SitesBLAST
Comparing 7023065 FitnessBrowser__ANA3:7023065 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)
4nbuB Crystal structure of fabg from bacillus sp (see paper)
37% identity, 96% coverage: 2:244/253 of query aligns to 4:242/244 of 4nbuB
- active site: G18 (= G16), N111 (= N111), S139 (= S140), Q149 (≠ T150), Y152 (= Y153), K156 (= K157)
- binding acetoacetyl-coenzyme a: D93 (≠ K93), K98 (≠ H98), S139 (= S140), N146 (≠ S147), V147 (≠ E148), Q149 (≠ T150), Y152 (= Y153), F184 (≠ R185), M189 (= M190), K200 (≠ H202)
- binding 1,4-dihydronicotinamide adenine dinucleotide: G14 (= G12), N17 (≠ G15), G18 (= G16), I19 (= I17), D38 (= D36), F39 (≠ L37), V59 (= V58), D60 (= D59), V61 (= V60), N87 (= N86), A88 (= A87), G89 (= G88), I90 (= I89), T137 (= T138), S139 (= S140), Y152 (= Y153), K156 (= K157), P182 (= P183), F184 (≠ R185), T185 (≠ V186), T187 (= T188), M189 (= M190)
2cfcA Structural basis for stereo selectivity in the (r)- and (s)-hydroxypropylethane thiosulfonate dehydrogenases (see paper)
35% identity, 92% coverage: 4:235/253 of query aligns to 1:238/250 of 2cfcA
- active site: G13 (= G16), S142 (= S140), Y155 (= Y153), K159 (= K157)
- binding (2-[2-ketopropylthio]ethanesulfonate: F149 (≠ S147), R152 (≠ T150), Y155 (= Y153), W195 (vs. gap), R196 (≠ Q193)
- binding nicotinamide-adenine-dinucleotide: G9 (= G12), S12 (≠ G15), G13 (= G16), N14 (≠ I17), D33 (= D36), L34 (= L37), A59 (≠ V58), D60 (= D59), V61 (= V60), N87 (= N86), A88 (= A87), G89 (= G88), I140 (≠ T138), P185 (= P183), G186 (= G184), M187 (≠ R185), I188 (≠ V186), T190 (= T188), P191 (= P189), M192 (= M190), T193 (≠ L191)
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)
35% identity, 92% coverage: 4:235/253 of query aligns to 1:238/250 of Q56840
- M1 (≠ L4) modified: Initiator methionine, Removed
- SGN 12:14 (≠ GGI 15:17) binding
- D33 (= D36) binding
- DV 60:61 (= DV 59:60) binding
- N87 (= N86) binding
- S142 (= S140) mutation to A: Retains weak activity. 120-fold decrease in kcat.; mutation to C: Loss of activity.
- R152 (≠ T150) 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 (= Y153) mutation Y->E,F: Loss of activity.
- K159 (= K157) mutation to A: Loss of activity.
- R179 (= R177) mutation to A: Loss of activity.
- IETPM 188:192 (≠ VDTPM 186:190) binding
- WR 195:196 (≠ -Q 193) binding
- R196 (≠ Q193) mutation to A: Almost loss of activity with the natural substrate 2-KPC, but does not affect activity with 2-butanone as substrate.
- R203 (≠ W200) mutation to A: Slight decrease in catalytic efficiency.
- R209 (≠ E206) mutation to A: Does not affect catalytic efficiency.
5itvA Crystal structure of bacillus subtilis bacc dihydroanticapsin 7- dehydrogenase in complex with nadh (see paper)
34% identity, 96% coverage: 1:244/253 of query aligns to 3:252/255 of 5itvA
- active site: G18 (= G16), S141 (= S140), Y154 (= Y153), K158 (= K157)
- binding 1,4-dihydronicotinamide adenine dinucleotide: G14 (= G12), S17 (≠ G15), G18 (= G16), I19 (= I17), D38 (= D36), I39 (≠ L37), T61 (≠ V58), I63 (≠ V60), N89 (= N86), G91 (= G88), T139 (= T138), S141 (= S140), Y154 (= Y153), K158 (= K157), P184 (= P183), G185 (= G184), I186 (≠ R185), I187 (≠ V186)
3osuA Crystal structure of the 3-oxoacyl-acyl carrier protein reductase, fabg, from staphylococcus aureus
35% identity, 95% coverage: 4:244/253 of query aligns to 3:244/246 of 3osuA
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)
33% identity, 96% coverage: 1:243/253 of query aligns to 1:246/251 of H9XP47
- N15 (≠ G15) binding
- M17 (≠ I17) binding
- D36 (= D36) binding
- D60 (= D59) binding
- V61 (= V60) binding
- N87 (= N86) binding
- S138 (= S140) binding ; binding
- V139 (= V141) mutation to Q: Retains 50% of activity with acetoin as substrate; when associated with A-247.
