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P0A2C9

- FABG_SALTY

UniProt

P0A2C9 - FABG_SALTY

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Protein

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

Gene

fabG

Organism
Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)
Status
Reviewed - 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.1 Publication

Catalytic activityi

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

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei37 – 371NADPBy similarity
Metal bindingi50 – 501Calcium 1; via carbonyl oxygen; shared with dimeric partnerBy similarity
Metal bindingi53 – 531Calcium 1; via carbonyl oxygen; shared with dimeric partnerBy similarity
Binding sitei86 – 861NADP; via carbonyl oxygenBy similarity
Binding sitei138 – 1381SubstrateBy similarity
Metal bindingi145 – 1451Calcium 2By similarity
Active sitei151 – 1511Proton acceptorPROSITE-ProRule annotation
Binding sitei184 – 1841NADP; via amide nitrogen and carbonyl oxygenBy similarity
Metal bindingi233 – 2331Calcium 3; shared with dimeric partnerBy similarity
Metal bindingi234 – 2341Calcium 3; via carbonyl oxygen; shared with dimeric partnerBy similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi12 – 154NADPBy similarity
Nucleotide bindingi59 – 602NADPBy similarity
Nucleotide bindingi151 – 1555NADPBy similarity

GO - Molecular functioni

  1. 3-oxoacyl-[acyl-carrier-protein] reductase (NADPH) activity Source: UniProtKB
  2. metal ion binding Source: UniProtKB-KW
  3. NAD binding Source: InterPro
  4. NADP binding Source: UniProtKB

GO - Biological processi

  1. fatty acid elongation Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Biological processi

Fatty acid biosynthesis, Fatty acid metabolism, Lipid biosynthesis, Lipid metabolism

Keywords - Ligandi

Calcium, Metal-binding, NADP

Enzyme and pathway databases

BioCyciSENT99287:GCTI-1204-MONOMER.
UniPathwayiUPA00094.

Names & Taxonomyi

Protein namesi
Recommended name:
3-oxoacyl-[acyl-carrier-protein] reductase FabG (EC:1.1.1.100)
Alternative name(s):
3-ketoacyl-acyl carrier protein reductase
Beta-Ketoacyl-acyl carrier protein reductase
Beta-ketoacyl-ACP reductase
Gene namesi
Name:fabG
Ordered Locus Names:STM1195
OrganismiSalmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)
Taxonomic identifieri99287 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeSalmonella
ProteomesiUP000001014: Chromosome

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi125 – 1251M → I: Loss of the temperature-sensitive phenotype; when associated with T-223. 1 Publication
Mutagenesisi223 – 2231A → T: Loss of the temperature-sensitive phenotype; when associated with I-125. 1 Publication
Mutagenesisi224 – 2241S → F: Distorts the local conformation and prevent stacking around Phe-221. The S224F mutation would additionally disrupt the hydrogen bond formed between Ser-224 and Glu-226. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 2442443-oxoacyl-[acyl-carrier-protein] reductase FabGPRO_0000054681Add
BLAST

Proteomic databases

PaxDbiP0A2C9.
PRIDEiP0A2C9.

Interactioni

Subunit structurei

Homotetramer.By similarity

Protein-protein interaction databases

STRINGi99287.STM1195.

Structurei

3D structure databases

ProteinModelPortaliP0A2C9.
SMRiP0A2C9. Positions 2-244.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

eggNOGiCOG1028.
KOiK00059.
OMAiDEFGAID.
OrthoDBiEOG6N3CR8.
PhylomeDBiP0A2C9.

