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Protein

Acetoacetyl-CoA reductase

Gene

phbB

Organism
Cupriavidus necator (strain ATCC 17699 / H16 / DSM 428 / Stanier 337) (Ralstonia eutropha)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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.4 Publications

Catalytic activityi

(R)-3-hydroxyacyl-CoA + NADP+ = 3-oxoacyl-CoA + NADPH.
(R)-3-hydroxybutanoyl-CoA + NADP+ = acetoacetyl-CoA + NADPH.

Kineticsi

kcat is 102 sec(-1).

  1. KM=5.7 µM for acetoacetyl-CoA1 Publication
  2. KM=149 µM for NADPH1 Publication

    Pathwayi: poly-(R)-3-hydroxybutanoate biosynthesis

    This protein is involved in the pathway poly-(R)-3-hydroxybutanoate biosynthesis, which is part of Biopolymer metabolism.2 Publications
    View all proteins of this organism that are known to be involved in the pathway poly-(R)-3-hydroxybutanoate biosynthesis and in Biopolymer metabolism.

    Sites

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Binding sitei35NADP; via amide nitrogen1 Publication1
    Binding sitei40NADP1 Publication1
    Binding sitei94Substrate1
    Active sitei153Proton acceptorPROSITE-ProRule annotation1
    Binding sitei195Substrate1

    Regions

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Nucleotide bindingi13 – 15NADP1 Publication3
    Nucleotide bindingi60 – 62NADP1 Publication3
    Nucleotide bindingi88 – 92NADP1 Publication5
    Nucleotide bindingi183 – 186NADP1 Publication4

    GO - Molecular functioni

    GO - Biological processi

    Complete GO annotation...

    Keywords - Molecular functioni

    Oxidoreductase

    Keywords - Biological processi

    PHB biosynthesis

    Keywords - Ligandi

    NADP

    Enzyme and pathway databases

    UniPathwayiUPA00917.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Acetoacetyl-CoA reductase (EC:1.1.1.36)
    Gene namesi
    Name:phbB
    Synonyms:phaB
    Ordered Locus Names:H16_A1439
    OrganismiCupriavidus necator (strain ATCC 17699 / H16 / DSM 428 / Stanier 337) (Ralstonia eutropha)
    Taxonomic identifieri381666 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaBetaproteobacteriaBurkholderialesBurkholderiaceaeCupriavidus
    Proteomesi
    • UP000008210 Componenti: Chromosome 1

    Subcellular locationi

    GO - Cellular componenti

    Complete GO annotation...

    Keywords - Cellular componenti

    Cytoplasm

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Mutagenesisi47Q → L: 2.4-fold increase in activity. 2-fold decrease in affinity for NADPH and 2.8-fold decrease in affinity for acetoacetyl-CoA. 2 Publications1
    Mutagenesisi94D → A: About 6% of wild-type activity. 1 Publication1
    Mutagenesisi99K → A: Nearly loss of activity. 1 Publication1
    Mutagenesisi147Q → A: About 30% of wild-type activity. 1 Publication1
    Mutagenesisi148F → A: About 30% of wild-type activity. 1 Publication1
    Mutagenesisi150Q → A: About 20% of wild-type activity. 1 Publication1
    Mutagenesisi173T → S: 3.5-fold increase in activity. 4-fold decrease in affinity for NADPH and 2.4-fold decrease in affinity for acetoacetyl-CoA. 2 Publications1
    Mutagenesisi185Y → A: Nearly loss of activity. 1 Publication1
    Mutagenesisi195R → A: Nearly loss of activity. 1 Publication1

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    ChainiPRO_00000547481 – 246Acetoacetyl-CoA reductaseAdd BLAST246

    Interactioni

    Subunit structurei

    Homotetramer.2 Publications

    Protein-protein interaction databases

    STRINGi381666.H16_A1439.

    Structurei

    Secondary structure

    1246
    Legend: HelixTurnBeta strandPDB Structure known for this area
    Show more details
    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Beta strandi5 – 8Combined sources4
    Turni9 – 12Combined sources4
    Helixi14 – 25Combined sources12
    Beta strandi29 – 34Combined sources6
    Helixi41 – 50Combined sources10
    Beta strandi56 – 59Combined sources4
    Helixi65 – 78Combined sources14
    Beta strandi82 – 87Combined sources6
    Helixi97 – 99Combined sources3
    Helixi102 – 112Combined sources11
    Helixi114 – 130Combined sources17
    Beta strandi133 – 138Combined sources6
    Helixi141 – 145Combined sources5
    Helixi151 – 171Combined sources21
    Helixi172 – 174Combined sources3
    Beta strandi176 – 183Combined sources8
    Beta strandi185 – 188Combined sources4
    Helixi189 – 192Combined sources4
    Helixi196 – 204Combined sources9
    Helixi214 – 225Combined sources12
    Helixi227 – 229Combined sources3
    Beta strandi236 – 240Combined sources5

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    PDB entryMethodResolution (Å)ChainPositionsPDBsum
    3VZPX-ray1.79A/B/C/D2-246[»]
    3VZQX-ray2.00A/B2-246[»]
    3VZRX-ray2.90A/B2-246[»]
    3VZSX-ray2.14A/B/C/D2-246[»]
    4N5LX-ray1.65A/B1-246[»]
    4N5MX-ray1.34A/B1-246[»]
    4N5NX-ray1.90A/B1-246[»]
    ProteinModelPortaliP14697.
    SMRiP14697.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Region

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Regioni147 – 150Substrate binding4
    Regioni184 – 185Substrate binding2

    Sequence similaritiesi

    Phylogenomic databases

    eggNOGiENOG4105CHR. Bacteria.
    ENOG410XNW1. LUCA.
    KOiK00023.
    OMAiETEMVMA.