- S140 (≠ Y142) binding
- Y151 (= Y153) binding ; binding ; binding
- K155 (= K157) binding
- V184 (= V186) binding
- T186 (= T188) binding
- RDK 197:199 (≠ RQE 209:211) mutation to SEAAGKPLGYGTET: Mimics longer alpha6 helix. Retains 3% of activity with acetoin as substrate.
Sites not aligning to the query:
- 247 Q→A: Retains 10% of activity with acetoin as substrate. Retains 50% of activity with acetoin as substrate; when associated with Q-139.
4wecA Crystal structure of a short chain dehydrogenase from mycobacterium smegmatis
35% identity, 99% coverage: 2:251/253 of query aligns to 7:258/258 of 4wecA
- active site: G21 (= G16), S143 (= S140), Q154 (vs. gap), Y157 (= Y153), K161 (= K157)
- binding nicotinamide-adenine-dinucleotide: G17 (= G12), A19 (= A14), S20 (≠ G15), G21 (= G16), I22 (= I17), D41 (= D36), I42 (≠ L37), V61 (= V58), D62 (= D59), V63 (= V60), N89 (= N86), T141 (= T138), Y157 (= Y153), K161 (= K157), P187 (= P183), P189 (≠ R185), V190 (= V186)
3sj7A Structure of beta-ketoacetyl-coa reductase (fabg) from staphylococcus aureus complex with NADPH (see paper)
36% identity, 94% coverage: 6:244/253 of query aligns to 2:237/239 of 3sj7A
- active site: G12 (= G16), S138 (= S140), Q148 (≠ T150), Y151 (= Y153), K155 (= K157)
- binding nadph dihydro-nicotinamide-adenine-dinucleotide phosphate: G8 (= G12), S10 (≠ A14), R11 (≠ G15), I13 (= I17), N31 (vs. gap), Y32 (vs. gap), A33 (= A35), G34 (≠ D36), S35 (≠ L37), A58 (vs. gap), N59 (≠ D59), V60 (= V60), N86 (= N86), A87 (= A87), T109 (≠ V110), S138 (= S140), Y151 (= Y153), K155 (= K157), P181 (= P183), G182 (= G184)
1iy8A Crystal structure of levodione reductase (see paper)
33% identity, 98% coverage: 2:249/253 of query aligns to 1:258/258 of 1iy8A
- active site: G15 (= G16), S143 (= S140), Q153 (≠ T150), Y156 (= Y153), K160 (= K157)
- binding nicotinamide-adenine-dinucleotide: G11 (= G12), S14 (≠ G15), G15 (= G16), L16 (≠ I17), D35 (= D36), V36 (≠ L37), A62 (≠ V58), D63 (= D59), V64 (= V60), N90 (= N86), G92 (= G88), I93 (= I89), T141 (= T138), S143 (= S140), Y156 (= Y153), K160 (= K157), P186 (= P183), G187 (= G184), T191 (= T188), P192 (= P189), M193 (= M190)
Q9LBG2 Levodione reductase; (6R)-2,2,6-trimethyl-1,4-cyclohexanedione reductase; EC 1.1.1.- from Leifsonia aquatica (Corynebacterium aquaticum) (see paper)
33% identity, 98% coverage: 2:249/253 of query aligns to 10:267/267 of Q9LBG2
- 17:42 (vs. 9:34, 38% identical) binding
- E103 (≠ G90) mutation E->A,D,N,Q: 26-fold increase in Km and a much lower enantiomeric excess of the reaction products.
