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P0AEK3 (FABG_SHIFL) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 53. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
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to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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 names
Name:fabG
Ordered Locus Names:SF1097, S1177
OrganismShigella flexneri [Complete proteome] [HAMAP]
Taxonomic identifier623 [NCBI]
Taxonomic lineageBacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Shigella

Protein attributes

Sequence length244 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Function

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 By similarity.

Catalytic activity

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

Pathway

Lipid metabolism; fatty acid biosynthesis.

Subunit structure

Homotetramer By similarity.

Miscellaneous

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

Sequence similarities

Belongs to the short-chain dehydrogenases/reductases (SDR) family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 2442443-oxoacyl-[acyl-carrier-protein] reductase FabG
PRO_0000054682

Regions

Nucleotide binding12 – 154NADP By similarity
Nucleotide binding59 – 602NADP By similarity
Nucleotide binding151 – 1555NADP By similarity

Sites

Active site1511Proton acceptor By similarity
Metal binding501Calcium 1; via carbonyl oxygen; shared with dimeric partner By similarity
Metal binding531Calcium 1; via carbonyl oxygen; shared with dimeric partner By similarity
Metal binding1451Calcium 2 By similarity
Metal binding2331Calcium 3; shared with dimeric partner By similarity
Metal binding2341Calcium 3; via carbonyl oxygen; shared with dimeric partner By similarity
Binding site371NADP By similarity
Binding site861NADP; via carbonyl oxygen By similarity
Binding site1381Substrate By similarity
Binding site1841NADP; via amide nitrogen and carbonyl oxygen By similarity

Sequences

Sequence LengthMass (Da)Tools
P0AEK3 [UniParc].

Last modified December 20, 2005. Version 1.
Checksum: 48EC1F2A7F7EEFD9

FASTA24425,560
        10         20         30         40         50         60 
MNFEGKIALV TGASRGIGRA IAETLAARGA KVIGTATSEN GAQAISDYLG ANGKGLMLNV 

        70         80         90        100        110        120 
TDPASIESVL EKIRAEFGEV DILVNNAGIT RDNLLMRMKD EEWNDIIETN LSSVFRLSKA 

       130        140        150        160        170        180 
VMRAMMKKRH GRIITIGSVV GTMGNGGQAN YAAAKAGLIG FSKSLAREVA SRGITVNVVA 

       190        200        210        220        230        240 
PGFIETDMTR ALSDDQRAGI LAQVPAGRLG GAQEIANAVA FLASDEAAYI TGETLHVNGG 


MYMV

« Hide

References

[1]"Genome sequence of Shigella flexneri 2a: insights into pathogenicity through comparison with genomes of Escherichia coli K12 and O157."
Jin Q., Yuan Z., Xu J., Wang Y., Shen Y., Lu W., Wang J., Liu H., Yang J., Yang F., Zhang X., Zhang J., Yang G., Wu H., Qu D., Dong J., Sun L., Xue Y. expand/collapse author list , Zhao A., Gao Y., Zhu J., Kan B., Ding K., Chen S., Cheng H., Yao Z., He B., Chen R., Ma D., Qiang B., Wen Y., Hou Y., Yu J.
Nucleic Acids Res. 30:4432-4441(2002) [PubMed: 12384590] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: 301 / Serotype 2a.
[2]"Complete genome sequence and comparative genomics of Shigella flexneri serotype 2a strain 2457T."
Wei J., Goldberg M.B., Burland V., Venkatesan M.M., Deng W., Fournier G., Mayhew G.F., Plunkett G. III, Rose D.J., Darling A., Mau B., Perna N.T., Payne S.M., Runyen-Janecky L.J., Zhou S., Schwartz D.C., Blattner F.R.
Infect. Immun. 71:2775-2786(2003) [PubMed: 12704152] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 700930 / 2457T / Serotype 2a.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		AE005674 Genomic DNA. Translation: AAN42716.1.
AE014073 Genomic DNA. Translation: AAP16604.1.
RefSeqNP_707009.1. NC_004337.2.
NP_836798.1. NC_004741.1.

3D structure databases

ProteinModelPortalP0AEK3.
SMRP0AEK3. Positions 2-244.
ModBaseSearch...

Proteomic databases

PRIDEP0AEK3.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaEBESCT00000088168; EBESCP00000084990; EBESCG00000087213.
EBESCT00000089818; EBESCP00000086454; EBESCG00000088862.
GeneID1026267.
1077578.
GenomeReviewsGene locus SF1097 in contig AE005674_GR.
Gene locus S1177 in contig AE014073_GR.
KEGGsfl:SF1097.
sfx:S1177.
PATRIC18703556. VBIShiFle31049_1283.

Organism-specific databases

CMRSearch...

Phylogenomic databases

GeneTreeEBGT00050000009181.
HOGENOMHBG750976.
OMAAFLIRMT.
ProtClustDBPRK05557.

Enzyme and pathway databases

BioCycSFLE198214:AAN42716.1-MONOMER.

Family and domain databases

InterProIPR011284. 3oxo_ACP_reduc.
IPR002198. DH_sc/Rdtase_SDR.
IPR002347. Glc/ribitol_DH.
IPR016040. NAD(P)-bd_dom.
IPR020904. Sc_DH/Rdtase_CS.
[Graphical view]
Gene3DG3DSA:3.40.50.720. NAD(P)-bd. 1 hit.
KOK00059.
PfamPF00106. adh_short. 1 hit.
[Graphical view]
PRINTSPR00081. GDHRDH.
PR00080. SDRFAMILY.
TIGRFAMsTIGR01830. 3oxo_ACP_reduc. 1 hit.
PROSITEPS00061. ADH_SHORT. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameFABG_SHIFL
AccessionPrimary (citable) accession number: P0AEK3
Secondary accession number(s): P25716, P78221, Q47202
Entry history
Integrated into UniProtKB/Swiss-Prot: December 20, 2005
Last sequence update: December 20, 2005
Last modified: January 25, 2012
This is version 53 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

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