SitesBLAST
Comparing H281DRAFT_02523 FitnessBrowser__Burk376:H281DRAFT_02523 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)
3rc1A Crystal structure of kijd10, a 3-ketoreductase from actinomadura kijaniata incomplex with NADP and tdp-benzene (see paper)
36% identity, 55% coverage: 9:173/301 of query aligns to 28:191/325 of 3rc1A
- active site: K95 (= K77), Y179 (= Y161)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: S35 (= S16), R36 (= R17), Y56 (= Y38), P71 (= P53), L72 (≠ V54), P73 (= P55), H77 (= H59), E94 (= E76), K95 (= K77), I162 (= I144), R163 (= R145), V168 (≠ L150), D175 (= D157), Y179 (= Y161)
- binding 5'-O-[(S)-hydroxy{[(S)-hydroxy(phenoxy)phosphoryl]oxy}phosphoryl]thymidine: F152 (= F134), I154 (≠ Y136), P155 (≠ F137)
Sites not aligning to the query:
B3TMR8 dTDP-3,4-didehydro-2,6-dideoxy-alpha-D-glucose 3-reductase; 3-ketoreductase; NADPH-dependent C3-ketoreductase; EC 1.1.1.384 from Actinomadura kijaniata (see paper)
36% identity, 55% coverage: 9:173/301 of query aligns to 35:198/332 of B3TMR8
- SR 42:43 (= SR 16:17) binding
- Y63 (= Y38) binding
- L79 (≠ V54) binding
- H84 (= H59) binding
- K102 (= K77) active site, Proton donor; mutation K->A,M,Q: Loss of reductase activity.; mutation to E: Retains some activity, but the catalytic efficiency is strongly reduced.
- R170 (= R145) binding
- D182 (= D157) binding
- Y186 (= Y161) mutation to F: Same affinity for dTDP-glucose and NADPH compared to the wild-type. Small reduction of the catalytic efficiency resulting from the conformational flexibility of the nicotinamide ring.
Sites not aligning to the query:
2poqX Dimeric dihydrodiol dehydrogenase complexed with inhibitor, isoascorbic acid (see paper)
33% identity, 53% coverage: 1:161/301 of query aligns to 20:179/331 of 2poqX
Sites not aligning to the query:
2o4uX Crystal structure of mammalian dimeric dihydrodiol dehydrogenase (see paper)
33% identity, 53% coverage: 1:161/301 of query aligns to 20:179/331 of 2o4uX
Sites not aligning to the query:
- binding phosphate ion: 1, 2, 8, 9, 232, 234, 236, 247, 250, 253, 292, 296, 318
Q7JK39 Trans-1,2-dihydrobenzene-1,2-diol dehydrogenase; D-xylose 1-dehydrogenase; D-xylose-NADP dehydrogenase; Dimeric dihydrodiol dehydrogenase; Jmo2DD; EC 1.3.1.20; EC 1.1.1.179 from Macaca fuscata fuscata (Japanese macaque) (see paper)
33% identity, 53% coverage: 1:161/301 of query aligns to 21:180/334 of Q7JK39
- H79 (= H59) mutation to E: Decrease in K(d) and K(m) value for NADPH. Elimination of the fluorescence-energy transfer and enhancement of NADPH fluorescence by the binary complex formation. Potent inhibition of the dehydrogenase activity by high ionic strength.
- Y180 (= Y161) mutation to F: Significant loss of activity. No effect on the high affinity for NADPH, fluorescence-energy transfer and enhancement of NADPH fluorescence by the binary complex formation.
Q9TQS6 Trans-1,2-dihydrobenzene-1,2-diol dehydrogenase; Cmo2DD; D-xylose 1-dehydrogenase; D-xylose-NADP dehydrogenase; Dimeric dihydrodiol dehydrogenase; EC 1.3.1.20; EC 1.1.1.179 from Macaca fascicularis (Crab-eating macaque) (Cynomolgus monkey) (see paper)
33% identity, 53% coverage: 1:161/301 of query aligns to 21:180/334 of Q9TQS6
- R148 (= R128) mutation to A: No effect on activity. Reduced activity and exhibits significant temperature sensitivity; when associated with A-202.
