESH
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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