SitesBLAST
Comparing 3609095 FitnessBrowser__Dino:3609095 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)
P20932 (S)-mandelate dehydrogenase; MDH; L(+)-mandelate dehydrogenase; EC 1.1.99.31 from Pseudomonas putida (Arthrobacter siderocapsulatus) (see 3 papers)
32% identity, 90% coverage: 10:359/389 of query aligns to 8:352/393 of P20932
- PTG 79:81 (≠ PVG 82:84) binding
- G81 (= G84) mutation to A: 23-fold decrease in catalytic activity with mandelate as substrate and DCPIP as electron acceptor, but no change in affinity for mandelate. Shows a modestly higher reactivity with molecular oxygen.
- S108 (= S111) binding
- Q129 (= Q132) binding
- T156 (= T160) binding
- K250 (= K255) binding
- DSGFR 303:307 (≠ DSGIE 310:314) binding
- GR 326:327 (= GR 333:334) binding
6bfgA Crystal structure of monotopic membrane protein (s)-mandelate dehydrogenase (see paper)
32% identity, 90% coverage: 10:359/389 of query aligns to 6:350/373 of 6bfgA
- active site: Y129 (= Y134), D156 (= D162), H272 (= H279)
- binding flavin mononucleotide: Y24 (= Y28), P77 (= P82), T78 (≠ V83), G79 (= G84), Q127 (= Q132), Y129 (= Y134), T154 (= T160), K248 (= K255), H272 (= H279), G273 (≠ S280), R275 (= R282), D301 (= D310), S302 (= S311), G303 (= G312), R305 (≠ E314), G324 (= G333), R325 (= R334)
5zzqA The crystal structure of mandelate oxidase with (s)-4-hydroxymandelic acid (see paper)
33% identity, 95% coverage: 7:375/389 of query aligns to 1:346/355 of 5zzqA
- active site: Y126 (= Y134), D154 (= D162), H250 (= H279)
- binding flavin mononucleotide: P75 (= P82), V76 (= V83), A77 (≠ G84), Q124 (= Q132), Y126 (= Y134), T152 (= T160), K226 (= K255), H250 (= H279), R253 (= R282), D281 (= D310), G283 (= G312), R285 (≠ E314), G304 (= G333), R305 (= R334)
- binding (2S)-hydroxy(4-hydroxyphenyl)ethanoic acid: L106 (≠ V113), Y126 (= Y134), M158 (≠ D166), R161 (= R169), T200 (≠ A228), F204 (≠ I232), H250 (= H279), R253 (= R282)
6a24A The crystal structure of mandelate oxidase with 3-fluoropyruvate (see paper)
33% identity, 95% coverage: 7:375/389 of query aligns to 1:346/354 of 6a24A
- active site: Y126 (= Y134), D154 (= D162), H250 (= H279)
- binding flavin mononucleotide: P75 (= P82), V76 (= V83), A77 (≠ G84), Q124 (= Q132), Y126 (= Y134), T152 (= T160), K226 (= K255), H250 (= H279), G251 (≠ S280), R253 (= R282), D281 (= D310), G282 (≠ S311), G283 (= G312), R285 (≠ E314), G304 (= G333), R305 (= R334)
- binding pyruvic acid: R161 (= R169), H250 (= H279), R253 (= R282)
6a1rA Mandelate oxidase mutant-y128f with the n5-phenylacetyl-fmn adduct (see paper)
32% identity, 95% coverage: 6:375/389 of query aligns to 1:324/332 of 6a1rA
- active site: F127 (≠ Y134), D155 (= D162), H228 (= H279)
- binding 1-deoxy-1-[7,8-dimethyl-2,4-dioxo-5-(phenylacetyl)-1,3,4,5-tetrahydrobenzo[g]pteridin-10(2H)-yl]-5-O-phosphono-D-ribitol: L24 (= L29), P76 (= P82), V77 (= V83), A78 (≠ G84), Q125 (= Q132), F127 (≠ Y134), T153 (= T160), M159 (≠ D166), F182 (≠ M225), K204 (= K255), H228 (= H279), G229 (≠ S280), R231 (= R282), D259 (= D310), G261 (= G312), R263 (≠ E314), G282 (= G333), R283 (= R334)
- binding magnesium ion: D259 (= D310), G260 (≠ S311), I262 (= I313), L280 (≠ M331)
5zztA The crystal structure of mandelate oxidase with 3,3-difluoro-2- hydroxy-3-phenylpropionic acid (see paper)
32% identity, 95% coverage: 7:375/389 of query aligns to 1:323/331 of 5zztA
- active site: Y126 (= Y134), D154 (= D162), H227 (= H279)
- binding (2R)-3,3-difluoro-2-hydroxy-3-phenylpropanoic acid: F22 (≠ Y28), Y126 (= Y134), M158 (≠ D166), R161 (= R169), H227 (= H279), R230 (= R282)
