SitesBLAST
Comparing HSERO_RS12375 FitnessBrowser__HerbieS:HSERO_RS12375 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)
H9XP47 Meso-2,3-butanediol dehydrogenase; BDH; meso-2,3-BDH; (R,S)-butane-2,3-diol dehydrogenase; NAD(H)-dependent meso-2,3-BDH; SmBdh; EC 1.1.1.- from Serratia marcescens (see paper)
56% identity, 96% coverage: 10:259/261 of query aligns to 1:248/251 of H9XP47
- N15 (≠ S24) binding
- M17 (≠ I26) binding
- D36 (= D45) binding
- D60 (= D69) binding
- V61 (= V70) binding
- N87 (≠ D96) binding
- S138 (= S147) binding ; binding
- V139 (= V148) mutation to Q: Retains 50% of activity with acetoin as substrate; when associated with A-247.
- S140 (= S149) binding
- Y151 (= Y160) binding ; binding ; binding
- K155 (= K164) binding
- V184 (≠ T193) binding
- T186 (= T195) binding
- RDK 197:199 (≠ LDK 208:210) mutation to SEAAGKPLGYGTET: Mimics longer alpha6 helix. Retains 3% of activity with acetoin as substrate.
- Q247 (= Q258) mutation to A: Retains 10% of activity with acetoin as substrate. Retains 50% of activity with acetoin as substrate; when associated with Q-139.
6xewA Structure of serratia marcescens 2,3-butanediol dehydrogenase (see paper)
56% identity, 95% coverage: 11:259/261 of query aligns to 2:248/251 of 6xewA
- active site: G16 (= G25), S138 (= S147), Y151 (= Y160)
- binding r,3-hydroxybutan-2-one: S138 (= S147), S140 (= S149), Y151 (= Y160)
- binding s,3-hydroxybutan-2-one: S138 (= S147), Y151 (= Y160), S182 (= S191)
- binding nicotinamide-adenine-dinucleotide: G12 (= G21), N15 (≠ S24), G16 (= G25), M17 (≠ I26), D36 (= D45), W37 (≠ R46), W37 (≠ R46), A38 (≠ D47), I59 (≠ T68), D60 (= D69), V61 (= V70), N87 (≠ D96), A88 (= A97), G89 (= G98), V110 (≠ T119), T136 (≠ V145), S138 (= S147), Y151 (= Y160), K155 (= K164), S182 (= S191), L183 (= L192), V184 (≠ T193), T186 (= T195), N187 (≠ A196), M188 (= M197), T189 (= T198)
6vspA Structure of serratia marcescens 2,3-butanediol dehydrogenase mutant q247a (see paper)
56% identity, 95% coverage: 11:259/261 of query aligns to 2:248/251 of 6vspA
- active site: G16 (= G25), S138 (= S147), Y151 (= Y160)
- binding nicotinamide-adenine-dinucleotide: G12 (= G21), N15 (≠ S24), G16 (= G25), M17 (≠ I26), D36 (= D45), W37 (≠ R46), W37 (≠ R46), A38 (≠ D47), I59 (≠ T68), D60 (= D69), V61 (= V70), N87 (≠ D96), A88 (= A97), G89 (= G98), V90 (= V99), V110 (≠ T119), T136 (≠ V145), S138 (= S147), Y151 (= Y160), K155 (= K164), P181 (= P190), S182 (= S191), L183 (= L192), V184 (≠ T193), T186 (= T195), N187 (≠ A196), M188 (= M197), T189 (= T198)
6vspB Structure of serratia marcescens 2,3-butanediol dehydrogenase mutant q247a (see paper)
56% identity, 95% coverage: 11:259/261 of query aligns to 4:250/252 of 6vspB
4nbuB Crystal structure of fabg from bacillus sp (see paper)
36% identity, 94% coverage: 8:253/261 of query aligns to 1:243/244 of 4nbuB
- active site: G18 (= G25), N111 (= N120), S139 (= S147), Q149 (≠ L157), Y152 (= Y160), K156 (= K164)
- binding acetoacetyl-coenzyme a: D93 (≠ E102), K98 (≠ E107), S139 (= S147), N146 (≠ D154), V147 (≠ W155), Q149 (≠ L157), Y152 (= Y160), F184 (≠ L192), M189 (= M197), K200 (= K210)
