SitesBLAST
Comparing SMc01564 FitnessBrowser__Smeli:SMc01564 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)
P07913 L-threonine 3-dehydrogenase; TDH; L-threonine dehydrogenase; EC 1.1.1.103 from Escherichia coli (strain K12) (see paper)
71% identity, 99% coverage: 5:344/344 of query aligns to 1:340/341 of P07913
- C38 (= C42) 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(+).
5kiaA Crystal structure of l-threonine 3-dehydrogenase from burkholderia thailandensis
65% identity, 99% coverage: 5:344/344 of query aligns to 2:338/339 of 5kiaA
- active site: C37 (= C42), G38 (= G43), T39 (= T44), H42 (= H47), H61 (= H67), E62 (= E68), C91 (= C97), C94 (= C100), C97 (= C103), C105 (= C111), V109 (≠ L115), P147 (= P153), A151 (= A157), K333 (= K339)
- binding calcium ion: D146 (= D152), N150 (= N156), E288 (= E294)
- binding zinc ion: C91 (= C97), C94 (= C100), C97 (= C103), C105 (= C111)
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)
44% identity, 99% coverage: 1:342/344 of query aligns to 1:345/348 of O58389
- C42 (= C42) binding
- T44 (= T44) mutation to A: Total loss of enzymatic activity.
- H67 (= H67) binding
- E68 (= E68) binding
- C97 (= C97) binding
- C100 (= C100) binding
- C103 (= C103) binding
- C111 (= C111) binding
- E152 (≠ D152) 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 (≠ I179) binding
- E199 (≠ D199) binding ; mutation to A: Large decrease in affinity for NAD(+).
- R204 (= R204) binding ; mutation to A: Large decrease in affinity for NAD(+).
- LGL 266:268 (≠ LGI 266:268) binding
- IT 291:292 (≠ IY 290:291) binding
- R294 (= R293) mutation to A: 4000-fold decrease in catalytic efficiency.
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)
44% identity, 99% coverage: 1:342/344 of query aligns to 1:345/350 of Q5JI69
2dfvA Hyperthermophilic threonine dehydrogenase from pyrococcus horikoshii (see paper)
44% identity, 98% coverage: 5:342/344 of query aligns to 3:343/346 of 2dfvA
- active site: C40 (= C42), G41 (= G43), T42 (= T44), H45 (= H47), H65 (= H67), E66 (= E68), C95 (= C97), C98 (= C100), C101 (= C103), C109 (= C111), K113 (≠ L115), P151 (= P153), A155 (= A157), K340 (= K339)
- binding nicotinamide-adenine-dinucleotide: G175 (= G177), P176 (= P178), L177 (≠ I179), E197 (≠ D199), P198 (≠ I200), R202 (= R204), F241 (≠ M243), S242 (= S244), A244 (= A246), L264 (= L266), G265 (= G267), L266 (≠ I268), I289 (= I290), T290 (≠ Y291)
- binding zinc ion: C95 (= C97), C101 (= C103), C109 (= C111)
3gfbA L-threonine dehydrogenase (tktdh) from the hyperthermophilic archaeon thermococcus kodakaraensis (see paper)
44% identity, 98% coverage: 5:342/344 of query aligns to 3:343/347 of 3gfbA
- active site: C40 (= C42), G41 (= G43), T42 (= T44), H45 (= H47), H65 (= H67), E66 (= E68), C95 (= C97), C98 (= C100), C101 (= C103), C109 (= C111), K113 (≠ L115), P151 (= P153), A155 (= A157), K340 (= K339)
- binding nicotinamide-adenine-dinucleotide: G173 (= G175), G175 (= G177), P176 (= P178), L177 (≠ I179), S196 (≠ T198), E197 (≠ D199), P198 (≠ I200), R202 (= R204), F241 (≠ M243), S242 (= S244), A244 (= A246), L264 (= L266), G265 (= G267), L266 (≠ I268), I289 (= I290), T290 (≠ Y291)
2ejvA Crystal structure of threonine 3-dehydrogenase complexed with NAD+
44% identity, 99% coverage: 5:343/344 of query aligns to 1:340/343 of 2ejvA
- active site: C38 (= C42), G39 (= G43), T40 (= T44), H43 (= H47), H63 (= H67), E64 (= E68), C93 (= C97), C96 (= C100), C99 (= C103), C107 (= C111), Q111 (≠ L115), P149 (= P153), A153 (= A157), K336 (= K339)
- binding nicotinamide-adenine-dinucleotide: G172 (= G175), G174 (= G177), P175 (= P178), I176 (= I179), S195 (≠ T198), D196 (= D199), P197 (≠ I200), R201 (= R204), F238 (≠ M243), S239 (= S244), N241 (≠ A246), A244 (= A249), L261 (= L266), G262 (= G267), I263 (= I268)
