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Acetoacetyl-CoA reductase (EC 1.1.1.36)

 PHAB_CUPNH              Reviewed;         246 AA.
P14697; Q0KBP7;
01-APR-1990, integrated into UniProtKB/Swiss-Prot.
01-APR-1990, sequence version 1.
18-JUL-2018, entry version 126.
RecName: Full=Acetoacetyl-CoA reductase;
EC=1.1.1.36;
Name=phaB {ECO:0000303|PubMed:1476773};
Synonyms=phbB {ECO:0000303|PubMed:2670935};
OrderedLocusNames=H16_A1439;
Cupriavidus necator (strain ATCC 17699 / H16 / DSM 428 / Stanier 337)
(Ralstonia eutropha).
Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
Burkholderiaceae; Cupriavidus.
NCBI_TaxID=381666;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], IDENTIFICATION, AND FUNCTION.
STRAIN=ATCC 17699 / H16 / DSM 428 / Stanier 337;
PubMed=2670935;
Peoples O.P., Sinskey A.J.;
"Poly-beta-hydroxybutyrate biosynthesis in Alcaligenes eutrophus H16.
Characterization of the genes encoding beta-ketothiolase and
acetoacetyl-CoA reductase.";
J. Biol. Chem. 264:15293-15297(1989).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=ATCC 17699 / H16 / DSM 428 / Stanier 337;
PubMed=16964242; DOI=10.1038/nbt1244;
Pohlmann A., Fricke W.F., Reinecke F., Kusian B., Liesegang H.,
Cramm R., Eitinger T., Ewering C., Poetter M., Schwartz E.,
Strittmatter A., Voss I., Gottschalk G., Steinbuechel A.,
Friedrich B., Bowien B.;
"Genome sequence of the bioplastic-producing 'Knallgas' bacterium
Ralstonia eutropha H16.";
Nat. Biotechnol. 24:1257-1262(2006).
[3]
FUNCTION IN PHB SYNTHESIS, AND PATHWAY.
STRAIN=ATCC 17699 / H16 / DSM 428 / Stanier 337;
PubMed=2670936;
Peoples O.P., Sinskey A.J.;
"Poly-beta-hydroxybutyrate (PHB) biosynthesis in Alcaligenes eutrophus
H16. Identification and characterization of the PHB polymerase gene
(phbC).";
J. Biol. Chem. 264:15298-15303(1989).
[4]
GENE NAME.
PubMed=1476773; DOI=10.1111/j.1574-6968.1992.tb05841.x;
Steinbuechel A., Hustede E., Liebergesell M., Pieper U., Timm A.,
Valentin H.;
"Molecular basis for biosynthesis and accumulation of
polyhydroxyalkanoic acids in bacteria.";
FEMS Microbiol. Rev. 9:217-230(1992).
[5]
X-RAY CRYSTALLOGRAPHY (1.79 ANGSTROMS) OF WILD-TYPE AND MUTANTS LEU-47
AND SER-173 IN COMPLEX WITH ACETOACETYL-COENZYME A AND NADP, FUNCTION,
CATALYTIC ACTIVITY, KINETIC PARAMETERS, SUBUNIT, PATHWAY, AND
MUTAGENESIS OF GLN-47 AND THR-173.
STRAIN=ATCC 17699 / H16 / DSM 428 / Stanier 337;
PubMed=23913421; DOI=10.1128/AEM.01768-13;
Matsumoto K., Tanaka Y., Watanabe T., Motohashi R., Ikeda K.,
Tobitani K., Yao M., Tanaka I., Taguchi S.;
"Directed evolution and structural analysis of NADPH-dependent
acetoacetyl coenzyme A (acetoacetyl-CoA) reductase from Ralstonia
eutropha reveals two mutations responsible for enhanced kinetics.";
Appl. Environ. Microbiol. 79:6134-6139(2013).
[6]
X-RAY CRYSTALLOGRAPHY (1.34 ANGSTROMS) OF APOENZYME AND IN COMPLEXES
WITH ACETOACETYL-COENZYME A AND NADP, SUBUNIT, FUNCTION, CATALYTIC
ACTIVITY, AND MUTAGENESIS OF GLN-47; ASP-94; LYS-99; GLN-147; PHE-148;
GLN-150; THR-173; TYR-185 AND ARG-195.
STRAIN=ATCC 17699 / H16 / DSM 428 / Stanier 337;
PubMed=24211201; DOI=10.1016/j.bbrc.2013.10.150;
Kim J., Chang J.H., Kim E.J., Kim K.J.;
"Crystal structure of (R)-3-hydroxybutyryl-CoA dehydrogenase PhaB from
Ralstonia eutropha.";
Biochem. Biophys. Res. Commun. 443:783-788(2014).