- binding flavin mononucleotide: P75 (= P82), V76 (= V83), A77 (≠ G84), Q124 (= Q132), Y126 (= Y134), T152 (= T160), K203 (= K255), H227 (= H279), G228 (≠ S280), R230 (= R282), D258 (= D310), G259 (≠ S311), G260 (= G312), R262 (≠ E314), G281 (= G333), R282 (= R334)
6a08A The crystal structure of mandelate oxidase with benzoyl-formic acid (see paper)
32% identity, 95% coverage: 6:375/389 of query aligns to 1:326/335 of 6a08A
- active site: Y127 (= Y134), D155 (= D162), H230 (= H279)
- binding benzoyl-formic acid: A78 (≠ G84), Y127 (= Y134), V156 (= V163), W158 (≠ A165), M159 (≠ D166), M159 (≠ D166), F184 (≠ H227), H230 (= H279), R233 (= R282)
- binding flavin mononucleotide: P76 (= P82), V77 (= V83), A78 (≠ G84), Q125 (= Q132), Y127 (= Y134), T153 (= T160), K206 (= K255), H230 (= H279), G231 (≠ S280), R233 (= R282), D261 (= D310), G263 (= G312), R265 (≠ E314), G284 (= G333), R285 (= R334)
- binding magnesium ion: D261 (= D310), G262 (≠ S311), I264 (= I313), L282 (≠ M331)
6a1hA Mandelate oxidase mutant-y128f with 5-deazariboflavin mononucleotide (see paper)
32% identity, 95% coverage: 7:375/389 of query aligns to 1:323/332 of 6a1hA
- active site: F126 (≠ Y134), D154 (= D162), H227 (= H279)
- binding 1-deoxy-1-(7,8-dimethyl-2,4-dioxo-3,4-dihydropyrimido[4,5-b]quinolin-10(2H)-yl)-5-O-phosphono-D-ribitol: A74 (= A81), P75 (= P82), V76 (= V83), A77 (≠ G84), Q124 (= Q132), F126 (≠ Y134), T152 (= T160), K203 (= K255), H227 (= H279), R230 (= R282), D258 (= D310), G260 (= G312), R262 (≠ E314), G281 (= G333), R282 (= R334)
6a0oA Mandelate oxidase mutant-y128f with benzaldehyde (see paper)
32% identity, 95% coverage: 7:375/389 of query aligns to 1:323/332 of 6a0oA
- active site: F126 (≠ Y134), D154 (= D162), H227 (= H279)
- binding flavin mononucleotide: P75 (= P82), V76 (= V83), A77 (≠ G84), Q124 (= Q132), F126 (≠ Y134), T152 (= T160), K203 (= K255), H227 (= H279), G228 (≠ S280), R230 (= R282), D258 (= D310), G260 (= G312), R262 (≠ E314), G281 (= G333), R282 (= R334)
- binding benzaldehyde: F22 (≠ Y28), R42 (≠ A49), V43 (≠ I50), F126 (≠ Y134), V155 (= V163), M158 (≠ D166), R161 (= R169), F181 (≠ M225), H227 (= H279)
Sites not aligning to the query:
6a1aA Mandelate oxidase mutant-y128f with 4-hydroxymandelic acid (see paper)
32% identity, 95% coverage: 6:375/389 of query aligns to 1:326/335 of 6a1aA
- active site: F127 (≠ Y134), D155 (= D162), H230 (= H279)
- binding flavin mononucleotide: P76 (= P82), V77 (= V83), A78 (≠ G84), Q125 (= Q132), F127 (≠ Y134), T153 (= T160), K206 (= K255), H230 (= H279), R233 (= R282), D261 (= D310), G263 (= G312), R265 (≠ E314), G284 (= G333), R285 (= R334)
- binding (2S)-hydroxy(4-hydroxyphenyl)ethanoic acid: A40 (= A46), R43 (≠ A49), L107 (≠ V113), F127 (≠ Y134), V156 (= V163), M159 (≠ D166), R162 (= R169), F184 (≠ H227), H230 (= H279), R233 (= R282), E243 (≠ T292)
Sites not aligning to the query:
6a1wA Mandelate oxidase with the enoyl fmn epoxide adduct (see paper)
32% identity, 95% coverage: 6:375/389 of query aligns to 1:325/334 of 6a1wA
- active site: Y127 (= Y134), D155 (= D162), H229 (= H279)
- binding 1-[(1aR,11R)-11-acetyl-8,9-dimethyl-2,4-dioxo-3,4-dihydrobenzo[g]oxazireno[3,2-e]pteridin-11-ium-6(2H)-yl]-1-deoxy-5-O-phosphono-D-ribitol: L24 (= L29), A75 (= A81), P76 (= P82), V77 (= V83), Q125 (= Q132), Y127 (= Y134), T153 (= T160), R162 (= R169), K205 (= K255), H229 (= H279), R232 (= R282), D260 (= D310), G262 (= G312), R264 (≠ E314), G283 (= G333), R284 (= R334)
- binding magnesium ion: D260 (= D310), G261 (≠ S311), I263 (= I313), L281 (≠ M331)
