SitesBLAST
Comparing Ac3H11_2762 3-oxoacyl-[acyl-carrier protein] reductase (EC 1.1.1.100) 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)
5itvA Crystal structure of bacillus subtilis bacc dihydroanticapsin 7- dehydrogenase in complex with nadh (see paper)
38% identity, 97% coverage: 3:250/255 of query aligns to 2:251/255 of 5itvA
- active site: G18 (= G19), S141 (= S139), Y154 (= Y152), K158 (= K156)
- binding 1,4-dihydronicotinamide adenine dinucleotide: G14 (= G15), S17 (= S18), G18 (= G19), I19 (≠ M20), D38 (= D39), I39 (≠ L40), T61 (≠ V60), I63 (≠ V62), N89 (≠ A88), G91 (= G90), T139 (≠ F137), S141 (= S139), Y154 (= Y152), K158 (= K156), P184 (= P182), G185 (≠ A183), I186 (= I184), I187 (≠ W185)
5itvD Crystal structure of bacillus subtilis bacc dihydroanticapsin 7- dehydrogenase in complex with nadh (see paper)
35% identity, 97% coverage: 3:250/255 of query aligns to 2:223/227 of 5itvD
- active site: G18 (= G19), S141 (= S139), Y154 (= Y152), K158 (= K156)
- binding 1,4-dihydronicotinamide adenine dinucleotide: G14 (= G15), S17 (= S18), G18 (= G19), I19 (≠ M20), D38 (= D39), I39 (≠ L40), T61 (≠ V60), D62 (= D61), I63 (≠ V62), N89 (≠ A88), T139 (≠ F137), S141 (= S139), Y154 (= Y152), K158 (= K156), P184 (= P182), G185 (≠ A183), I187 (≠ W185)
3ak4A Crystal structure of nadh-dependent quinuclidinone reductase from agrobacterium tumefaciens
38% identity, 98% coverage: 3:253/255 of query aligns to 2:257/258 of 3ak4A
- active site: G18 (= G19), S141 (= S139), L151 (≠ K149), Y154 (= Y152), K158 (= K156), E199 (≠ R193)
- binding nicotinamide-adenine-dinucleotide: K17 (≠ S18), G18 (= G19), I19 (≠ M20), D38 (= D39), L39 (= L40), V60 (= V60), D61 (= D61), V62 (= V62), N88 (≠ A88), A89 (= A89), G90 (= G90), T139 (≠ F137), S141 (= S139), Y154 (= Y152), K158 (= K156), G185 (≠ A183), V187 (≠ I184), T189 (= T186), M191 (= M188)
1vl8B Crystal structure of gluconate 5-dehydrogenase (tm0441) from thermotoga maritima at 2.07 a resolution
39% identity, 97% coverage: 3:250/255 of query aligns to 1:248/252 of 1vl8B
- active site: G17 (= G19), S143 (= S139), I154 (≠ K149), Y157 (= Y152), K161 (= K156)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: G13 (= G15), R16 (≠ S18), G17 (= G19), L18 (≠ M20), S37 (≠ D39), R38 (≠ L40), C63 (≠ V60), D64 (= D61), V65 (= V62), A91 (= A88), A92 (= A89), G93 (= G90), I94 (= I91), V114 (= V111), I141 (≠ F137), S143 (= S139), Y157 (= Y152), K161 (= K156), P187 (= P182), G188 (≠ A183), Y190 (≠ W185), T192 (= T186), M194 (= M188), T195 (≠ Y189)
8cxaA Crystal structure of 3-oxoacyl-[acyl-carrier-protein] reductase from mycobacterium smegmatis with bound NAD
39% identity, 96% coverage: 6:250/255 of query aligns to 3:247/251 of 8cxaA
- binding nicotinamide-adenine-dinucleotide: G12 (= G15), Q15 (≠ S18), G16 (= G19), I17 (≠ M20), D36 (= D39), V63 (= V62), N89 (≠ A88), A91 (≠ G90), S94 (≠ P93), I142 (≠ F137), S143 (≠ A138), S144 (= S139), Y157 (= Y152), K161 (= K156), P187 (= P182), H188 (vs. gap), I190 (= I184), I194 (≠ M188)
Q9LBG2 Levodione reductase; (6R)-2,2,6-trimethyl-1,4-cyclohexanedione reductase; EC 1.1.1.- from Leifsonia aquatica (Corynebacterium aquaticum) (see paper)
36% identity, 97% coverage: 4:250/255 of query aligns to 9:262/267 of Q9LBG2
- 17:42 (vs. 12:37, 42% identical) binding
- E103 (vs. gap) mutation E->A,D,N,Q: 26-fold increase in Km and a much lower enantiomeric excess of the reaction products.
