SitesBLAST
Comparing HSERO_RS05485 HSERO_RS05485 phosphoesterase 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
44% identity, 91% coverage: 30:344/345 of query aligns to 35:346/346 of 6dkhC
3qe3A Sheep liver sorbitol dehydrogenase (see paper)
36% identity, 99% coverage: 5:345/345 of query aligns to 6:345/351 of 3qe3A
- active site: C39 (= C38), G40 (= G39), S41 (= S40), H44 (= H43), H64 (= H63), E65 (= E64), R94 (≠ C93), D97 (≠ C96), C100 (= C99), S108 (≠ C107), F112 (≠ R111), P151 (= P154), G155 (≠ A158), K339 (= K339)
- binding glycerol: Y45 (= Y44), F54 (≠ V53), T116 (= T119), R293 (= R292)
- binding zinc ion: C39 (= C38), H64 (= H63), E65 (= E64)
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)
36% identity, 99% coverage: 5:345/345 of query aligns to 12:351/357 of P27867
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, 99% coverage: 5:345/345 of query aligns to 10:348/354 of P07846
- C43 (= C38) binding
- Y49 (= Y44) binding
- H67 (= H63) binding
- E68 (= E64) binding
- E153 (= E153) binding
- R296 (= R292) binding
- Y297 (≠ F293) binding
1pl6A Human sdh/nadh/inhibitor complex (see paper)
35% identity, 94% coverage: 5:329/345 of query aligns to 11:335/356 of 1pl6A
- active site: C44 (= C38), G45 (= G39), S46 (= S40), H49 (= H43), H69 (= H63), E70 (= E64), R99 (≠ C93), D102 (≠ C96), C105 (= C99), S113 (≠ C107), F117 (≠ R111), P156 (= P154), G160 (≠ A158)
- binding 4-[2-(hydroxymethyl)pyrimidin-4-yl]-n,n-dimethylpiperazine-1-sulfonamide: C44 (= C38), S46 (= S40), I56 (≠ F50), F59 (≠ V53), H69 (= H63), E155 (= E153), L274 (= L269), F297 (= F291)
- binding nicotinamide-adenine-dinucleotide: G181 (= G179), P182 (= P180), I183 (= I181), D203 (= D201), L204 (≠ V202), R208 (≠ P206), C249 (≠ A244), T250 (≠ S245), V272 (= V267), G273 (= G268), L274 (= L269), F297 (= F291), R298 (= R292)
- binding zinc ion: C44 (= C38), H69 (= H63)
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)
35% identity, 94% coverage: 5:329/345 of query aligns to 12:336/357 of Q00796
- C45 (= C38) binding
- H70 (= H63) binding
- E71 (= E64) binding
- R110 (≠ K103) to P: in SORDD; results in protein aggregation
- H135 (≠ I132) to R: in SORDD; results in protein aggregation
- A153 (= A150) to D: in SORDD; uncertain significance; results in protein aggregation; dbSNP:rs145813597
- I184 (= I181) binding
- D204 (= D201) binding
- R209 (≠ P206) binding
- Q239 (≠ A233) to L: in dbSNP:rs1042079
- N269 (≠ I263) to T: in dbSNP:rs930337
- VGL 273:275 (= VGL 267:269) binding
- VFR 297:299 (≠ AFR 290:292) binding
- V322 (≠ I315) to I: in SORDD; uncertain significance; dbSNP:rs149975952
Sites not aligning to the query:
- 1 modified: Initiator methionine, Removed
1e3jA Ketose reductase (sorbitol dehydrogenase) from silverleaf whitefly (see paper)
33% identity, 98% coverage: 6:343/345 of query aligns to 6:345/348 of 1e3jA
- active site: C38 (= C38), G39 (= G39), S40 (= S40), H43 (= H43), H63 (= H63), E64 (= E64), C93 (= C93), C96 (= C96), C99 (= C99), C107 (= C107), T111 (≠ R111), P150 (= P154), G154 (≠ A158), K341 (= K339)
- binding phosphate ion: A174 (≠ C178), A196 (≠ D201), R197 (≠ V202), S198 (≠ A203), R201 (≠ P206)
- binding zinc ion: C38 (= C38), H63 (= H63), E64 (= E64), C93 (= C93), C96 (= C96), C99 (= C99), C107 (= C107)
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)
29% identity, 98% coverage: 4:342/345 of query aligns to 13:370/386 of A2QAC0
- M70 (≠ V53) mutation to F: Abolishes enzyme activity.