- binding 1,4-dihydronicotinamide adenine dinucleotide: G14 (= G21), N17 (≠ S24), G18 (= G25), I19 (= I26), D38 (= D45), F39 (≠ R46), V59 (≠ T68), D60 (= D69), V61 (= V70), N87 (≠ D96), A88 (= A97), G89 (= G98), I90 (≠ V99), T137 (≠ V145), S139 (= S147), Y152 (= Y160), K156 (= K164), P182 (= P190), F184 (≠ L192), T185 (= T193), T187 (= T195), M189 (= M197)
5t5qC Crystal structure of short-chain dehydrogenase/reductase sdr:glucose/ribitol dehydrogenase from brucella melitensis
38% identity, 92% coverage: 12:252/261 of query aligns to 5:242/245 of 5t5qC
- active site: G18 (= G25), S140 (= S147), N150 (≠ L157), Y153 (= Y160), K157 (= K164)
- binding nicotinamide-adenine-dinucleotide: N16 (≠ A23), G17 (≠ S24), G18 (= G25), I19 (= I26), D38 (= D45), L39 (≠ R46), D63 (= D69), A64 (≠ V70), S90 (≠ D96), I113 (≠ T119), Y153 (= Y160), K157 (= K164), P182 (= P190), I185 (≠ T193), T187 (= T195), M189 (= M197)
4wecA Crystal structure of a short chain dehydrogenase from mycobacterium smegmatis
37% identity, 96% coverage: 10:259/261 of query aligns to 6:257/258 of 4wecA
- active site: G21 (= G25), S143 (= S147), Q154 (≠ L157), Y157 (= Y160), K161 (= K164)
- binding nicotinamide-adenine-dinucleotide: G17 (= G21), A19 (= A23), S20 (= S24), G21 (= G25), I22 (= I26), D41 (= D45), I42 (≠ R46), V61 (≠ T68), D62 (= D69), V63 (= V70), N89 (≠ D96), T141 (≠ V145), Y157 (= Y160), K161 (= K164), P187 (= P190), P189 (≠ L192), V190 (≠ T193)
2cfcA Structural basis for stereo selectivity in the (r)- and (s)-hydroxypropylethane thiosulfonate dehydrogenases (see paper)
39% identity, 92% coverage: 15:254/261 of query aligns to 3:249/250 of 2cfcA
- active site: G13 (= G25), S142 (= S147), Y155 (= Y160), K159 (= K164)
- binding (2-[2-ketopropylthio]ethanesulfonate: F149 (≠ D154), R152 (≠ L157), Y155 (= Y160), W195 (≠ D200), R196 (≠ M201)
- binding nicotinamide-adenine-dinucleotide: G9 (= G21), S12 (= S24), G13 (= G25), N14 (≠ I26), D33 (= D45), L34 (≠ R46), A59 (≠ T68), D60 (= D69), V61 (= V70), N87 (≠ D96), A88 (= A97), G89 (= G98), I140 (≠ V145), P185 (= P190), G186 (≠ S191), M187 (≠ L192), I188 (≠ T193), T190 (= T195), P191 (≠ A196), M192 (= M197), T193 (= T198)
Q56840 2-(R)-hydroxypropyl-CoM dehydrogenase; R-HPCDH; 2-[(R)-2-hydroxypropylthio]ethanesulfonate dehydrogenase; Aliphatic epoxide carboxylation component III; Epoxide carboxylase component III; RHPCDH1; EC 1.1.1.268 from Xanthobacter autotrophicus (strain ATCC BAA-1158 / Py2) (see 4 papers)
39% identity, 92% coverage: 15:254/261 of query aligns to 3:249/250 of Q56840
- SGN 12:14 (≠ SGI 24:26) binding
- D33 (= D45) binding
- DV 60:61 (= DV 69:70) binding
- N87 (≠ D96) binding
- S142 (= S147) mutation to A: Retains weak activity. 120-fold decrease in kcat.; mutation to C: Loss of activity.
- R152 (≠ L157) binding ; mutation to A: Almost loss of activity with the natural substrate 2-KPC, but does not affect activity with 2-butanone as substrate.
- Y155 (= Y160) mutation Y->E,F: Loss of activity.
- K159 (= K164) mutation to A: Loss of activity.
- R179 (= R184) mutation to A: Loss of activity.
- IETPM 188:192 (≠ THTAM 193:197) binding
- WR 195:196 (≠ DM 200:201) binding
- R196 (≠ M201) mutation to A: Almost loss of activity with the natural substrate 2-KPC, but does not affect activity with 2-butanone as substrate.
- R203 (≠ L208) mutation to A: Slight decrease in catalytic efficiency.
- R209 (= R214) mutation to A: Does not affect catalytic efficiency.
