SitesBLAST
Comparing 15894 FitnessBrowser__Keio:15894 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)
2ejvA Crystal structure of threonine 3-dehydrogenase complexed with NAD+
31% identity, 98% coverage: 1:352/358 of query aligns to 1:339/343 of 2ejvA
- active site: C38 (= C39), G39 (= G40), T40 (≠ A41), H43 (≠ K44), H63 (= H61), E64 (= E62), C93 (= C92), C96 (= C95), C99 (= C98), C107 (= C106), Q111 (≠ V110), P149 (= P158), A153 (= A162), K336 (= K349)
- binding nicotinamide-adenine-dinucleotide: G172 (= G182), G174 (= G184), P175 (= P185), I176 (≠ L186), S195 (≠ Q208), D196 (≠ E209), P197 (≠ D210), R201 (= R214), F238 (≠ C253), S239 (= S254), N241 (≠ A256), A244 (= A259), L261 (≠ V276), G262 (= G277), I263 (≠ M278)
- binding zinc ion: C38 (= C39), H63 (= H61), E64 (= E62), C96 (= C95), C99 (= C98), C107 (= C106)
2dq4A Crystal structure of threonine 3-dehydrogenase
31% identity, 98% coverage: 1:352/358 of query aligns to 1:339/343 of 2dq4A
- active site: C38 (= C39), G39 (= G40), T40 (≠ A41), H43 (≠ K44), H63 (= H61), E64 (= E62), C93 (= C92), C96 (= C95), C99 (= C98), C107 (= C106), Q111 (≠ V110), P149 (= P158), A153 (= A162), K336 (= K349)
- binding zinc ion: C38 (= C39), H63 (= H61), E64 (= E62), C93 (= C92), C96 (= C95), C107 (= C106)
Q5SKS4 L-threonine 3-dehydrogenase; TDH; EC 1.1.1.103 from Thermus thermophilus (strain ATCC 27634 / DSM 579 / HB8)
31% identity, 98% coverage: 1:352/358 of query aligns to 1:339/343 of Q5SKS4
P07913 L-threonine 3-dehydrogenase; TDH; L-threonine dehydrogenase; EC 1.1.1.103 from Escherichia coli (strain K12) (see paper)
31% identity, 99% coverage: 1:355/358 of query aligns to 1:341/341 of P07913
- C38 (= C39) 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(+).
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)
30% identity, 94% coverage: 17:352/358 of query aligns to 22:345/348 of O58389
- C42 (= C39) binding
- T44 (≠ A41) mutation to A: Total loss of enzymatic activity.
- H67 (= H61) binding
- E68 (= E62) binding
- C97 (= C92) binding
- C100 (= C95) binding
- C103 (= C98) binding
- C111 (= C106) binding
- E152 (≠ D157) 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 (= L186) binding
- E199 (= E209) binding ; mutation to A: Large decrease in affinity for NAD(+).
- R204 (= R214) binding ; mutation to A: Large decrease in affinity for NAD(+).
- LGL 266:268 (≠ VGM 276:278) binding
- IT 291:292 (≠ II 297:298) binding
- R294 (≠ H300) mutation to A: 4000-fold decrease in catalytic efficiency.
2dfvA Hyperthermophilic threonine dehydrogenase from pyrococcus horikoshii (see paper)
30% identity, 94% coverage: 17:352/358 of query aligns to 20:343/346 of 2dfvA
- active site: C40 (= C39), G41 (= G40), T42 (≠ A41), H45 (≠ K44), H65 (= H61), E66 (= E62), C95 (= C92), C98 (= C95), C101 (= C98), C109 (= C106), K113 (≠ V110), P151 (= P158), A155 (= A162), K340 (= K349)
- binding nicotinamide-adenine-dinucleotide: G175 (= G184), P176 (= P185), L177 (= L186), E197 (= E209), P198 (≠ D210), R202 (= R214), F241 (≠ C253), S242 (= S254), A244 (= A256), L264 (≠ V276), G265 (= G277), L266 (≠ M278), I289 (= I297), T290 (≠ I298)
- binding zinc ion: C95 (= C92), C101 (= C98), C109 (= C106)
5kiaA Crystal structure of l-threonine 3-dehydrogenase from burkholderia thailandensis
31% identity, 99% coverage: 1:354/358 of query aligns to 2:338/339 of 5kiaA
- active site: C37 (= C39), G38 (= G40), T39 (≠ A41), H42 (≠ K44), H61 (= H61), E62 (= E62), C91 (= C92), C94 (= C95), C97 (= C98), C105 (= C106), V109 (= V110), P147 (= P158), A151 (= A162), K333 (= K349)
- binding calcium ion: D146 (= D157), N150 (= N161), E288 (≠ M301)
