SitesBLAST
Comparing GFF927 FitnessBrowser__Phaeo:GFF927 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)
35% identity, 92% coverage: 6:375/401 of query aligns to 1:367/393 of P20932
- PTG 79:81 (≠ PVG 84:86) binding
- G81 (= G86) 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 (= S113) binding
- Q129 (= Q134) binding
- T156 (= T162) binding
- K250 (= K258) binding
- DSGFR 303:307 (≠ DSGIE 311:315) binding
- GR 326:327 (= GR 334:335) binding
6bfgA Crystal structure of monotopic membrane protein (s)-mandelate dehydrogenase (see paper)
35% identity, 92% coverage: 8:375/401 of query aligns to 1:365/373 of 6bfgA
- active site: Y129 (= Y136), D156 (= D164), H272 (= H282)
- binding flavin mononucleotide: Y24 (= Y31), P77 (= P84), T78 (≠ V85), G79 (= G86), Q127 (= Q134), Y129 (= Y136), T154 (= T162), K248 (= K258), H272 (= H282), G273 (≠ A283), R275 (= R285), D301 (= D311), S302 (= S312), G303 (= G313), R305 (≠ E315), G324 (= G334), R325 (= R335)
1huvA Crystal structure of a soluble mutant of the membrane-associated (s)- mandelate dehydrogenase from pseudomonas putida at 2.15a resolution (see paper)
34% identity, 91% coverage: 13:375/401 of query aligns to 5:341/349 of 1huvA
- active site: S105 (= S113), Y128 (= Y136), T153 (= T162), D155 (= D164), K224 (= K258), H248 (= H282)
- binding flavin mononucleotide: Y23 (= Y31), P76 (= P84), T77 (≠ V85), G78 (= G86), S105 (= S113), Q126 (= Q134), Y128 (= Y136), T153 (= T162), K224 (= K258), H248 (= H282), G249 (≠ A283), R251 (= R285), D277 (= D311), S278 (= S312), G279 (= G313), R281 (≠ E315), G300 (= G334), R301 (= R335)
2a85A Crystal structure of the g81a mutant of the active chimera of (s)- mandelate dehydrogenase in complex with its substrate 2- hydroxyoctanoate (see paper)
34% identity, 91% coverage: 13:375/401 of query aligns to 5:345/353 of 2a85A
- active site: S105 (= S113), Y128 (= Y136), T153 (= T162), D155 (= D164), K228 (= K258), H252 (= H282)
- binding flavin mononucleotide: Y23 (= Y31), P76 (= P84), T77 (≠ V85), A78 (≠ G86), S105 (= S113), Q126 (= Q134), Y128 (= Y136), T153 (= T162), K228 (= K258), H252 (= H282), G253 (≠ A283), R255 (= R285), D281 (= D311), S282 (= S312), G283 (= G313), R285 (≠ E315), G304 (= G334), R305 (= R335)
- binding (2s)-2-hydroxyoctanoic acid: Y128 (= Y136), N159 (≠ A168), G160 (≠ S169), R162 (= R171), H252 (= H282), R255 (= R285)
2a7pA Crystal structure of the g81a mutant of the active chimera of (s)- mandelate dehydrogenase in complex with its substrate 3-indolelactate (see paper)
34% identity, 91% coverage: 13:375/401 of query aligns to 5:345/353 of 2a7pA
- active site: S105 (= S113), Y128 (= Y136), T153 (= T162), D155 (= D164), K228 (= K258), H252 (= H282)
- binding 3-(indol-3-yl) lactate: Y128 (= Y136), R162 (= R171), H252 (= H282)