6xewA Structure of serratia marcescens 2,3-butanediol dehydrogenase (see paper)
33% identity, 96% coverage: 2:243/253 of query aligns to 2:246/251 of 6xewA
- active site: G16 (= G16), S138 (= S140), Y151 (= Y153)
- binding r,3-hydroxybutan-2-one: S138 (= S140), S140 (≠ Y142), Y151 (= Y153)
- binding s,3-hydroxybutan-2-one: S138 (= S140), Y151 (= Y153), S182 (≠ G184)
- binding nicotinamide-adenine-dinucleotide: G12 (= G12), N15 (≠ G15), G16 (= G16), M17 (≠ I17), D36 (= D36), W37 (≠ L37), W37 (≠ L37), A38 (≠ S38), I59 (≠ V58), D60 (= D59), V61 (= V60), N87 (= N86), A88 (= A87), G89 (= G88), V110 (= V110), T136 (= T138), S138 (= S140), Y151 (= Y153), K155 (= K157), S182 (≠ G184), L183 (≠ R185), V184 (= V186), T186 (= T188), N187 (≠ P189), M188 (= M190), T189 (≠ L191)
6vspA Structure of serratia marcescens 2,3-butanediol dehydrogenase mutant q247a (see paper)
33% identity, 96% coverage: 2:243/253 of query aligns to 2:246/251 of 6vspA
- active site: G16 (= G16), S138 (= S140), Y151 (= Y153)
- binding nicotinamide-adenine-dinucleotide: G12 (= G12), N15 (≠ G15), G16 (= G16), M17 (≠ I17), D36 (= D36), W37 (≠ L37), W37 (≠ L37), A38 (≠ S38), I59 (≠ V58), D60 (= D59), V61 (= V60), N87 (= N86), A88 (= A87), G89 (= G88), V90 (≠ I89), V110 (= V110), T136 (= T138), S138 (= S140), Y151 (= Y153), K155 (= K157), P181 (= P183), S182 (≠ G184), L183 (≠ R185), V184 (= V186), T186 (= T188), N187 (≠ P189), M188 (= M190), T189 (≠ L191)
6vspB Structure of serratia marcescens 2,3-butanediol dehydrogenase mutant q247a (see paper)
33% identity, 96% coverage: 2:243/253 of query aligns to 4:248/252 of 6vspB
7tzpG Crystal structure of putataive short-chain dehydrogenase/reductase (fabg) from klebsiella pneumoniae subsp. Pneumoniae ntuh-k2044 in complex with nadh (see paper)
36% identity, 96% coverage: 1:244/253 of query aligns to 4:245/247 of 7tzpG
- binding 1,4-dihydronicotinamide adenine dinucleotide: G15 (= G12), R18 (≠ G15), G19 (= G16), I20 (= I17), D39 (= D36), R40 (≠ L37), C63 (≠ V58), I65 (≠ V60), N91 (= N86), G93 (= G88), I94 (= I89), V114 (= V110), Y155 (= Y153), K159 (= K157), I188 (≠ V186), T190 (= T188), T193 (≠ L191)
3ak4A Crystal structure of nadh-dependent quinuclidinone reductase from agrobacterium tumefaciens
35% identity, 95% coverage: 3:243/253 of query aligns to 5:254/258 of 3ak4A
- active site: G18 (= G16), S141 (= S140), L151 (≠ T150), Y154 (= Y153), K158 (= K157), E199 (= E201)
- binding nicotinamide-adenine-dinucleotide: K17 (≠ G15), G18 (= G16), I19 (= I17), D38 (= D36), L39 (= L37), V60 (= V58), D61 (= D59), V62 (= V60), N88 (= N86), A89 (= A87), G90 (= G88), T139 (= T138), S141 (= S140), Y154 (= Y153), K158 (= K157), G185 (= G184), V187 (= V186), T189 (= T188), M191 (= M190)
O18404 3-hydroxyacyl-CoA dehydrogenase type-2; 17-beta-hydroxysteroid dehydrogenase 10; 17-beta-HSD 10; 3-hydroxyacyl-CoA dehydrogenase type II; Hydroxysteroid dehydrogenase; Mitochondrial ribonuclease P protein 2; Mitochondrial RNase P protein 2; Scully protein; Type II HADH; EC 1.1.1.35; EC 1.1.1.51; EC 1.1.1.62; EC 1.1.1.-; EC 1.1.1.53 from Drosophila melanogaster (Fruit fly) (see 3 papers)
35% identity, 86% coverage: 5:222/253 of query aligns to 4:231/255 of O18404
- L33 (≠ A34) mutation to Q: Lethal allele.
- F120 (≠ Y116) mutation to I: Lethal allele.
- Q159 (≠ T150) mutation Missing: Pupal lethal; pupation is developmentally delayed and pupae fail to enclose into adults. Larvae also display reduced levels of ATP, abnormal neuroblast mitochondrial morphology, and the accumulation of unprocessed mitochondrial tRNAs transcripts for tRNA(Ile), tRNA(Gly), tRNA(Val) and tRNA(Leu) (CUN).
