SitesBLAST
Comparing WP_058931176.1 NCBI__GCF_001484605.1:WP_058931176.1 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)
3qe3A Sheep liver sorbitol dehydrogenase (see paper)
43% identity, 92% coverage: 24:349/353 of query aligns to 7:342/351 of 3qe3A
- active site: C39 (= C56), G40 (= G57), S41 (= S58), H44 (= H61), H64 (= H81), E65 (= E82), R94 (≠ C111), D97 (≠ C114), C100 (= C117), S108 (≠ C125), F112 (≠ E129), P151 (= P168), G155 (= G172), K339 (= K346)
- binding glycerol: Y45 (= Y62), F54 (≠ Y71), T116 (= T133), R293 (= R300)
- binding zinc ion: C39 (= C56), H64 (= H81), E65 (= E82)
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)
42% identity, 92% coverage: 24:349/353 of query aligns to 13:348/357 of P27867
- C45 (= C56) binding Zn(2+)
- H70 (= H81) binding Zn(2+)
- E71 (= E82) binding Zn(2+)
- E156 (= E167) binding Zn(2+)
- D204 (= D215) binding NAD(+)
- R209 (= R220) binding NAD(+)
- VGM 273:275 (≠ VGL 274:276) binding NAD(+)
- VFR 297:299 (= VFR 298:300) binding NAD(+)
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)
43% identity, 92% coverage: 24:349/353 of query aligns to 11:345/354 of P07846
- C43 (= C56) binding Zn(2+)
- Y49 (= Y62) binding substrate
- H67 (= H81) binding Zn(2+)
- E68 (= E82) binding Zn(2+)
- E153 (= E167) binding substrate
- R296 (= R300) binding substrate
- Y297 (= Y301) binding substrate
1e3jA Ketose reductase (sorbitol dehydrogenase) from silverleaf whitefly (see paper)
42% identity, 91% coverage: 22:341/353 of query aligns to 4:334/348 of 1e3jA
- active site: C38 (= C56), G39 (= G57), S40 (= S58), H43 (= H61), H63 (= H81), E64 (= E82), C93 (= C111), C96 (= C114), C99 (= C117), C107 (= C125), T111 (≠ E129), P150 (= P168), G154 (= G172)
- binding phosphate ion: A174 (= A192), A196 (≠ D215), R197 (≠ I216), S198 (≠ A217), R201 (= R220)
- binding zinc ion: C38 (= C56), H63 (= H81), E64 (= E82), C93 (= C111), C96 (= C114), C99 (= C117), C107 (= C125)
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)
41% identity, 92% coverage: 24:349/353 of query aligns to 13:348/357 of Q00796
- C45 (= C56) binding Zn(2+)
- H70 (= H81) binding Zn(2+)
- E71 (= E82) binding Zn(2+)
- R110 (= R121) to P: in HMNR8; results in protein aggregation
- H135 (≠ I146) to R: in HMNR8; results in protein aggregation
- A153 (= A164) to D: in HMNR8; uncertain significance; results in protein aggregation; dbSNP:rs145813597
- I184 (= I195) binding NAD(+)
- D204 (= D215) binding NAD(+)
- R209 (= R220) binding NAD(+)
- Q239 (vs. gap) to L: in dbSNP:rs1042079
- N269 (≠ R270) to T: in dbSNP:rs930337
- VGL 273:275 (= VGL 274:276) binding NAD(+)
- VFR 297:299 (= VFR 298:300) binding NAD(+)
- V322 (= V323) to I: in HMNR8; uncertain significance; dbSNP:rs149975952
Sites not aligning to the query:
- 1 modified: Initiator methionine, Removed
1pl6A Human sdh/nadh/inhibitor complex (see paper)
41% identity, 92% coverage: 24:349/353 of query aligns to 12:347/356 of 1pl6A
- active site: C44 (= C56), G45 (= G57), S46 (= S58), H49 (= H61), H69 (= H81), E70 (= E82), R99 (≠ C111), D102 (≠ C114), C105 (= C117), S113 (≠ C125), F117 (≠ E129), P156 (= P168), G160 (= G172), K344 (= K346)
- binding 4-[2-(hydroxymethyl)pyrimidin-4-yl]-n,n-dimethylpiperazine-1-sulfonamide: C44 (= C56), S46 (= S58), I56 (= I68), F59 (≠ Y71), H69 (= H81), E155 (= E167), L274 (= L276), F297 (= F299)
- binding nicotinamide-adenine-dinucleotide: G181 (= G193), P182 (= P194), I183 (= I195), D203 (= D215), L204 (≠ I216), R208 (= R220), C249 (≠ A251), T250 (≠ S252), V272 (= V274), G273 (= G275), L274 (= L276), F297 (= F299), R298 (= R300)
- binding zinc ion: C44 (= C56), H69 (= H81)
7y9pA Xylitol dehydrogenase s96c/s99c/y102c mutant(thermostabilized form) from pichia stipitis (see paper)
38% identity, 90% coverage: 24:342/353 of query aligns to 7:349/357 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)
40% identity, 86% coverage: 45:346/353 of query aligns to 42:351/363 of Q7SI09
- C53 (= C56) binding Zn(2+)
- F59 (≠ Y62) mutation F->A,S,Y: No effect.