- binding zinc ion: C91 (= C92), C94 (= C95), C97 (= C98), C105 (= C106)
3gfbA L-threonine dehydrogenase (tktdh) from the hyperthermophilic archaeon thermococcus kodakaraensis (see paper)
29% identity, 98% coverage: 1:352/358 of query aligns to 3:343/347 of 3gfbA
- active site: C40 (= C39), G41 (= G40), T42 (≠ A41), H45 (≠ K44), H65 (= H61), E66 (= E62), C95 (= C92), C98 (= C95), C101 (= C98), C109 (= C106), K113 (≠ V110), P151 (= P158), A155 (= A162), K340 (= K349)
- binding nicotinamide-adenine-dinucleotide: G173 (= G182), G175 (= G184), P176 (= P185), L177 (= L186), S196 (≠ Q208), E197 (= E209), P198 (≠ D210), R202 (= R214), F241 (≠ C253), S242 (= S254), A244 (= A256), L264 (≠ V276), G265 (= G277), L266 (≠ M278), I289 (= I297), T290 (≠ I298)
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)
29% identity, 98% coverage: 1:352/358 of query aligns to 5:345/350 of Q5JI69
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)
28% identity, 97% coverage: 12:358/358 of query aligns to 18:354/357 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)
27% identity, 96% coverage: 12:355/358 of query aligns to 18:351/357 of Q00796
- C45 (= C39) binding
- H70 (= H61) binding
- E71 (= E62) binding
- R110 (≠ K109) to P: in SORDD; results in protein aggregation
- H135 (= H139) to R: in SORDD; results in protein aggregation
- A153 (= A154) to D: in SORDD; uncertain significance; results in protein aggregation; dbSNP:rs145813597
- I184 (≠ L186) binding
- D204 (≠ G206) binding
- R209 (= R214) binding
- Q239 (≠ K244) to L: in dbSNP:rs1042079
- N269 (≠ E272) to T: in dbSNP:rs930337
- VGL 273:275 (≠ VGM 276:278) binding
- VFR 297:299 (≠ HMA 300:302) binding
- V322 (≠ I326) to I: in SORDD; uncertain significance; dbSNP:rs149975952
Sites not aligning to the query:
- 1 modified: Initiator methionine, Removed
4ejmA Crystal structure of a putative zinc-binding dehydrogenase (target psi-012003) from sinorhizobium meliloti 1021 bound to NADP
30% identity, 89% coverage: 15:334/358 of query aligns to 18:322/342 of 4ejmA
- active site: C40 (= C39), G41 (= G40), T42 (≠ A41), H45 (≠ K44), H61 (= H61), E62 (= E62), C91 (= C92), C94 (= C95), C97 (= C98), C105 (= C106), R109 (≠ V110), P147 (= P158), C151 (≠ A162)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: G170 (= G182), G172 (= G184), V173 (≠ P185), I174 (≠ L186), T194 (≠ G206), R195 (≠ L207), Q196 (= Q208), K199 (≠ R214), C240 (= C253), E245 (≠ I258), T246 (≠ A259), L263 (≠ V276), V265 (vs. gap), I291 (= I297)
- binding zinc ion: C91 (= C92), C94 (= C95), C97 (= C98), C105 (= C106)
Sites not aligning to the query:
4ej6A Crystal structure of a putative zinc-binding dehydrogenase (target psi-012003) from sinorhizobium meliloti 1021
30% identity, 89% coverage: 15:334/358 of query aligns to 18:322/343 of 4ej6A
- active site: C40 (= C39), G41 (= G40), T42 (≠ A41), H45 (≠ K44), H61 (= H61), E62 (= E62), C91 (= C92), C94 (= C95), C97 (= C98), C105 (= C106), R109 (≠ V110), P147 (= P158), C151 (≠ A162)
- binding zinc ion: C91 (= C92), C94 (= C95), C97 (= C98), C105 (= C106)
Sites not aligning to the query:
1pl6A Human sdh/nadh/inhibitor complex (see paper)
27% identity, 96% coverage: 12:355/358 of query aligns to 17:350/356 of 1pl6A
- active site: C44 (= C39), G45 (= G40), S46 (≠ A41), H49 (≠ K44), H69 (= H61), E70 (= E62), R99 (≠ E99), D102 (= D102), C105 (= C105), S113 (≠ G113), F117 (≠ K125), P156 (= P158), G160 (≠ A162), K344 (= K349)
- binding 4-[2-(hydroxymethyl)pyrimidin-4-yl]-n,n-dimethylpiperazine-1-sulfonamide: C44 (= C39), S46 (≠ A41), I56 (≠ G51), F59 (vs. gap), H69 (= H61), E155 (≠ D157), L274 (≠ M278), F297 (≠ M301)