Family and domain databases

Gene3Di3.40.50.720. 1 hit.
InterProiIPR011284. 3oxo_ACP_reduc.
IPR002198. DH_sc/Rdtase_SDR.
IPR002347. Glc/ribitol_DH.
IPR016040. NAD(P)-bd_dom.
IPR020904. Sc_DH/Rdtase_CS.
[Graphical view]
PfamiPF00106. adh_short. 1 hit.
[Graphical view]
PRINTSiPR00081. GDHRDH.
PR00080. SDRFAMILY.
TIGRFAMsiTIGR01830. 3oxo_ACP_reduc. 1 hit.
PROSITEiPS00061. ADH_SHORT. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P0A2C9-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MSFEGKIALV TGASRGIGRA IAETLVARGA KVIGTATSEN GAKNISDYLG
60 70 80 90 100
ANGKGLMLNV TDPASIESVL ENIRAEFGEV DILVNNAGIT RDNLLMRMKD
110 120 130 140 150
DEWNDIIETN LSSVFRLSKA VMRAMMKKRC GRIITIGSVV GTMGNAGQAN
160 170 180 190 200
YAAAKAGLIG FSKSLAREVA SRGITVNVVA PGFIETDMTR ALSDDQRAGI
210 220 230 240
LAQVPAGRLG GAQEIASAVA FLASDEASYI TGETLHVNGG MYMV
Length:244
Mass (Da):25,545
Last modified:March 15, 2005 - v1
Checksum:i86D71DA3E9AF0363
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF044668 Genomic DNA. Translation: AAC38650.1.
AE006468 Genomic DNA. Translation: AAL20124.1.
RefSeqiNP_460165.1. NC_003197.1.

Genome annotation databases

EnsemblBacteriaiAAL20124; AAL20124; STM1195.
GeneIDi1252713.
KEGGistm:STM1195.
PATRICi32380839. VBISalEnt20916_1264.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF044668 Genomic DNA. Translation: AAC38650.1 .
AE006468 Genomic DNA. Translation: AAL20124.1 .
RefSeqi NP_460165.1. NC_003197.1.

3D structure databases

ProteinModelPortali P0A2C9.
SMRi P0A2C9. Positions 2-244.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 99287.STM1195.

Proteomic databases

PaxDbi P0A2C9.
PRIDEi P0A2C9.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai AAL20124 ; AAL20124 ; STM1195 .
GeneIDi 1252713.
KEGGi stm:STM1195.
PATRICi 32380839. VBISalEnt20916_1264.

Phylogenomic databases

eggNOGi COG1028.
KOi K00059.
OMAi DEFGAID.
OrthoDBi EOG6N3CR8.
PhylomeDBi P0A2C9.

Enzyme and pathway databases

UniPathwayi UPA00094 .
BioCyci SENT99287:GCTI-1204-MONOMER.

Family and domain databases

Gene3Di 3.40.50.720. 1 hit.
InterProi IPR011284. 3oxo_ACP_reduc.
IPR002198. DH_sc/Rdtase_SDR.
IPR002347. Glc/ribitol_DH.
IPR016040. NAD(P)-bd_dom.
IPR020904. Sc_DH/Rdtase_CS.
[Graphical view ]
Pfami PF00106. adh_short. 1 hit.
[Graphical view ]
PRINTSi PR00081. GDHRDH.
PR00080. SDRFAMILY.
TIGRFAMsi TIGR01830. 3oxo_ACP_reduc. 1 hit.
PROSITEi PS00061. ADH_SHORT. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Transcriptional analysis of essential genes of the Escherichia coli fatty acid biosynthesis gene cluster by functional replacement with the analogous Salmonella typhimurium gene cluster."
    Zhang Y., Cronan J.E. Jr.
    J. Bacteriol. 180:3295-3303(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: LT2.
  2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: LT2 / SGSC1412 / ATCC 700720.
  3. "Isolation and characterization of beta-ketoacyl-acyl carrier protein reductase (fabG) mutants of Escherichia coli and Salmonella enterica serovar Typhimurium."
    Lai C.Y., Cronan J.E.
    J. Bacteriol. 186:1869-1878(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN FATTY ACID BIOSYNTHESIS, MUTAGENESIS OF MET-125; ALA-223 AND SER-224.

Entry informationi

Entry nameiFABG_SALTY
AccessioniPrimary (citable) accession number: P0A2C9
Secondary accession number(s): O85141
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 15, 2005
Last sequence update: March 15, 2005
Last modified: October 1, 2014
This is version 70 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Miscellaneous

Calcium ions stabilize the structure, and may inhibit FabG activity by obstructing access to the active site.By similarity

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3