- binding flavin mononucleotide: Y23 (= Y31), P76 (= P84), T77 (≠ V85), A78 (≠ G86), S105 (= S113), Q126 (= Q134), Y128 (= Y136), T153 (= T162), K228 (= K258), H252 (= H282), G253 (≠ A283), R255 (= R285), D281 (= D311), S282 (= S312), G283 (= G313), R285 (≠ E315), G304 (= G334), R305 (= R335)
5zzqA The crystal structure of mandelate oxidase with (s)-4-hydroxymandelic acid (see paper)
36% identity, 92% coverage: 10:377/401 of query aligns to 1:347/355 of 5zzqA
- active site: Y126 (= Y136), D154 (= D164), H250 (= H282)
- binding flavin mononucleotide: P75 (= P84), V76 (= V85), A77 (≠ G86), Q124 (= Q134), Y126 (= Y136), T152 (= T162), K226 (= K258), H250 (= H282), R253 (= R285), D281 (= D311), G283 (= G313), R285 (≠ E315), G304 (= G334), R305 (= R335)
- binding (2S)-hydroxy(4-hydroxyphenyl)ethanoic acid: L106 (≠ V115), Y126 (= Y136), M158 (≠ A168), R161 (= R171), T200 (= T228), F204 (≠ T237), H250 (= H282), R253 (= R285)
6a24A The crystal structure of mandelate oxidase with 3-fluoropyruvate (see paper)
36% identity, 92% coverage: 10:377/401 of query aligns to 1:347/354 of 6a24A
- active site: Y126 (= Y136), D154 (= D164), H250 (= H282)
- binding flavin mononucleotide: P75 (= P84), V76 (= V85), A77 (≠ G86), Q124 (= Q134), Y126 (= Y136), T152 (= T162), K226 (= K258), H250 (= H282), G251 (≠ A283), R253 (= R285), D281 (= D311), G282 (≠ S312), G283 (= G313), R285 (≠ E315), G304 (= G334), R305 (= R335)
- binding pyruvic acid: R161 (= R171), H250 (= H282), R253 (= R285)
5zbmB Structure of glycolate oxidase containing fmn from nicotiana benthamiana (see paper)
34% identity, 89% coverage: 20:377/401 of query aligns to 12:345/353 of 5zbmB
- active site: Y128 (= Y136), D156 (= D164), H248 (= H282)
- binding flavin mononucleotide: Y23 (= Y31), Y24 (≠ L32), P76 (= P84), T77 (≠ V85), W107 (≠ V115), Q126 (= Q134), Y128 (= Y136), T154 (= T162), K224 (= K258), H248 (= H282), G249 (≠ A283), R251 (= R285), D279 (= D311), G280 (≠ S312), R283 (≠ E315), G302 (= G334), R303 (= R335)
6a1wA Mandelate oxidase with the enoyl fmn epoxide adduct (see paper)
34% identity, 92% coverage: 10:377/401 of query aligns to 2:326/334 of 6a1wA
- active site: Y127 (= Y136), D155 (= D164), H229 (= H282)
- 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 (= L32), A75 (= A83), P76 (= P84), V77 (= V85), Q125 (= Q134), Y127 (= Y136), T153 (= T162), R162 (= R171), K205 (= K258), H229 (= H282), R232 (= R285), D260 (= D311), G262 (= G313), R264 (≠ E315), G283 (= G334), R284 (= R335)
- binding magnesium ion: D260 (= D311), G261 (≠ S312), I263 (= I314), L281 (≠ M332)
6a00A The crystal structure of mandelate oxidase with (s)-2-phenylpropionate (see paper)
34% identity, 92% coverage: 10:377/401 of query aligns to 2:326/334 of 6a00A
- active site: Y127 (= Y136), D155 (= D164), H229 (= H282)
