SitesBLAST
Comparing Ac3H11_1767 FitnessBrowser__acidovorax_3H11:Ac3H11_1767 to proteins with known functional sites using BLASTp with E ≤ 0.001.
Or try Sites on a Tree, PaperBLAST, Conserved Domains, or compare to all protein structures
Found 20 (the maximum) hits to proteins with known functional sites (download)
6bfgA Crystal structure of monotopic membrane protein (s)-mandelate dehydrogenase (see paper)
38% identity, 90% coverage: 38:414/419 of query aligns to 1:370/373 of 6bfgA
- active site: Y129 (= Y165), D156 (= D193), H272 (= H314)
- binding flavin mononucleotide: Y24 (= Y61), P77 (= P114), T78 (≠ M115), G79 (= G116), Q127 (= Q163), Y129 (= Y165), T154 (= T191), K248 (= K290), H272 (= H314), G273 (= G315), R275 (= R317), D301 (= D345), S302 (≠ G346), G303 (= G347), R305 (= R349), G324 (= G368), R325 (= R369)
P20932 (S)-mandelate dehydrogenase; MDH; L(+)-mandelate dehydrogenase; EC 1.1.99.31 from Pseudomonas putida (Arthrobacter siderocapsulatus) (see 3 papers)
38% identity, 90% coverage: 38:414/419 of query aligns to 3:372/393 of P20932
- PTG 79:81 (≠ PMG 114:116) binding
- G81 (= G116) 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 (= S143) binding
- Q129 (= Q163) binding
- T156 (= T191) binding
- K250 (= K290) binding
- DSGFR 303:307 (≠ DGGFR 345:349) binding
- GR 326:327 (= GR 368:369) binding
1huvA Crystal structure of a soluble mutant of the membrane-associated (s)- mandelate dehydrogenase from pseudomonas putida at 2.15a resolution (see paper)
38% identity, 89% coverage: 40:414/419 of query aligns to 2:346/349 of 1huvA
- active site: S105 (= S143), Y128 (= Y165), T153 (= T191), D155 (= D193), K224 (= K290), H248 (= H314)
- binding flavin mononucleotide: Y23 (= Y61), P76 (= P114), T77 (≠ M115), G78 (= G116), S105 (= S143), Q126 (= Q163), Y128 (= Y165), T153 (= T191), K224 (= K290), H248 (= H314), G249 (= G315), R251 (= R317), D277 (= D345), S278 (≠ G346), G279 (= G347), R281 (= R349), G300 (= G368), R301 (= R369)
2a85A Crystal structure of the g81a mutant of the active chimera of (s)- mandelate dehydrogenase in complex with its substrate 2- hydroxyoctanoate (see paper)
37% identity, 89% coverage: 40:414/419 of query aligns to 2:350/353 of 2a85A
- active site: S105 (= S143), Y128 (= Y165), T153 (= T191), D155 (= D193), K228 (= K290), H252 (= H314)
- binding flavin mononucleotide: Y23 (= Y61), P76 (= P114), T77 (≠ M115), A78 (≠ G116), S105 (= S143), Q126 (= Q163), Y128 (= Y165), T153 (= T191), K228 (= K290), H252 (= H314), G253 (= G315), R255 (= R317), D281 (= D345), S282 (≠ G346), G283 (= G347), R285 (= R349), G304 (= G368), R305 (= R369)
- binding (2s)-2-hydroxyoctanoic acid: Y128 (= Y165), N159 (≠ S197), G160 (≠ A198), R162 (= R200), H252 (= H314), R255 (= R317)
2a7pA Crystal structure of the g81a mutant of the active chimera of (s)- mandelate dehydrogenase in complex with its substrate 3-indolelactate (see paper)
37% identity, 89% coverage: 40:414/419 of query aligns to 2:350/353 of 2a7pA
- active site: S105 (= S143), Y128 (= Y165), T153 (= T191), D155 (= D193), K228 (= K290), H252 (= H314)
- binding 3-(indol-3-yl) lactate: Y128 (= Y165), R162 (= R200), H252 (= H314)
- binding flavin mononucleotide: Y23 (= Y61), P76 (= P114), T77 (≠ M115), A78 (≠ G116), S105 (= S143), Q126 (= Q163), Y128 (= Y165), T153 (= T191), K228 (= K290), H252 (= H314), G253 (= G315), R255 (= R317), D281 (= D345), S282 (≠ G346), G283 (= G347), R285 (= R349), G304 (= G368), R305 (= R369)