- H78 (= H81) binding Zn(2+)
- E79 (= E82) binding Zn(2+)
- C108 (= C111) binding Zn(2+)
- C111 (= C114) binding Zn(2+)
- C114 (= C117) binding Zn(2+)
- C122 (= C125) binding Zn(2+)
- E163 (= E167) binding Zn(2+)
- PI 190:191 (= PI 194:195) binding NAD(+)
- D211 (= D215) binding NAD(+)
- DI 211:212 (= DI 215:216) mutation to SR: Alters cofactor specificity from NAD to NADP; when associated with T-348.
- R216 (= R220) binding NAD(+)
- I282 (≠ V274) binding NAD(+)
- QYR 306:308 (≠ VFR 298:300) binding NAD(+)
- S348 (≠ G343) mutation to T: Alters cofactor specificity from NAD to NADP; when associated with 211-SR-212.
3m6iA L-arabinitol 4-dehydrogenase (see paper)
40% identity, 86% coverage: 45:346/353 of query aligns to 38:347/358 of 3m6iA
- active site: C49 (= C56), G50 (= G57), S51 (= S58), H54 (= H61), H74 (= H81), E75 (= E82), C104 (= C111), C107 (= C114), C110 (= C117), C118 (= C125), D122 (≠ E129), P160 (= P168), A164 (≠ G172)
- binding nicotinamide-adenine-dinucleotide: C49 (= C56), V163 (= V171), G185 (= G193), P186 (= P194), I187 (= I195), D207 (= D215), R212 (= R220), C255 (≠ A251), T256 (≠ S252), I278 (≠ V274), G279 (= G275), V280 (≠ L276), R304 (= R300)
- binding zinc ion: C49 (= C56), H74 (= H81), C104 (= C111), C107 (= C114), C110 (= C117), C118 (= C125)
Sites not aligning to the query:
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)
40% identity, 86% coverage: 43:346/353 of query aligns to 41:361/385 of B6HI95
- DI 212:213 (= DI 215:216) mutation to SR: Alters cofactor specificity from NAD to NADP; when associated with T-358.
- S358 (≠ G343) mutation to T: Alters cofactor specificity from NAD to NADP; when associated with 212-SR-213.
5vm2A Crystal structure of eck1772, an oxidoreductase/dehydrogenase of unknown specificity involved in membrane biogenesis from escherichia coli
36% identity, 89% coverage: 23:337/353 of query aligns to 6:329/347 of 5vm2A
- active site: C39 (= C56), G40 (= G57), S41 (= S58), H44 (= H61), H65 (= H81), E66 (= E82), C95 (= C111), C98 (= C114), C101 (= C117), C109 (= C125), D113 (≠ E129), P153 (= P168), G157 (= G172)
- binding magnesium ion: H65 (= H81), E66 (= E82), E152 (= E167)
- binding zinc ion: C95 (= C111), C98 (= C114), C101 (= C117), C109 (= C125)
Sites not aligning to the query:
Q96V44 L-arabinitol 4-dehydrogenase; LAD; EC 1.1.1.12 from Hypocrea jecorina (Trichoderma reesei) (see paper)
37% identity, 86% coverage: 45:349/353 of query aligns to 55:373/377 of Q96V44
- DI 224:225 (= DI 215:216) mutation to SR: Alters cofactor specificity from NAD to NADP; when associated with T-362.
- A362 (= A338) mutation to T: Alters cofactor specificity from NAD to NADP; when associated with 224-SR-225.
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)
39% identity, 86% coverage: 45:346/353 of query aligns to 44:362/386 of A2QAC0
- M70 (≠ Y71) mutation to F: Abolishes enzyme activity.
- DI 213:214 (= DI 215:216) mutation to SR: Alters cofactor specificity from NAD to NADP; when associated with T-359.
- Y318 (≠ F299) mutation to F: Increases affinity for D-sorbitol.
- A359 (≠ G343) mutation to T: Alters cofactor specificity from NAD to NADP; when associated with 213-SR-214.
6dkhC The crystal structure of l-idonate 5-dehydrogenase from escherichia coli str. K-12 substr. Mg1655
30% identity, 84% coverage: 42:337/353 of query aligns to 29:331/346 of 6dkhC
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, 90% coverage: 38:353/353 of query aligns to 24:349/350 of Q5JI69
- L179 (≠ I195) binding NAD(+)
- E199 (≠ D215) binding NAD(+)
- R204 (= R220) binding NAD(+)
- LGL 266:268 (≠ VGL 274:276) binding NAD(+)
- IT 291:292 (≠ IQ 288:289) binding NAD(+)
P07913 L-threonine 3-dehydrogenase; TDH; L-threonine dehydrogenase; EC 1.1.1.103 from Escherichia coli (strain K12) (see paper)
31% identity, 93% coverage: 20:349/353 of query aligns to 1:337/341 of P07913
- C38 (= C56) 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(+).