Sites not aligning to the query:
- 202 R→A: No effect on activity. Reduced activity and exhibits significant temperature sensitivity; when associated with A-148.
1rydA Crystal structure of glucose-fructose oxidoreductase from zymomonas mobilis
29% identity, 55% coverage: 9:175/301 of query aligns to 57:231/381 of 1rydA
- active site: K129 (= K77), Y217 (= Y161)
- binding nadph dihydro-nicotinamide-adenine-dinucleotide phosphate: S64 (= S16), G65 (≠ R17), K69 (= K21), Y87 (≠ T35), L106 (≠ V54), P107 (= P55), N108 (= N56), L110 (= L58), H111 (= H59), E128 (= E76), K129 (= K77), R157 (≠ H109), A196 (= A142), W199 (vs. gap), R200 (vs. gap), Y217 (= Y161)
Sites not aligning to the query:
1h6dA Oxidized precursor form of glucose-fructose oxidoreductase from zymomonas mobilis complexed with glycerol (see paper)
29% identity, 55% coverage: 9:175/301 of query aligns to 59:233/383 of 1h6dA
- active site: K131 (= K77), Y219 (= Y161)
- binding glycerol: K131 (= K77), R202 (vs. gap), D215 (= D157), Y219 (= Y161)
- binding nadph dihydro-nicotinamide-adenine-dinucleotide phosphate: S66 (= S16), G67 (≠ R17), K71 (= K21), Y89 (≠ T35), I107 (≠ P53), L108 (≠ V54), P109 (= P55), N110 (= N56), H113 (= H59), E130 (= E76), K131 (= K77), R159 (≠ H109), A198 (= A142), W201 (vs. gap), R202 (vs. gap), Y219 (= Y161)
Sites not aligning to the query:
1evjA Crystal structure of glucose-fructose oxidoreductase (gfor) delta1-22 s64d (see paper)
29% identity, 55% coverage: 9:175/301 of query aligns to 28:202/340 of 1evjA
- active site: K100 (= K77), Y188 (= Y161)
- binding nicotinamide-adenine-dinucleotide: D35 (≠ S16), L77 (≠ V54), P78 (= P55), N79 (= N56), H82 (= H59), E99 (= E76), K100 (= K77), R128 (≠ H109), W170 (vs. gap), R171 (vs. gap), Y188 (= Y161)
Sites not aligning to the query:
5a05A Crystal structure of aldose-aldose oxidoreductase from caulobacter crescentus complexed with maltotriose (see paper)
27% identity, 73% coverage: 9:229/301 of query aligns to 28:257/335 of 5a05A
- active site: K100 (= K77), Y185 (= Y161)
- binding beta-D-glucopyranose: K100 (= K77), F159 (≠ Y136), D181 (= D157), Y185 (= Y161)
- binding nadph dihydro-nicotinamide-adenine-dinucleotide phosphate: S35 (= S16), G36 (≠ R17), T37 (≠ D18), K40 (= K21), Y58 (≠ T35), I76 (≠ P53), T77 (≠ V54), P78 (= P55), N79 (= N56), L81 (= L58), H82 (= H59), E99 (= E76), K100 (= K77), R128 (≠ H109), W167 (≠ I144), R168 (= R145), Y185 (= Y161)
Sites not aligning to the query:
5a04A Crystal structure of aldose-aldose oxidoreductase from caulobacter crescentus complexed with glucose (see paper)
27% identity, 73% coverage: 9:229/301 of query aligns to 28:257/335 of 5a04A
- active site: K100 (= K77), Y185 (= Y161)
- binding beta-D-glucopyranose: K100 (= K77), F159 (≠ Y136), R168 (= R145), D181 (= D157), Y185 (= Y161)
