SitesBLAST
Comparing WP_012991441.1 NCBI__GCF_000025605.1:WP_012991441.1 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)
5yvmA Crystal structure of the archaeal halo-thermophilic red sea brine pool alcohol dehydrogenase adh/d1 bound to nzq (see paper)
37% identity, 99% coverage: 1:382/384 of query aligns to 4:402/403 of 5yvmA
- binding manganese (ii) ion: D207 (= D198), H211 (= H202), H276 (= H267), H291 (= H282)
- binding 5,6-dihydroxy-nadp: G41 (= G37), N44 (≠ S40), M45 (≠ A41), P73 (= P70), N74 (= N71), G100 (= G97), G101 (= G98), S102 (= S99), D105 (= D102), S151 (≠ T142), T152 (= T143), T155 (= T146), T160 (≠ N151), Y162 (= Y153), V164 (= V155), K173 (= K164), E195 (≠ S186), L200 (= L191), H211 (= H202), H276 (= H267), H280 (= H271), H291 (= H282)
5yvrA Crystal structure of the h277a mutant of adh/d1, an archaeal halo- thermophilic red sea brine pool alcohol dehydrogenase (see paper)
36% identity, 99% coverage: 1:382/384 of query aligns to 4:402/403 of 5yvrA
- binding manganese (ii) ion: D207 (= D198), H211 (= H202), H276 (= H267), H291 (= H282)
- binding nadph dihydro-nicotinamide-adenine-dinucleotide phosphate: G41 (= G37), S43 (≠ Q39), N44 (≠ S40), M45 (≠ A41), G100 (= G97), G101 (= G98), S102 (= S99), D105 (= D102), S151 (≠ T142), T152 (= T143), T155 (= T146), T160 (≠ N151), Y162 (= Y153), V164 (= V155), K173 (= K164), E195 (≠ S186), M196 (= M187), L200 (= L191), D207 (= D198), H211 (= H202), H291 (= H282)
3bfjA Crystal structure analysis of 1,3-propanediol oxidoreductase (see paper)
33% identity, 99% coverage: 3:383/384 of query aligns to 3:382/382 of 3bfjA
P31005 NAD-dependent methanol dehydrogenase; MDH; MEDH; Type 3 alcohol dehydrogenase; EC 1.1.1.244 from Bacillus methanolicus (see 3 papers)
32% identity, 98% coverage: 5:382/384 of query aligns to 4:380/381 of P31005
- G13 (= G14) mutation to A: Shows a reduced dehydrogenase activity.
- G15 (= G16) mutation to A: Shows almost the same dehydrogenase activity as the wild-type.
- D88 (= D90) mutation to N: Shows almost the same dehydrogenase activity as the wild-type.
- G95 (= G97) mutation to A: Shows a 10-fold decreased affinity for NAD and NADH and a strongly reduced dehydrogenase activity. Completely insensitive to the stimulating effect of the activator protein Act.
- S97 (= S99) mutation to G: Shows an increase of the dehydrogenase activity and a decrease of the affinity for NAD and NADH. Completely insensitive to the stimulating effect of the activator protein Act. It does not bind NAD.; mutation to T: Shows an increase of the dehydrogenase activity and affinity for NAD and NADH.
- D100 (= D102) mutation to N: Loss of dehydrogenase activity. It still binds NADH.
- K103 (= K105) mutation to R: Loss of dehydrogenase activity. It does not bind NADH.
