SitesBLAST
Comparing WP_058932695.1 NCBI__GCF_001484605.1:WP_058932695.1 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)
3qe3A Sheep liver sorbitol dehydrogenase (see paper)
43% identity, 95% coverage: 14:341/345 of query aligns to 7:342/351 of 3qe3A
- active site: C39 (= C46), G40 (= G47), S41 (= S48), H44 (= H51), H64 (= H71), E65 (= E72), R94 (≠ C101), D97 (≠ C104), C100 (= C107), S108 (≠ C115), F112 (≠ E119), P151 (= P158), G155 (≠ A162), K339 (= K338)
- binding glycerol: Y45 (= Y52), F54 (= F61), T116 (= T123), R293 (= R292)
- binding zinc ion: C39 (= C46), H64 (= H71), E65 (= E72)
1e3jA Ketose reductase (sorbitol dehydrogenase) from silverleaf whitefly (see paper)
43% identity, 94% coverage: 12:335/345 of query aligns to 4:336/348 of 1e3jA
- active site: C38 (= C46), G39 (= G47), S40 (= S48), H43 (= H51), H63 (= H71), E64 (= E72), C93 (= C101), C96 (= C104), C99 (= C107), C107 (= C115), T111 (≠ E119), P150 (= P158), G154 (≠ A162)
- binding phosphate ion: A174 (= A182), A196 (≠ D205), R197 (≠ L206), S198 (≠ V207), R201 (≠ K210)
- binding zinc ion: C38 (= C46), H63 (= H71), E64 (= E72), C93 (= C101), C96 (= C104), C99 (= C107), C107 (= C115)
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)
42% identity, 98% coverage: 1:338/345 of query aligns to 1:345/357 of Q00796
- M1 (= M1) modified: Initiator methionine, Removed
- C45 (= C46) binding Zn(2+)
- H70 (= H71) binding Zn(2+)
- E71 (= E72) binding Zn(2+)
- R110 (≠ L111) to P: in HMNR8; results in protein aggregation
- H135 (≠ I136) to R: in HMNR8; results in protein aggregation
- A153 (= A154) to D: in HMNR8; uncertain significance; results in protein aggregation; dbSNP:rs145813597
- I184 (= I185) binding NAD(+)
- D204 (= D205) binding NAD(+)
- R209 (≠ K210) binding NAD(+)
- Q239 (vs. gap) to L: in dbSNP:rs1042079
- N269 (≠ H262) to T: in dbSNP:rs930337
- VGL 273:275 (= VGL 266:268) binding NAD(+)
- VFR 297:299 (≠ IFR 290:292) binding NAD(+)
- V322 (= V315) to I: in HMNR8; uncertain significance; dbSNP:rs149975952
1pl6A Human sdh/nadh/inhibitor complex (see paper)
44% identity, 94% coverage: 14:338/345 of query aligns to 12:344/356 of 1pl6A
- active site: C44 (= C46), G45 (= G47), S46 (= S48), H49 (= H51), H69 (= H71), E70 (= E72), R99 (≠ C101), D102 (≠ C104), C105 (= C107), S113 (≠ C115), F117 (≠ E119), P156 (= P158), G160 (≠ A162), K344 (= K338)
- binding 4-[2-(hydroxymethyl)pyrimidin-4-yl]-n,n-dimethylpiperazine-1-sulfonamide: C44 (= C46), S46 (= S48), I56 (= I58), F59 (= F61), H69 (= H71), E155 (= E157), L274 (= L268), F297 (= F291)
- binding nicotinamide-adenine-dinucleotide: G181 (= G183), P182 (= P184), I183 (= I185), D203 (= D205), L204 (= L206), R208 (≠ K210), C249 (≠ A243), T250 (≠ S244), V272 (= V266), G273 (= G267), L274 (= L268), F297 (= F291), R298 (= R292)
- binding zinc ion: C44 (= C46), H69 (= H71)
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, 95% coverage: 14:341/345 of query aligns to 11:345/354 of P07846
- C43 (= C46) binding Zn(2+)
- Y49 (= Y52) binding substrate
- H67 (= H71) binding Zn(2+)
- E68 (= E72) binding Zn(2+)
- E153 (= E157) binding substrate
- R296 (= R292) binding substrate
- Y297 (= Y293) binding substrate
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)
41% identity, 95% coverage: 14:341/345 of query aligns to 13:348/357 of P27867
- C45 (= C46) binding Zn(2+)
- H70 (= H71) binding Zn(2+)
- E71 (= E72) binding Zn(2+)
- E156 (= E157) binding Zn(2+)
- D204 (= D205) binding NAD(+)
- R209 (≠ K210) binding NAD(+)
- VGM 273:275 (≠ VGL 266:268) binding NAD(+)
- VFR 297:299 (≠ IFR 290:292) binding NAD(+)
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)
39% identity, 88% coverage: 35:336/345 of query aligns to 42:352/363 of Q7SI09
- C53 (= C46) binding Zn(2+)
- F59 (≠ Y52) mutation F->A,S,Y: No effect.