- binding (2~{S})-2-phenylpropanoic acid: L107 (≠ V115), Y127 (= Y136), M159 (≠ A168), H229 (= H282), R232 (= R285)
- binding flavin mononucleotide: P76 (= P84), V77 (= V85), A78 (≠ G86), Q125 (= Q134), Y127 (= Y136), T153 (= T162), K205 (= K258), H229 (= H282), R232 (= R285), D260 (= D311), G262 (= G313), R264 (≠ E315), G283 (= G334), R284 (= R335)
- binding magnesium ion: D260 (= D311), G261 (≠ S312), I263 (= I314), L281 (≠ M332)
5zzrA The crystal structure of mandelate oxidase with (s)-mandelic acid (see paper)
34% identity, 92% coverage: 10:377/401 of query aligns to 2:326/334 of 5zzrA
- active site: Y127 (= Y136), D155 (= D164), H229 (= H282)
- binding flavin mononucleotide: P76 (= P84), V77 (= V85), A78 (≠ G86), Q125 (= Q134), Y127 (= Y136), T153 (= T162), K205 (= K258), H229 (= H282), R232 (= R285), D260 (= D311), G262 (= G313), R264 (≠ E315), G283 (= G334), R284 (= R335)
- binding (s)-mandelic acid: V44 (≠ L52), L107 (≠ V115), Y127 (= Y136), M159 (≠ A168), R162 (= R171), H229 (= H282), R232 (= R285), E242 (= E295)
Sites not aligning to the query:
6a08A The crystal structure of mandelate oxidase with benzoyl-formic acid (see paper)
34% identity, 92% coverage: 10:377/401 of query aligns to 2:327/335 of 6a08A
- active site: Y127 (= Y136), D155 (= D164), H230 (= H282)
- binding benzoyl-formic acid: A78 (≠ G86), Y127 (= Y136), V156 (= V165), W158 (≠ V167), M159 (≠ A168), M159 (≠ A168), F184 (≠ V193), H230 (= H282), R233 (= R285)
- binding flavin mononucleotide: P76 (= P84), V77 (= V85), A78 (≠ G86), Q125 (= Q134), Y127 (= Y136), T153 (= T162), K206 (= K258), H230 (= H282), G231 (≠ A283), R233 (= R285), D261 (= D311), G263 (= G313), R265 (≠ E315), G284 (= G334), R285 (= R335)
- binding magnesium ion: D261 (= D311), G262 (≠ S312), I264 (= I314), L282 (≠ M332)
6a21A Mandelate oxidase mutant-y128f with the n5-malonyl-fmn adduct (see paper)
34% identity, 92% coverage: 10:377/401 of query aligns to 1:325/333 of 6a21A
- active site: F126 (≠ Y136), D154 (= D164), H228 (= H282)
- binding 3-[7,8-dimethyl-2,4-bis(oxidanylidene)-10-[(2S,3S,4R)-2,3,4-tris(oxidanyl)-5-phosphonooxy-pentyl]-1H-benzo[g]pteridin-5-yl]-3-oxidanylidene-propanoic acid: P75 (= P84), V76 (= V85), A77 (≠ G86), Q124 (= Q134), F126 (≠ Y136), T152 (= T162), M158 (≠ A168), K204 (= K258), H228 (= H282), R231 (= R285), D259 (= D311), G261 (= G313), R263 (≠ E315), G282 (= G334), R283 (= R335)
P05414 Glycolate oxidase; GAO; GOX; Short chain alpha-hydroxy acid oxidase; EC 1.1.3.15 from Spinacia oleracea (Spinach) (see 4 papers)
33% identity, 89% coverage: 20:377/401 of query aligns to 13:351/369 of P05414
- Y24 (= Y31) mutation to F: 10-fold decrease in affinity for glycolate.
- PTA 77:79 (≠ PVG 84:86) binding
- S106 (= S113) binding
- W108 (≠ V115) mutation to S: 100-fold decrease in affinity for glycolate and 500-fold decrease in activity.
