SitesBLAST
Comparing SM_b20445 FitnessBrowser__Smeli:SM_b20445 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)
6dkhC The crystal structure of l-idonate 5-dehydrogenase from escherichia coli str. K-12 substr. Mg1655
40% identity, 98% coverage: 7:350/352 of query aligns to 7:346/346 of 6dkhC
3qe3A Sheep liver sorbitol dehydrogenase (see paper)
36% identity, 92% coverage: 13:337/352 of query aligns to 8:332/351 of 3qe3A
- active site: C39 (= C44), G40 (= G45), S41 (= S46), H44 (= H49), H64 (= H69), E65 (= E70), R94 (≠ C99), D97 (≠ C102), C100 (= C105), S108 (≠ C113), F112 (≠ R117), P151 (= P160), G155 (≠ C164)
- binding glycerol: Y45 (= Y50), F54 (≠ V59), T116 (≠ S121), R293 (= R298)
- binding zinc ion: C39 (= C44), H64 (= H69), E65 (= E70)
Sites not aligning to the query:
1pl6A Human sdh/nadh/inhibitor complex (see paper)
36% identity, 92% coverage: 13:335/352 of query aligns to 13:335/356 of 1pl6A
- active site: C44 (= C44), G45 (= G45), S46 (= S46), H49 (= H49), H69 (= H69), E70 (= E70), R99 (≠ C99), D102 (≠ C102), C105 (= C105), S113 (≠ C113), F117 (≠ R117), P156 (= P160), G160 (≠ C164)
- binding 4-[2-(hydroxymethyl)pyrimidin-4-yl]-n,n-dimethylpiperazine-1-sulfonamide: C44 (= C44), S46 (= S46), I56 (≠ F56), F59 (≠ V59), H69 (= H69), E155 (= E159), L274 (≠ V275), F297 (≠ Q297)
- binding nicotinamide-adenine-dinucleotide: G181 (= G185), P182 (= P186), I183 (= I187), D203 (= D207), L204 (= L208), R208 (≠ A212), C249 (= C250), T250 (≠ S251), V272 (= V273), G273 (= G274), L274 (≠ V275), F297 (≠ Q297), R298 (= R298)
- binding zinc ion: C44 (= C44), H69 (= H69)
Sites not aligning to the query:
Q00796 Sorbitol dehydrogenase; SDH; (R,R)-butanediol dehydrogenase; L-iditol 2-dehydrogenase; Polyol dehydrogenase; Ribitol dehydrogenase; RDH; Xylitol dehydrogenase; XDH; EC 1.1.1.-; EC 1.1.1.4; EC 1.1.1.14; EC 1.1.1.56; EC 1.1.1.9 from Homo sapiens (Human) (see 10 papers)
36% identity, 92% coverage: 13:335/352 of query aligns to 14:336/357 of Q00796
- C45 (= C44) binding
- H70 (= H69) binding
- E71 (= E70) binding
- R110 (≠ L109) to P: in SORDD; results in protein aggregation
- H135 (≠ V138) to R: in SORDD; results in protein aggregation
- A153 (= A156) to D: in SORDD; uncertain significance; results in protein aggregation; dbSNP:rs145813597
- I184 (= I187) binding
- D204 (= D207) binding
- R209 (≠ A212) binding
- Q239 (≠ D240) to L: in dbSNP:rs1042079
- N269 (≠ T269) to T: in dbSNP:rs930337
- VGL 273:275 (≠ VGV 273:275) binding
- VFR 297:299 (≠ SQR 296:298) binding
- V322 (≠ I321) to I: in SORDD; uncertain significance; dbSNP:rs149975952
Sites not aligning to the query:
- 1 modified: Initiator methionine, Removed
P07846 Sorbitol dehydrogenase; SDH; L-iditol 2-dehydrogenase; Polyol dehydrogenase; Xylitol dehydrogenase; XDH; EC 1.1.1.-; EC 1.1.1.14; EC 1.1.1.9 from Ovis aries (Sheep) (see paper)
36% identity, 92% coverage: 13:337/352 of query aligns to 12:335/354 of P07846
- C43 (= C44) binding
- Y49 (= Y50) binding
- H67 (= H69) binding
- E68 (= E70) binding
- E153 (= E159) binding
- R296 (= R298) binding
- Y297 (≠ F299) binding
1e3jA Ketose reductase (sorbitol dehydrogenase) from silverleaf whitefly (see paper)