-!- FUNCTION: Catalyzes the chiral reduction of acetoacetyl-CoA to
(R)-3-hydroxybutyryl-CoA. Is involved in the biosynthesis of
polyhydroxybutyrate (PHB), which is accumulated as an
intracellular energy reserve material when cells grow under
conditions of nutrient limitation. {ECO:0000269|PubMed:23913421,
ECO:0000269|PubMed:24211201, ECO:0000269|PubMed:2670935,
ECO:0000269|PubMed:2670936}.
-!- CATALYTIC ACTIVITY: (R)-3-hydroxyacyl-CoA + NADP(+) = 3-oxoacyl-
CoA + NADPH.
-!- CATALYTIC ACTIVITY: (R)-3-hydroxybutanoyl-CoA + NADP(+) =
acetoacetyl-CoA + NADPH.
-!- BIOPHYSICOCHEMICAL PROPERTIES:
Kinetic parameters:
KM=5.7 uM for acetoacetyl-CoA {ECO:0000269|PubMed:23913421};
KM=149 uM for NADPH {ECO:0000269|PubMed:23913421};
Note=kcat is 102 sec(-1).;
-!- PATHWAY: Biopolymer metabolism; poly-(R)-3-hydroxybutanoate
biosynthesis. {ECO:0000269|PubMed:23913421,
ECO:0000269|PubMed:2670936}.
-!- SUBUNIT: Homotetramer. {ECO:0000269|PubMed:23913421,
ECO:0000269|PubMed:24211201}.
-!- SUBCELLULAR LOCATION: Cytoplasm.
-!- SIMILARITY: Belongs to the short-chain dehydrogenases/reductases
(SDR) family. {ECO:0000305}.
-----------------------------------------------------------------------
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EMBL; J04987; AAA21973.1; -; Genomic_DNA.
EMBL; AM260479; CAJ92574.1; -; Genomic_DNA.
PIR; B34340; RDALAE.
RefSeq; WP_010810131.1; NC_008313.1.
PDB; 3VZP; X-ray; 1.79 A; A/B/C/D=2-246.
PDB; 3VZQ; X-ray; 2.00 A; A/B=2-246.
PDB; 3VZR; X-ray; 2.90 A; A/B=2-246.
PDB; 3VZS; X-ray; 2.14 A; A/B/C/D=2-246.
PDB; 4N5L; X-ray; 1.65 A; A/B=1-246.
PDB; 4N5M; X-ray; 1.34 A; A/B=1-246.
PDB; 4N5N; X-ray; 1.90 A; A/B=1-246.
PDBsum; 3VZP; -.
PDBsum; 3VZQ; -.
PDBsum; 3VZR; -.
PDBsum; 3VZS; -.
PDBsum; 4N5L; -.
PDBsum; 4N5M; -.
PDBsum; 4N5N; -.
ProteinModelPortal; P14697; -.
SMR; P14697; -.
STRING; 381666.H16_A1439; -.
EnsemblBacteria; CAJ92574; CAJ92574; H16_A1439.
KEGG; reh:H16_A1439; -.
eggNOG; ENOG4105CHR; Bacteria.
eggNOG; ENOG410XNW1; LUCA.
KO; K00023; -.
OMA; NGGLYMH; -.
UniPathway; UPA00917; -.
Proteomes; UP000008210; Chromosome 1.
GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
GO; GO:0018454; F:acetoacetyl-CoA reductase activity; IEA:UniProtKB-EC.
GO; GO:0042619; P:poly-hydroxybutyrate biosynthetic process; IEA:UniProtKB-KW.
InterPro; IPR011283; Acetoacetyl-CoA_reductase.
InterPro; IPR036291; NAD(P)-bd_dom_sf.
InterPro; IPR020904; Sc_DH/Rdtase_CS.
InterPro; IPR002347; SDR_fam.
Pfam; PF00106; adh_short; 1.
PRINTS; PR00081; GDHRDH.
PRINTS; PR00080; SDRFAMILY.
SUPFAM; SSF51735; SSF51735; 1.
TIGRFAMs; TIGR01829; AcAcCoA_reduct; 1.
PROSITE; PS00061; ADH_SHORT; 1.
1: Evidence at protein level;
3D-structure; Complete proteome; Cytoplasm; NADP; Oxidoreductase;
PHB biosynthesis; Reference proteome.
CHAIN 1 246 Acetoacetyl-CoA reductase.
/FTId=PRO_0000054748.
