SitesBLAST
Comparing CA265_RS08610 CA265_RS08610 alcohol dehydrogenase 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)
4ilkA Crystal structure of short chain alcohol dehydrogenase (rspb) from e. Coli cft073 (efi target efi-506413) complexed with cofactor nadh
32% identity, 94% coverage: 1:318/339 of query aligns to 4:318/337 of 4ilkA
- active site: C40 (= C37), G41 (= G38), S42 (≠ T39), H45 (= H42), H59 (= H59), E60 (= E60), C89 (= C88), C92 (= C91), C95 (= C94), C103 (= C102), A107 (≠ Q106), P145 (= P143), A149 (≠ G147)
- binding manganese (ii) ion: C40 (= C37), H59 (= H59), E60 (= E60), E144 (= E142)
- binding 1,4-dihydronicotinamide adenine dinucleotide: G168 (= G166), G170 (= G168), P171 (= P169), I172 (= I170), D193 (= D189), R194 (≠ I190), R198 (= R194), N213 (= N209), A235 (= A234), A236 (≠ T235), C237 (≠ G236), I241 (≠ A240), M258 (≠ I257), F260 (≠ L259)
- binding zinc ion: C89 (= C88), C92 (= C91), C95 (= C94), C103 (= C102)
Sites not aligning to the query:
1e3jA Ketose reductase (sorbitol dehydrogenase) from silverleaf whitefly (see paper)
31% identity, 94% coverage: 20:336/339 of query aligns to 21:345/348 of 1e3jA
- active site: C38 (= C37), G39 (= G38), S40 (≠ T39), H43 (= H42), H63 (= H59), E64 (= E60), C93 (= C88), C96 (= C91), C99 (= C94), C107 (= C102), T111 (≠ Q106), P150 (= P143), G154 (= G147), K341 (= K332)
- binding phosphate ion: A174 (= A167), A196 (≠ D189), R197 (≠ I190), S198 (≠ N191), R201 (= R194)
- binding zinc ion: C38 (= C37), H63 (= H59), E64 (= E60), C93 (= C88), C96 (= C91), C99 (= C94), C107 (= C102)
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)
31% identity, 93% coverage: 21:335/339 of query aligns to 37:359/363 of Q7SI09
- C53 (= C37) binding
- F59 (≠ A43) mutation F->A,S,Y: No effect.
- H78 (= H59) binding
- E79 (= E60) binding
- C108 (= C88) binding
- C111 (= C91) binding
- C114 (= C94) binding
- C122 (= C102) binding
- E163 (= E142) binding
- PI 190:191 (= PI 169:170) binding
- D211 (= D189) binding
- DI 211:212 (= DI 189:190) mutation to SR: Alters cofactor specificity from NAD to NADP; when associated with T-348.
- R216 (= R194) binding
- I282 (= I257) binding
- QYR 306:308 (≠ SRN 281:283) binding
- S348 (≠ L324) mutation to T: Alters cofactor specificity from NAD to NADP; when associated with 211-SR-212.
3m6iA L-arabinitol 4-dehydrogenase (see paper)
31% identity, 93% coverage: 21:335/339 of query aligns to 33:355/358 of 3m6iA
- active site: C49 (= C37), G50 (= G38), S51 (≠ T39), H54 (= H42), H74 (= H59), E75 (= E60), C104 (= C88), C107 (= C91), C110 (= C94), C118 (= C102), D122 (≠ Q106), P160 (= P143), A164 (≠ G147), K352 (= K332)
- binding nicotinamide-adenine-dinucleotide: C49 (= C37), V163 (≠ I146), G185 (= G168), P186 (= P169), I187 (= I170), D207 (= D189), R212 (= R194), C255 (≠ A234), T256 (= T235), I278 (= I257), G279 (= G258), V280 (≠ L259), R304 (≠ N283)
- binding zinc ion: C49 (= C37), H74 (= H59), C104 (= C88), C107 (= C91), C110 (= C94), C118 (= C102)
Q96V44 L-arabinitol 4-dehydrogenase; LAD; EC 1.1.1.12 from Hypocrea jecorina (Trichoderma reesei) (see paper)
29% identity, 93% coverage: 21:335/339 of query aligns to 50:373/377 of Q96V44
- DI 224:225 (= DI 189:190) mutation to SR: Alters cofactor specificity from NAD to NADP; when associated with T-362.
- A362 (≠ L324) mutation to T: Alters cofactor specificity from NAD to NADP; when associated with 224-SR-225.
