P0AEK3 (FABG_SHIFL) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

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 names

Name:	fabG
Ordered Locus Names:	SF1097, S1177

Organism

Shigella flexneri [Complete proteome] [HAMAP]

Taxonomic identifier

623 [NCBI]

Taxonomic lineage

cellular organisms › Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Shigella

Protein attributes

Sequence length	244 AA.
Sequence status	Complete.
Protein existence	Inferred 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.

Ontologies

Keywords
Biological process	Fatty acid biosynthesis Fatty acid metabolism Lipid biosynthesis Lipid metabolism
Ligand	Calcium Metal-binding NADP
Molecular function	Oxidoreductase
Technical term	Complete proteome
Gene Ontology (GO)
Biological_process	fatty acid elongation Inferred from sequence or structural similarity. Source: UniProtKB
Molecular_function	3-oxoacyl-[acyl-carrier-protein] reductase (NADPH) activity Inferred from sequence or structural similarity. Source: UniProtKB NAD binding Inferred from electronic annotation. Source: InterPro NADP binding Inferred from sequence or structural similarity. Source: UniProtKB metal ion binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 244	244	3-oxoacyl-[acyl-carrier-protein] reductase FabG		PRO_0000054682
Regions
	Nucleotide binding	12 – 15	4	NADP By similarity
	Nucleotide binding	59 – 60	2	NADP By similarity
	Nucleotide binding	151 – 155	5	NADP By similarity
Sites
	Active site	151	1	Proton acceptor By similarity
	Metal binding	50	1	Calcium 1; via carbonyl oxygen; shared with dimeric partner By similarity
	Metal binding	53	1	Calcium 1; via carbonyl oxygen; shared with dimeric partner By similarity
	Metal binding	145	1	Calcium 2 By similarity
	Metal binding	233	1	Calcium 3; shared with dimeric partner By similarity
	Metal binding	234	1	Calcium 3; via carbonyl oxygen; shared with dimeric partner By similarity
	Binding site	37	1	NADP By similarity
	Binding site	86	1	NADP; via carbonyl oxygen By similarity
	Binding site	138	1	Substrate By similarity
	Binding site	184	1	NADP; via amide nitrogen and carbonyl oxygen By similarity

Sequences

	Sequence		Length	Mass (Da)
	P0AEK3 [UniParc]. Last modified December 20, 2005. Version 1. Checksum: 48EC1F2A7F7EEFD9	FASTA	244	25,560
	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

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. , 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] [Europe PMC] [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] [Europe PMC] [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.
RefSeq	NP_707009.1. NC_004337.2. NP_836798.1. NC_004741.1.
3D structure databases
ProteinModelPortal	P0AEK3.
SMR	P0AEK3. Positions 2-244.
ModBase	Search...
Protein-protein interaction databases
STRING	198214.SF1097.
Proteomic databases
PaxDb	P0AEK3.
PRIDE	P0AEK3.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	AAN42716; AAN42716; SF1097. AAP16604; AAP16604; S1177.
GeneID	1026267. 1077578.
KEGG	sfl:SF1097. sfx:S1177.
PATRIC	18703556. VBIShiFle31049_1283.
Organism-specific databases
CMR	Search...
Phylogenomic databases
eggNOG	COG1028.
KO	K00059.
OMA	GMELNVT.
ProtClustDB	PRK05557.
Enzyme and pathway databases
UniPathway	UPA00094.
Family and domain databases
Gene3D	3.40.50.720. 1 hit.
InterPro	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]
Pfam	PF00106. adh_short. 1 hit. [Graphical view]
PRINTS	PR00081. GDHRDH. PR00080. SDRFAMILY.
TIGRFAMs	TIGR01830. 3oxo_ACP_reduc. 1 hit.
PROSITE	PS00061. ADH_SHORT. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

FABG_SHIFL

Accession

Primary (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:	May 1, 2013
This is version 63 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program