- S163 (≠ N154) mutation to F: Pupal lethal; pupation is developmentally delayed and pupae fail to enclose into adults. Larvae also display reduced levels of ATP, abnormal neuroblast mitochondrial morphology, and the accumulation of unprocessed mitochondrial tRNAs transcripts for tRNA(Ile), tRNA(Gly), tRNA(Val) and tRNA(Leu) (CUN).
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)
34% identity, 93% coverage: 2:236/253 of query aligns to 4:230/260 of P9WGT1
- I6 (≠ L4) mutation to T: Maximal improvement in solubility; when associated with M-47 and K-69.
- RGM 17:19 (≠ GGI 15:17) binding
- D38 (= D36) binding
- V47 (≠ F45) mutation to M: Maximal improvement in solubility; when associated with T-6 and K-69.
- DV 61:62 (= DV 59:60) binding
- T69 (≠ E67) mutation to K: Maximal improvement in solubility; when associated with T-6 and M-47.
- N88 (= N86) binding
- S140 (= S140) mutation to A: Complete loss of both oxidation of androsterone and reduction of progesterone; when associated with T6; M-47 and K-69.
- Y153 (= Y153) 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 (= K157) binding
- 183:191 (vs. 183:191, 67% identical) binding
6ixmC Crystal structure of the ketone reductase chkred20 from the genome of chryseobacterium sp. Ca49 complexed with NAD (see paper)
32% identity, 92% coverage: 3:235/253 of query aligns to 3:236/248 of 6ixmC
- active site: G16 (= G16), S142 (= S140), Y155 (= Y153), K159 (= K157)
- binding nicotinamide-adenine-dinucleotide: G12 (= G12), S15 (≠ G15), G16 (= G16), I17 (= I17), D36 (= D36), I37 (≠ L37), A61 (≠ V58), D62 (= D59), T63 (≠ V60), N89 (= N86), A90 (= A87), M140 (≠ T138), S142 (= S140), Y155 (= Y153), K159 (= K157), P185 (= P183), A186 (≠ G184), Y187 (≠ R185), I188 (≠ V186), L192 (≠ M190)
1nfqA Rv2002 gene product from mycobacterium tuberculosis (see paper)
34% identity, 93% coverage: 2:236/253 of query aligns to 3:229/244 of 1nfqA
- active site: G17 (= G16), S139 (= S140), Y152 (= Y153), K156 (= K157)
- binding Androsterone: L91 (= L91), E141 (≠ Y142), C149 (≠ T150), Y152 (= Y153), V193 (≠ Y194), I197 (= I203), F198 (≠ R204)
- binding 1,4-dihydronicotinamide adenine dinucleotide: R16 (≠ G15), G17 (= G16), M18 (≠ I17), D37 (= D36), L39 (≠ S38), L59 (≠ V58), D60 (= D59), V61 (= V60), N87 (= N86), A88 (= A87), I137 (≠ T138), S139 (= S140), Y152 (= Y153), K156 (= K157), P182 (= P183), V185 (= V186), T187 (= T188), P188 (= P189), M189 (= M190), T190 (≠ L191)
1nffA Crystal structure of rv2002 gene product from mycobacterium tuberculosis (see paper)
34% identity, 93% coverage: 2:236/253 of query aligns to 3:229/244 of 1nffA
- active site: G17 (= G16), S139 (= S140), Y152 (= Y153), K156 (= K157)
- binding nicotinamide-adenine-dinucleotide: G13 (= G12), R16 (≠ G15), G17 (= G16), M18 (≠ I17), D37 (= D36), I38 (≠ L37), L39 (≠ S38), L59 (≠ V58), D60 (= D59), V61 (= V60), N87 (= N86), A88 (= A87), G89 (= G88), I90 (= I89), I137 (≠ T138), S139 (= S140), Y152 (= Y153), K156 (= K157), P182 (= P183), V185 (= V186), T187 (= T188), P188 (= P189), M189 (= M190), T190 (≠ L191)
Query Sequence
>7023065 FitnessBrowser__ANA3:7023065
MRLLNKTAVVTGAAGGIGQAIIRKLLAEGARVVAADLSADALKVFNDFPADKLVTFSVDV
TDYKQVEAMVKHAADQFGQLDILINNAGIGLAKPLLQHDPINDFEPVTNVNQKGVYHGIL
AGGRQFQAQGSRGVILNTSSVYAQIASEMTFTYNVSKAAVDMMTKCAALELAPLGVRVCA
VAPGRVDTPMLRQYEALGLWEHIRKEQMRQEFTQPNEIADVVAFLVSDEANCINGCTVNA
SDGFENFKYPLLG
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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