3gfbA L-threonine dehydrogenase (tktdh) from the hyperthermophilic archaeon thermococcus kodakaraensis (see paper)
32% identity, 90% coverage: 38:353/353 of query aligns to 22:347/347 of 3gfbA
- active site: C40 (= C56), G41 (= G57), T42 (≠ S58), H45 (= H61), H65 (= H81), E66 (= E82), C95 (= C111), C98 (= C114), C101 (= C117), C109 (= C125), K113 (≠ E129), P151 (= P168), A155 (≠ G172), K340 (= K346)
- binding nicotinamide-adenine-dinucleotide: G173 (= G191), G175 (= G193), P176 (= P194), L177 (≠ I195), S196 (≠ T214), E197 (≠ D215), P198 (≠ I216), R202 (= R220), F241 (≠ A251), S242 (= S252), A244 (= A254), L264 (≠ V274), G265 (= G275), L266 (= L276), I289 (= I288), T290 (≠ Q289)
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)
32% identity, 86% coverage: 38:340/353 of query aligns to 24:339/348 of O58389
- C42 (= C56) binding Zn(2+)
- T44 (≠ S58) mutation to A: Total loss of enzymatic activity.
- H67 (= H81) binding Zn(2+)
- E68 (= E82) binding Zn(2+)
- C97 (= C111) binding Zn(2+)
- C100 (= C114) binding Zn(2+)
- C103 (= C117) binding Zn(2+)
- C111 (= C125) binding Zn(2+)
- E152 (= E167) 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 (≠ I195) binding NAD(+)
- E199 (≠ D215) binding NAD(+); mutation to A: Large decrease in affinity for NAD(+).
- R204 (= R220) binding NAD(+); mutation to A: Large decrease in affinity for NAD(+).
- LGL 266:268 (≠ VGL 274:276) binding NAD(+)
- IT 291:292 (≠ IQ 288:289) binding NAD(+)
- R294 (= R291) mutation to A: 4000-fold decrease in catalytic efficiency.
2dfvA Hyperthermophilic threonine dehydrogenase from pyrococcus horikoshii (see paper)
32% identity, 86% coverage: 38:340/353 of query aligns to 22:337/346 of 2dfvA
- active site: C40 (= C56), G41 (= G57), T42 (≠ S58), H45 (= H61), H65 (= H81), E66 (= E82), C95 (= C111), C98 (= C114), C101 (= C117), C109 (= C125), K113 (≠ E129), P151 (= P168), A155 (≠ G172)
- binding nicotinamide-adenine-dinucleotide: G175 (= G193), P176 (= P194), L177 (≠ I195), E197 (≠ D215), P198 (≠ I216), R202 (= R220), F241 (≠ A251), S242 (= S252), A244 (= A254), L264 (≠ V274), G265 (= G275), L266 (= L276), I289 (= I288), T290 (≠ Q289)
- binding zinc ion: C95 (= C111), C101 (= C117), C109 (= C125)
Sites not aligning to the query:
4ej6A Crystal structure of a putative zinc-binding dehydrogenase (target psi-012003) from sinorhizobium meliloti 1021
31% identity, 95% coverage: 18:351/353 of query aligns to 2:342/343 of 4ej6A
- active site: C40 (= C56), G41 (= G57), T42 (≠ S58), H45 (= H61), H61 (= H81), E62 (= E82), C91 (= C111), C94 (= C114), C97 (= C117), C105 (= C125), R109 (≠ E129), P147 (= P168), C151 (≠ G172), K337 (= K346)
- binding zinc ion: C91 (= C111), C94 (= C114), C97 (= C117), C105 (= C125)
Query Sequence
>WP_058931176.1 NCBI__GCF_001484605.1:WP_058931176.1
MTTPTAQSTTLAPAELPATMRASVLKRQGDMVMETLPLPQPDADQVLVQVAAVGVCGSDV
HYYEHGRIGDYVVDHPLILGHELSGRIAAVGSAVDPARIGNRVAVEPQRPCRTCKQCKAG
RYNLCPDIEFYATPPIDGAFAEYVTIQSDFAYDIPDSVSDEAAALIEPLSVGLWACERAE
IKPGSRVLIAGAGPIGIIAAQAARAFGATEIYITDIAEDRLAFALEHGATHALNAKTDSV
EGLDVDAFIDASGAPQAVRSGIKAVGPAGRVILVGLGADDVELPVSYIQNREIWLSGVFR
YTNTWPLAIQLIADGKVDLDILVTGKFTLAESEEALKAGKQAGQLKAVVYPGR
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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