SitesBLAST
Comparing AZOBR_RS27605 FitnessBrowser__azobra:AZOBR_RS27605 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)
3bfjA Crystal structure analysis of 1,3-propanediol oxidoreductase (see paper)
35% identity, 98% coverage: 10:373/373 of query aligns to 8:382/382 of 3bfjA
P31005 NAD-dependent methanol dehydrogenase; MDH; MEDH; Type 3 alcohol dehydrogenase; EC 1.1.1.244 from Bacillus methanolicus (see 3 papers)
30% identity, 97% coverage: 10:372/373 of query aligns to 7:380/381 of P31005
- G13 (= G16) mutation to A: Shows a reduced dehydrogenase activity.
- G15 (= G18) mutation to A: Shows almost the same dehydrogenase activity as the wild-type.
- D88 (≠ Q84) mutation to N: Shows almost the same dehydrogenase activity as the wild-type.
- G95 (= G91) 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 (= S93) 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 (= D96) mutation to N: Loss of dehydrogenase activity. It still binds NADH.
- K103 (= K99) 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, 92% coverage: 30:373/373 of query aligns to 28:382/382 of 3ox4A
- binding fe (ii) ion: D193 (= D188), H197 (= H192), H262 (= H257), H276 (= H271)
- binding nicotinamide-adenine-dinucleotide: D38 (= D40), F40 (= F42), M41 (vs. gap), N70 (≠ E65), G96 (= G91), G97 (= G92), S98 (= S93), T137 (= T132), T138 (= T133), F148 (≠ R143), I150 (≠ L145), G181 (≠ T176), M182 (≠ V177), L186 (≠ V181), H276 (= H271)
3owoA Structures of iron-dependent alcohol dehydrogenase 2 from zymomonas mobilis zm4 with and without NAD cofactor (see paper)
32% identity, 92% coverage: 30:373/373 of query aligns to 28:382/382 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, 92% coverage: 30:373/373 of query aligns to 29:383/383 of P0DJA2
- D39 (= D40) binding
- N71 (≠ E65) binding
- G98 (= G92) binding
- S99 (= S93) binding
- T138 (= T132) binding
- T139 (= T133) binding
- T147 (≠ G141) binding
- F149 (≠ R143) binding
- K160 (= K154) binding
- L179 (= L173) binding
- G182 (≠ T176) binding
- M183 (≠ V177) binding
- D194 (= D188) binding
- H198 (= H192) binding
- H263 (= H257) binding
- H267 (≠ Y261) binding
- H277 (= H271) binding ; binding
Sites not aligning to the query:
- 1 modified: Initiator methionine, Removed
3zdrA Structure of the alcohol dehydrogenase (adh) domain of a bifunctional adhe dehydrogenase from geobacillus thermoglucosidasius ncimb 11955 (see paper)
30% identity, 98% coverage: 10:373/373 of query aligns to 8:400/403 of 3zdrA
6jkpA Crystal structure of sulfoacetaldehyde reductase from bifidobacterium kashiwanohense in complex with NAD+ (see paper)
31% identity, 98% coverage: 6:370/373 of query aligns to 5:370/376 of 6jkpA
- binding nicotinamide-adenine-dinucleotide: F42 (vs. gap), G96 (= G92), D100 (= D96), T137 (= T132), T138 (= T133), T141 (= T136), S143 (= S138), T146 (≠ G141), S181 (≠ T176), V182 (= V177), P183 (= P178)
6jkoA Crystal structure of sulfoacetaldehyde reductase from bifidobacterium kashiwanohense (see paper)
31% identity, 98% coverage: 6:370/373 of query aligns to 5:370/376 of 6jkoA
1o2dA Crystal structure of alcohol dehydrogenase, iron-containing (tm0920) from thermotoga maritima at 1.30 a resolution (see paper)
30% identity, 98% coverage: 6:372/373 of query aligns to 3:356/359 of 1o2dA
- binding fe (iii) ion: D189 (= D188), H193 (= H192), H256 (= H257), H270 (= H271)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: S38 (≠ F42), S39 (≠ N43), E68 (≠ P64), N69 (≠ E65), G95 (= G91), G96 (= G92), S97 (= S93), D100 (= D96), T136 (= T132), T137 (= T133), T140 (= T136), S142 (= S138), Y147 (≠ R143), I149 (≠ L145), K157 (≠ S153), S177 (≠ T176), M178 (≠ V177), L182 (≠ V181), D189 (= D188), H193 (= H192), H270 (= H271)
1vhdA Crystal structure of an iron containing alcohol dehydrogenase (see paper)
30% identity, 98% coverage: 6:372/373 of query aligns to 4:357/361 of 1vhdA
