SitesBLAST
Comparing SMa0512 FitnessBrowser__Smeli:SMa0512 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
43% identity, 99% coverage: 2:342/343 of query aligns to 9:346/346 of 6dkhC
3qe3A Sheep liver sorbitol dehydrogenase (see paper)
38% identity, 99% coverage: 3:340/343 of query aligns to 5:342/351 of 3qe3A
- active site: C39 (= C37), G40 (= G38), S41 (= S39), H44 (= H42), H64 (= H62), E65 (= E63), R94 (≠ C92), D97 (≠ C95), C100 (= C98), S108 (≠ C106), F112 (≠ R110), P151 (= P152), G155 (≠ T156), K339 (= K337)
- binding glycerol: Y45 (= Y43), F54 (≠ V52), T116 (≠ S114), R293 (= R290)
- binding zinc ion: C39 (= C37), H64 (= H62), E65 (= E63)
1pl6A Human sdh/nadh/inhibitor complex (see paper)
37% identity, 99% coverage: 3:340/343 of query aligns to 10:347/356 of 1pl6A
- active site: C44 (= C37), G45 (= G38), S46 (= S39), H49 (= H42), H69 (= H62), E70 (= E63), R99 (≠ C92), D102 (≠ C95), C105 (= C98), S113 (≠ C106), F117 (≠ R110), P156 (= P152), G160 (≠ T156), K344 (= K337)
- binding 4-[2-(hydroxymethyl)pyrimidin-4-yl]-n,n-dimethylpiperazine-1-sulfonamide: C44 (= C37), S46 (= S39), I56 (≠ F49), F59 (≠ V52), H69 (= H62), E155 (= E151), L274 (= L267), F297 (= F289)
- binding nicotinamide-adenine-dinucleotide: G181 (= G177), P182 (= P178), I183 (= I179), D203 (= D199), L204 (= L200), R208 (≠ A204), C249 (= C242), T250 (≠ S243), V272 (≠ L265), G273 (= G266), L274 (= L267), F297 (= F289), R298 (= R290)
- binding zinc ion: C44 (= C37), H69 (= H62)
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)
37% identity, 99% coverage: 3:340/343 of query aligns to 11:348/357 of Q00796
- C45 (= C37) binding
- H70 (= H62) binding
- E71 (= E63) binding
- R110 (≠ L102) to P: in SORDD; results in protein aggregation
- H135 (≠ A131) to R: in SORDD; results in protein aggregation
- A153 (= A148) to D: in SORDD; uncertain significance; results in protein aggregation; dbSNP:rs145813597
- I184 (= I179) binding
- D204 (= D199) binding
- R209 (≠ A204) binding
- Q239 (≠ T235) to L: in dbSNP:rs1042079
- N269 (≠ V261) to T: in dbSNP:rs930337
- VGL 273:275 (≠ LGL 265:267) binding
- VFR 297:299 (≠ SFR 288:290) binding
- V322 (≠ I313) to I: in SORDD; uncertain significance; dbSNP:rs149975952
Sites not aligning to the query:
- 1 modified: Initiator methionine, Removed
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)
37% identity, 99% coverage: 3:340/343 of query aligns to 9:345/354 of P07846
- C43 (= C37) binding
- Y49 (= Y43) binding
- H67 (= H62) binding
- E68 (= E63) binding
- E153 (= E151) binding
- R296 (= R290) binding
- Y297 (≠ F291) binding
1e3jA Ketose reductase (sorbitol dehydrogenase) from silverleaf whitefly (see paper)
36% identity, 98% coverage: 5:341/343 of query aligns to 6:345/348 of 1e3jA
- active site: C38 (= C37), G39 (= G38), S40 (= S39), H43 (= H42), H63 (= H62), E64 (= E63), C93 (= C92), C96 (= C95), C99 (= C98), C107 (= C106), T111 (≠ R110), P150 (= P152), G154 (≠ T156), K341 (= K337)
- binding phosphate ion: A174 (≠ C176), A196 (≠ D199), R197 (≠ L200), S198 (= S201), R201 (≠ A204)
- binding zinc ion: C38 (= C37), H63 (= H62), E64 (= E63), C93 (= C92), C96 (= C95), C99 (= C98), C107 (= C106)
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)
35% identity, 99% coverage: 3:340/343 of query aligns to 11:348/357 of P27867
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)
37% identity, 92% coverage: 25:340/343 of query aligns to 42:369/385 of B6HI95
- DI 212:213 (≠ DL 199:200) mutation to SR: Alters cofactor specificity from NAD to NADP; when associated with T-358.