- binding nadph dihydro-nicotinamide-adenine-dinucleotide phosphate: S35 (= S16), G36 (≠ R17), T37 (≠ D18), K40 (= K21), Y58 (≠ T35), I76 (≠ P53), T77 (≠ V54), P78 (= P55), N79 (= N56), L81 (= L58), H82 (= H59), E99 (= E76), K100 (= K77), R128 (≠ H109), W167 (≠ I144), R168 (= R145), Y185 (= Y161)
Sites not aligning to the query:
5a03E Crystal structure of aldose-aldose oxidoreductase from caulobacter crescentus complexed with xylose (see paper)
27% identity, 73% coverage: 9:229/301 of query aligns to 28:257/335 of 5a03E
- active site: K100 (= K77), Y185 (= Y161)
- binding nadph dihydro-nicotinamide-adenine-dinucleotide phosphate: S35 (= S16), G36 (≠ R17), T37 (≠ D18), K40 (= K21), Y58 (≠ T35), I76 (≠ P53), T77 (≠ V54), P78 (= P55), N79 (= N56), H82 (= H59), E99 (= E76), K100 (= K77), R128 (≠ H109), W167 (≠ I144), R168 (= R145), Y185 (= Y161)
- binding beta-D-xylopyranose: K100 (= K77), F159 (≠ Y136), R168 (= R145), D181 (= D157), Y185 (= Y161), E205 (≠ S184), T207 (= T186), R209 (≠ G188)
- binding alpha-D-xylopyranose: H134 (vs. gap)
Sites not aligning to the query:
5a02A Crystal structure of aldose-aldose oxidoreductase from caulobacter crescentus complexed with glycerol (see paper)
27% identity, 73% coverage: 9:229/301 of query aligns to 28:257/335 of 5a02A
- active site: K100 (= K77), Y185 (= Y161)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: S35 (= S16), G36 (≠ R17), T37 (≠ D18), K40 (= K21), Y58 (≠ T35), I76 (≠ P53), T77 (≠ V54), P78 (= P55), L81 (= L58), H82 (= H59), E99 (= E76), K100 (= K77), R128 (≠ H109), W167 (≠ I144), R168 (= R145), Y185 (= Y161)
Sites not aligning to the query:
5a06A Crystal structure of aldose-aldose oxidoreductase from caulobacter crescentus complexed with sorbitol (see paper)
27% identity, 73% coverage: 9:229/301 of query aligns to 29:258/336 of 5a06A
- active site: K101 (= K77), Y186 (= Y161)
- binding nadph dihydro-nicotinamide-adenine-dinucleotide phosphate: S36 (= S16), G37 (≠ R17), T38 (≠ D18), K41 (= K21), Y59 (≠ T35), I77 (≠ P53), T78 (≠ V54), P79 (= P55), N80 (= N56), L82 (= L58), H83 (= H59), E100 (= E76), K101 (= K77), R129 (≠ H109), W168 (≠ I144), R169 (= R145), Y186 (= Y161)
- binding sorbitol: D72 (= D48), H96 (= H72), K101 (= K77), R122 (≠ E102), R122 (≠ E102), L124 (≠ I104), F160 (≠ Y136), R169 (= R145), D182 (= D157), Y186 (= Y161)
Sites not aligning to the query:
- binding nadph dihydro-nicotinamide-adenine-dinucleotide phosphate: 11, 12, 13, 14, 264
- binding sorbitol: 2, 287, 296, 299, 306, 310, 311
5a03C Crystal structure of aldose-aldose oxidoreductase from caulobacter crescentus complexed with xylose (see paper)
27% identity, 73% coverage: 9:229/301 of query aligns to 29:258/336 of 5a03C
- active site: K101 (= K77), Y186 (= Y161)
- binding nadph dihydro-nicotinamide-adenine-dinucleotide phosphate: S36 (= S16), G37 (≠ R17), T38 (≠ D18), K41 (= K21), Y59 (≠ T35), I77 (≠ P53), T78 (≠ V54), P79 (= P55), N80 (= N56), L82 (= L58), H83 (= H59), E100 (= E76), K101 (= K77), R129 (≠ H109), W168 (≠ I144), R169 (= R145), Y186 (= Y161)
