SitesBLAST
Comparing SMa2313 FitnessBrowser__Smeli:SMa2313 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)
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)
27% identity, 50% coverage: 7:347/677 of query aligns to 3:334/334 of Q7JK39
- H79 (= H80) 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 (= Y184) 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)
27% identity, 50% coverage: 7:347/677 of query aligns to 3:334/334 of Q9TQS6
- R148 (= R149) mutation to A: No effect on activity. Reduced activity and exhibits significant temperature sensitivity; when associated with A-202.
- R202 (≠ H212) mutation to A: No effect on activity. Reduced activity and exhibits significant temperature sensitivity; when associated with A-148.
2poqX Dimeric dihydrodiol dehydrogenase complexed with inhibitor, isoascorbic acid (see paper)
27% identity, 50% coverage: 7:342/677 of query aligns to 2:328/331 of 2poqX
2o4uX Crystal structure of mammalian dimeric dihydrodiol dehydrogenase (see paper)
27% identity, 50% coverage: 7:342/677 of query aligns to 2:328/331 of 2o4uX
- binding phosphate ion: L2 (≠ I7), S8 (≠ G13), V9 (≠ P14), A35 (= A38), R36 (= R39), R40 (≠ K43), Y57 (= Y59), N101 (≠ S103), A103 (= A105), D145 (= D147), R147 (= R149), K155 (vs. gap), Q232 (≠ E243), S234 (≠ E245), T236 (≠ V247), Q247 (≠ E258), N250 (≠ Q261), W253 (≠ G271), R292 (≠ G304), R296 (= R308), E318 (≠ D332)
Sites not aligning to the query:
2glxA Crystal structure analysis of bacterial 1,5-af reductase (see paper)
29% identity, 44% coverage: 8:307/677 of query aligns to 2:293/332 of 2glxA
- active site: K93 (= K98), H179 (≠ Y184)
- binding acetate ion: K93 (= K98), H179 (≠ Y184)
- binding nadph dihydro-nicotinamide-adenine-dinucleotide phosphate: G7 (= G13), A8 (≠ P14), S9 (≠ G15), T10 (≠ N16), I11 (= I17), S32 (≠ A38), T33 (≠ R39), R37 (≠ K43), S69 (≠ A74), T70 (= T75), N72 (≠ H77), H75 (= H80), E92 (= E97), K93 (= K98), H121 (≠ M126), W161 (≠ H166), R162 (= R167), Y282 (= Y296)
5a06A Crystal structure of aldose-aldose oxidoreductase from caulobacter crescentus complexed with sorbitol (see paper)
30% identity, 41% coverage: 59:337/677 of query aligns to 62:328/336 of 5a06A
- active site: K101 (= K98), Y186 (= Y184)
- binding nadph dihydro-nicotinamide-adenine-dinucleotide phosphate: I77 (≠ A74), T78 (= T75), P79 (≠ V76), N80 (≠ H77), L82 (= L79), H83 (= H80), E100 (= E97), K101 (= K98), R129 (≠ M126), W168 (≠ R167), R169 (≠ L168), Y186 (= Y184), Y264 (≠ A265)
- binding sorbitol: D72 (= D69), H96 (= H93), K101 (= K98), R122 (≠ T119), R122 (≠ T119), L124 (≠ M121), F160 (= F157), R169 (≠ L168), D182 (= D180), Y186 (= Y184), K287 (≠ R293), H296 (≠ A302), E299 (≠ D305), E306 (≠ T312), G310 (≠ S320), G311 (≠ R321)
Sites not aligning to the query:
5a03C Crystal structure of aldose-aldose oxidoreductase from caulobacter crescentus complexed with xylose (see paper)
30% identity, 41% coverage: 59:337/677 of query aligns to 62:328/336 of 5a03C
- active site: K101 (= K98), Y186 (= Y184)
- binding nadph dihydro-nicotinamide-adenine-dinucleotide phosphate: I77 (≠ A74), T78 (= T75), P79 (≠ V76), N80 (≠ H77), L82 (= L79), H83 (= H80), E100 (= E97), K101 (= K98), R129 (≠ M126), W168 (≠ R167), R169 (≠ L168), Y186 (= Y184), Y264 (≠ A265)