- H78 (= H71) binding Zn(2+)
- E79 (= E72) binding Zn(2+)
- C108 (= C101) binding Zn(2+)
- C111 (= C104) binding Zn(2+)
- C114 (= C107) binding Zn(2+)
- C122 (= C115) binding Zn(2+)
- E163 (= E157) binding Zn(2+)
- PI 190:191 (= PI 184:185) binding NAD(+)
- D211 (= D205) binding NAD(+)
- DI 211:212 (≠ DL 205:206) mutation to SR: Alters cofactor specificity from NAD to NADP; when associated with T-348.
- R216 (≠ K210) binding NAD(+)
- I282 (≠ V266) binding NAD(+)
- QYR 306:308 (≠ IFR 290:292) binding NAD(+)
- S348 (≠ Q332) mutation to T: Alters cofactor specificity from NAD to NADP; when associated with 211-SR-212.
3m6iA L-arabinitol 4-dehydrogenase (see paper)
39% identity, 88% coverage: 35:336/345 of query aligns to 38:348/358 of 3m6iA
- active site: C49 (= C46), G50 (= G47), S51 (= S48), H54 (= H51), H74 (= H71), E75 (= E72), C104 (= C101), C107 (= C104), C110 (= C107), C118 (= C115), D122 (≠ E119), P160 (= P158), A164 (= A162)
- binding nicotinamide-adenine-dinucleotide: C49 (= C46), V163 (= V161), G185 (= G183), P186 (= P184), I187 (= I185), D207 (= D205), R212 (≠ K210), C255 (≠ A243), T256 (≠ S244), I278 (≠ V266), G279 (= G267), V280 (≠ L268), R304 (= R292)
- binding zinc ion: C49 (= C46), H74 (= H71), C104 (= C101), C107 (= C104), C110 (= C107), C118 (= C115)
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, 88% coverage: 35:336/345 of query aligns to 55:366/377 of Q96V44
- D-I 224:225 (≠ DLV 205:207) mutation to SR: Alters cofactor specificity from NAD to NADP; when associated with T-362.
- A362 (≠ Q332) 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)
36% identity, 88% coverage: 35:336/345 of query aligns to 44:363/386 of A2QAC0
- M70 (≠ F61) mutation to F: Abolishes enzyme activity.
- DI 213:214 (≠ DL 205:206) 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 (≠ Q332) 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)
35% identity, 88% coverage: 35:336/345 of query aligns to 43:362/385 of B6HI95
- DI 212:213 (≠ D- 205) mutation to SR: Alters cofactor specificity from NAD to NADP; when associated with T-358.
- S358 (≠ Q332) mutation to T: Alters cofactor specificity from NAD to NADP; when associated with 212-SR-213.
7y9pA Xylitol dehydrogenase s96c/s99c/y102c mutant(thermostabilized form) from pichia stipitis (see paper)
35% identity, 92% coverage: 14:329/345 of query aligns to 7:341/357 of 7y9pA
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)
37% identity, 88% coverage: 28:329/345 of query aligns to 24:333/348 of O58389
- C42 (= C46) binding Zn(2+)
- T44 (≠ S48) mutation to A: Total loss of enzymatic activity.
- H67 (= H71) binding Zn(2+)
- E68 (= E72) binding Zn(2+)
- C97 (= C101) binding Zn(2+)
- C100 (= C104) binding Zn(2+)
- C103 (= C107) binding Zn(2+)
- C111 (= C115) binding Zn(2+)
- E152 (= E157) 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 (≠ I185) binding NAD(+)
- E199 (≠ D205) binding NAD(+); mutation to A: Large decrease in affinity for NAD(+).
- R204 (≠ K210) binding NAD(+); mutation to A: Large decrease in affinity for NAD(+).
- LGL 266:268 (≠ VGL 266:268) binding NAD(+)
- IT 291:292 (≠ IF 290:291) binding NAD(+)
- R294 (vs. gap) mutation to A: 4000-fold decrease in catalytic efficiency.
