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Protein

3-oxoacyl-[acyl-carrier-protein] reductase

Gene

fabG

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 NADPH-dependent reduction of beta-ketoacyl-ACP substrates to beta-hydroxyacyl-ACP products, the first reductive step in the elongation cycle of fatty acid biosynthesis (Probable). Is capable of reducing acetoacetyl-CoA, but less well than its paralog PhaB (PubMed:26358291).1 Publication1 Publication

Catalytic activityi

(3R)-3-hydroxyacyl-[acyl-carrier-protein] + NADP+ = 3-oxoacyl-[acyl-carrier-protein] + NADPH.1 Publication

Pathwayi: fatty acid biosynthesis

This protein is involved in the pathway fatty acid biosynthesis, which is part of Lipid metabolism.
View all proteins of this organism that are known to be involved in the pathway fatty acid biosynthesis and in Lipid metabolism.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Binding sitei143SubstrateBy similarity1
Active sitei156Proton acceptorPROSITE-ProRule annotation1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi11 – 35NADPBy similarityAdd BLAST25

GO - Molecular functioni

GO - Biological processi

Keywordsi

Molecular functionOxidoreductase
Biological processFatty acid biosynthesis, Fatty acid metabolism, Lipid biosynthesis, Lipid metabolism
LigandNADP

Enzyme and pathway databases

UniPathwayiUPA00094.

Names & Taxonomyi

Protein namesi
Recommended name:
3-oxoacyl-[acyl-carrier-protein] reductase1 Publication (EC:1.1.1.1001 Publication)
Alternative name(s):
3-ketoacyl-acyl carrier protein reductase
Gene namesi
Name:fabG
Ordered Locus Names:slr0886
OrganismiSynechocystis sp. (strain PCC 6803 / Kazusa)
Taxonomic identifieri1111708 [NCBI]
Taxonomic lineageiBacteriaCyanobacteriaSynechococcalesMerismopediaceaeSynechocystis
Proteomesi
  • UP000001425 Componenti: Chromosome

Pathology & Biotechi

Biotechnological usei

Mutation of key residues to match those found in its paralog PhaB increases it activity on acetoacetyl-CoA, not its usual substrate, which might help shift cellular metabolism to make poly(3-hydroxybutyrate) (PHB), a compound that has potential uses as a renewable, biodegradable thermoplastic (PubMed:26358291). 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.1 Publication

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi14A → G: 4.2-fold increase in activity on acetoacetyl-CoA. 1 Publication1
Mutagenesisi151P → F: 2.7-fold increase in activity on acetoacetyl-CoA. 1 Publication1
Mutagenesisi151P → V: 5.7-fold increase in activity on acetoacetyl-CoA. 1 Publication1
Mutagenesisi160K → A: Almost no activity on acetoacetyl-CoA. 1 Publication1
Mutagenesisi188F → Y: 3.3-fold increase in activity on acetoacetyl-CoA. 1 Publication1
Mutagenesisi198N → R: 3.5-fold increase in activity on acetoacetyl-CoA. 1 Publication1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000546911 – 2473-oxoacyl-[acyl-carrier-protein] reductaseAdd BLAST247

Interactioni

Protein-protein interaction databases

IntActiP73574. 1 interactor.

Structurei

Secondary structure

1247
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi4 – 6Combined sources3
Beta strandi8 – 13Combined sources6
Helixi17 – 28Combined sources12
Beta strandi32 – 39Combined sources8
Helixi41 – 53Combined sources13
Beta strandi57 – 62Combined sources6
Helixi68 – 82Combined sources15
Beta strandi87 – 90Combined sources4
Helixi100 – 102Combined sources3
Helixi105 – 115Combined sources11
Helixi117 – 132Combined sources16
Beta strandi137 – 141Combined sources5
Helixi144 – 148Combined sources5
Helixi154 – 174Combined sources21
Helixi175 – 177Combined sources3
Beta strandi180 – 186Combined sources7
Helixi203 – 205Combined sources3
Helixi214 – 226Combined sources13
Helixi228 – 232Combined sources5
Beta strandi237 – 241Combined sources5

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
4RZHX-ray2.20A/B1-247[»]
ProteinModelPortaliP73574.
SMRiP73574.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

InParanoidiP73574.
KOiK00059.
OMAiCTQIANL.
PhylomeDBiP73574.

Family and domain databases

InterProiView protein in InterPro
IPR011284. 3oxo_ACP_reduc.
IPR016040. NAD(P)-bd_dom.
IPR020904. Sc_DH/Rdtase_CS.
IPR002347. SDR_fam.
PRINTSiPR00081. GDHRDH.
PR00080. SDRFAMILY.
SUPFAMiSSF51735. SSF51735. 1 hit.
TIGRFAMsiTIGR01830. 3oxo_ACP_reduc. 1 hit.
PROSITEiView protein in PROSITE
PS00061. ADH_SHORT. 1 hit.

Sequencei

Sequence statusi: Complete.

P73574-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MTALTAQVAL VTGASRGIGK ATALALAATG MKVVVNYAQS STAADAVVAE
60 70 80 90 100
IIANGGEAIA VQANVANADE VDQLIKTTLD KFSRIDVLVN NAGITRDTLL
110 120 130 140 150
LRMKLEDWQA VIDLNLTGVF LCTKAVSKLM LKQKSGRIIN ITSVAGMMGN
160 170 180 190 200
PGQANYSAAK AGVIGFTKTV AKELASRGVT VNAVAPGFIA TDMTENLNAE
210 220 230 240
PILQFIPLAR YGQPEEVAGT IRFLATDPAA AYITGQTFNV DGGMVMF
Length:247
Mass (Da):25,724
Last modified:February 1, 1997 - v1
Checksum:i91EBF9409C777F20
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BA000022 Genomic DNA. Translation: BAA17614.1.
PIRiS77280.

Genome annotation databases

EnsemblBacteriaiBAA17614; BAA17614; BAA17614.
KEGGisyn:slr0886.
PATRICi23839140. VBISynSp132158_1134.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BA000022 Genomic DNA. Translation: BAA17614.1.
PIRiS77280.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
4RZHX-ray2.20A/B1-247[»]
ProteinModelPortaliP73574.
SMRiP73574.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiP73574. 1 interactor.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiBAA17614; BAA17614; BAA17614.
KEGGisyn:slr0886.
PATRICi23839140. VBISynSp132158_1134.

Phylogenomic databases

InParanoidiP73574.
KOiK00059.
OMAiCTQIANL.
PhylomeDBiP73574.

Enzyme and pathway databases

UniPathwayiUPA00094.

Family and domain databases

InterProiView protein in InterPro
IPR011284. 3oxo_ACP_reduc.
IPR016040. NAD(P)-bd_dom.
IPR020904. Sc_DH/Rdtase_CS.
IPR002347. SDR_fam.
PRINTSiPR00081. GDHRDH.
PR00080. SDRFAMILY.
SUPFAMiSSF51735. SSF51735. 1 hit.
TIGRFAMsiTIGR01830. 3oxo_ACP_reduc. 1 hit.
PROSITEiView protein in PROSITE
PS00061. ADH_SHORT. 1 hit.
ProtoNetiSearch...

Entry informationi

Entry nameiFABG_SYNY3
AccessioniPrimary (citable) accession number: P73574
Entry historyiIntegrated into UniProtKB/Swiss-Prot: December 15, 1998
Last sequence update: February 1, 1997
Last modified: May 10, 2017
This is version 116 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.