- QLY 127:129 (= QLY 134:136) binding
- T155 (= T162) binding
- K230 (= K258) binding
- S252 (= S280) binding
- DGGVR 285:289 (≠ DSGIE 311:315) binding
- GR 308:309 (= GR 334:335) binding
Sites not aligning to the query:
- 1 modified: N-acetylmethionine
6a36A Mandelate oxidase mutant-y128f with the 3-fluoropyruvic acid fmn adduct (see paper)
34% identity, 92% coverage: 10:377/401 of query aligns to 1:325/331 of 6a36A
- active site: F126 (≠ Y136), D154 (= D164), H228 (= H282)
- binding 1-{5-[(3S)-3-carboxy-4-fluoro-3-hydroxybutanoyl]-7,8-dimethyl-2,4-dioxo-1,3,4,5-tetrahydrobenzo[g]pteridin-10(2H)-yl}-1-deoxy-5-O-phosphono-D-ribitol: L23 (= L32), P75 (= P84), V76 (= V85), A77 (≠ G86), Q124 (= Q134), F126 (≠ Y136), T152 (= T162), M158 (≠ A168), R161 (= R171), K204 (= K258), H228 (= H282), R231 (= R285), D259 (= D311), G260 (≠ S312), G261 (= G313), R263 (≠ E315), G282 (= G334), R283 (= R335)
- binding 1-deoxy-1-{5-[(1S)-2-fluoro-1-hydroxyethyl]-7,8-dimethyl-2,4-dioxo-1,3,4,5-tetrahydrobenzo[g]pteridin-10(2H)-yl}-5-O-phosphono-D-ribitol: P75 (= P84), V76 (= V85), Q124 (= Q134), F126 (≠ Y136), T152 (= T162), K204 (= K258), H228 (= H282), R231 (= R285), D259 (= D311), G260 (≠ S312), G261 (= G313), R263 (≠ E315), G282 (= G334), R283 (= R335)
6a1nA Mandelate oxidase mutant-y128f with (2r,3s)-3-fluoro-2-hydroxy-3- phenylpropanoic acid (see paper)
34% identity, 92% coverage: 10:377/401 of query aligns to 1:325/332 of 6a1nA
- active site: F126 (≠ Y136), D154 (= D164), H228 (= H282)
- binding (2R,3S)-3-fluoro-2-hydroxy-3-phenylpropanoic acid: R42 (≠ Q51), V43 (≠ L52), A77 (≠ G86), Y78 (≠ M87), L106 (≠ V115), M158 (≠ A168), R161 (= R171), H228 (= H282), R231 (= R285), E241 (= E295)
- binding flavin mononucleotide: P75 (= P84), V76 (= V85), A77 (≠ G86), Q124 (= Q134), F126 (≠ Y136), T152 (= T162), K204 (= K258), H228 (= H282), G229 (≠ A283), R231 (= R285), D259 (= D311), G260 (≠ S312), G261 (= G313), R263 (≠ E315), G282 (= G334), R283 (= R335)
Sites not aligning to the query:
6a23A Mandelate oxidase mutant-y128f with the n5-benzyl-fmn adduct (see paper)
34% identity, 92% coverage: 10:377/401 of query aligns to 1:325/333 of 6a23A
- active site: F126 (≠ Y136), D154 (= D164), H228 (= H282)
- binding benzoyl-formic acid: F126 (≠ Y136), V155 (= V165), W157 (≠ V167), M158 (≠ A168), F182 (≠ M195)
- binding 1-[5-(benzenecarbonyl)-7,8-dimethyl-2,4-dioxo-1,3,4,5-tetrahydrobenzo[g]pteridin-10(2H)-yl]-1-deoxy-5-O-phosphono-D-ribitol: L23 (= L32), P75 (= P84), V76 (= V85), A77 (≠ G86), L106 (≠ V115), Q124 (= Q134), F126 (≠ Y136), T152 (= T162), M158 (≠ A168), K204 (= K258), H228 (= H282), R231 (= R285), D259 (= D311), G261 (= G313), R263 (≠ E315), G282 (= G334), R283 (= R335)