1iy8A Crystal structure of levodione reductase (see paper)
37% identity, 95% coverage: 9:250/255 of query aligns to 5:253/258 of 1iy8A
- active site: G15 (= G19), S143 (= S139), Q153 (≠ K149), Y156 (= Y152), K160 (= K156)
- binding nicotinamide-adenine-dinucleotide: G11 (= G15), S14 (= S18), G15 (= G19), L16 (≠ M20), D35 (= D39), V36 (≠ L40), A62 (vs. gap), D63 (= D61), V64 (= V62), N90 (≠ A88), G92 (= G90), I93 (= I91), T141 (≠ F137), S143 (= S139), Y156 (= Y152), K160 (= K156), P186 (= P182), G187 (vs. gap), T191 (= T186), P192 (= P187), M193 (= M188)
4nbuB Crystal structure of fabg from bacillus sp (see paper)
35% identity, 98% coverage: 3:253/255 of query aligns to 2:244/244 of 4nbuB
- active site: G18 (= G19), N111 (= N112), S139 (= S139), Q149 (≠ K149), Y152 (= Y152), K156 (= K156)
- binding acetoacetyl-coenzyme a: D93 (≠ S94), K98 (≠ G99), S139 (= S139), N146 (≠ L146), V147 (≠ P147), Q149 (≠ K149), Y152 (= Y152), F184 (≠ I184), M189 (≠ Y189), K200 (≠ Q200)
- binding 1,4-dihydronicotinamide adenine dinucleotide: G14 (= G15), N17 (≠ S18), G18 (= G19), I19 (≠ M20), D38 (= D39), F39 (≠ L40), V59 (= V60), D60 (= D61), V61 (= V62), N87 (≠ A88), A88 (= A89), G89 (= G90), I90 (= I91), T137 (≠ F137), S139 (= S139), Y152 (= Y152), K156 (= K156), P182 (= P182), F184 (≠ I184), T185 (≠ W185), T187 (≠ P187), M189 (≠ Y189)
7wbcA Hydroxysteroid dehydrogenase wild-type complexed with NAD+ and (4s)-2- 2-methyl-2,4-pentanediol
31% identity, 98% coverage: 5:255/255 of query aligns to 2:250/250 of 7wbcA
- binding calcium ion: Y115 (≠ T114), P116 (≠ G115), H119 (≠ L118)
- binding nicotinamide-adenine-dinucleotide: G12 (= G15), G16 (= G19), I17 (≠ M20), D36 (= D39), V37 (≠ L40), A61 (≠ V60), D62 (= D61), I63 (≠ V62), N89 (≠ A88), F138 (= F137), S140 (= S139), Y153 (= Y152), K157 (= K156), P183 (= P182), F184 (≠ A183), A185 (≠ I184), T187 (= T186), G189 (≠ M188), V190 (≠ Y189)
Q48436 Diacetyl reductase [(S)-acetoin forming]; Acetoin(diacetyl) reductase; AR; Meso-2,3-butanediol dehydrogenase; EC 1.1.1.304 from Klebsiella pneumoniae (see paper)
35% identity, 95% coverage: 12:253/255 of query aligns to 6:255/256 of Q48436
- 6:33 (vs. 12:39, 32% identical) binding
- D59 (= D61) binding
- K156 (= K156) binding
1gegE Cryatal structure analysis of meso-2,3-butanediol dehydrogenase (see paper)
35% identity, 95% coverage: 12:253/255 of query aligns to 6:255/256 of 1gegE
- active site: G13 (= G19), S139 (= S139), Y152 (= Y152), K156 (= K156), V197 (≠ R193)
- binding alpha-D-glucopyranose: R63 (≠ E65), D64 (≠ G66), F67 (≠ A69), E123 (≠ P125)
- binding nicotinamide-adenine-dinucleotide: G9 (= G15), Q12 (≠ S18), I14 (≠ M20), D33 (= D39), Y34 (≠ L40), V58 (= V60), D59 (= D61), V60 (= V62), N86 (≠ A88), A87 (= A89), I109 (≠ V111), S139 (= S139), Y152 (= Y152), K156 (= K156), P182 (= P182), V185 (vs. gap), T187 (= T186), M189 (= M188)
5ha5D Crystal structure of an NAD-bound oxidoreductase from brucella ovis
33% identity, 97% coverage: 6:252/255 of query aligns to 4:242/244 of 5ha5D
- active site: G17 (= G19), S142 (= S139), Y155 (= Y152), K159 (= K156)
- binding nicotinamide-adenine-dinucleotide: G13 (= G15), R16 (≠ S18), G17 (= G19), L18 (≠ M20), D37 (= D39), I38 (≠ L40), L62 (≠ V60), D63 (= D61), V64 (= V62), N90 (≠ A88), A91 (= A89), S142 (= S139), Y155 (= Y152), K159 (= K156), G186 (≠ A183), M188 (≠ W185), S190 (= S197)