6a24A The crystal structure of mandelate oxidase with 3-fluoropyruvate (see paper)
37% identity, 88% coverage: 41:410/419 of query aligns to 2:343/354 of 6a24A
- active site: Y126 (= Y165), D154 (= D193), H250 (= H314)
- binding flavin mononucleotide: P75 (= P114), V76 (≠ M115), A77 (≠ G116), Q124 (= Q163), Y126 (= Y165), T152 (= T191), K226 (= K290), H250 (= H314), G251 (= G315), R253 (= R317), D281 (= D345), G282 (= G346), G283 (= G347), R285 (= R349), G304 (= G368), R305 (= R369)
- binding pyruvic acid: R161 (= R200), H250 (= H314), R253 (= R317)
5zzqA The crystal structure of mandelate oxidase with (s)-4-hydroxymandelic acid (see paper)
37% identity, 88% coverage: 41:410/419 of query aligns to 2:343/355 of 5zzqA
- active site: Y126 (= Y165), D154 (= D193), H250 (= H314)
- binding flavin mononucleotide: P75 (= P114), V76 (≠ M115), A77 (≠ G116), Q124 (= Q163), Y126 (= Y165), T152 (= T191), K226 (= K290), H250 (= H314), R253 (= R317), D281 (= D345), G283 (= G347), R285 (= R349), G304 (= G368), R305 (= R369)
- binding (2S)-hydroxy(4-hydroxyphenyl)ethanoic acid: L106 (≠ T145), Y126 (= Y165), M158 (≠ S197), R161 (= R200), T200 (≠ V261), F204 (= F265), H250 (= H314), R253 (= R317)
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)
37% identity, 88% coverage: 41:409/419 of query aligns to 8:358/365 of Q8Z0C8
- M82 (= M115) 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 (≠ T145) mutation to W: Impairs oxidation of L-lactate. Shows a 2-fold decrease in the L-lactate/glycolate oxidase activity ratio.
- F212 (≠ G253) mutation to V: Impairs oxidation of L-lactate. Shows a 27-fold decrease in the L-lactate/glycolate oxidase activity ratio.
6a1wA Mandelate oxidase with the enoyl fmn epoxide adduct (see paper)
37% identity, 88% coverage: 41:410/419 of query aligns to 3:322/334 of 6a1wA
- active site: Y127 (= Y165), D155 (= D193), H229 (= H314)
- 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 (≠ I62), A75 (= A113), P76 (= P114), V77 (≠ M115), Q125 (= Q163), Y127 (= Y165), T153 (= T191), R162 (= R200), K205 (= K290), H229 (= H314), R232 (= R317), D260 (= D345), G262 (= G347), R264 (= R349), G283 (= G368), R284 (= R369)
- binding magnesium ion: D260 (= D345), G261 (= G346), I263 (≠ F348), L281 (= L366)
6a0bA The crystal structure of mandelate oxidase mutant y128f with (r)-3,3, 3-trifluoro-2-hydroxy-propionic acid (see paper)
37% identity, 88% coverage: 41:410/419 of query aligns to 2:321/332 of 6a0bA
- active site: F126 (≠ Y165), D154 (= D193), H228 (= H314)
- binding (2R)-3,3,3-trifluoro-2-hydroxypropanoic acid: F126 (≠ Y165), R161 (= R200), H228 (= H314), R231 (= R317)
- binding flavin mononucleotide: P75 (= P114), V76 (≠ M115), A77 (≠ G116), C104 (≠ S143), Q124 (= Q163), F126 (≠ Y165), T152 (= T191), K204 (= K290), H228 (= H314), R231 (= R317), D259 (= D345), G261 (= G347), R263 (= R349), G282 (= G368), R283 (= R369)
6a36A Mandelate oxidase mutant-y128f with the 3-fluoropyruvic acid fmn adduct (see paper)
37% identity, 88% coverage: 41:410/419 of query aligns to 2:321/331 of 6a36A
- active site: F126 (≠ Y165), D154 (= D193), H228 (= H314)
- 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 (≠ I62), P75 (= P114), V76 (≠ M115), A77 (≠ G116), Q124 (= Q163), F126 (≠ Y165), T152 (= T191), M158 (≠ S197), R161 (= R200), K204 (= K290), H228 (= H314), R231 (= R317), D259 (= D345), G260 (= G346), G261 (= G347), R263 (= R349), G282 (= G368), R283 (= R369)
