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Protein

Acetoacetyl-CoA reductase

Gene

phaB

Organism
Synechocystis sp. (strain PCC 6803 / Kazusa)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Catalyzes the reduction of acetoacetyl-CoA to (R)-3-hydroxybutyryl-CoA (PubMed:26358291). When expressed in E.coli with Synechocystis PhaA, PhaC and PhaE confers the ability to synthesize up to 12% (w/w) poly(3-hydroxybutyrate) (PHB) depending on the carbon source (PubMed:11010896).1 Publication1 Publication

Miscellaneous

Nitrogen-free medium induces chlorosis in Synechocystis, leading to the degradation of the photosynthetic apparatus and concomitant accumulation of cytoplasmic polyhydroxyalkanoic acid (PHA) granules which in this cyanobacterium are composed of PHB.Curated

Catalytic activityi

(R)-3-hydroxyacyl-CoA + NADP+ = 3-oxoacyl-CoA + NADPH.1 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.1 Publication
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 sitei134Substrate1 Publication1
Active sitei147Proton acceptorPROSITE-ProRule annotation1 Publication1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi18 – 20NADPBy similarity3
Nucleotide bindingi82 – 86NADPBy similarity5
Nucleotide bindingi177 – 180NADPBy similarity4

GO - Molecular functioni

GO - Biological processi

Keywordsi

Molecular functionOxidoreductase
Biological processPHB biosynthesis
LigandNADP

Enzyme and pathway databases

UniPathwayiUPA00917.

Names & Taxonomyi

Protein namesi
Recommended name:
Acetoacetyl-CoA reductase1 Publication (EC:1.1.1.361 Publication)
Gene namesi
Name:phaB1 Publication
Ordered Locus Names:slr1994
OrganismiSynechocystis sp. (strain PCC 6803 / Kazusa)
Taxonomic identifieri1111708 [NCBI]
Taxonomic lineageiBacteriaCyanobacteriaSynechococcalesMerismopediaceaeSynechocystis
Proteomesi
  • UP000001425 Componenti: Chromosome

Pathology & Biotechi

Biotechnological usei

Poly(3-hydroxyalkanoic acids) (PHA), of which PHB is among the most common compounds, are prokaryotic intracellular storage compounds with potential uses as a renewable, biodegradable thermoplastic. Cyanobacterial PHB synthesis is particularly attractive as cyanobacteria use CO2 as the carbon source.Curated

Disruption phenotypei

Double deletion of phaA and phaB leads to loss of synthesis of PHB, no visible growth phenotype.1 Publication

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi134S → A: 12% enzymatic activity. 1 Publication1
Mutagenesisi147Y → A: No enzymatic activity. 1 Publication1
Mutagenesisi151K → A: 5% enzymatic activity. 1 Publication1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000546921 – 240Acetoacetyl-CoA reductaseAdd BLAST240

Structurei

Secondary structure

1240
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Turni5 – 8Combined sources4
Beta strandi10 – 14Combined sources5
Helixi19 – 29Combined sources11
Turni30 – 32Combined sources3
Beta strandi34 – 40Combined sources7
Beta strandi51 – 53Combined sources3
Helixi59 – 73Combined sources15
Beta strandi78 – 81Combined sources4
Helixi91 – 93Combined sources3
Helixi96 – 106Combined sources11
Helixi108 – 124Combined sources17
Beta strandi127 – 132Combined sources6
Helixi135 – 139Combined sources5
Helixi145 – 165Combined sources21
Helixi166 – 168Combined sources3
Beta strandi170 – 177Combined sources8
Helixi185 – 187Combined sources3
Helixi190 – 197Combined sources8
Helixi208 – 219Combined sources12
Turni221 – 223Combined sources3
Beta strandi231 – 235Combined sources5

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
4RZIX-ray2.89A/B/C1-240[»]
ProteinModelPortaliP73826.
SMRiP73826.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni141 – 144Substrate bindingBy similarity4
Regioni178 – 179Substrate bindingBy similarity2

Sequence similaritiesi

Phylogenomic databases

InParanoidiP73826.
KOiK00059.
OMAiNTHFPEC.
PhylomeDBiP73826.

Family and domain databases

Gene3Di3.40.50.720. 2 hits.
InterProiView protein in InterPro
IPR016040. NAD(P)-bd_dom.
IPR020904. Sc_DH/Rdtase_CS.
IPR002347. SDR_fam.
PRINTSiPR00081. GDHRDH.
PR00080. SDRFAMILY.
SUPFAMiSSF51735. SSF51735. 1 hit.
PROSITEiView protein in PROSITE
PS00061. ADH_SHORT. 1 hit.

Sequencei

Sequence statusi: Complete.

P73826-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MLSLGLEDKV IVVTGGNRGI GAAIVKLLQE MGAKVAFTDL ATDGGNTEAL
60 70 80 90 100
GVVANVTDLE SMTAAAAEIT DKLGPVYGVV ANAGITKDNF FPKLTPADWD
110 120 130 140 150
AVLNVNLKGV AYSIKPFIEG MYERKAGSIV AISSISGERG NVGQTNYSAT
160 170 180 190 200
KAGVIGMMKS LAREGARYGV RANAVAPGFI DTEMTLAIRE DIREKITKEI
210 220 230 240
PFRRFGKPEE IAWAVAFLLS PVASSYVTGE VLRVNGAHHT
Length:240
Mass (Da):25,333
Last modified:February 1, 1997 - v1
Checksum:i7C2F8A33C434645F
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BA000022 Genomic DNA. Translation: BAA17883.1.
PIRiS75021.

Genome annotation databases

EnsemblBacteriaiBAA17883; BAA17883; BAA17883.
KEGGisyn:slr1994.
PATRICi23839731. VBISynSp132158_1427.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BA000022 Genomic DNA. Translation: BAA17883.1.
PIRiS75021.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
4RZIX-ray2.89A/B/C1-240[»]
ProteinModelPortaliP73826.
SMRiP73826.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiBAA17883; BAA17883; BAA17883.
KEGGisyn:slr1994.
PATRICi23839731. VBISynSp132158_1427.

Phylogenomic databases

InParanoidiP73826.
KOiK00059.
OMAiNTHFPEC.
PhylomeDBiP73826.

Enzyme and pathway databases

UniPathwayiUPA00917.

Family and domain databases

Gene3Di3.40.50.720. 2 hits.
InterProiView protein in InterPro
IPR016040. NAD(P)-bd_dom.
IPR020904. Sc_DH/Rdtase_CS.
IPR002347. SDR_fam.
PRINTSiPR00081. GDHRDH.
PR00080. SDRFAMILY.
SUPFAMiSSF51735. SSF51735. 1 hit.
PROSITEiView protein in PROSITE
PS00061. ADH_SHORT. 1 hit.
ProtoNetiSearch...

Entry informationi

Entry nameiPHAB_SYNY3
AccessioniPrimary (citable) accession number: P73826
Entry historyiIntegrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: February 1, 1997
Last modified: April 12, 2017
This is version 111 of the entry and version 1 of the sequence. See 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
  4. Synechocystis PCC 6803
    Synechocystis (strain PCC 6803): entries and gene names

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.