2dfvA Hyperthermophilic threonine dehydrogenase from pyrococcus horikoshii (see paper)
28% identity, 99% coverage: 1:335/339 of query aligns to 3:345/346 of 2dfvA
- active site: C40 (= C37), G41 (= G38), T42 (= T39), H45 (= H42), H65 (= H59), E66 (= E60), C95 (= C88), C98 (= C91), C101 (= C94), C109 (= C102), K113 (≠ Q106), P151 (= P143), A155 (≠ G147), K340 (≠ V330)
- binding nicotinamide-adenine-dinucleotide: G175 (= G168), P176 (= P169), L177 (≠ I170), E197 (≠ I190), P198 (≠ N191), R202 (≠ L195), F241 (≠ A234), S242 (≠ T235), A244 (≠ N237), L264 (≠ I257), G265 (= G258), L266 (= L259), I289 (≠ S280), T290 (≠ S281)
- binding zinc ion: C95 (= C88), C101 (= C94), C109 (= C102)
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)
28% identity, 99% coverage: 1:335/339 of query aligns to 5:347/348 of O58389
- C42 (= C37) binding
- T44 (= T39) mutation to A: Total loss of enzymatic activity.
- H67 (= H59) binding
- E68 (= E60) binding
- C97 (= C88) binding
- C100 (= C91) binding
- C103 (= C94) binding
- C111 (= C102) binding
- E152 (= E142) 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 (≠ I170) binding
- E199 (≠ I190) binding ; mutation to A: Large decrease in affinity for NAD(+).
- R204 (≠ L195) binding ; mutation to A: Large decrease in affinity for NAD(+).
- LGL 266:268 (≠ IGL 257:259) binding
- IT 291:292 (≠ SS 280:281) binding
- R294 (≠ N283) mutation to A: 4000-fold decrease in catalytic efficiency.
5vm2A Crystal structure of eck1772, an oxidoreductase/dehydrogenase of unknown specificity involved in membrane biogenesis from escherichia coli
28% identity, 98% coverage: 9:339/339 of query aligns to 11:347/347 of 5vm2A
- active site: C39 (= C37), G40 (= G38), S41 (≠ T39), H44 (= H42), H65 (= H59), E66 (= E60), C95 (= C88), C98 (= C91), C101 (= C94), C109 (= C102), D113 (≠ K104), P153 (= P143), G157 (= G147), K340 (= K332)
- binding magnesium ion: H65 (= H59), E66 (= E60), E152 (= E142)
- binding zinc ion: C95 (= C88), C98 (= C91), C101 (= C94), C109 (= C102)
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)
27% identity, 93% coverage: 22:335/339 of query aligns to 39:369/385 of B6HI95
- DI 212:213 (= DI 189:190) mutation to SR: Alters cofactor specificity from NAD to NADP; when associated with T-358.
- S358 (≠ L324) 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)
28% identity, 96% coverage: 11:335/339 of query aligns to 18:354/357 of 7y9pA
2eerB Structural study of project id st2577 from sulfolobus tokodaii strain7
29% identity, 89% coverage: 20:322/339 of query aligns to 21:333/347 of 2eerB
- active site: C38 (= C37), H39 (≠ G38), S40 (≠ T39), H43 (= H42), H68 (= H59), E69 (= E60), E98 (≠ C88), C101 (= C91), C104 (= C94), C112 (= C102), R116 (≠ Q106), C154 (≠ A148), T158 (vs. gap)
- binding nicotinamide-adenine-dinucleotide: C38 (= C37), H39 (≠ G38), S40 (≠ T39), H43 (= H42), C154 (≠ A148), T158 (vs. gap), G178 (= G166), G181 (≠ P169), G182 (= G171), L183 (= L172), D203 (= D189), V204 (≠ I190), R205 (≠ N191), L247 (≠ A234), N248 (≠ T235), V270 (≠ I257), G271 (= G258), L272 (= L259), F273 (≠ Q260), L295 (≠ R282), V296 (≠ N283)
- binding zinc ion: E98 (≠ C88), C101 (= C91), C104 (= C94), C112 (= C102)
Sites not aligning to the query:
3gfbA L-threonine dehydrogenase (tktdh) from the hyperthermophilic archaeon thermococcus kodakaraensis (see paper)
29% identity, 95% coverage: 1:321/339 of query aligns to 3:331/347 of 3gfbA
- active site: C40 (= C37), G41 (= G38), T42 (= T39), H45 (= H42), H65 (= H59), E66 (= E60), C95 (= C88), C98 (= C91), C101 (= C94), C109 (= C102), K113 (≠ Q106), P151 (= P143), A155 (≠ G147)
- binding nicotinamide-adenine-dinucleotide: G173 (= G166), G175 (= G168), P176 (= P169), L177 (≠ I170), S196 (≠ L188), E197 (≠ D189), P198 (≠ I190), R202 (= R194), F241 (≠ A234), S242 (≠ T235), A244 (≠ N237), L264 (≠ I257), G265 (= G258), L266 (= L259), I289 (≠ S280), T290 (≠ S281)
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)
29% identity, 95% coverage: 1:321/339 of query aligns to 5:333/350 of Q5JI69
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)
27% identity, 93% coverage: 22:335/339 of query aligns to 40:370/386 of A2QAC0
- M70 (≠ F50) mutation to F: Abolishes enzyme activity.