Sites not aligning to the query:
- 1 modified: Initiator methionine, Removed
5itvA Crystal structure of bacillus subtilis bacc dihydroanticapsin 7- dehydrogenase in complex with nadh (see paper)
34% identity, 95% coverage: 9:255/261 of query aligns to 2:255/255 of 5itvA
- active site: G18 (= G25), S141 (= S147), Y154 (= Y160), K158 (= K164)
- binding 1,4-dihydronicotinamide adenine dinucleotide: G14 (= G21), S17 (= S24), G18 (= G25), I19 (= I26), D38 (= D45), I39 (≠ R46), T61 (= T68), I63 (≠ V70), N89 (≠ D96), G91 (= G98), T139 (≠ V145), S141 (= S147), Y154 (= Y160), K158 (= K164), P184 (= P190), G185 (≠ S191), I186 (≠ L192), I187 (≠ T193)
2dtxA Structure of thermoplasma acidophilum aldohexose dehydrogenase (aldt) in complex with d-mannose (see paper)
37% identity, 91% coverage: 15:252/261 of query aligns to 8:245/255 of 2dtxA
2dteA Structure of thermoplasma acidophilum aldohexose dehydrogenase (aldt) in complex with nadh (see paper)
37% identity, 91% coverage: 15:252/261 of query aligns to 8:245/255 of 2dteA
- active site: G18 (= G25), S132 (= S147), Y145 (= Y160), S148 (= S163), K149 (= K164)
- binding 1,4-dihydronicotinamide adenine dinucleotide: G14 (= G21), S16 (≠ A23), M17 (≠ S24), G18 (= G25), I19 (= I26), S38 (≠ A44), I39 (≠ D45), C52 (≠ T68), D53 (= D69), V54 (= V70), N80 (≠ D96), A81 (= A97), I130 (≠ V145), S132 (= S147), Y145 (= Y160), K149 (= K164), P174 (= P190), A175 (≠ S191), T176 (vs. gap), I177 (vs. gap), T179 (vs. gap), P180 (vs. gap), L181 (= L192), V182 (≠ T193)
1vl8B Crystal structure of gluconate 5-dehydrogenase (tm0441) from thermotoga maritima at 2.07 a resolution
35% identity, 93% coverage: 14:255/261 of query aligns to 6:252/252 of 1vl8B
- active site: G17 (= G25), S143 (= S147), I154 (≠ L157), Y157 (= Y160), K161 (= K164)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: G13 (= G21), R16 (≠ S24), G17 (= G25), L18 (≠ I26), S37 (≠ D45), R38 (= R46), C63 (≠ T68), D64 (= D69), V65 (= V70), A91 (≠ D96), A92 (= A97), G93 (= G98), I94 (≠ V99), V114 (≠ T119), I141 (≠ V145), S143 (= S147), Y157 (= Y160), K161 (= K164), P187 (= P190), G188 (≠ S191), Y190 (≠ T193), T192 (= T195), M194 (= M197), T195 (= T198)
1g6kA Crystal structure of glucose dehydrogenase mutant e96a complexed with NAD+
35% identity, 93% coverage: 10:252/261 of query aligns to 3:250/261 of 1g6kA
- active site: G18 (= G25), S145 (= S147), Y158 (= Y160), K162 (= K164)
- binding nicotinamide-adenine-dinucleotide: T17 (≠ S24), G18 (= G25), L19 (≠ I26), R39 (= R46), D65 (= D69), V66 (= V70), N92 (≠ D96), A93 (= A97), G94 (= G98), M143 (≠ V145), S145 (= S147), Y158 (= Y160), P188 (= P190), G189 (≠ S191), I191 (≠ T193), T193 (= T195)
P40288 Glucose 1-dehydrogenase; EC 1.1.1.47 from Priestia megaterium (Bacillus megaterium) (see 2 papers)
35% identity, 93% coverage: 10:252/261 of query aligns to 3:250/261 of P40288
- 11:35 (vs. 18:42, 40% identical) binding
- E96 (≠ F100) mutation E->A,G,K: Heat stable.
- D108 (= D112) mutation to N: Heat stable.
- V112 (= V116) mutation to A: Heat stable.
- E133 (≠ K137) mutation to K: Heat stable.
- V183 (≠ I185) mutation to I: Heat stable.
- P194 (≠ A196) mutation to Q: Heat stable.
- E210 (≠ A212) mutation to K: Heat stable.
- Y217 (≠ R219) mutation to H: Heat stable.
Sites not aligning to the query:
- 252 Q→L: Heat stable.
- 253 Y→C: Heat stable.
- 258 A→G: Heat stable.