6a00A The crystal structure of mandelate oxidase with (s)-2-phenylpropionate (see paper)
32% identity, 95% coverage: 6:375/389 of query aligns to 1:325/334 of 6a00A
- active site: Y127 (= Y134), D155 (= D162), H229 (= H279)
- binding (2~{S})-2-phenylpropanoic acid: L107 (≠ V113), Y127 (= Y134), M159 (≠ D166), H229 (= H279), R232 (= R282)
- binding flavin mononucleotide: P76 (= P82), V77 (= V83), A78 (≠ G84), Q125 (= Q132), Y127 (= Y134), T153 (= T160), K205 (= K255), H229 (= H279), R232 (= R282), D260 (= D310), G262 (= G312), R264 (≠ E314), G283 (= G333), R284 (= R334)
- binding magnesium ion: D260 (= D310), G261 (≠ S311), I263 (= I313), L281 (≠ M331)
5zzrA The crystal structure of mandelate oxidase with (s)-mandelic acid (see paper)
32% identity, 95% coverage: 6:375/389 of query aligns to 1:325/334 of 5zzrA
- active site: Y127 (= Y134), D155 (= D162), H229 (= H279)
- binding flavin mononucleotide: P76 (= P82), V77 (= V83), A78 (≠ G84), Q125 (= Q132), Y127 (= Y134), T153 (= T160), K205 (= K255), H229 (= H279), R232 (= R282), D260 (= D310), G262 (= G312), R264 (≠ E314), G283 (= G333), R284 (= R334)
- binding (s)-mandelic acid: V44 (≠ I50), L107 (≠ V113), Y127 (= Y134), M159 (≠ D166), R162 (= R169), H229 (= H279), R232 (= R282), E242 (≠ T292)
Sites not aligning to the query:
6a1bA Mandelate oxidase mutant-y128f with 3,3,3-trifluoro-2,2- dihydroxypropanoic acid (see paper)
32% identity, 95% coverage: 6:375/389 of query aligns to 1:325/334 of 6a1bA
- active site: F127 (≠ Y134), D155 (= D162), H229 (= H279)
- binding 3,3,3-trifluoro-2,2-dihydroxypropanoic acid: F127 (≠ Y134), M159 (≠ D166), R162 (= R169), H229 (= H279), R232 (= R282)
- binding flavin mononucleotide: P76 (= P82), V77 (= V83), A78 (≠ G84), Q125 (= Q132), F127 (≠ Y134), T153 (= T160), K205 (= K255), H229 (= H279), R232 (= R282), D260 (= D310), G261 (≠ S311), G262 (= G312), R264 (≠ E314), G283 (= G333), R284 (= R334)
6a11A Mandelate oxidase mutant-y128f with phenylpyruvic acid (see paper)
32% identity, 95% coverage: 6:375/389 of query aligns to 1:325/334 of 6a11A
- active site: F127 (≠ Y134), D155 (= D162), H229 (= H279)
- binding flavin mononucleotide: P76 (= P82), V77 (= V83), A78 (≠ G84), Q125 (= Q132), F127 (≠ Y134), T153 (= T160), K205 (= K255), H229 (= H279), R232 (= R282), D260 (= D310), G262 (= G312), R264 (≠ E314), G283 (= G333), R284 (= R334)
- binding 3-phenylpyruvic acid: Y79 (≠ M85), M159 (≠ D166), R162 (= R169), H229 (= H279), R232 (= R282)
6a01A The crystal structure of mandelate oxidase y128f with 3,3-difluoro-2, 2-dihydroxy-3-phenylpropionic acid (see paper)
31% identity, 95% coverage: 7:375/389 of query aligns to 1:325/333 of 6a01A
- active site: F126 (≠ Y134), D154 (= D162), H229 (= H279)
- binding 3,3-difluoro-2,2-dihydroxy-3-phenylpropanoic acid: F22 (≠ Y28), F126 (≠ Y134), M158 (≠ D166), R161 (= R169), H229 (= H279), R232 (= R282)
- binding flavin mononucleotide: P75 (= P82), V76 (= V83), A77 (≠ G84), Q124 (= Q132), F126 (≠ Y134), T152 (= T160), K205 (= K255), H229 (= H279), R232 (= R282), D260 (= D310), G262 (= G312), R264 (≠ E314), G283 (= G333), R284 (= R334)
Q8Z0C8 L-lactate oxidase; LOX; Glyoxylate oxidase; No-LOX; EC 1.1.3.-; EC 1.2.3.5 from Nostoc sp. (strain PCC 7120 / SAG 25.82 / UTEX 2576) (see paper)
33% identity, 93% coverage: 12:374/389 of query aligns to 12:358/365 of Q8Z0C8
- M82 (≠ V83) mutation to T: Increases oxidation activity with both L-lactate and glycolate. Shows a 6-fold decrease in the L-lactate/glycolate oxidase activity ratio.