- binding magnesium ion: D259 (= D311), G260 (≠ S312), I262 (= I314)
5zztA The crystal structure of mandelate oxidase with 3,3-difluoro-2- hydroxy-3-phenylpropionic acid (see paper)
34% identity, 92% coverage: 10:377/401 of query aligns to 1:324/331 of 5zztA
- active site: Y126 (= Y136), D154 (= D164), H227 (= H282)
- binding (2R)-3,3-difluoro-2-hydroxy-3-phenylpropanoic acid: F22 (≠ Y31), Y126 (= Y136), M158 (≠ A168), R161 (= R171), H227 (= H282), R230 (= R285)
- binding flavin mononucleotide: P75 (= P84), V76 (= V85), A77 (≠ G86), Q124 (= Q134), Y126 (= Y136), T152 (= T162), K203 (= K258), H227 (= H282), G228 (≠ A283), R230 (= R285), D258 (= D311), G259 (≠ S312), G260 (= G313), R262 (≠ E315), G281 (= G334), R282 (= R335)
6a1rA Mandelate oxidase mutant-y128f with the n5-phenylacetyl-fmn adduct (see paper)
34% identity, 92% coverage: 10:377/401 of query aligns to 2:325/332 of 6a1rA
- active site: F127 (≠ Y136), D155 (= D164), H228 (= H282)
- 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 (= L32), P76 (= P84), V77 (= V85), A78 (≠ G86), Q125 (= Q134), F127 (≠ Y136), T153 (= T162), M159 (≠ A168), F182 (≠ V218), K204 (= K258), H228 (= H282), G229 (≠ A283), R231 (= R285), D259 (= D311), G261 (= G313), R263 (≠ E315), G282 (= G334), R283 (= R335)
- binding magnesium ion: D259 (= D311), G260 (≠ S312), I262 (= I314), L280 (≠ M332)
1al7A Three-dimensional structures of glycolate oxidase with bound active- site inhibitors (see paper)
33% identity, 89% coverage: 20:377/401 of query aligns to 13:342/350 of 1al7A
- active site: S106 (= S113), Y129 (= Y136), T155 (= T162), D157 (= D164), K221 (= K258), H245 (= H282)
- binding flavin mononucleotide: Y24 (= Y31), Y25 (≠ L32), P77 (= P84), T78 (≠ V85), A79 (≠ G86), S106 (= S113), Q127 (= Q134), T155 (= T162), K221 (= K258), H245 (= H282), R248 (= R285), D276 (= D311), G277 (≠ S312), R280 (≠ E315), G299 (= G334), R300 (= R335)
- binding 4-carboxy-5-(1-pentyl)hexylsulfanyl-1,2,3-triazole: Y24 (= Y31), W108 (≠ V115), Y129 (= Y136), R164 (= R171), F172 (≠ L179), I198 (≠ L235), H245 (= H282), R248 (= R285)
Query Sequence
>GFF927 FitnessBrowser__Phaeo:GFF927
MRNMDLHQRYPALSDLRQRARRRLPRFVWEYLDSGTGTEATKARNRAALDQLGFAPSILH
GPQTPDLSRRFLGIDRPLPFGVAPVGMSGLIWPDAERLLARCAAAQGLPYCLSTVASQSP
EDLVDDLGAAPWFQLYPPKDPDIRRDLLARAKAAGFAGLVLTVDVPVASRRERQTRSGLT
QPPRLTPRLLAQVAMRPAWAVGMARRGLPHMKTLDTYVSGAGASLSSTAHVGYLLRTSPD
WDYVQWLRDHWDGPLIIKGVMRAEDAAPLEAIGADALWVSNHAGRQFDAAPSTIEALPGI
RAATRLPLIFDSGIESGLDILRALALGADYVMLGRAFHFALAALGSRGPDHLVDILRKDL
DANMGQLGLETLSALPRPLGLASFANPFTTDRSDTDINAPP
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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