- binding beta-D-xylopyranose: K101 (= K77), F160 (≠ Y136), R169 (= R145), D182 (= D157), Y186 (= Y161)
Sites not aligning to the query:
2glxA Crystal structure analysis of bacterial 1,5-af reductase (see paper)
25% identity, 93% coverage: 3:283/301 of query aligns to 19:301/332 of 2glxA
- active site: K93 (= K77), H179 (≠ Y161)
- binding acetate ion: K93 (= K77), H179 (≠ Y161)
- binding nadph dihydro-nicotinamide-adenine-dinucleotide phosphate: S32 (= S16), T33 (≠ R17), R37 (≠ K21), S69 (≠ P53), T70 (≠ V54), N72 (= N56), H75 (= H59), E92 (= E76), K93 (= K77), H121 (≠ M105), W161 (vs. gap), R162 (vs. gap), Y282 (= Y265)
Sites not aligning to the query:
4koaA Crystal structure analysis of 1,5-anhydro-d-fructose reductase from sinorhizobium meliloti (see paper)
24% identity, 91% coverage: 3:276/301 of query aligns to 20:294/333 of 4koaA
Sites not aligning to the query:
Q2I8V6 1,5-anhydro-D-fructose reductase; Anhydrofructose reductase; 1,5-anhydro-D-fructose reductase (1,5-anhydro-D-mannitol-forming); EC 1.1.1.292 from Ensifer adhaerens (Sinorhizobium morelense) (see paper)
25% identity, 93% coverage: 3:283/301 of query aligns to 20:302/333 of Q2I8V6
- S33 (= S16) mutation to D: No activity.
- ST 33:34 (≠ SR 16:17) binding
- R38 (≠ K21) binding
- TTNELH 71:76 (≠ VPNALH 54:59) binding
- EK 93:94 (= EK 76:77) binding
- K94 (= K77) mutation to G: Less than 1% remaining activity.
- N120 (≠ A103) binding
- WR 162:163 (vs. gap) binding
- D176 (= D157) mutation to A: Less than 1% remaining activity.
- H180 (≠ Y161) mutation to A: Less than 2% remaining activity.
- G206 (= G188) mutation to I: No effect.
- Y283 (= Y265) binding
Sites not aligning to the query:
- 9:12 binding
- 10 S→G: Almost no effect.
- 13 A→G: Can use NAD as cosubstrate as well as NADP.
7xreC Crystal structure of dgpa
31% identity, 44% coverage: 33:163/301 of query aligns to 57:189/363 of 7xreC
Sites not aligning to the query:
7xr9A Crystal structure of dgpa with glucose (see paper)
31% identity, 44% coverage: 33:163/301 of query aligns to 47:179/344 of 7xr9A
- binding beta-D-glucopyranose: K91 (= K77), R150 (≠ Y136), W157 (vs. gap), F160 (≠ I144), D173 (= D157), H177 (≠ Y161)
- binding nicotinamide-adenine-dinucleotide: D51 (≠ K37), Y52 (= Y38), C67 (≠ P53), T68 (≠ V54), P69 (= P55), H73 (= H59), E90 (= E76), K91 (= K77), P92 (= P78), Q119 (≠ M105), V159 (≠ S143), F160 (≠ I144), Q166 (≠ L150)
Sites not aligning to the query:
Query Sequence
>H281DRAFT_02523 FitnessBrowser__Burk376:H281DRAFT_02523
MPSIQRIGSRITIVASRDIEKATLLARKHAVNHVTAKYEDVLSHPEVDAVYVPVPNALHF
PWTVAALQAGKHVLCEKPICMNASEVRRLIEERDRSGLVCAEAIMMVHHPQWESVRQAIC
SGEIGDLRQVGGAFTYFRADPASIRNNLSLGGGSLRDVGMYPIVGTAFATGRDPVGAQGD
LSFSATSGTDIASDCVIDFGDFKLRSFCSTLVGRRQSMLFHGEKGWIEMTAPFTTNNYHD
ASVIKHIDGDDQLHVEHYGRTLEQYERMLLDFEKSVETGTPVAYPLERSLIVQGQLDALL
Q
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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