Sites not aligning to the query:
- 1 modified: Initiator methionine, Removed
3ox4A Structures of iron-dependent alcohol dehydrogenase 2 from zymomonas mobilis zm4 complexed with NAD cofactor (see paper)
32% identity, 99% coverage: 5:383/384 of query aligns to 5:382/382 of 3ox4A
- binding fe (ii) ion: D193 (= D198), H197 (= H202), H262 (= H267), H276 (= H282)
- binding nicotinamide-adenine-dinucleotide: D38 (≠ R38), F40 (≠ S40), M41 (≠ A41), N70 (= N71), G96 (= G97), G97 (= G98), S98 (= S99), T137 (= T142), T138 (= T143), F148 (≠ Y153), I150 (≠ V155), G181 (≠ S186), M182 (= M187), L186 (= L191), H276 (= H282)
3owoA Structures of iron-dependent alcohol dehydrogenase 2 from zymomonas mobilis zm4 with and without NAD cofactor (see paper)
32% identity, 99% coverage: 5:383/384 of query aligns to 5:382/382 of 3owoA
P0DJA2 Alcohol dehydrogenase 2; Alcohol dehydrogenase II; ADH II; EC 1.1.1.1 from Zymomonas mobilis subsp. mobilis (strain ATCC 31821 / ZM4 / CP4) (see 2 papers)
32% identity, 99% coverage: 5:383/384 of query aligns to 6:383/383 of P0DJA2
- D39 (≠ R38) binding NAD(+)
- N71 (= N71) binding NAD(+)
- G98 (= G98) binding NAD(+)
- S99 (= S99) binding NAD(+)
- T138 (= T142) binding NAD(+)
- T139 (= T143) binding NAD(+)
- T147 (≠ N151) binding NAD(+)
- F149 (≠ Y153) binding NAD(+)
- K160 (= K164) binding NAD(+)
- L179 (= L183) binding NAD(+)
- G182 (≠ S186) binding NAD(+)
- M183 (= M187) binding NAD(+)
- D194 (= D198) binding Fe(2+)
- H198 (= H202) binding Fe(2+)
- H263 (= H267) binding Fe(2+)
- H267 (= H271) binding NAD(+)
- H277 (= H282) binding Fe(2+); binding NAD(+)
Sites not aligning to the query:
- 1 modified: Initiator methionine, Removed
1o2dA Crystal structure of alcohol dehydrogenase, iron-containing (tm0920) from thermotoga maritima at 1.30 a resolution (see paper)
34% identity, 99% coverage: 3:384/384 of query aligns to 2:358/359 of 1o2dA
- binding fe (iii) ion: D189 (= D198), H193 (= H202), H256 (= H267), H270 (= H282)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: S38 (≠ Q39), S39 (= S40), E68 (≠ P70), N69 (= N71), G95 (= G97), G96 (= G98), S97 (= S99), D100 (= D102), T136 (= T142), T137 (= T143), T140 (= T146), S142 (= S148), Y147 (= Y153), I149 (≠ V155), K157 (≠ E163), S177 (= S186), M178 (= M187), L182 (= L191), D189 (= D198), H193 (= H202), H270 (= H282)
1vhdA Crystal structure of an iron containing alcohol dehydrogenase (see paper)
34% identity, 99% coverage: 3:384/384 of query aligns to 3:359/361 of 1vhdA
- binding nadp nicotinamide-adenine-dinucleotide phosphate: S39 (≠ Q39), S40 (= S40), E69 (≠ P70), N70 (= N71), G96 (= G97), G97 (= G98), S98 (= S99), D101 (= D102), T137 (= T142), T138 (= T143), T141 (= T146), S143 (= S148), T146 (≠ N151), Y148 (= Y153), I150 (≠ V155), K158 (≠ E163), S178 (= S186), M179 (= M187), L183 (= L191), D190 (= D198), H194 (= H202), H271 (= H282)
- binding zinc ion: D190 (= D198), H194 (= H202), H257 (= H267), H271 (= H282)
A0A0S1X9S7 Alcohol dehydrogenase; EC 1.1.1.1 from Thermococcus barophilus (see paper)
33% identity, 100% coverage: 1:383/384 of query aligns to 1:376/378 of A0A0S1X9S7
- D195 (= D198) mutation to A: Disrupts the overall structure of the enzyme. Lack of acetaldehyde reduction activity and displays weak ethanol oxidation activity.
- H199 (= H202) mutation to A: Disrupts the overall structure of the enzyme. Retains 10% of ethanol oxidation and acetaldehyde reduction activities.
- H262 (= H267) mutation to A: Disrupts the overall structure of the enzyme. Displays weak ethanol oxidation and acetaldehyde reduction activities.