2dfvA Hyperthermophilic threonine dehydrogenase from pyrococcus horikoshii (see paper)
37% identity, 88% coverage: 28:329/345 of query aligns to 22:331/346 of 2dfvA
- active site: C40 (= C46), G41 (= G47), T42 (≠ S48), H45 (= H51), H65 (= H71), E66 (= E72), C95 (= C101), C98 (= C104), C101 (= C107), C109 (= C115), K113 (≠ E119), P151 (= P158), A155 (= A162)
- binding nicotinamide-adenine-dinucleotide: G175 (= G183), P176 (= P184), L177 (≠ I185), E197 (≠ D205), P198 (≠ L206), R202 (≠ K210), F241 (≠ A243), S242 (= S244), A244 (≠ S246), L264 (≠ V266), G265 (= G267), L266 (= L268), I289 (= I290), T290 (≠ F291)
- binding zinc ion: C95 (= C101), C101 (= C107), C109 (= C115)
Sites not aligning to the query:
3gfbA L-threonine dehydrogenase (tktdh) from the hyperthermophilic archaeon thermococcus kodakaraensis (see paper)
34% identity, 97% coverage: 10:345/345 of query aligns to 7:347/347 of 3gfbA
- active site: C40 (= C46), G41 (= G47), T42 (≠ S48), H45 (= H51), H65 (= H71), E66 (= E72), C95 (= C101), C98 (= C104), C101 (= C107), C109 (= C115), K113 (≠ E119), P151 (= P158), A155 (= A162), K340 (= K338)
- binding nicotinamide-adenine-dinucleotide: G173 (= G181), G175 (= G183), P176 (= P184), L177 (≠ I185), S196 (≠ T204), E197 (≠ D205), P198 (≠ L206), R202 (≠ K210), F241 (≠ A243), S242 (= S244), A244 (≠ S246), L264 (≠ V266), G265 (= G267), L266 (= L268), I289 (= I290), T290 (≠ F291)
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)
34% identity, 97% coverage: 10:345/345 of query aligns to 9:349/350 of Q5JI69
- L179 (≠ I185) binding NAD(+)
- E199 (≠ D205) binding NAD(+)
- R204 (≠ K210) binding NAD(+)
- LGL 266:268 (≠ VGL 266:268) binding NAD(+)
- IT 291:292 (≠ IF 290:291) binding NAD(+)
5vm2A Crystal structure of eck1772, an oxidoreductase/dehydrogenase of unknown specificity involved in membrane biogenesis from escherichia coli
34% identity, 90% coverage: 20:329/345 of query aligns to 13:329/347 of 5vm2A
- active site: C39 (= C46), G40 (= G47), S41 (= S48), H44 (= H51), H65 (= H71), E66 (= E72), C95 (= C101), C98 (= C104), C101 (= C107), C109 (= C115), D113 (≠ E119), P153 (= P158), G157 (≠ A162)
- binding magnesium ion: H65 (= H71), E66 (= E72), E152 (= E157)
- binding zinc ion: C95 (= C101), C98 (= C104), C101 (= C107), C109 (= C115)
Sites not aligning to the query:
6dkhC The crystal structure of l-idonate 5-dehydrogenase from escherichia coli str. K-12 substr. Mg1655
30% identity, 96% coverage: 11:342/345 of query aligns to 9:346/346 of 6dkhC
P07913 L-threonine 3-dehydrogenase; TDH; L-threonine dehydrogenase; EC 1.1.1.103 from Escherichia coli (strain K12) (see paper)
31% identity, 95% coverage: 13:341/345 of query aligns to 5:338/341 of P07913
- C38 (= C46) 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(+).
4ilkA Crystal structure of short chain alcohol dehydrogenase (rspb) from e. Coli cft073 (efi target efi-506413) complexed with cofactor nadh
31% identity, 94% coverage: 10:332/345 of query aligns to 4:327/337 of 4ilkA
- active site: C40 (= C46), G41 (= G47), S42 (= S48), H45 (= H51), H59 (= H71), E60 (= E72), C89 (= C101), C92 (= C104), C95 (= C107), C103 (= C115), A107 (≠ E119), P145 (= P158), A149 (= A162)
- binding manganese (ii) ion: C40 (= C46), H59 (= H71), E60 (= E72), E144 (= E157)
- binding 1,4-dihydronicotinamide adenine dinucleotide: G168 (= G181), G170 (= G183), P171 (= P184), I172 (= I185), D193 (= D205), R194 (≠ L206), R198 (≠ K210), N213 (vs. gap), A235 (= A243), A236 (≠ S244), C237 (≠ G245), I241 (≠ A249), M258 (≠ V266), F260 (≠ L268)
- binding zinc ion: C89 (= C101), C92 (= C104), C95 (= C107), C103 (= C115)
Sites not aligning to the query:
Query Sequence
>WP_058932695.1 NCBI__GCF_001484605.1:WP_058932695.1
MSTSNLPESMRTSVLVGVKNLTIEDRKLPAYGTDEVLVKIAAVGVCGSDVHYFRHGRIGD
FVVDGPLVLGHEVSGTIVAVGDSVDPSRVGQRVAIEPQRPCGKCRECRAGLYNLCPHMEF
YATPPIDGAFAEYAVIQDAFAHAIPDNLTDEAAALLEPLSVAITTMRKAHVVPGSSVLIA
GAGPIGIICAQTAKAFGAAEVIVTDLVAEKRERALKYGATRVIDPVEVDIANEGLDVNAF
IDASGSPRAVTAGIKAVRPAGHVVLVGLGNPEMTLPVEHIQNYEINVTGIFRYTDTWPAA
IHLVSSGLVELDSLVTGRFGLDQAEEALESDQDPASLKSVVYPSK
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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