3rwbA Crystal structure of complex of 4pal (4-pyridoxolactone) and pldh (tetrameric pyridoxal 4-dehydrogenase) from mesorhizobium loti
37% identity, 98% coverage: 6:255/255 of query aligns to 4:246/247 of 3rwbA
- active site: G17 (= G19), S140 (= S139), Y153 (= Y152), K157 (= K156)
- binding 7-hydroxy-6-methylfuro[3,4-c]pyridin-1(3H)-one: S140 (= S139), N141 (≠ A140), T142 (≠ A141), M150 (≠ K149), Y153 (= Y152), L185 (≠ I184), H196 (≠ S197)
- binding nicotinamide-adenine-dinucleotide: G13 (= G15), Q16 (≠ S18), G17 (= G19), I18 (≠ M20), D37 (= D39), I38 (≠ L40), D60 (= D61), I61 (≠ V62), N87 (≠ A88), A88 (= A89), S89 (≠ G90), I138 (≠ F137), S140 (= S139), Y153 (= Y152), K157 (= K156), P183 (= P182), L185 (≠ I184), I186 (≠ W185), S188 (≠ P187), G190 (≠ Q191), V191 (≠ T192)
3ndrA Crystal structure of tetrameric pyridoxal 4-dehydrogenase from mesorhizobium loti
37% identity, 98% coverage: 6:255/255 of query aligns to 4:246/247 of 3ndrA
- active site: G17 (= G19), S140 (= S139), Y153 (= Y152), K157 (= K156)
- binding nicotinamide-adenine-dinucleotide: G13 (= G15), Q16 (≠ S18), G17 (= G19), I18 (≠ M20), D37 (= D39), I38 (≠ L40), D60 (= D61), I61 (≠ V62), N87 (≠ A88), A88 (= A89), S89 (≠ G90), V110 (= V111), I138 (≠ F137), S140 (= S139), Y153 (= Y152), K157 (= K156), P183 (= P182), L185 (≠ I184), I186 (≠ W185), S188 (≠ P187), G190 (≠ Q191), V191 (≠ T192)
1nfqA Rv2002 gene product from mycobacterium tuberculosis (see paper)
37% identity, 97% coverage: 6:252/255 of query aligns to 4:238/244 of 1nfqA
- active site: G17 (= G19), S139 (= S139), Y152 (= Y152), K156 (= K156)
- binding Androsterone: L91 (≠ A92), E141 (≠ A141), C149 (≠ K149), Y152 (= Y152), V193 (≠ T192), I197 (≠ L201), F198 (≠ L214)
- binding 1,4-dihydronicotinamide adenine dinucleotide: R16 (≠ S18), G17 (= G19), M18 (= M20), D37 (= D39), L39 (≠ N41), L59 (≠ V60), D60 (= D61), V61 (= V62), N87 (≠ A88), A88 (= A89), I137 (≠ F137), S139 (= S139), Y152 (= Y152), K156 (= K156), P182 (= P182), V185 (≠ I184), T187 (= T186), P188 (= P187), M189 (= M188), T190 (≠ Y189)
1nffA Crystal structure of rv2002 gene product from mycobacterium tuberculosis (see paper)
37% identity, 97% coverage: 6:252/255 of query aligns to 4:238/244 of 1nffA
- active site: G17 (= G19), S139 (= S139), Y152 (= Y152), K156 (= K156)
- binding nicotinamide-adenine-dinucleotide: G13 (= G15), R16 (≠ S18), G17 (= G19), M18 (= M20), D37 (= D39), I38 (≠ L40), L39 (≠ N41), L59 (≠ V60), D60 (= D61), V61 (= V62), N87 (≠ A88), A88 (= A89), G89 (= G90), I90 (= I91), I137 (≠ F137), S139 (= S139), Y152 (= Y152), K156 (= K156), P182 (= P182), V185 (≠ I184), T187 (= T186), P188 (= P187), M189 (= M188), T190 (≠ Y189)
P9WGT1 3-alpha-(or 20-beta)-hydroxysteroid dehydrogenase; NADH-dependent 3alpha, 20beta-hydroxysteroid dehydrogenase; EC 1.1.1.53 from Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv) (see paper)
37% identity, 97% coverage: 6:252/255 of query aligns to 5:239/260 of P9WGT1
- I6 (≠ A7) mutation to T: Maximal improvement in solubility; when associated with M-47 and K-69.
- RGM 17:19 (≠ SGM 18:20) binding
- D38 (= D39) binding
- V47 (= V48) mutation to M: Maximal improvement in solubility; when associated with T-6 and K-69.