    Family and domain databases

    Gene3Di3.40.50.720. 1 hit.
    InterProiIPR011283. Acetoacetyl-CoA_reductase.
    IPR016040. NAD(P)-bd_dom.
    IPR020904. Sc_DH/Rdtase_CS.
    IPR002347. SDR_fam.
    [Graphical view]
    PANTHERiPTHR24322. PTHR24322. 2 hits.
    PfamiPF00106. adh_short. 1 hit.
    [Graphical view]
    PRINTSiPR00081. GDHRDH.
    PR00080. SDRFAMILY.
    SUPFAMiSSF51735. SSF51735. 1 hit.
    TIGRFAMsiTIGR01829. AcAcCoA_reduct. 1 hit.
    PROSITEiPS00061. ADH_SHORT. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    P14697-1 [UniParc]FASTAAdd to basket

    « Hide

            10         20         30         40         50
    MTQRIAYVTG GMGGIGTAIC QRLAKDGFRV VAGCGPNSPR REKWLEQQKA
    60 70 80 90 100
    LGFDFIASEG NVADWDSTKT AFDKVKSEVG EVDVLINNAG ITRDVVFRKM
    110 120 130 140 150
    TRADWDAVID TNLTSLFNVT KQVIDGMADR GWGRIVNISS VNGQKGQFGQ
    160 170 180 190 200
    TNYSTAKAGL HGFTMALAQE VATKGVTVNT VSPGYIATDM VKAIRQDVLD
    210 220 230 240
    KIVATIPVKR LGLPEEIASI CAWLSSEESG FSTGADFSLN GGLHMG
    Length:246
    Mass (Da):26,370
    Last modified:April 1, 1990 - v1
    Checksum:iAD6739E0F5C93C06
    GO

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    J04987 Genomic DNA. Translation: AAA21973.1.
    AM260479 Genomic DNA. Translation: CAJ92574.1.
    PIRiB34340. RDALAE.
    RefSeqiWP_010810131.1. NC_008313.1.

    Genome annotation databases

    EnsemblBacteriaiCAJ92574; CAJ92574; H16_A1439.
    GeneIDi4249784.
    KEGGireh:H16_A1439.
    PATRICi35232343. VBIRalEut6770_1828.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    J04987 Genomic DNA. Translation: AAA21973.1.
    AM260479 Genomic DNA. Translation: CAJ92574.1.
    PIRiB34340. RDALAE.
    RefSeqiWP_010810131.1. NC_008313.1.

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    PDB entryMethodResolution (Å)ChainPositionsPDBsum
    3VZPX-ray1.79A/B/C/D2-246[»]
    3VZQX-ray2.00A/B2-246[»]
    3VZRX-ray2.90A/B2-246[»]
    3VZSX-ray2.14A/B/C/D2-246[»]
    4N5LX-ray1.65A/B1-246[»]
    4N5MX-ray1.34A/B1-246[»]
    4N5NX-ray1.90A/B1-246[»]
    ProteinModelPortaliP14697.
    SMRiP14697.
    ModBaseiSearch...
    MobiDBiSearch...

    Protein-protein interaction databases

    STRINGi381666.H16_A1439.

    Protocols and materials databases

    Structural Biology KnowledgebaseSearch...

    Genome annotation databases

    EnsemblBacteriaiCAJ92574; CAJ92574; H16_A1439.
    GeneIDi4249784.
    KEGGireh:H16_A1439.
    PATRICi35232343. VBIRalEut6770_1828.

    Phylogenomic databases

    eggNOGiENOG4105CHR. Bacteria.
    ENOG410XNW1. LUCA.
    KOiK00023.
    OMAiETEMVMA.

    Enzyme and pathway databases

    UniPathwayiUPA00917.

    Family and domain databases

    Gene3Di3.40.50.720. 1 hit.
    InterProiIPR011283. Acetoacetyl-CoA_reductase.
    IPR016040. NAD(P)-bd_dom.
    IPR020904. Sc_DH/Rdtase_CS.
    IPR002347. SDR_fam.
    [Graphical view]
    PANTHERiPTHR24322. PTHR24322. 2 hits.
    PfamiPF00106. adh_short. 1 hit.
    [Graphical view]
    PRINTSiPR00081. GDHRDH.
    PR00080. SDRFAMILY.
    SUPFAMiSSF51735. SSF51735. 1 hit.
    TIGRFAMsiTIGR01829. AcAcCoA_reduct. 1 hit.
    PROSITEiPS00061. ADH_SHORT. 1 hit.
    [Graphical view]
    ProtoNetiSearch...

    Entry informationi

    Entry nameiPHBB_CUPNH
    AccessioniPrimary (citable) accession number: P14697
    Secondary accession number(s): Q0KBP7
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: April 1, 1990
    Last sequence update: April 1, 1990
    Last modified: November 2, 2016
    This is version 118 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programProkaryotic Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. PATHWAY comments
      Index of metabolic and biosynthesis pathways
    2. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    3. SIMILARITY comments
      Index of protein domains and families

    Similar proteinsi

    Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
    100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
    90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
    50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.