- 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 (= P114), V76 (≠ M115), Q124 (= Q163), F126 (≠ Y165), T152 (= T191), K204 (= K290), H228 (= H314), R231 (= R317), D259 (= D345), G260 (= G346), G261 (= G347), R263 (= R349), G282 (= G368), R283 (= R369)
6a1bA Mandelate oxidase mutant-y128f with 3,3,3-trifluoro-2,2- dihydroxypropanoic acid (see paper)
37% identity, 88% coverage: 41:410/419 of query aligns to 3:322/334 of 6a1bA
- active site: F127 (≠ Y165), D155 (= D193), H229 (= H314)
- binding 3,3,3-trifluoro-2,2-dihydroxypropanoic acid: F127 (≠ Y165), M159 (≠ S197), R162 (= R200), H229 (= H314), R232 (= R317)
- binding flavin mononucleotide: P76 (= P114), V77 (≠ M115), A78 (≠ G116), Q125 (= Q163), F127 (≠ Y165), T153 (= T191), K205 (= K290), H229 (= H314), R232 (= R317), D260 (= D345), G261 (= G346), G262 (= G347), R264 (= R349), G283 (= G368), R284 (= R369)
6a11A Mandelate oxidase mutant-y128f with phenylpyruvic acid (see paper)
37% identity, 88% coverage: 41:410/419 of query aligns to 3:322/334 of 6a11A
- active site: F127 (≠ Y165), D155 (= D193), H229 (= H314)
- binding flavin mononucleotide: P76 (= P114), V77 (≠ M115), A78 (≠ G116), Q125 (= Q163), F127 (≠ Y165), T153 (= T191), K205 (= K290), H229 (= H314), R232 (= R317), D260 (= D345), G262 (= G347), R264 (= R349), G283 (= G368), R284 (= R369)
- binding 3-phenylpyruvic acid: Y79 (≠ I117), M159 (≠ S197), R162 (= R200), H229 (= H314), R232 (= R317)
6a21A Mandelate oxidase mutant-y128f with the n5-malonyl-fmn adduct (see paper)
37% identity, 88% coverage: 41:410/419 of query aligns to 2:321/333 of 6a21A
- active site: F126 (≠ Y165), D154 (= D193), H228 (= H314)
- 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 (= P114), V76 (≠ M115), A77 (≠ G116), Q124 (= Q163), F126 (≠ Y165), T152 (= T191), M158 (≠ S197), K204 (= K290), H228 (= H314), R231 (= R317), D259 (= D345), G261 (= G347), R263 (= R349), G282 (= G368), R283 (= R369)
6a08A The crystal structure of mandelate oxidase with benzoyl-formic acid (see paper)
36% identity, 88% coverage: 41:410/419 of query aligns to 3:323/335 of 6a08A
- active site: Y127 (= Y165), D155 (= D193), H230 (= H314)
- binding benzoyl-formic acid: A78 (≠ G116), Y127 (= Y165), V156 (≠ I194), W158 (≠ I196), M159 (≠ S197), M159 (≠ S197), F184 (≠ R268), H230 (= H314), R233 (= R317)
- binding flavin mononucleotide: P76 (= P114), V77 (≠ M115), A78 (≠ G116), Q125 (= Q163), Y127 (= Y165), T153 (= T191), K206 (= K290), H230 (= H314), G231 (= G315), R233 (= R317), D261 (= D345), G263 (= G347), R265 (= R349), G284 (= G368), R285 (= R369)
- binding magnesium ion: D261 (= D345), G262 (= G346), I264 (≠ F348), L282 (= L366)
6a0gA The crystal structure of mandelate oxidase mutant y128f with b- phenyllactate (see paper)
36% identity, 88% coverage: 41:410/419 of query aligns to 2:321/331 of 6a0gA
- active site: F126 (≠ Y165), D154 (= D193), H228 (= H314)
- binding flavin mononucleotide: P75 (= P114), V76 (≠ M115), A77 (≠ G116), Q124 (= Q163), F126 (≠ Y165), T152 (= T191), K204 (= K290), H228 (= H314), R231 (= R317), D259 (= D345), R263 (= R349), G282 (= G368), R283 (= R369)
- binding alpha-hydroxy-beta-phenyl-propionic acid: F22 (≠ Y61), V43 (≠ Y82), L106 (≠ T145), M158 (≠ S197), H228 (= H314), R231 (= R317), E241 (≠ R327)