- H266 (= H271) mutation to A: Disrupts the overall structure of the enzyme. Displays higher acetaldehyde reduction activity (134%) but lower ethanol oxidation activity (36%).
- H274 (= H282) mutation to A: Disrupts the overall structure of the enzyme. Retains 20% of ethanol oxidation and acetaldehyde reduction activities.
1vljB Crystal structure of nadh-dependent butanol dehydrogenase a (tm0820) from thermotoga maritima at 1.78 a resolution
31% identity, 93% coverage: 3:358/384 of query aligns to 9:368/400 of 1vljB
- binding fe (iii) ion: D200 (= D198), H204 (= H202), H273 (= H267), H287 (= H282)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: G45 (≠ R38), S47 (= S40), P76 (= P70), G103 (= G97), G104 (= G98), S105 (= S99), D108 (= D102), T144 (= T142), I145 (≠ T143), T148 (= T146), T150 (≠ S148), N153 (= N151), N155 (≠ Y153), K166 (= K164), T188 (≠ S186), L189 (≠ M187), Q193 (≠ L191), H204 (= H202), H287 (= H282)
7qlgAAA Lactaldehyde reductase (see paper)
32% identity, 97% coverage: 13:383/384 of query aligns to 12:381/383 of 7qlgAAA
- binding fe (iii) ion: D194 (= D198), H198 (= H202), H261 (= H267), H275 (= H282)
- binding 1,4-dihydronicotinamide adenine dinucleotide: D37 (≠ R38), T39 (≠ S40), L40 (≠ A41), N69 (= N71), G95 (= G97), G96 (= G98), S97 (= S99), D100 (= D102), T138 (= T142), T139 (= T143), T142 (= T146), T147 (≠ N151), N149 (≠ Y153), K160 (= K164), L187 (= L191), H198 (= H202), H275 (= H282)
7qlqAAA Lactaldehyde reductase (see paper)
31% identity, 97% coverage: 13:383/384 of query aligns to 12:381/383 of 7qlqAAA
- binding adenosine-5-diphosphoribose: D37 (≠ R38), T39 (≠ S40), L40 (≠ A41), G95 (= G97), G96 (= G98), S97 (= S99), T138 (= T142), T139 (= T143), T142 (= T146), K160 (= K164), G182 (≠ S186), M183 (= M187), L187 (= L191), H275 (= H282)
- binding 2-(3,4-dimethoxyphenyl)ethanamide: G149 (≠ Y153), V164 (≠ S168), H198 (= H202), F252 (≠ I258), S253 (≠ D259), H261 (= H267), C360 (≠ Y356)
- binding fe (iii) ion: D194 (= D198), H198 (= H202), H261 (= H267), H275 (= H282)
2bi4A Lactaldehyde:1,2-propanediol oxidoreductase of escherichia coli (see paper)
31% identity, 97% coverage: 13:383/384 of query aligns to 13:382/382 of 2bi4A
- binding fe (iii) ion: D195 (= D198), H199 (= H202), H262 (= H267), H276 (= H282)
- binding nicotinamide-adenine-dinucleotide: D38 (≠ R38), T40 (≠ S40), L41 (≠ A41), G96 (= G97), G97 (= G98), S98 (= S99), T139 (= T142), T140 (= T143), V152 (= V155), K161 (= K164), G183 (≠ S186), M184 (= M187), L188 (= L191), D195 (= D198), H199 (= H202), H262 (= H267), H276 (= H282)
P0A9S1 Lactaldehyde reductase; Propanediol oxidoreductase; EC 1.1.1.77 from Escherichia coli (strain K12) (see paper)
31% identity, 97% coverage: 13:383/384 of query aligns to 13:382/382 of P0A9S1
- G16 (= G16) mutation to D: No effect on enzyme activity.
- D38 (≠ R38) mutation to G: Enzyme can now use NADP.
- G96 (= G97) mutation to E: Loss of NAD binding and enzyme activity.
- D195 (= D198) mutation to L: Complete loss of iron-binding.
- H199 (= H202) mutation H->A,F: Complete loss of iron-binding.
Sites not aligning to the query:
- 1:9 MANRMILNE→M: Loss of enzyme activity, loss of dimerization.