36% identity, 94% coverage: 11:341/352 of query aligns to 5:336/348 of 1e3jA
- active site: C38 (= C44), G39 (= G45), S40 (= S46), H43 (= H49), H63 (= H69), E64 (= E70), C93 (= C99), C96 (= C102), C99 (= C105), C107 (= C113), T111 (≠ R117), P150 (= P160), G154 (≠ C164)
- binding phosphate ion: A174 (= A184), A196 (≠ D207), R197 (≠ L208), S198 (≠ A209), R201 (≠ A212)
- binding zinc ion: C38 (= C44), H63 (= H69), E64 (= E70), C93 (= C99), C96 (= C102), C99 (= C105), C107 (= C113)
Sites not aligning to the query:
P27867 Sorbitol dehydrogenase; SDH; L-iditol 2-dehydrogenase; Polyol dehydrogenase; Xylitol dehydrogenase; XDH; EC 1.1.1.-; EC 1.1.1.14; EC 1.1.1.9 from Rattus norvegicus (Rat) (see paper)
35% identity, 92% coverage: 13:337/352 of query aligns to 14:338/357 of P27867
A2QAC0 L-arabinitol 4-dehydrogenase; LAD; EC 1.1.1.12 from Aspergillus niger (strain ATCC MYA-4892 / CBS 513.88 / FGSC A1513) (see 2 papers)
33% identity, 90% coverage: 32:348/352 of query aligns to 43:370/386 of A2QAC0
- M70 (≠ V59) mutation to F: Abolishes enzyme activity.
- DI 213:214 (≠ DL 207:208) mutation to SR: Alters cofactor specificity from NAD to NADP; when associated with T-359.
- Y318 (≠ Q297) mutation to F: Increases affinity for D-sorbitol.
- A359 (≠ G338) mutation to T: Alters cofactor specificity from NAD to NADP; when associated with 213-SR-214.
B6HI95 L-arabinitol 4-dehydrogenase; LAD; EC 1.1.1.12 from Penicillium rubens (strain ATCC 28089 / DSM 1075 / NRRL 1951 / Wisconsin 54-1255) (Penicillium chrysogenum) (see paper)
32% identity, 90% coverage: 32:348/352 of query aligns to 42:369/385 of B6HI95
- DI 212:213 (≠ DL 207:208) mutation to SR: Alters cofactor specificity from NAD to NADP; when associated with T-358.
- S358 (≠ G338) mutation to T: Alters cofactor specificity from NAD to NADP; when associated with 212-SR-213.
Q96V44 L-arabinitol 4-dehydrogenase; LAD; EC 1.1.1.12 from Hypocrea jecorina (Trichoderma reesei) (see paper)
34% identity, 91% coverage: 32:351/352 of query aligns to 54:376/377 of Q96V44
- DI 224:225 (≠ DL 207:208) mutation to SR: Alters cofactor specificity from NAD to NADP; when associated with T-362.
- A362 (≠ G338) mutation to T: Alters cofactor specificity from NAD to NADP; when associated with 224-SR-225.
3m6iA L-arabinitol 4-dehydrogenase (see paper)
33% identity, 91% coverage: 31:351/352 of query aligns to 36:358/358 of 3m6iA
- active site: C49 (= C44), G50 (= G45), S51 (= S46), H54 (= H49), H74 (= H69), E75 (= E70), C104 (= C99), C107 (= C102), C110 (= C105), C118 (= C113), D122 (≠ R117), P160 (= P160), A164 (≠ C164), K352 (= K345)
- binding nicotinamide-adenine-dinucleotide: C49 (= C44), V163 (= V163), G185 (= G185), P186 (= P186), I187 (= I187), D207 (= D207), R212 (≠ A212), C255 (= C250), T256 (≠ S251), I278 (≠ V273), G279 (= G274), V280 (= V275), R304 (= R298)
- binding zinc ion: C49 (= C44), H74 (= H69), C104 (= C99), C107 (= C102), C110 (= C105), C118 (= C113)
Q7SI09 L-arabinitol 4-dehydrogenase; LAD; EC 1.1.1.12 from Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987) (see 2 papers)
33% identity, 91% coverage: 31:351/352 of query aligns to 40:362/363 of Q7SI09
- C53 (= C44) binding
- F59 (≠ Y50) mutation F->A,S,Y: No effect.