Sites not aligning to the query:
6a1nA Mandelate oxidase mutant-y128f with (2r,3s)-3-fluoro-2-hydroxy-3- phenylpropanoic acid (see paper)
36% identity, 88% coverage: 41:410/419 of query aligns to 2:321/332 of 6a1nA
- active site: F126 (≠ Y165), D154 (= D193), H228 (= H314)
- binding (2R,3S)-3-fluoro-2-hydroxy-3-phenylpropanoic acid: R42 (≠ E81), V43 (≠ Y82), A77 (≠ G116), Y78 (≠ I117), L106 (≠ T145), M158 (≠ S197), R161 (= R200), H228 (= H314), R231 (= R317), E241 (≠ R327)
- binding flavin mononucleotide: P75 (= P114), V76 (≠ M115), A77 (≠ G116), Q124 (= Q163), F126 (≠ Y165), T152 (= T191), K204 (= K290), H228 (= H314), G229 (= G315), R231 (= R317), D259 (= D345), G260 (= G346), G261 (= G347), R263 (= R349), G282 (= G368), R283 (= R369)
Sites not aligning to the query:
6a23A Mandelate oxidase mutant-y128f with the n5-benzyl-fmn adduct (see paper)
36% identity, 88% coverage: 41:410/419 of query aligns to 2:321/333 of 6a23A
- active site: F126 (≠ Y165), D154 (= D193), H228 (= H314)
- binding benzoyl-formic acid: F126 (≠ Y165), V155 (≠ I194), W157 (≠ I196), M158 (≠ S197), F182 (≠ N247)
- 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 (≠ I62), P75 (= P114), V76 (≠ M115), A77 (≠ G116), L106 (≠ T145), Q124 (= Q163), F126 (≠ Y165), T152 (= T191), M158 (≠ S197), K204 (= K290), H228 (= H314), R231 (= R317), D259 (= D345), G261 (= G347), R263 (= R349), G282 (= G368), R283 (= R369)
- binding magnesium ion: D259 (= D345), G260 (= G346), I262 (≠ F348)
7bsrA Mandelate oxidase with the 2-hydroxy-3-oxosuccinic acid (see paper)
37% identity, 88% coverage: 42:410/419 of query aligns to 1:319/330 of 7bsrA
- active site: F124 (≠ Y165), D152 (= D193), H226 (= H314)
- binding (2~{S})-2-oxidanyl-3-oxidanylidene-butanedioic acid: R159 (= R200), H226 (= H314), R229 (= R317)
- binding 3-pyridin-4-yl-2,4-dihydro-indeno[1,2-.c.]pyrazole: L21 (≠ I62), P73 (= P114), V74 (≠ M115), Q122 (= Q163), F124 (≠ Y165), T150 (= T191), K202 (= K290), H226 (= H314), R229 (= R317), D257 (= D345), R261 (= R349), G280 (= G368), R281 (= R369)
6a39A The crystal structure of mandelate oxidase y128f with c4a-malic acid- monooxide-fmn adduct
37% identity, 88% coverage: 42:410/419 of query aligns to 1:319/330 of 6a39A
- active site: F124 (≠ Y165), D152 (= D193), H226 (= H314)
- binding (~{E})-2-[[(4~{a}~{S})-7,8-dimethyl-2,4-bis(oxidanylidene)-10-[(2~{S},3~{S},4~{S})-2,3,4-tris(oxidanyl)-5-phosphonooxy-pentyl]-5~{H}-benzo[g]pteridin-4~{a}-yl]oxy]-3-oxidanyl-but-2-enedioic acid: P73 (= P114), V74 (≠ M115), A75 (≠ G116), Q122 (= Q163), F124 (≠ Y165), T150 (= T191), R159 (= R200), K202 (= K290), H226 (= H314), G227 (= G315), R229 (= R317), D257 (= D345), G259 (= G347), R261 (= R349), G280 (= G368), R281 (= R369)
Query Sequence
>Ac3H11_1767 FitnessBrowser__acidovorax_3H11:Ac3H11_1767
MRLSACTDVHTMTTAIDSVSPALSPTPGAPQRSPAVLRRMLSLHDFEDAARRRLPRPIFG
YIAGAAEDNASLRDNREVFGEYAFTTRVLRDVSQRSQAVELFGERYSSPFGIAPMGINAL
STYRGDLVLACAAQRAGIVSVMSGTSLIPMEEVARESPGTWFQAYLPGDQARIDALIDRV
ERAGFRTLVVTVDIPISANRENNIRTGFSTPLRPGLRLAWDGLVRPRWVAGTFVRTLLRH
GMPHFENSFATRGAPIVSSSVLRDFSARDHLSWNHLEAIRRRWKGPLVVKGVLRVEDALQ
ARNLGADGVVLSNHGGRQLDGAVSAMRVLEAVVAAVGPAFPVLIDGGFRRGSDVLKAIAL
GARMVLVGRPFNYAAAVAGEAGVQHAIGLLRDEVDRNLAMLGARACTDLGPGHIVRRHG
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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