- binding beta-D-xylopyranose: K101 (= K98), F160 (= F157), R169 (≠ L168), D182 (= D180), Y186 (= Y184)
Sites not aligning to the query:
5a05A Crystal structure of aldose-aldose oxidoreductase from caulobacter crescentus complexed with maltotriose (see paper)
30% identity, 42% coverage: 57:337/677 of query aligns to 59:327/335 of 5a05A
- active site: K100 (= K98), Y185 (= Y184)
- binding beta-D-glucopyranose: K100 (= K98), F159 (= F157), D181 (= D180), Y185 (= Y184)
- binding alpha-D-glucopyranose: P259 (≠ Q261), S262 (≠ F264)
- binding nadph dihydro-nicotinamide-adenine-dinucleotide phosphate: I76 (≠ A74), T77 (= T75), P78 (≠ V76), N79 (≠ H77), L81 (= L79), H82 (= H80), E99 (= E97), K100 (= K98), R128 (≠ M126), W167 (≠ R167), R168 (≠ L168), Y185 (= Y184), Y263 (≠ A265)
Sites not aligning to the query:
5a04A Crystal structure of aldose-aldose oxidoreductase from caulobacter crescentus complexed with glucose (see paper)
30% identity, 42% coverage: 57:337/677 of query aligns to 59:327/335 of 5a04A
- active site: K100 (= K98), Y185 (= Y184)
- binding beta-D-glucopyranose: K100 (= K98), F159 (= F157), R168 (≠ L168), D181 (= D180), Y185 (= Y184)
- binding nadph dihydro-nicotinamide-adenine-dinucleotide phosphate: I76 (≠ A74), T77 (= T75), P78 (≠ V76), N79 (≠ H77), L81 (= L79), H82 (= H80), E99 (= E97), K100 (= K98), R128 (≠ M126), W167 (≠ R167), R168 (≠ L168), Y185 (= Y184), Y263 (≠ A265)
Sites not aligning to the query:
5a03E Crystal structure of aldose-aldose oxidoreductase from caulobacter crescentus complexed with xylose (see paper)
30% identity, 42% coverage: 57:337/677 of query aligns to 59:327/335 of 5a03E
- active site: K100 (= K98), Y185 (= Y184)
- binding nadph dihydro-nicotinamide-adenine-dinucleotide phosphate: I76 (≠ A74), T77 (= T75), P78 (≠ V76), N79 (≠ H77), H82 (= H80), E99 (= E97), K100 (= K98), R128 (≠ M126), W167 (≠ R167), R168 (≠ L168), Y185 (= Y184), Y263 (≠ A265)
- binding beta-D-xylopyranose: K100 (= K98), F159 (= F157), R168 (≠ L168), D181 (= D180), Y185 (= Y184), E205 (≠ G211), T207 (≠ L213), R209 (= R215)
- binding alpha-D-xylopyranose: H134 (≠ L132), M268 (≠ I275), R279 (≠ E286), E280 (≠ V287)
Sites not aligning to the query:
5a02A Crystal structure of aldose-aldose oxidoreductase from caulobacter crescentus complexed with glycerol (see paper)
30% identity, 42% coverage: 57:337/677 of query aligns to 59:327/335 of 5a02A
- active site: K100 (= K98), Y185 (= Y184)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: I76 (≠ A74), T77 (= T75), P78 (≠ V76), L81 (= L79), H82 (= H80), E99 (= E97), K100 (= K98), R128 (≠ M126), W167 (≠ R167), R168 (≠ L168), Y185 (= Y184), Y263 (≠ A265)
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)
27% identity, 49% coverage: 7:335/677 of query aligns to 10:323/332 of B3TMR8
- 17:23 (vs. 14:20, 29% identical) binding
- SR 42:43 (≠ AR 38:39) binding
- Y63 (= Y59) binding
- L79 (≠ T75) binding
- H84 (= H80) binding
- K102 (= K98) 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 (≠ L168) binding
- D182 (= D180) binding
- Y186 (= Y184) 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.