Q9LBG2 Levodione reductase; (6R)-2,2,6-trimethyl-1,4-cyclohexanedione reductase; EC 1.1.1.- from Leifsonia aquatica (Corynebacterium aquaticum) (see paper)
37% identity, 94% coverage: 11:255/261 of query aligns to 10:266/267 of Q9LBG2
- 17:42 (vs. 18:43, 50% identical) binding
- E103 (≠ F100) 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, 94% coverage: 11:255/261 of query aligns to 1:257/258 of 1iy8A
- active site: G15 (= G25), S143 (= S147), Q153 (≠ L157), Y156 (= Y160), K160 (= K164)
- binding nicotinamide-adenine-dinucleotide: G11 (= G21), S14 (= S24), G15 (= G25), L16 (≠ I26), D35 (= D45), V36 (≠ R46), A62 (≠ T68), D63 (= D69), V64 (= V70), N90 (≠ D96), G92 (= G98), I93 (≠ V99), T141 (≠ V145), S143 (= S147), Y156 (= Y160), K160 (= K164), P186 (= P190), G187 (≠ S191), T191 (= T195), P192 (≠ A196), M193 (= M197)
1nfqA Rv2002 gene product from mycobacterium tuberculosis (see paper)
35% identity, 93% coverage: 11:254/261 of query aligns to 3:239/244 of 1nfqA
- active site: G17 (= G25), S139 (= S147), Y152 (= Y160), K156 (= K164)
- binding Androsterone: L91 (≠ F100), E141 (≠ S149), C149 (≠ L157), Y152 (= Y160), V193 (≠ M201), I197 (≠ A212), F198 (≠ E213)
- binding 1,4-dihydronicotinamide adenine dinucleotide: R16 (≠ S24), G17 (= G25), M18 (≠ I26), D37 (= D45), L39 (≠ D47), L59 (≠ T68), D60 (= D69), V61 (= V70), N87 (≠ D96), A88 (= A97), I137 (≠ V145), S139 (= S147), Y152 (= Y160), K156 (= K164), P182 (= P190), V185 (≠ T193), T187 (= T195), P188 (≠ A196), M189 (= M197), T190 (= T198)
1nffA Crystal structure of rv2002 gene product from mycobacterium tuberculosis (see paper)
35% identity, 93% coverage: 11:254/261 of query aligns to 3:239/244 of 1nffA
- active site: G17 (= G25), S139 (= S147), Y152 (= Y160), K156 (= K164)
- binding nicotinamide-adenine-dinucleotide: G13 (= G21), R16 (≠ S24), G17 (= G25), M18 (≠ I26), D37 (= D45), I38 (≠ R46), L39 (≠ D47), L59 (≠ T68), D60 (= D69), V61 (= V70), N87 (≠ D96), A88 (= A97), G89 (= G98), I90 (≠ V99), I137 (≠ V145), S139 (= S147), Y152 (= Y160), K156 (= K164), P182 (= P190), V185 (≠ T193), T187 (= T195), P188 (≠ A196), M189 (= M197), T190 (= T198)
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)
35% identity, 93% coverage: 11:254/261 of query aligns to 4:240/260 of P9WGT1
- I6 (≠ E13) mutation to T: Maximal improvement in solubility; when associated with M-47 and K-69.
- RGM 17:19 (≠ SGI 24:26) binding
- D38 (= D45) binding
- V47 (≠ F55) mutation to M: Maximal improvement in solubility; when associated with T-6 and K-69.
- DV 61:62 (= DV 69:70) binding
- T69 (≠ R77) mutation to K: Maximal improvement in solubility; when associated with T-6 and M-47.
- N88 (≠ D96) binding
- S140 (= S147) mutation to A: Complete loss of both oxidation of androsterone and reduction of progesterone; when associated with T6; M-47 and K-69.
- Y153 (= Y160) 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 (= K164) binding
- 183:191 (vs. 190:198, 56% identical) binding
Query Sequence
>HSERO_RS12375 FitnessBrowser__HerbieS:HSERO_RS12375
MSALNPSRLQRFEGKVVIVTGAASGIGEATARRFSDEGARVLLADRDAAALGKVFDSLPP
ERTAARETDVSHHEQVRQLVDFAIERFGQLDVLVSDAGVFAEGNVTEVSPEDWHRVQATN
VNGVFYGAREALPHLEKTRGCIVNVASVSGLAADWNLSAYNASKGAVCNLTRAMALDFGR
KGVRINAVCPSLTHTAMTADMADDPPLLDKFAERIALGRGADPLEIAAVITFLASPDASF
VNGVNLPVDGGLMASNGQPPQ
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