NP_BIND 13 15 NADP. {ECO:0000269|PubMed:23913421}.
NP_BIND 60 62 NADP. {ECO:0000269|PubMed:23913421}.
NP_BIND 88 92 NADP. {ECO:0000269|PubMed:23913421}.
NP_BIND 183 186 NADP. {ECO:0000269|PubMed:23913421}.
REGION 147 150 Substrate binding.
REGION 184 185 Substrate binding.
ACT_SITE 153 153 Proton acceptor. {ECO:0000255|PROSITE-
ProRule:PRU10001}.
BINDING 35 35 NADP; via amide nitrogen.
{ECO:0000269|PubMed:23913421}.
BINDING 40 40 NADP. {ECO:0000269|PubMed:23913421}.
BINDING 94 94 Substrate.
BINDING 195 195 Substrate.
MUTAGEN 47 47 Q->L: 2.4-fold increase in activity. 2-
fold decrease in affinity for NADPH and
2.8-fold decrease in affinity for
acetoacetyl-CoA.
{ECO:0000269|PubMed:23913421,
ECO:0000269|PubMed:24211201}.
MUTAGEN 94 94 D->A: About 6% of wild-type activity.
{ECO:0000269|PubMed:24211201}.
MUTAGEN 99 99 K->A: Nearly loss of activity.
{ECO:0000269|PubMed:24211201}.
MUTAGEN 147 147 Q->A: About 30% of wild-type activity.
{ECO:0000269|PubMed:24211201}.
MUTAGEN 148 148 F->A: About 30% of wild-type activity.
{ECO:0000269|PubMed:24211201}.
MUTAGEN 150 150 Q->A: About 20% of wild-type activity.
{ECO:0000269|PubMed:24211201}.
MUTAGEN 173 173 T->S: 3.5-fold increase in activity. 4-
fold decrease in affinity for NADPH and
2.4-fold decrease in affinity for
acetoacetyl-CoA.
{ECO:0000269|PubMed:23913421,
ECO:0000269|PubMed:24211201}.
MUTAGEN 185 185 Y->A: Nearly loss of activity.
{ECO:0000269|PubMed:24211201}.
MUTAGEN 195 195 R->A: Nearly loss of activity.
{ECO:0000269|PubMed:24211201}.
STRAND 5 8 {ECO:0000244|PDB:4N5M}.
TURN 9 12 {ECO:0000244|PDB:4N5M}.
HELIX 14 25 {ECO:0000244|PDB:4N5M}.
STRAND 29 34 {ECO:0000244|PDB:4N5M}.
HELIX 41 50 {ECO:0000244|PDB:4N5M}.
STRAND 56 59 {ECO:0000244|PDB:4N5M}.
HELIX 65 78 {ECO:0000244|PDB:4N5M}.
STRAND 82 87 {ECO:0000244|PDB:4N5M}.
HELIX 97 99 {ECO:0000244|PDB:4N5M}.
HELIX 102 112 {ECO:0000244|PDB:4N5M}.
HELIX 114 130 {ECO:0000244|PDB:4N5M}.
STRAND 133 138 {ECO:0000244|PDB:4N5M}.
HELIX 141 145 {ECO:0000244|PDB:4N5M}.
HELIX 151 171 {ECO:0000244|PDB:4N5M}.
HELIX 172 174 {ECO:0000244|PDB:4N5M}.
STRAND 176 183 {ECO:0000244|PDB:4N5M}.
STRAND 185 188 {ECO:0000244|PDB:4N5M}.
HELIX 189 192 {ECO:0000244|PDB:4N5M}.
HELIX 196 204 {ECO:0000244|PDB:4N5M}.
HELIX 214 225 {ECO:0000244|PDB:4N5M}.
HELIX 227 229 {ECO:0000244|PDB:3VZP}.
STRAND 236 240 {ECO:0000244|PDB:4N5M}.
SEQUENCE 246 AA; 26370 MW; AD6739E0F5C93C06 CRC64;
MTQRIAYVTG GMGGIGTAIC QRLAKDGFRV VAGCGPNSPR REKWLEQQKA LGFDFIASEG
NVADWDSTKT AFDKVKSEVG EVDVLINNAG ITRDVVFRKM TRADWDAVID TNLTSLFNVT
KQVIDGMADR GWGRIVNISS VNGQKGQFGQ TNYSTAKAGL HGFTMALAQE VATKGVTVNT
VSPGYIATDM VKAIRQDVLD KIVATIPVKR LGLPEEIASI CAWLSSEESG FSTGADFSLN
GGLHMG


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