3rc1A Crystal structure of kijd10, a 3-ketoreductase from actinomadura kijaniata incomplex with NADP and tdp-benzene (see paper)
27% identity, 49% coverage: 7:335/677 of query aligns to 3:316/325 of 3rc1A
- active site: K95 (= K98), Y179 (= Y184)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: C10 (≠ P14), A11 (≠ G15), D12 (≠ N16), I13 (= I17), S35 (≠ A38), R36 (= R39), Y56 (= Y59), P71 (≠ A74), L72 (≠ T75), P73 (≠ V76), H77 (= H80), E94 (= E97), K95 (= K98), I162 (≠ R167), R163 (≠ L168), V168 (≠ M173), D175 (= D180), Y179 (= Y184)
- binding phosphate ion: H278 (= H294), K283 (≠ F298)
- binding 5'-O-[(S)-hydroxy{[(S)-hydroxy(phenoxy)phosphoryl]oxy}phosphoryl]thymidine: R16 (≠ D20), R17 (≠ F21), F152 (= F155), I154 (≠ F157), P155 (≠ A158), Y233 (≠ Q244), T253 (≠ K268)
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)
29% identity, 44% coverage: 8:307/677 of query aligns to 3:294/333 of Q2I8V6
- ASTI 9:12 (≠ PGNI 14:17) binding
- S10 (≠ G15) mutation to G: Almost no effect.
- A13 (= A18) mutation to G: Can use NAD as cosubstrate as well as NADP.
- S33 (≠ A38) mutation to D: No activity.
- ST 33:34 (≠ AR 38:39) binding
- R38 (≠ K43) binding
- TTNELH 71:76 (≠ TVHPLH 75:80) binding
- EK 93:94 (= EK 97:98) binding
- K94 (= K98) mutation to G: Less than 1% remaining activity.
- N120 (≠ A124) binding
- WR 162:163 (≠ HR 166:167) binding
- D176 (= D180) mutation to A: Less than 1% remaining activity.
- H180 (≠ Y184) mutation to A: Less than 2% remaining activity.
- G206 (= G214) mutation to I: No effect.
- Y283 (= Y296) binding
4koaA Crystal structure analysis of 1,5-anhydro-d-fructose reductase from sinorhizobium meliloti (see paper)
30% identity, 44% coverage: 7:307/677 of query aligns to 2:294/333 of 4koaA
- active site: K94 (= K98), H180 (≠ Y184)
- binding nadph dihydro-nicotinamide-adenine-dinucleotide phosphate: G8 (= G13), A9 (≠ P14), S10 (≠ G15), T11 (≠ N16), I12 (= I17), S33 (≠ A38), S34 (≠ R39), R38 (≠ K43), T71 (= T75), N73 (≠ H77), H76 (= H80), K94 (= K98), Q160 (≠ E164)
1h6dA Oxidized precursor form of glucose-fructose oxidoreductase from zymomonas mobilis complexed with glycerol (see paper)
30% identity, 31% coverage: 1:212/677 of query aligns to 28:240/383 of 1h6dA
- active site: K131 (= K98), Y219 (= Y184)
- binding glycerol: K131 (= K98), R202 (≠ L168), D215 (= D180), Y219 (= Y184)
- binding nadph dihydro-nicotinamide-adenine-dinucleotide phosphate: G40 (= G13), L41 (≠ P14), G42 (= G15), K43 (≠ N16), Y44 (≠ I17), S66 (≠ A38), G67 (≠ R39), K71 (= K43), Y89 (vs. gap), I107 (≠ A74), L108 (≠ T75), P109 (≠ V76), N110 (≠ H77), H113 (= H80), E130 (= E97), K131 (= K98), R159 (≠ M126), A198 (≠ G165), W201 (vs. gap), R202 (≠ L168), Y219 (= Y184)