- binding nicotinamide-adenine-dinucleotide: G181 (= G184), P182 (= P185), I183 (≠ L186), D203 (≠ G206), L204 (= L207), R208 (= R214), C249 (= C253), T250 (≠ S254), V272 (= V276), G273 (= G277), L274 (≠ M278), F297 (≠ M301), R298 (≠ A302)
- binding zinc ion: C44 (= C39), H69 (= H61)
5vm2A Crystal structure of eck1772, an oxidoreductase/dehydrogenase of unknown specificity involved in membrane biogenesis from escherichia coli
28% identity, 93% coverage: 12:344/358 of query aligns to 12:333/347 of 5vm2A
- active site: C39 (= C39), G40 (= G40), S41 (≠ A41), H44 (≠ Y46), H65 (= H61), E66 (= E62), C95 (= C92), C98 (= C95), C101 (= C98), C109 (= C106), D113 (≠ N111), P153 (= P158), G157 (≠ A162)
- binding magnesium ion: H65 (= H61), E66 (= E62), E152 (≠ D157)
- binding zinc ion: C95 (= C92), C98 (= C95), C101 (= C98), C109 (= C106)
Sites not aligning to the query:
4oh1A Crystal structure of a putative zinc-binding dehydrogenase (gutb) from clostridium scindens atcc 35704 at 2.00 a resolution
28% identity, 97% coverage: 10:355/358 of query aligns to 17:350/351 of 4oh1A
- active site: C46 (= C39), G47 (= G40), S48 (≠ A41), H51 (≠ K44), H74 (= H61), E75 (= E62), C106 (= C92), C109 (= C95), C112 (= C98), C120 (= C106), P158 (= P158), A162 (= A162), K344 (= K349)
- binding zinc ion: C46 (= C39), H74 (= H61), E75 (= E62), C106 (= C92), C109 (= C95), C112 (= C98), C120 (= C106), E157 (≠ D157)
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)
27% identity, 96% coverage: 12:355/358 of query aligns to 16:348/354 of P07846
- C43 (= C39) binding
- Y49 (≠ H45) binding
- H67 (= H61) binding
- E68 (= E62) binding
- E153 (≠ D157) binding
- R296 (≠ A302) binding
- Y297 (= Y303) binding
3qe3A Sheep liver sorbitol dehydrogenase (see paper)
27% identity, 96% coverage: 12:355/358 of query aligns to 12:345/351 of 3qe3A
- active site: C39 (= C39), G40 (= G40), S41 (≠ A41), H44 (≠ K44), H64 (= H61), E65 (= E62), R94 (≠ E99), D97 (= D102), C100 (= C105), S108 (≠ G113), F112 (≠ K125), P151 (= P158), G155 (≠ A162), K339 (= K349)
- binding glycerol: Y45 (≠ H45), F54 (vs. gap), T116 (≠ V129), R293 (≠ A302)
- binding zinc ion: C39 (= C39), H64 (= H61), E65 (= E62)
4cpdA Alcohol dehydrogenase tadh from thermus sp. Atn1
28% identity, 99% coverage: 1:353/358 of query aligns to 1:344/346 of 4cpdA
- active site: C38 (= C39), G39 (= G40), S40 (≠ A41), H43 (≠ K44), H59 (= H61), E60 (= E62), C89 (= C92), C92 (= C95), C95 (= C98), C103 (= C106), G107 (≠ V110), D152 (= D157), T156 (≠ N161), K340 (= K349)
- binding nicotinamide-adenine-dinucleotide: G39 (= G40), S40 (≠ A41), T156 (≠ N161), G178 (= G184), P179 (= P185), V180 (≠ L186), D200 (≠ E209), R201 (≠ D210), R205 (= R214), A243 (≠ C253), V244 (≠ S254), V266 (= V276), V268 (≠ M278), L292 (≠ S296), A293 (≠ I297), F333 (≠ M342)
- binding zinc ion: C38 (= C39), H59 (= H61), C89 (= C92), C92 (= C95), C95 (= C98), C103 (= C106), D152 (= D157)
7y9pA Xylitol dehydrogenase s96c/s99c/y102c mutant(thermostabilized form) from pichia stipitis (see paper)
26% identity, 95% coverage: 14:352/358 of query aligns to 16:354/357 of 7y9pA
Query Sequence
>15894 FitnessBrowser__Keio:15894
MKALARFGKAFGGYKMIDVPQPMCGPEDVVIEIKAAAICGADMKHYNVDSGSDEFNSIRG
HEFAGCIAQVGEKVKDWKVGQRVVSDNSGHVCGVCPACEQGDFLCCTEKVNLGLDNNTWG
GGFSKYCLVPGEILKIHRHALWEIPDGVDYEDAAVLDPICNAYKSIAQQSKFLPGQDVVV
IGTGPLGLFSVQMARIMGAVNIVVVGLQEDVAVRFPVAKELGATAVVNGSTEDVVARCQQ
ICGKDNLGLVIECSGANIALKQAIEMLRPNGEVVRVGMGFKPLDFSINDITAWNKSIIGH
MAYDSTSWRNAIRLLASGAIKVKPMITHRIGLSQWREGFDAMVDKTAIKVIMTYDFDE
Or try a new SitesBLAST search
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