- binding nadp nicotinamide-adenine-dinucleotide phosphate: S39 (≠ F42), S40 (≠ N43), E69 (≠ P64), N70 (≠ E65), G96 (= G91), G97 (= G92), S98 (= S93), D101 (= D96), T137 (= T132), T138 (= T133), T141 (= T136), S143 (= S138), T146 (≠ G141), Y148 (≠ R143), I150 (≠ L145), K158 (≠ S153), S178 (≠ T176), M179 (≠ V177), L183 (≠ V181), D190 (= D188), H194 (= H192), H271 (= H271)
- binding zinc ion: D190 (= D188), H194 (= H192), H257 (= H257), H271 (= H271)
7qlgAAA Lactaldehyde reductase (see paper)
29% identity, 96% coverage: 15:373/373 of query aligns to 12:381/383 of 7qlgAAA
- binding fe (iii) ion: D194 (= D188), H198 (= H192), H261 (= H257), H275 (= H271)
- binding 1,4-dihydronicotinamide adenine dinucleotide: D37 (= D40), T39 (vs. gap), L40 (vs. gap), N69 (≠ E65), G95 (= G91), G96 (= G92), S97 (= S93), D100 (= D96), T138 (= T132), T139 (= T133), T142 (= T136), T147 (≠ G141), N149 (≠ R143), K160 (= K154), L187 (≠ V181), H198 (= H192), H275 (= H271)
1rrmA Crystal structure of lactaldehyde reductase
29% identity, 96% coverage: 15:373/373 of query aligns to 13:382/385 of 1rrmA
- binding adenosine-5-diphosphoribose: D38 (= D40), T40 (vs. gap), L41 (vs. gap), N70 (≠ E65), G96 (= G91), G97 (= G92), S98 (= S93), T139 (= T132), T140 (= T133), T143 (= T136), V152 (≠ L145), K161 (= K154), G183 (≠ T176), M184 (≠ V177), L188 (≠ V181), H276 (= H271)
- binding fe (ii) ion: L258 (≠ T253), C361 (vs. gap)
- binding zinc ion: D195 (= D188), H199 (= H192), H262 (= H257), H276 (= H271)
2bi4A Lactaldehyde:1,2-propanediol oxidoreductase of escherichia coli (see paper)
29% identity, 96% coverage: 15:373/373 of query aligns to 13:382/382 of 2bi4A
- binding fe (iii) ion: D195 (= D188), H199 (= H192), H262 (= H257), H276 (= H271)
- binding nicotinamide-adenine-dinucleotide: D38 (= D40), T40 (vs. gap), L41 (vs. gap), G96 (= G91), G97 (= G92), S98 (= S93), T139 (= T132), T140 (= T133), V152 (≠ L145), K161 (= K154), G183 (≠ T176), M184 (≠ V177), L188 (≠ V181), D195 (= D188), H199 (= H192), H262 (= H257), H276 (= H271)
P0A9S1 Lactaldehyde reductase; Propanediol oxidoreductase; EC 1.1.1.77 from Escherichia coli (strain K12) (see paper)
29% identity, 96% coverage: 15:373/373 of query aligns to 13:382/382 of P0A9S1
- G16 (= G18) mutation to D: No effect on enzyme activity.
- D38 (= D40) mutation to G: Enzyme can now use NADP.
- G96 (= G91) mutation to E: Loss of NAD binding and enzyme activity.
- D195 (= D188) mutation to L: Complete loss of iron-binding.
- H199 (= H192) 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.
5br4A E. Coli lactaldehyde reductase (fuco) m185c mutant (see paper)
29% identity, 96% coverage: 15:373/373 of query aligns to 14:383/385 of 5br4A
- binding nicotinamide-adenine-dinucleotide: D39 (= D40), T41 (vs. gap), L42 (vs. gap), P70 (= P64), G97 (= G91), G98 (= G92), S99 (= S93), D102 (= D96), T140 (= T132), T141 (= T133), T144 (= T136), T149 (≠ G141), N151 (≠ R143), V153 (≠ L145), K162 (= K154), G184 (≠ T176), C185 (≠ V177), L189 (≠ V181), H277 (= H271)
- binding zinc ion: D196 (= D188), H200 (= H192), H263 (= H257), H277 (= H271)
7qlqAAA Lactaldehyde reductase (see paper)
29% identity, 96% coverage: 15:373/373 of query aligns to 12:381/383 of 7qlqAAA
- binding adenosine-5-diphosphoribose: D37 (= D40), T39 (vs. gap), L40 (vs. gap), G95 (= G91), G96 (= G92), S97 (= S93), T138 (= T132), T139 (= T133), T142 (= T136), K160 (= K154), G182 (≠ T176), M183 (≠ V177), L187 (≠ V181), H275 (= H271)
- binding 2-(3,4-dimethoxyphenyl)ethanamide: G149 (≠ R143), V164 (≠ Q158), H198 (= H192), F252 (≠ L248), S253 (≠ G249), H261 (= H257), C360 (vs. gap)
- binding fe (iii) ion: D194 (= D188), H198 (= H192), H261 (= H257), H275 (= H271)
Q59104 4-hydroxybutyrate dehydrogenase; 4HbD; Gamma-hydroxybutyrate dehydrogenase; GHBDH; EC 1.1.1.61 from Cupriavidus necator (Alcaligenes eutrophus) (Ralstonia eutropha) (see paper)
35% identity, 86% coverage: 18:337/373 of query aligns to 15:347/382 of Q59104
- D193 (= D188) mutation to A: Retains very low activity.