- S358 (= S330) mutation to T: Alters cofactor specificity from NAD to NADP; when associated with 212-SR-213.
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)
35% identity, 92% coverage: 24:340/343 of query aligns to 42:370/386 of A2QAC0
- M70 (≠ V52) mutation to F: Abolishes enzyme activity.
- DI 213:214 (≠ DL 199:200) mutation to SR: Alters cofactor specificity from NAD to NADP; when associated with T-359.
- Y318 (≠ F289) mutation to F: Increases affinity for D-sorbitol.
- A359 (≠ S330) mutation to T: Alters cofactor specificity from NAD to NADP; when associated with 213-SR-214.
3m6iA L-arabinitol 4-dehydrogenase (see paper)
36% identity, 92% coverage: 25:340/343 of query aligns to 37:355/358 of 3m6iA
- active site: C49 (= C37), G50 (= G38), S51 (= S39), H54 (= H42), H74 (= H62), E75 (= E63), C104 (= C92), C107 (= C95), C110 (= C98), C118 (= C106), D122 (≠ R110), P160 (= P152), A164 (≠ T156), K352 (= K337)
- binding nicotinamide-adenine-dinucleotide: C49 (= C37), V163 (= V155), G185 (= G177), P186 (= P178), I187 (= I179), D207 (= D199), R212 (≠ A204), C255 (= C242), T256 (≠ S243), I278 (≠ L265), G279 (= G266), V280 (≠ L267), R304 (= R290)
- binding zinc ion: C49 (= C37), H74 (= H62), C104 (= C92), C107 (= C95), C110 (= C98), C118 (= C106)
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)
36% identity, 92% coverage: 25:340/343 of query aligns to 41:359/363 of Q7SI09
- C53 (= C37) binding
- F59 (≠ Y43) mutation F->A,S,Y: No effect.
- H78 (= H62) binding
- E79 (= E63) binding
- C108 (= C92) binding
- C111 (= C95) binding
- C114 (= C98) binding
- C122 (= C106) binding
- E163 (= E151) binding
- PI 190:191 (= PI 178:179) binding
- D211 (= D199) binding
- DI 211:212 (≠ DL 199:200) mutation to SR: Alters cofactor specificity from NAD to NADP; when associated with T-348.
- R216 (≠ A204) binding
- I282 (≠ L265) binding
- QYR 306:308 (≠ SFR 288:290) binding
- S348 (= S330) mutation to T: Alters cofactor specificity from NAD to NADP; when associated with 211-SR-212.
Q96V44 L-arabinitol 4-dehydrogenase; LAD; EC 1.1.1.12 from Hypocrea jecorina (Trichoderma reesei) (see paper)
35% identity, 92% coverage: 24:340/343 of query aligns to 53:373/377 of Q96V44
- DI 224:225 (≠ DL 199:200) mutation to SR: Alters cofactor specificity from NAD to NADP; when associated with T-362.
- A362 (≠ S330) mutation to T: Alters cofactor specificity from NAD to NADP; when associated with 224-SR-225.
7y9pA Xylitol dehydrogenase s96c/s99c/y102c mutant(thermostabilized form) from pichia stipitis (see paper)
34% identity, 95% coverage: 3:328/343 of query aligns to 5:342/357 of 7y9pA
2dfvA Hyperthermophilic threonine dehydrogenase from pyrococcus horikoshii (see paper)
36% identity, 87% coverage: 16:315/343 of query aligns to 19:318/346 of 2dfvA
- active site: C40 (= C37), G41 (= G38), T42 (≠ S39), H45 (= H42), H65 (= H62), E66 (= E63), C95 (= C92), C98 (= C95), C101 (= C98), C109 (= C106), K113 (≠ R110), P151 (= P152), A155 (≠ T156)
- binding nicotinamide-adenine-dinucleotide: G175 (= G177), P176 (= P178), L177 (≠ I179), E197 (≠ D199), P198 (≠ L200), R202 (≠ A204), F241 (≠ C242), S242 (= S243), A244 (= A245), L264 (= L265), G265 (= G266), L266 (= L267), I289 (≠ S288), T290 (≠ F289)
- binding zinc ion: C95 (= C92), C101 (= C98), C109 (= C106)
Sites not aligning to the query:
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)
36% identity, 87% coverage: 16:315/343 of query aligns to 21:320/348 of O58389
- C42 (= C37) binding
- T44 (≠ S39) mutation to A: Total loss of enzymatic activity.