- binding zinc ion: C38 (= C42), H63 (= H67), E64 (= E68), C96 (= C100), C99 (= C103), C107 (= C111)
2dq4A Crystal structure of threonine 3-dehydrogenase
44% identity, 99% coverage: 5:343/344 of query aligns to 1:340/343 of 2dq4A
- active site: C38 (= C42), G39 (= G43), T40 (= T44), H43 (= H47), H63 (= H67), E64 (= E68), C93 (= C97), C96 (= C100), C99 (= C103), C107 (= C111), Q111 (≠ L115), P149 (= P153), A153 (= A157), K336 (= K339)
- binding zinc ion: C38 (= C42), H63 (= H67), E64 (= E68), C93 (= C97), C96 (= C100), C107 (= C111)
Q5SKS4 L-threonine 3-dehydrogenase; TDH; EC 1.1.1.103 from Thermus thermophilus (strain ATCC 27634 / DSM 579 / HB8)
44% identity, 99% coverage: 5:343/344 of query aligns to 1:340/343 of Q5SKS4
4ejmA Crystal structure of a putative zinc-binding dehydrogenase (target psi-012003) from sinorhizobium meliloti 1021 bound to NADP
31% identity, 94% coverage: 3:327/344 of query aligns to 2:325/342 of 4ejmA
- active site: C40 (= C42), G41 (= G43), T42 (= T44), H45 (= H47), H61 (= H67), E62 (= E68), C91 (= C97), C94 (= C100), C97 (= C103), C105 (= C111), R109 (≠ L115), P147 (= P153), C151 (≠ A157)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: G170 (= G175), G172 (= G177), V173 (≠ P178), I174 (= I179), T194 (≠ D199), R195 (≠ I200), Q196 (≠ N201), K199 (≠ R204), C240 (≠ M243), E245 (≠ P248), T246 (≠ A249), L263 (= L266), V265 (≠ I268), I291 (≠ G292)
- binding zinc ion: C91 (= C97), C94 (= C100), C97 (= C103), C105 (= C111)
Sites not aligning to the query:
4ej6A Crystal structure of a putative zinc-binding dehydrogenase (target psi-012003) from sinorhizobium meliloti 1021
31% identity, 94% coverage: 3:327/344 of query aligns to 2:325/343 of 4ej6A
- active site: C40 (= C42), G41 (= G43), T42 (= T44), H45 (= H47), H61 (= H67), E62 (= E68), C91 (= C97), C94 (= C100), C97 (= C103), C105 (= C111), R109 (≠ L115), P147 (= P153), C151 (≠ A157)
- binding zinc ion: C91 (= C97), C94 (= C100), C97 (= C103), C105 (= C111)
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)
29% identity, 95% coverage: 17:342/344 of query aligns to 20:348/357 of P27867
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)
29% identity, 95% coverage: 17:342/344 of query aligns to 20:348/357 of Q00796
- C45 (= C42) binding
- H70 (= H67) binding
- E71 (= E68) binding
- R110 (= R107) to P: in SORDD; results in protein aggregation
- H135 (≠ L131) to R: in SORDD; results in protein aggregation
- A153 (= A149) to D: in SORDD; uncertain significance; results in protein aggregation; dbSNP:rs145813597
- I184 (= I179) binding
- D204 (= D199) binding
- R209 (= R204) binding
- Q239 (≠ T234) to L: in dbSNP:rs1042079
- N269 (≠ K262) to T: in dbSNP:rs930337
- VGL 273:275 (≠ LGI 266:268) binding
- VF--R 297:299 (≠ IYGRE 290:294) binding
- V322 (≠ I316) to I: in SORDD; uncertain significance; dbSNP:rs149975952
Sites not aligning to the query:
- 1 modified: Initiator methionine, Removed
1pl6A Human sdh/nadh/inhibitor complex (see paper)
29% identity, 95% coverage: 17:342/344 of query aligns to 19:347/356 of 1pl6A
- active site: C44 (= C42), G45 (= G43), S46 (≠ T44), H49 (= H47), H69 (= H67), E70 (= E68), R99 (≠ C97), D102 (≠ C100), C105 (= C103), S113 (≠ C111), F117 (≠ L115), P156 (= P153), G160 (≠ A157), K344 (= K339)
- binding 4-[2-(hydroxymethyl)pyrimidin-4-yl]-n,n-dimethylpiperazine-1-sulfonamide: C44 (= C42), S46 (≠ T44), I56 (≠ W54), F59 (≠ K57), H69 (= H67), E155 (≠ D152), L274 (≠ I268), F297 (≠ Y291)