- H78 (= H69) binding
- E79 (= E70) binding
- C108 (= C99) binding
- C111 (= C102) binding
- C114 (= C105) binding
- C122 (= C113) binding
- E163 (= E159) binding
- PI 190:191 (= PI 186:187) binding
- D211 (= D207) binding
- DI 211:212 (≠ DL 207:208) mutation to SR: Alters cofactor specificity from NAD to NADP; when associated with T-348.
- R216 (≠ A212) binding
- I282 (≠ V273) binding
- QYR 306:308 (≠ SQR 296:298) binding
- S348 (≠ G338) mutation to T: Alters cofactor specificity from NAD to NADP; when associated with 211-SR-212.
O58389 L-threonine 3-dehydrogenase; L-ThrDH; TDH; L-threonine dehydrogenase; EC 1.1.1.103 from Pyrococcus horikoshii (strain ATCC 700860 / DSM 12428 / JCM 9974 / NBRC 100139 / OT-3) (see 2 papers)
34% identity, 88% coverage: 25:335/352 of query aligns to 23:333/348 of O58389
- C42 (= C44) binding
- T44 (≠ S46) mutation to A: Total loss of enzymatic activity.
- H67 (= H69) binding
- E68 (= E70) binding
- C97 (= C99) binding
- C100 (= C102) binding
- C103 (= C105) binding
- C111 (= C113) binding
- E152 (= E159) mutation E->A,Q: Almost complete loss of enzymatic activity.; mutation to C: 120-fold decrease in catalytic efficiency.; mutation to D: Shows 3-fold higher turnover rate and reduced affinities toward L-threonine and NAD(+), compared to wild-type.; mutation to K: Total loss of enzymatic activity.
- L179 (≠ I187) binding
- E199 (≠ D207) binding ; mutation to A: Large decrease in affinity for NAD(+).
- R204 (≠ A212) binding ; mutation to A: Large decrease in affinity for NAD(+).
- LGL 266:268 (≠ VGV 273:275) binding
- IT 291:292 (≠ -S 296) binding
- R294 (= R298) mutation to A: 4000-fold decrease in catalytic efficiency.
2dfvA Hyperthermophilic threonine dehydrogenase from pyrococcus horikoshii (see paper)
34% identity, 88% coverage: 25:335/352 of query aligns to 21:331/346 of 2dfvA
- active site: C40 (= C44), G41 (= G45), T42 (≠ S46), H45 (= H49), H65 (= H69), E66 (= E70), C95 (= C99), C98 (= C102), C101 (= C105), C109 (= C113), K113 (≠ R117), P151 (= P160), A155 (≠ C164)
- binding nicotinamide-adenine-dinucleotide: G175 (= G185), P176 (= P186), L177 (≠ I187), E197 (≠ D207), P198 (≠ L208), R202 (≠ A212), F241 (≠ C250), S242 (= S251), A244 (= A253), L264 (≠ V273), G265 (= G274), L266 (≠ V275), I289 (vs. gap), T290 (≠ S296)
- binding zinc ion: C95 (= C99), C101 (= C105), C109 (= C113)
Sites not aligning to the query:
7y9pA Xylitol dehydrogenase s96c/s99c/y102c mutant(thermostabilized form) from pichia stipitis (see paper)
31% identity, 94% coverage: 18:347/352 of query aligns to 13:355/357 of 7y9pA
3gfbA L-threonine dehydrogenase (tktdh) from the hyperthermophilic archaeon thermococcus kodakaraensis (see paper)
32% identity, 88% coverage: 25:335/352 of query aligns to 21:331/347 of 3gfbA