- DV 61:62 (= DV 61:62) binding
- T69 (≠ A69) mutation to K: Maximal improvement in solubility; when associated with T-6 and M-47.
- N88 (≠ A88) binding
- S140 (= S139) mutation to A: Complete loss of both oxidation of androsterone and reduction of progesterone; when associated with T6; M-47 and K-69.
- Y153 (= Y152) binding ; mutation to F: Complete loss of both oxidation of androsterone and reduction of progesterone; when associated with T6; M-47 and K-69.
- K157 (= K156) binding
- 183:191 (vs. 182:189, 44% identical) binding
4gh5A Crystal structure of s-2-hydroxypropyl coenzyme m dehydrogenase (s- hpcdh) (see paper)
36% identity, 86% coverage: 32:250/255 of query aligns to 29:244/248 of 4gh5A
- active site: N113 (= N112), S141 (= S139), Y154 (= Y152), K158 (= K156)
- binding nicotinamide-adenine-dinucleotide: D36 (= D39), L37 (= L40), A61 (≠ V60), D62 (= D61), V63 (= V62), N89 (≠ A88), A90 (= A89), V112 (= V111), F139 (= F137), S141 (= S139), Y154 (= Y152), K158 (= K156), P184 (= P182), V187 (≠ W185), T190 (vs. gap), G191 (vs. gap), M192 (= M188)
Sites not aligning to the query:
A7IQH5 2-(S)-hydroxypropyl-CoM dehydrogenase 3; S-HPCDH 3; 2-[(S)-2-hydroxypropylthio]ethanesulfonate dehydrogenase 3; Aliphatic epoxide carboxylation component IV; Epoxide carboxylase component IV; SHPCDH3; EC 1.1.1.269 from Xanthobacter autotrophicus (strain ATCC BAA-1158 / Py2) (see 2 papers)
37% identity, 86% coverage: 32:250/255 of query aligns to 31:251/255 of A7IQH5
- D38 (= D39) binding
- DV 64:65 (= DV 61:62) binding
- N91 (≠ A88) binding
- S143 (= S139) binding ; mutation to A: Retains very weak activity.
- Y156 (= Y152) binding ; mutation to A: Retains some activity but with more than 2200-fold decrease in catalytic efficiency.; mutation to F: Loss of activity.
- K160 (= K156) binding ; mutation to A: Loss of activity.
- T188 (≠ I184) binding
- VTSTG 189:193 (≠ WTP-- 185:187) binding
- R211 (≠ V211) mutation to A: Severely impaired in the oxidation of S-HPC or reduction of 2-KPC but largely unaffected in the oxidation and reduction of aliphatic alcohols and ketones.
- K214 (vs. gap) mutation to A: Severely impaired in the oxidation of S-HPC or reduction of 2-KPC but largely unaffected in the oxidation and reduction of aliphatic alcohols and ketones.
- Y215 (vs. gap) binding
Sites not aligning to the query:
4ituA Crystal structure of s-2-hydroxypropyl coenzyme m dehydrogenase (s- hpcdh) bound to s-hpc and nadh (see paper)
37% identity, 86% coverage: 32:250/255 of query aligns to 29:249/253 of 4ituA
- active site: N113 (= N112), S141 (= S139), Y154 (= Y152), K158 (= K156)
- binding 2-{[(2S)-2-hydroxypropyl]sulfanyl}ethanesulfonic acid: S141 (= S139), Y154 (= Y152), T186 (≠ I184), R209 (≠ V211), Y213 (vs. gap)
- binding 1,4-dihydronicotinamide adenine dinucleotide: D36 (= D39), L37 (= L40), D62 (= D61), V63 (= V62), N89 (≠ A88), V112 (= V111), F139 (= F137), S141 (= S139), Y154 (= Y152), K158 (= K156), P184 (= P182), T186 (≠ I184), V187 (≠ W185), T190 (vs. gap), M192 (= M188)
Sites not aligning to the query:
Query Sequence
>Ac3H11_2762 3-oxoacyl-[acyl-carrier protein] reductase (EC 1.1.1.100)
MSVSELAGRRILITGGASGMGEGLVRSLTGMGALVVSMDLNRERGEAVAKAAGARGFMEV
DVADEGSVARAVDAACTRLGGLDVLIHAAGIAPSSPAQGTSLALWEKVFAVNATGTFLMN
RAVFPHMREQGGSIINFASAAGALGLPNKSAYSAAKGAVLAWTRTVAQEWGPYNIRVNAI
APAIWTPMYDQTRSEMSPEQLSAHDALMARVIPLGGKLGDMAQDLVPVLAFLASPGARFM
TGQIFAVDGGTLMVR
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