- binding nicotinamide-adenine-dinucleotide: G181 (= G177), P182 (= P178), I183 (= I179), D203 (= D199), L204 (≠ I200), R208 (= R204), C249 (≠ M243), T250 (≠ S244), V272 (≠ L266), G273 (= G267), L274 (≠ I268), F297 (≠ Y291), R298 (≠ E294)
- binding zinc ion: C44 (= C42), H69 (= H67)
7y9pA Xylitol dehydrogenase s96c/s99c/y102c mutant(thermostabilized form) from pichia stipitis (see paper)
31% identity, 93% coverage: 17:335/344 of query aligns to 14:346/357 of 7y9pA
3qe3A Sheep liver sorbitol dehydrogenase (see paper)
29% identity, 95% coverage: 17:342/344 of query aligns to 14:342/351 of 3qe3A
- active site: C39 (= C42), G40 (= G43), S41 (≠ T44), H44 (= H47), H64 (= H67), E65 (= E68), R94 (= R101), D97 (vs. gap), C100 (= C103), S108 (≠ R112), F112 (≠ G116), P151 (= P153), G155 (≠ A157), K339 (= K339)
- binding glycerol: Y45 (≠ I48), F54 (≠ K57), T116 (≠ N120), R293 (≠ E294)
- binding zinc ion: C39 (= C42), H64 (= H67), E65 (= E68)
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)
29% identity, 95% coverage: 17:342/344 of query aligns to 18:345/354 of P07846
- C43 (= C42) binding
- Y49 (≠ I48) binding
- H67 (= H67) binding
- E68 (= E68) binding
- E153 (≠ D152) binding
- R296 (≠ E294) binding
- Y297 (≠ M295) binding
1e3jA Ketose reductase (sorbitol dehydrogenase) from silverleaf whitefly (see paper)
29% identity, 95% coverage: 17:344/344 of query aligns to 13:346/348 of 1e3jA
- active site: C38 (= C42), G39 (= G43), S40 (≠ T44), H43 (= H47), H63 (= H67), E64 (= E68), C93 (= C97), C96 (= C100), C99 (= C103), C107 (= C111), T111 (= T114), P150 (= P153), G154 (≠ A157), K341 (= K339)
- binding phosphate ion: A174 (= A176), A196 (≠ D199), R197 (≠ I200), S198 (≠ N201), R201 (= R204)
- binding zinc ion: C38 (= C42), H63 (= H67), E64 (= E68), C93 (= C97), C96 (= C100), C99 (= C103), C107 (= C111)
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)
29% identity, 97% coverage: 9:340/344 of query aligns to 12:355/363 of Q7SI09
- C53 (= C42) binding
- F59 (≠ I48) mutation F->A,S,Y: No effect.
- H78 (= H67) binding
- E79 (= E68) binding
- C108 (= C97) binding
- C111 (= C100) binding
- C114 (= C103) binding
- C122 (= C111) binding
- E163 (≠ D152) binding
- PI 190:191 (= PI 178:179) binding
- D211 (= D199) binding
- DI 211:212 (= DI 199:200) mutation to SR: Alters cofactor specificity from NAD to NADP; when associated with T-348.
- R216 (= R204) binding
- I282 (≠ L266) binding
- QY--R 306:308 (≠ IYGRE 290:294) binding
- S348 (≠ R333) mutation to T: Alters cofactor specificity from NAD to NADP; when associated with 211-SR-212.
3m6iA L-arabinitol 4-dehydrogenase (see paper)
29% identity, 97% coverage: 9:340/344 of query aligns to 8:351/358 of 3m6iA
- active site: C49 (= C42), G50 (= G43), S51 (≠ T44), H54 (= H47), H74 (= H67), E75 (= E68), C104 (= C97), C107 (= C100), C110 (= C103), C118 (= C111), D122 (≠ L115), P160 (= P153), A164 (= A157)
- binding nicotinamide-adenine-dinucleotide: C49 (= C42), V163 (≠ N156), G185 (= G177), P186 (= P178), I187 (= I179), D207 (= D199), R212 (= R204), C255 (≠ M243), T256 (≠ S244), I278 (≠ L266), G279 (= G267), V280 (≠ I268), R304 (≠ E294)
- binding zinc ion: C49 (= C42), H74 (= H67), C104 (= C97), C107 (= C100), C110 (= C103), C118 (= C111)
Sites not aligning to the query:
Query Sequence
>SMc01564 FitnessBrowser__Smeli:SMc01564
MTNMMKALVKTKPEVGLWMERVPVPEIGPNDVLIRVRKSAICGTDVHIWNWDQWAEKTIP
VPMVVGHEFMGEVVEVGPAVSKHHVGERVSGEGHIVCGKCRNCRAGRGHLCRNTLGVGVN
RPGSFAEFVCLPEYNVVSIPDDVPDEIAAIFDPFGNAVHTALSFDLVGEDVLVTGAGPIG
IMGAMVAKRCGARKVVITDINPVRLDLARKLGIDHVVDASKEKLADVMRVIGMTEGFDVG
LEMSGAAPAFRDMIDKMNNGGKIAILGIAPAGFEIDWNKVIFKMLNLKGIYGREMFETWY
KMIAFVQGGLDLSPIITHRIGIDDFRDGFEAMRSGNSGKVVMDW
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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