- DI 213:214 (= DI 189:190) mutation to SR: Alters cofactor specificity from NAD to NADP; when associated with T-359.
- Y318 (≠ R282) mutation to F: Increases affinity for D-sorbitol.
- A359 (≠ L324) mutation to T: Alters cofactor specificity from NAD to NADP; when associated with 213-SR-214.
4ejmA Crystal structure of a putative zinc-binding dehydrogenase (target psi-012003) from sinorhizobium meliloti 1021 bound to NADP
29% identity, 88% coverage: 1:298/339 of query aligns to 4:332/342 of 4ejmA
- active site: C40 (= C37), G41 (= G38), T42 (= T39), H45 (= H42), H61 (= H59), E62 (= E60), C91 (= C88), C94 (= C91), C97 (= C94), C105 (= C102), R109 (≠ Q106), P147 (= P143), C151 (≠ G147)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: G170 (= G166), G172 (= G168), V173 (≠ P169), I174 (= I170), T194 (≠ I190), R195 (≠ N191), Q196 (≠ E192), K199 (≠ L195), C240 (≠ A234), E245 (≠ K239), T246 (≠ A240), L263 (≠ I257), V265 (vs. gap), I291 (vs. gap)
- binding zinc ion: C91 (= C88), C94 (= C91), C97 (= C94), C105 (= C102)
Sites not aligning to the query:
4ej6A Crystal structure of a putative zinc-binding dehydrogenase (target psi-012003) from sinorhizobium meliloti 1021
29% identity, 88% coverage: 1:298/339 of query aligns to 4:332/343 of 4ej6A
- active site: C40 (= C37), G41 (= G38), T42 (= T39), H45 (= H42), H61 (= H59), E62 (= E60), C91 (= C88), C94 (= C91), C97 (= C94), C105 (= C102), R109 (≠ Q106), P147 (= P143), C151 (≠ G147)
- binding zinc ion: C91 (= C88), C94 (= C91), C97 (= C94), C105 (= C102)
Sites not aligning to the query:
P07913 L-threonine 3-dehydrogenase; TDH; L-threonine dehydrogenase; EC 1.1.1.103 from Escherichia coli (strain K12) (see paper)
32% identity, 72% coverage: 20:264/339 of query aligns to 21:269/341 of P07913
- C38 (= C37) 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(+).
5ylnA Zinc dependent alcohol dehydrogenase 2 from streptococcus pneumonia - apo form
28% identity, 95% coverage: 1:321/339 of query aligns to 5:327/348 of 5ylnA
6iqdA Crystal structure of alcohol dehydrogenase from geobacillus stearothermophilus (see paper)
29% identity, 92% coverage: 11:321/339 of query aligns to 12:321/336 of 6iqdA
- active site: C38 (= C37), T40 (= T39), H43 (= H42), H61 (= H59), C148 (≠ A148)
- binding zinc ion: C38 (= C37), H61 (= H59), E62 (= E60), C92 (= C88), C95 (= C91), C98 (= C94), C106 (= C102), C148 (≠ A148)
5kiaA Crystal structure of l-threonine 3-dehydrogenase from burkholderia thailandensis
27% identity, 98% coverage: 1:331/339 of query aligns to 2:334/339 of 5kiaA
- active site: C37 (= C37), G38 (= G38), T39 (= T39), H42 (= H42), H61 (= H59), E62 (= E60), C91 (= C88), C94 (= C91), C97 (= C94), C105 (= C102), V109 (≠ Q106), P147 (= P143), A151 (≠ G147), K333 (≠ V330)
- binding calcium ion: D146 (≠ E142), N150 (≠ I146), E288 (≠ N283)
- binding zinc ion: C91 (= C88), C94 (= C91), C97 (= C94), C105 (= C102)
Query Sequence
>CA265_RS08610 CA265_RS08610 alcohol dehydrogenase
MKTLTCTTPGTFEYSETTKPELKKDHAIIKIKRIGICGTDLHAFEGTQPFFNYPRVLGHE
LSGELVEADGADGFKIGEAVTFIPYFNCGECIACRMNKPNCCVKMQVCGVHVDGGMREYL
QVPSRTLLHGEGLSYDELALVEPLAIGAHGVRRADVQPGEFVLVIGAGPIGLGTMEFARI
AGANVIALDINEDRLAFCKDKLKVAHVVNALSPDVVQQLSDITNGDMPTVVIDATGNQKA
INNAINYMAHGARFVLIGLQKGDLIFNHPEFHKRESTLMSSRNATIEDFEHVIKSMKAGL
VNPTNYITHQVQFEAVKDEFESWLDPKNGVIKAMVSLGN
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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