- H67 (= H62) binding
- E68 (= E63) binding
- C97 (= C92) binding
- C100 (= C95) binding
- C103 (= C98) binding
- C111 (= C106) binding
- E152 (= E151) 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 (≠ A204) binding ; mutation to A: Large decrease in affinity for NAD(+).
- LGL 266:268 (= LGL 265:267) binding
- IT 291:292 (≠ SF 288:289) binding
- R294 (≠ F291) mutation to A: 4000-fold decrease in catalytic efficiency.
3gfbA L-threonine dehydrogenase (tktdh) from the hyperthermophilic archaeon thermococcus kodakaraensis (see paper)
35% identity, 87% coverage: 16:315/343 of query aligns to 19:318/347 of 3gfbA
- active site: C40 (= C37), G41 (= G38), T42 (≠ S39), H45 (= H42), H65 (= H62), E66 (= E63), C95 (= C92), C98 (= C95), C101 (= C98), C109 (= C106), K113 (≠ R110), P151 (= P152), A155 (≠ T156)
- binding nicotinamide-adenine-dinucleotide: G173 (= G175), G175 (= G177), P176 (= P178), L177 (≠ I179), S196 (≠ A198), E197 (≠ D199), P198 (≠ L200), R202 (≠ A204), F241 (≠ C242), S242 (= S243), A244 (= A245), L264 (= L265), G265 (= G266), L266 (= L267), I289 (≠ S288), T290 (≠ F289)
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)
35% identity, 87% coverage: 16:315/343 of query aligns to 21:320/350 of Q5JI69
2ejvA Crystal structure of threonine 3-dehydrogenase complexed with NAD+
35% identity, 93% coverage: 19:338/343 of query aligns to 20:337/343 of 2ejvA
- active site: C38 (= C37), G39 (= G38), T40 (≠ S39), H43 (= H42), H63 (= H62), E64 (= E63), C93 (= C92), C96 (= C95), C99 (= C98), C107 (= C106), Q111 (≠ R110), P149 (= P152), A153 (≠ T156), K336 (= K337)
- binding nicotinamide-adenine-dinucleotide: G172 (= G175), G174 (= G177), P175 (= P178), I176 (= I179), S195 (≠ A198), D196 (= D199), P197 (≠ L200), R201 (≠ A204), F238 (≠ C242), S239 (= S243), N241 (≠ A245), A244 (= A248), L261 (= L265), G262 (= G266), I263 (≠ L267)
- binding zinc ion: C38 (= C37), H63 (= H62), E64 (= E63), C96 (= C95), C99 (= C98), C107 (= C106)
2dq4A Crystal structure of threonine 3-dehydrogenase
35% identity, 93% coverage: 19:338/343 of query aligns to 20:337/343 of 2dq4A
- active site: C38 (= C37), G39 (= G38), T40 (≠ S39), H43 (= H42), H63 (= H62), E64 (= E63), C93 (= C92), C96 (= C95), C99 (= C98), C107 (= C106), Q111 (≠ R110), P149 (= P152), A153 (≠ T156), K336 (= K337)
- binding zinc ion: C38 (= C37), H63 (= H62), E64 (= E63), 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)
35% identity, 93% coverage: 19:338/343 of query aligns to 20:337/343 of Q5SKS4
- C38 (= C37) binding
- H63 (= H62) binding
- E64 (= E63) binding
- C93 (= C92) binding
- C96 (= C95) binding
- C99 (= C98) binding
- C107 (= C106) binding
- I176 (= I179) binding
- D196 (= D199) binding
- R201 (≠ A204) binding
- LGI 261:263 (≠ LGL 265:267) binding
- IAG 286:288 (vs. gap) binding
Query Sequence
>SMa0512 FitnessBrowser__Smeli:SMa0512
MKAIVIHTAKDLRVEECAVEKPGPGEVEIRLAAGGICGSDLHYYNHGGFGTVRLKEPMIL
GHEVSGHVAALGEGVSDLAIGDLVAVSPSRPCGACDYCLKGLPNHCFHMRFYGSAMPFPH
IQGAFRERLVAKASQCVKAEGLSAGEAAMAEPLSVTLHATRRAGEMLGKRVLVTGCGPIG
TLSILAARRAGAAEIVAADLSERALGFARAVGADRTVNLSEDRDGLVPFSENKGTFDVLY
ECSGAQPALVAGIQALRPRGVIVQLGLGGDMALPMMAITAKELDLRGSFRFHEEFATAVK
LMQGGLIDVKPLITHTLPLGEALKAFEIASDKGQSMKTQIAFA
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