Sites not aligning to the query:
1rydA Crystal structure of glucose-fructose oxidoreductase from zymomonas mobilis
30% identity, 31% coverage: 1:212/677 of query aligns to 26:238/381 of 1rydA
- active site: K129 (= K98), Y217 (= Y184)
- binding alpha-D-glucopyranose: Y236 (≠ L210)
- binding nadph dihydro-nicotinamide-adenine-dinucleotide phosphate: L39 (≠ P14), G40 (= G15), K41 (≠ N16), Y42 (≠ I17), S64 (≠ A38), G65 (≠ R39), K69 (= K43), Y87 (vs. gap), L106 (≠ T75), P107 (≠ V76), N108 (≠ H77), L110 (= L79), H111 (= H80), E128 (= E97), K129 (= K98), R157 (≠ M126), A196 (≠ G165), W199 (vs. gap), R200 (≠ L168), Y217 (= Y184)
Sites not aligning to the query:
1evjA Crystal structure of glucose-fructose oxidoreductase (gfor) delta1-22 s64d (see paper)
33% identity, 23% coverage: 58:212/677 of query aligns to 60:209/340 of 1evjA
- active site: K100 (= K98), Y188 (= Y184)
- binding nicotinamide-adenine-dinucleotide: L77 (≠ T75), P78 (≠ V76), N79 (≠ H77), H82 (= H80), E99 (= E97), K100 (= K98), R128 (≠ M126), W170 (vs. gap), R171 (≠ L168), Y188 (= Y184)
Sites not aligning to the query:
1pz0A Structure of NADPH-dependent family 11 aldo-keto reductase akr11a(holo) (see paper)
25% identity, 39% coverage: 405:666/677 of query aligns to 47:304/311 of 1pz0A
- active site: D52 (= D410), Y57 (= Y415), N91 (≠ S446), H124 (= H476)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: H124 (= H476), Q174 (= Q543), Y202 (≠ W571), F203 (≠ S572), P204 (≠ S573), L205 (≠ Q574), S207 (≠ R576), G208 (= G577), A211 (= A583), K213 (≠ R585)
P46336 Aldo-keto reductase IolS; AKR11A; Vegetative protein 147; VEG147; EC 1.1.1.- from Bacillus subtilis (strain 168) (see paper)
25% identity, 39% coverage: 405:666/677 of query aligns to 48:305/310 of P46336
Query Sequence
>SMa2313 FitnessBrowser__Smeli:SMa2313
MNEPTRIRWGILGPGNIAKDFFAGALQSANGKVVAIGARNPAKSGLAEDFPGARIVDGYD
ALIDDPGIDAVYIATVHPLHAEWAIKAAEKGKHVLCEKPMGLSTAEADAMFEAARKAGTF
MAEAYMYRLHPLTARIVELVKNGMVGDVRKIQSSFGFAKLPFDEGHRLFSNEMAGGGILD
VGGYTTSMARLIAGIGTSSGVMEPAEVTALGHLGRTGVDEWTSALLSFPNGIIAELSCSV
SLEQENVLRILGTKGRIEVDQFWFAGGKPGGTSIIRIVHADGRQEEVPLVEPRHLYSFEV
EAAGDAIRAGRTEFAYPGMSRADTLGNLRVMDKWRAAIGLEYEGEKHTTRTRTVRGDKLA
RKTSLVRSGRIDGLQKEISHAALGLMEFSTFSSAAIVLDAFFEAGGNLVDTAFLYGNGVQ
DRLVGEWMRSRGVRQETVVIAKGAHSPLCYPDVIGKQLTTSLERMGTDYVDIYFMHRDNP
DIPVGEFVDAMDAEVAAGRIRGPIGGSNWTRERFEEAIAYAERAGKTKPSVLSNNFSLAE
MVQPVWAGCISSSDDAWMRWLEENDVTNFAWSSQARGFFTDRAGRGKLDDLELARSWYSE
GNFARRDRAIALGRKLGKDPIQIALAYVLAQKGRVIPLIGPRLLAELNHSLDAFAVTLSP
GDVQWLRDGDPGESSAA
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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