- active site: C40 (= C44), G41 (= G45), T42 (≠ S46), H45 (= H49), H65 (= H69), E66 (= E70), C95 (= C99), C98 (= C102), C101 (= C105), C109 (= C113), K113 (≠ R117), P151 (= P160), A155 (≠ C164)
- binding nicotinamide-adenine-dinucleotide: G173 (= G183), G175 (= G185), P176 (= P186), L177 (≠ I187), S196 (≠ T206), E197 (≠ D207), P198 (≠ L208), R202 (≠ A212), F241 (≠ C250), S242 (= S251), A244 (= A253), L264 (≠ V273), G265 (= G274), L266 (≠ V275), I289 (≠ L293), T290 (≠ V294)
Sites not aligning to the query:
Q5JI69 L-threonine 3-dehydrogenase; TDH; L-threonine dehydrogenase; EC 1.1.1.103 from Thermococcus kodakarensis (strain ATCC BAA-918 / JCM 12380 / KOD1) (Pyrococcus kodakaraensis (strain KOD1)) (see paper)
32% identity, 88% coverage: 25:335/352 of query aligns to 23:333/350 of Q5JI69
P07913 L-threonine 3-dehydrogenase; TDH; L-threonine dehydrogenase; EC 1.1.1.103 from Escherichia coli (strain K12) (see paper)
31% identity, 89% coverage: 21:335/352 of query aligns to 13:326/341 of P07913
- C38 (= C44) mutation to D: Shows only 1% of wild-type catalytic activity. This mutant can be stimulated to the wild-type activity level after incubation with Zn(+).; mutation to S: Loss of catalytic activity. This mutant cannot be stimulated to the wild-type activity level after incubation with Zn(+).
5vm2A Crystal structure of eck1772, an oxidoreductase/dehydrogenase of unknown specificity involved in membrane biogenesis from escherichia coli
29% identity, 94% coverage: 7:337/352 of query aligns to 2:331/347 of 5vm2A
- active site: C39 (= C44), G40 (= G45), S41 (= S46), H44 (= H49), H65 (= H69), E66 (= E70), C95 (= C99), C98 (= C102), C101 (= C105), C109 (= C113), D113 (≠ R117), P153 (= P160), G157 (≠ C164)
- binding magnesium ion: H65 (= H69), E66 (= E70), E152 (= E159)
- binding zinc ion: C95 (= C99), C98 (= C102), C101 (= C105), C109 (= C113)
Sites not aligning to the query:
5kiaA Crystal structure of l-threonine 3-dehydrogenase from burkholderia thailandensis
30% identity, 90% coverage: 19:334/352 of query aligns to 12:323/339 of 5kiaA
- active site: C37 (= C44), G38 (= G45), T39 (≠ S46), H42 (= H49), H61 (= H69), E62 (= E70), C91 (= C99), C94 (= C102), C97 (= C105), C105 (= C113), V109 (≠ R117), P147 (= P160), A151 (≠ C164)
- binding calcium ion: D146 (≠ E159), N150 (≠ V163), E288 (≠ Q297)
- binding zinc ion: C91 (= C99), C94 (= C102), C97 (= C105), C105 (= C113)
Sites not aligning to the query:
Query Sequence
>SM_b20445 FitnessBrowser__Smeli:SM_b20445
MSGAPTRTRFARLYGPRDLRLEVADVPAPGDGEVLLKMAAGGICGSDLHYYQDGGFGPVR
VREPIIPGHEASGRVAVLGAGVSGLAIDDLVAVNPSQPCGTCRFCGEGLPVHCLDMRFLG
SAMRLPHTQGMFRDWLVVPAVQCHPAGSQVSPGEAACAEPLAVCLHAAAQAGEIRGKKVL
VTGAGPIGALVVAAARHAGADEIVVTDLADAALDRAKAMGATRIVNVHRDPAGLAAYEAD
KGKFHVAFECSAAEPALRGAVAAVRPRGTIVQVGVTGEITLPLHALVGKELRLVGSQRFD
GEFALAVALISDRRIDVRPIISHQFPVDEAVRAFEQAGDRSAACKVQLTFLS
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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