- DI 213:214 (≠ DV 201:202) mutation to SR: Alters cofactor specificity from NAD to NADP; when associated with T-359.
- Y318 (≠ F291) mutation to F: Increases affinity for D-sorbitol.
- A359 (≠ G332) mutation to T: Alters cofactor specificity from NAD to NADP; when associated with 213-SR-214.
7y9pA Xylitol dehydrogenase s96c/s99c/y102c mutant(thermostabilized form) from pichia stipitis (see paper)
32% identity, 94% coverage: 5:330/345 of query aligns to 6:342/357 of 7y9pA
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)
31% identity, 98% coverage: 4:342/345 of query aligns to 11:359/363 of Q7SI09
- C53 (= C38) binding
- F59 (≠ Y44) mutation F->A,S,Y: No effect.
- H78 (= H63) binding
- E79 (= E64) binding
- C108 (= C93) binding
- C111 (= C96) binding
- C114 (= C99) binding
- C122 (= C107) binding
- E163 (= E153) binding
- PI 190:191 (= PI 180:181) binding
- D211 (= D201) binding
- DI 211:212 (≠ DV 201:202) mutation to SR: Alters cofactor specificity from NAD to NADP; when associated with T-348.
- R216 (≠ P206) binding
- I282 (≠ V267) binding
- QYR 306:308 (≠ AFR 290:292) binding
- S348 (≠ G332) mutation to T: Alters cofactor specificity from NAD to NADP; when associated with 211-SR-212.
3m6iA L-arabinitol 4-dehydrogenase (see paper)
31% identity, 98% coverage: 4:342/345 of query aligns to 7:355/358 of 3m6iA
- active site: C49 (= C38), G50 (= G39), S51 (= S40), H54 (= H43), H74 (= H63), E75 (= E64), C104 (= C93), C107 (= C96), C110 (= C99), C118 (= C107), D122 (≠ R111), P160 (= P154), A164 (= A158), K352 (= K339)
- binding nicotinamide-adenine-dinucleotide: C49 (= C38), V163 (= V157), G185 (= G179), P186 (= P180), I187 (= I181), D207 (= D201), R212 (≠ P206), C255 (≠ A244), T256 (≠ S245), I278 (≠ V267), G279 (= G268), V280 (≠ L269), R304 (= R292)
- binding zinc ion: C49 (= C38), H74 (= H63), C104 (= C93), C107 (= C96), C110 (= C99), C118 (= C107)
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)
30% identity, 98% coverage: 4:342/345 of query aligns to 12:369/385 of B6HI95
- DI 212:213 (≠ DV 201:202) mutation to SR: Alters cofactor specificity from NAD to NADP; when associated with T-358.
- S358 (≠ G332) 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)
30% identity, 98% coverage: 4:342/345 of query aligns to 24:373/377 of Q96V44
- DI 224:225 (≠ DV 201:202) mutation to SR: Alters cofactor specificity from NAD to NADP; when associated with T-362.
- A362 (≠ G332) mutation to T: Alters cofactor specificity from NAD to NADP; when associated with 224-SR-225.
5vm2A Crystal structure of eck1772, an oxidoreductase/dehydrogenase of unknown specificity involved in membrane biogenesis from escherichia coli
30% identity, 96% coverage: 6:336/345 of query aligns to 7:336/347 of 5vm2A
- active site: C39 (= C38), G40 (= G39), S41 (= S40), H44 (= H43), H65 (= H63), E66 (= E64), C95 (= C93), C98 (= C96), C101 (= C99), C109 (= C107), D113 (≠ R111), P153 (= P154), G157 (≠ A158)
- binding magnesium ion: H65 (= H63), E66 (= E64), E152 (= E153)
- binding zinc ion: C95 (= C93), C98 (= C96), C101 (= C99), C109 (= C107)
Sites not aligning to the query:
3gfbA L-threonine dehydrogenase (tktdh) from the hyperthermophilic archaeon thermococcus kodakaraensis (see paper)
32% identity, 89% coverage: 25:330/345 of query aligns to 27:332/347 of 3gfbA
- active site: C40 (= C38), G41 (= G39), T42 (≠ S40), H45 (= H43), H65 (= H63), E66 (= E64), C95 (= C93), C98 (= C96), C101 (= C99), C109 (= C107), K113 (≠ R111), P151 (= P154), A155 (= A158)
- binding nicotinamide-adenine-dinucleotide: G173 (= G177), G175 (= G179), P176 (= P180), L177 (≠ I181), S196 (≠ T200), E197 (≠ D201), P198 (≠ V202), R202 (≠ P206), F241 (≠ A244), S242 (= S245), A244 (≠ N247), L264 (≠ V267), G265 (= G268), L266 (= L269), I289 (≠ A290), T290 (≠ F291)
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, 89% coverage: 25:330/345 of query aligns to 29:334/350 of Q5JI69
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)
31% identity, 89% coverage: 25:330/345 of query aligns to 29:334/348 of O58389
- C42 (= C38) binding
- T44 (≠ S40) mutation to A: Total loss of enzymatic activity.