1rrmA Crystal structure of lactaldehyde reductase
31% identity, 97% coverage: 13:383/384 of query aligns to 13:382/385 of 1rrmA
- binding adenosine-5-diphosphoribose: D38 (≠ R38), T40 (≠ S40), L41 (≠ A41), N70 (= N71), G96 (= G97), G97 (= G98), S98 (= S99), T139 (= T142), T140 (= T143), T143 (= T146), V152 (= V155), K161 (= K164), G183 (≠ S186), M184 (= M187), L188 (= L191), H276 (= H282)
- binding fe (ii) ion: L258 (≠ V263), C361 (≠ Y356)
- binding zinc ion: D195 (= D198), H199 (= H202), H262 (= H267), H276 (= H282)
5br4A E. Coli lactaldehyde reductase (fuco) m185c mutant (see paper)
31% identity, 97% coverage: 13:383/384 of query aligns to 14:383/385 of 5br4A
- binding nicotinamide-adenine-dinucleotide: D39 (≠ R38), T41 (≠ S40), L42 (≠ A41), P70 (= P70), G97 (= G97), G98 (= G98), S99 (= S99), D102 (= D102), T140 (= T142), T141 (= T143), T144 (= T146), T149 (≠ N151), N151 (≠ Y153), V153 (= V155), K162 (= K164), G184 (≠ S186), C185 (≠ M187), L189 (= L191), H277 (= H282)
- binding zinc ion: D196 (= D198), H200 (= H202), H263 (= H267), H277 (= H282)
6c75B Structure of iron containing alcohol dehydrogenase from thermococcus thioreducens in a monoclinic crystal form (see paper)
32% identity, 99% coverage: 5:383/384 of query aligns to 2:375/378 of 6c75B
6c75A Structure of iron containing alcohol dehydrogenase from thermococcus thioreducens in a monoclinic crystal form (see paper)
32% identity, 99% coverage: 5:383/384 of query aligns to 2:375/378 of 6c75A
- binding fe (iii) ion: D193 (= D198), H197 (= H202), H260 (= H267), H272 (= H279)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: S33 (≠ R38), S35 (= S40), G91 (= G97), G92 (= G98), S93 (= S99), D96 (= D102), S139 (≠ T142), T140 (= T143), A143 (≠ T146), S148 (≠ N151), V152 (= V155), K159 (= K162), T181 (≠ S186), M182 (= M187), P183 (≠ S188), V186 (≠ L191), F251 (≠ I258), H272 (= H279)
6jkpA Crystal structure of sulfoacetaldehyde reductase from bifidobacterium kashiwanohense in complex with NAD+ (see paper)
29% identity, 99% coverage: 1:380/384 of query aligns to 2:370/376 of 6jkpA
- binding nicotinamide-adenine-dinucleotide: F42 (≠ A41), G96 (= G98), D100 (= D102), T137 (= T142), T138 (= T143), T141 (= T146), S143 (= S148), T146 (≠ N151), S181 (= S186), V182 (≠ M187), P183 (≠ S188)
Query Sequence
>WP_012991441.1 NCBI__GCF_000025605.1:WP_012991441.1
MKFEFYLPVEVIFGVGSLNRLGEVARRFGFKAILVTGRQSARKSGALEKAIDSLKRHGIK
EVLVFDEVEPNPTDTTVNQLSRLIVEEKVDFIVGLGGGSALDVAKASSLVSSNEGSAWDY
VNYPEGPRLIPFLNRPVICVPTTAGTGSEVNRYSVISSPVRKEKMVISHSLNYPKAAIVD
PELTVSMSRKLTAVTGVDAFMHALEAFTNRVEDTFADHLAITALSIIKEWLPIALEEPEN
LKARAQMSYAATLAGIAIDRKRVALIHGMEHPVSAHYPHVAHGEGLAALAPAVTEFNYRG
NPEKYKVVAEVLGCGSEPHRAVDCVVRFLEKVGLLITLKDLGVEKEKLERLAEDVYLLAR
GLFLINPVEPSIEDIYKLYEKAYG
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