- H197 (= H192) mutation to A: Loss of activity.
- H261 (= H257) mutation to A: Loss of activity.
- H265 (≠ Y261) mutation to A: 75% decrease in Vmax. Optimum pH is 9.5.; mutation to C: 95% decrease in Vmax. Optimum pH is 8.5.; mutation to D: Retains very low activity.; mutation to Y: Loss of activity.
- H280 (= H271) mutation to A: Retains very low activity.
5yvmA Crystal structure of the archaeal halo-thermophilic red sea brine pool alcohol dehydrogenase adh/d1 bound to nzq (see paper)
27% identity, 97% coverage: 13:372/373 of query aligns to 15:402/403 of 5yvmA
- binding manganese (ii) ion: D207 (= D188), H211 (= H192), H276 (= H257), H291 (= H271)
- binding 5,6-dihydroxy-nadp: G41 (≠ A39), N44 (vs. gap), M45 (vs. gap), P73 (= P64), N74 (≠ E65), G100 (= G91), G101 (= G92), S102 (= S93), D105 (= D96), S151 (≠ T132), T152 (= T133), T155 (= T136), T160 (≠ G141), Y162 (≠ R143), V164 (≠ L145), K173 (= K154), E195 (≠ T176), L200 (≠ V181), H211 (= H192), H276 (= H257), H280 (≠ Y261), H291 (= H271)
6scgA Structure of adhe form 1 (see paper)
30% identity, 85% coverage: 30:346/373 of query aligns to 28:373/406 of 6scgA
- binding fe (iii) ion: D204 (= D188), H208 (= H192), H274 (= H257), H288 (= H271)
- binding nicotinamide-adenine-dinucleotide: D38 (= D40), F40 (= F42), A69 (≠ P64), D70 (≠ E65), G96 (= G91), G97 (= G92), S98 (= S93), T148 (= T132), T149 (= T133), T152 (= T136), V161 (≠ L145), L197 (≠ V181), H278 (≠ Y261)
5yvrA Crystal structure of the h277a mutant of adh/d1, an archaeal halo- thermophilic red sea brine pool alcohol dehydrogenase (see paper)
27% identity, 97% coverage: 13:372/373 of query aligns to 15:402/403 of 5yvrA
- binding manganese (ii) ion: D207 (= D188), H211 (= H192), H276 (= H257), H291 (= H271)
- binding nadph dihydro-nicotinamide-adenine-dinucleotide phosphate: G41 (≠ A39), S43 (≠ A41), N44 (vs. gap), M45 (vs. gap), G100 (= G91), G101 (= G92), S102 (= S93), D105 (= D96), S151 (≠ T132), T152 (= T133), T155 (= T136), T160 (≠ G141), Y162 (≠ R143), V164 (≠ L145), K173 (= K154), E195 (≠ T176), M196 (≠ V177), L200 (≠ V181), D207 (= D188), H211 (= H192), H291 (= H271)
Query Sequence
>AZOBR_RS27605 FitnessBrowser__azobra:AZOBR_RS27605
MFTPIELVRPPRVLFGGGLVASVGAWARENGIARTLVVADAFNAARVGLLDLPGAVTVFD
RVRPEPDTANLDDLLAVAEAAEPQFVVGFGGGSAMDLAKLAAVLPGSGQTLADVAGAERV
RAKRAALAQVPTTAGTGSEAGTRALVTDPATASKIAVQSLRMLADLAVVDPDLTMTVPRA
VTAATGVDALAHCVEAYTNRKAHPAIDLYALAGIRLIGRWLPRAVADGSDREARAGLALA
SLYGGFCLGPVNTAAGHAVAYPLGTRHHVPHGAANALVFPHVLAFNAPAVPEKTAGVLAA
LGLKPVREPAAVLQAAHGWCLALGCTMSLSDLGVPEDDLPRMAEEAHAIRRLLDNNPRPV
GRDDILAMYRAAY
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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