- H67 (= H63) binding
- E68 (= E64) binding
- C97 (= C93) binding
- C100 (= C96) binding
- C103 (= C99) binding
- C111 (= C107) binding
- E152 (= E153) 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 (≠ I181) binding
- E199 (≠ D201) binding ; mutation to A: Large decrease in affinity for NAD(+).
- R204 (≠ P206) binding ; mutation to A: Large decrease in affinity for NAD(+).
- LGL 266:268 (≠ VGL 267:269) binding
- IT 291:292 (≠ AF 290:291) binding
- R294 (≠ F293) mutation to A: 4000-fold decrease in catalytic efficiency.
2dfvA Hyperthermophilic threonine dehydrogenase from pyrococcus horikoshii (see paper)
31% identity, 89% coverage: 25:330/345 of query aligns to 27:332/346 of 2dfvA
- active site: C40 (= C38), G41 (= G39), T42 (≠ S40), H45 (= H43), H65 (= H63), E66 (= E64), C95 (= C93), C98 (= C96), C101 (= C99), C109 (= C107), K113 (≠ R111), P151 (= P154), A155 (= A158)
- binding nicotinamide-adenine-dinucleotide: G175 (= G179), P176 (= P180), L177 (≠ I181), E197 (≠ D201), P198 (≠ V202), R202 (≠ P206), F241 (≠ A244), S242 (= S245), A244 (≠ N247), L264 (≠ V267), G265 (= G268), L266 (= L269), I289 (≠ A290), T290 (≠ F291)
- binding zinc ion: C95 (= C93), C101 (= C99), C109 (= C107)
Sites not aligning to the query:
4ilkA Crystal structure of short chain alcohol dehydrogenase (rspb) from e. Coli cft073 (efi target efi-506413) complexed with cofactor nadh
30% identity, 99% coverage: 3:344/345 of query aligns to 5:337/337 of 4ilkA
- active site: C40 (= C38), G41 (= G39), S42 (= S40), H45 (= H43), H59 (= H63), E60 (= E64), C89 (= C93), C92 (= C96), C95 (= C99), C103 (= C107), A107 (≠ R111), P145 (= P154), A149 (= A158), K332 (= K339)
- binding manganese (ii) ion: C40 (= C38), H59 (= H63), E60 (= E64), E144 (= E153)
- binding 1,4-dihydronicotinamide adenine dinucleotide: G168 (= G177), G170 (= G179), P171 (= P180), I172 (= I181), D193 (= D201), R194 (≠ V202), R198 (≠ P206), N213 (≠ M221), A235 (= A244), A236 (≠ S245), C237 (≠ G246), I241 (≠ A250), M258 (≠ V267), F260 (≠ L269)
- binding zinc ion: C89 (= C93), C92 (= C96), C95 (= C99), C103 (= C107)
P07913 L-threonine 3-dehydrogenase; TDH; L-threonine dehydrogenase; EC 1.1.1.103 from Escherichia coli (strain K12) (see paper)
29% identity, 94% coverage: 23:345/345 of query aligns to 23:341/341 of P07913
- C38 (= C38) 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(+).
Query Sequence
>HSERO_RS05485 HSERO_RS05485 phosphoesterase
MQQGLVIHAPHDLRIQALDTGALQPQQLKVKVKAGGICGSDLHYYHHGGFGVVRIKEPMV
LGHEVSGQIAEVGTAVTDIAPGTRIAISPSRPCGACKYCQEGKQNHCLDMRFYGSAMRTP
HVQGAFRQEIIIERSQAHVVADHVSDGEAAMAEPLSVALHAVRRAGPLVGKRVLVTGCGP
IGALVVVAARRAGALEVVVTDVASMPLQAALQVGADSAINMAETPAALKAYAADKGTFDV
LFEASGNERALVGALEALRPQAIIVQVGLGGDIQFPANLLVGKELEWRGAFRFHEEFAMA
VELMNRKLVDVKPLITATYPIAQAVEAFEIAGDRSRMMKVQISFD
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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