- L112 (≠ V113) mutation to W: Impairs oxidation of L-lactate. Shows a 2-fold decrease in the L-lactate/glycolate oxidase activity ratio.
- F212 (≠ M225) mutation to V: Impairs oxidation of L-lactate. Shows a 27-fold decrease in the L-lactate/glycolate oxidase activity ratio.
2a85A Crystal structure of the g81a mutant of the active chimera of (s)- mandelate dehydrogenase in complex with its substrate 2- hydroxyoctanoate (see paper)
30% identity, 90% coverage: 10:359/389 of query aligns to 5:330/353 of 2a85A
- active site: S105 (= S111), Y128 (= Y134), T153 (= T160), D155 (= D162), K228 (= K255), H252 (= H279)
- binding flavin mononucleotide: Y23 (= Y28), P76 (= P82), T77 (≠ V83), A78 (≠ G84), S105 (= S111), Q126 (= Q132), Y128 (= Y134), T153 (= T160), K228 (= K255), H252 (= H279), G253 (≠ S280), R255 (= R282), D281 (= D310), S282 (= S311), G283 (= G312), R285 (≠ E314), G304 (= G333), R305 (= R334)
- binding (2s)-2-hydroxyoctanoic acid: Y128 (= Y134), N159 (≠ D166), G160 (≠ S167), R162 (= R169), H252 (= H279), R255 (= R282)
2a7pA Crystal structure of the g81a mutant of the active chimera of (s)- mandelate dehydrogenase in complex with its substrate 3-indolelactate (see paper)
30% identity, 90% coverage: 10:359/389 of query aligns to 5:330/353 of 2a7pA
- active site: S105 (= S111), Y128 (= Y134), T153 (= T160), D155 (= D162), K228 (= K255), H252 (= H279)
- binding 3-(indol-3-yl) lactate: Y128 (= Y134), R162 (= R169), H252 (= H279)
- binding flavin mononucleotide: Y23 (= Y28), P76 (= P82), T77 (≠ V83), A78 (≠ G84), S105 (= S111), Q126 (= Q132), Y128 (= Y134), T153 (= T160), K228 (= K255), H252 (= H279), G253 (≠ S280), R255 (= R282), D281 (= D310), S282 (= S311), G283 (= G312), R285 (≠ E314), G304 (= G333), R305 (= R334)
P0DUR7 FMN-dependent alpha-hydroxy acid dehydrogenase qulF; Quinolactacin A2 biosynthesis cluster protein F; EC 1.13.12.- from Penicillium citrinum (see paper)
30% identity, 97% coverage: 5:383/389 of query aligns to 27:394/402 of P0DUR7
- H289 (= H279) mutation to A: Blocks the formatin of 2-aminobenzoylacetamide.
Query Sequence
>3609095 FitnessBrowser__Dino:3609095
MDFDTTHPAISDLRRAARRRIPGFVFEYLDSATGDREIGVQTTRAALDAIHLLPGILHGQ
ITPELETPLLGQTYARPFGIAPVGMSGLIWPDAERLLAAEAATARIPYGLSTVATQTPER
VGPVAGEMGWFQLYPPADPGIRDDIMARARASGFGTLVLTVDVPADSRRERQRRANLTIP
PKITPRMIFQMILHPTWALGMARHGTPSLKLAESYVEKTGAASYMAHAGKAIRGAPDWAY
LDAVRAGWDGPLVVKGVLRPEDAVRLRAAGVDAIWVSDHSARQFEGGPGAITQLPAIRRA
VGPDCPVIYDSGIEGGLDILRAVGLGADFVMLGRAWHFALAGLGPAGVRHLIHILTQDLV
TNMQICGIAKLADFRDQLATHSYGVSGQA
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