P0AEK6 (FABI_SHIFL) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Enoyl-[acyl-carrier-protein] reductase [NADH] FabI
Short name=ENR
EC=1.3.1.9

Alternative name(s):
NADH-dependent enoyl-ACP reductase

Gene names

Name:	fabI
Ordered Locus Names:	SF1293, S1375

Organism

Shigella flexneri [Complete proteome] [HAMAP]

Taxonomic identifier

623 [NCBI]

Taxonomic lineage

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

Protein attributes

Sequence length	262 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Inferred from homology

General annotation (Comments)

Function	Catalyzes the reduction of a carbon-carbon double bond in an enoyl moiety that is covalently linked to an acyl carrier protein (ACP). Involved in the elongation cycle of fatty acid which are used in the lipid metabolism and in the biotin biosynthesis By similarity.
Catalytic activity	Acyl-[acyl-carrier-protein] + NAD+ = trans-2,3-dehydroacyl-[acyl-carrier-protein] + NADH.
Pathway	Lipid metabolism; fatty acid biosynthesis. Cofactor biosynthesis; biotin biosynthesis.
Subunit structure	Homotetramer By similarity.
Miscellaneous	The antibiotic diazaborine interferes with the activity by binding to the protein By similarity.
Sequence similarities	Belongs to the short-chain dehydrogenases/reductases (SDR) family. FabI subfamily.

Ontologies

Keywords
Biological process	Antibiotic resistance Biotin biosynthesis Fatty acid biosynthesis Fatty acid metabolism Lipid biosynthesis Lipid metabolism
Ligand	NAD
Molecular function	Oxidoreductase
Technical term	Complete proteome
Gene Ontology (GO)
Biological_process	biotin biosynthetic process Inferred from sequence or structural similarity. Source: UniProtKB fatty acid elongation Inferred from sequence or structural similarity. Source: UniProtKB protein homotetramerization Inferred from sequence or structural similarity. Source: UniProtKB response to antibiotic Inferred from electronic annotation. Source: UniProtKB-KW
Molecular_function	enoyl-[acyl-carrier-protein] reductase (NADH) activity Inferred from sequence or structural similarity. Source: UniProtKB nucleotide binding Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Initiator methionine	1	1	Removed By similarity
	Chain	2 – 262	261	Enoyl-[acyl-carrier-protein] reductase [NADH] FabI		PRO_0000054911
Regions
	Nucleotide binding	19 – 20	2	NAD By similarity
	Nucleotide binding	64 – 65	2	NAD By similarity
	Nucleotide binding	192 – 196	5	NAD By similarity
Sites
	Active site	146	1	Proton acceptor By similarity
	Active site	156	1	Proton acceptor By similarity
	Binding site	13	1	NAD; via carbonyl oxygen By similarity
	Binding site	40	1	NAD By similarity
	Binding site	92	1	NAD; via carbonyl oxygen By similarity
	Binding site	95	1	Substrate; via amide nitrogen and carbonyl oxygen By similarity
	Binding site	163	1	NAD By similarity
	Site	201	1	Involved in acyl-ACP binding By similarity
	Site	204	1	Involved in acyl-ACP binding By similarity
	Site	205	1	Involved in acyl-ACP binding By similarity

Sequences

	Sequence		Length	Mass (Da)
	P0AEK6 [UniParc]. Last modified January 23, 2007. Version 2. Checksum: 436A89AF349D1866	FASTA	262	27,864
	10 20 30 40 50 60 MGFLSGKRIL VTGVASKLSI AYGIAQAMHR EGAELAFTYQ NDKLKGRVEE FAAQLGSDIV 70 80 90 100 110 120 LQCDVAEDAS IDTMFAELGK VWPKFDGFVH SIGFAPGDQL DGDYVNAVTR EGFKIAHDIS 130 140 150 160 170 180 SYSFVAMAKA CRSMLNPGSA LLTLSYLGAE RAIPNYNVMG LAKASLEANV RYMANAMGPE 190 200 210 220 230 240 GVRVNAISAG PIRTLAASGI KDFRKMLAHC EAVTPIRRTV TIEDVGNSAA FLCSDLSAGI 250 260 SGEVVHVDGG FSIAAMNELE LK

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: AAN42904.1. AE014073 Genomic DNA. Translation: AAP16787.1.
RefSeq	NP_707197.1. NC_004337.2. NP_836980.1. NC_004741.1.
3D structure databases
ProteinModelPortal	P0AEK6.
SMR	P0AEK6. Positions 2-260.
ModBase	Search...
Protein-protein interaction databases
STRING	198214.SF1293.
Proteomic databases
PaxDb	P0AEK6.
PRIDE	P0AEK6.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	AAN42904; AAN42904; SF1293. AAP16787; AAP16787; S1375.
GeneID	1024254. 1077753.
KEGG	sfl:SF1293. sfx:S1375.
PATRIC	18704006. VBIShiFle31049_1507.
Organism-specific databases
CMR	Search...
Phylogenomic databases
eggNOG	COG0623.
KO	K00208.
OMA	DCDVGSD.
ProtClustDB	PRK07984.
Enzyme and pathway databases
UniPathway	UPA00078. UPA00094.
Family and domain databases
Gene3D	3.40.50.720. 1 hit.
InterPro	IPR014358. Enoyl-ACP_Rdtase_NADH. IPR002347. Glc/ribitol_DH. IPR016040. NAD(P)-bd_dom. [Graphical view]
PIRSF	PIRSF000094. Enoyl-ACP_rdct. 1 hit.
PRINTS	PR00081. GDHRDH.
ProtoNet	Search...
Other
BindingDB	P0AEK6.

Entry information

Entry name

FABI_SHIFL

Accession

Primary (citable) accession number: P0AEK6
Secondary accession number(s): P29132

Entry history

Integrated into UniProtKB/Swiss-Prot:	December 20, 2005
Last sequence update:	January 23, 2007
Last modified:	May 1, 2013
This is version 68 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program