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UniProtKB/Swiss-Prot entry P0AEK5

[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

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Entry information
Entry name FABI_ECO57
Primary accession number P0AEK5
Secondary accession number P29132
Integrated into Swiss-Prot on December 20, 2005
Sequence was last modified on January 23, 2007 (Sequence version 2)
Annotations were last modified on    December 16, 2008 (Entry version 28)
Name and origin of the protein
Protein name Enoyl-[acyl-carrier-protein] reductase [NADH]
Synonyms EC 1.3.1.9
NADH-dependent enoyl-ACP reductase
Gene name
Name: fabI
OrderedLocusNames: Z2512, ECs1861
From
Escherichia coli O157:H7 [TaxID: 83334] [HAMAP proteome]
Taxonomy Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; Enterobacteriaceae; Escherichia.
Protein existence 3: Inferred from homology;
References
[1]
 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=O157:H7 / EDL933 / ATCC 700927 / EHEC;
DOI=10.1038/35054089; PubMed=11206551 [NCBI, ExPASy, EBI, Israel, Japan]
Perna N.T., Plunkett G. III, Burland V., Mau B., Glasner J.D., Rose D.J., Mayhew G.F., Evans P.S., Gregor J., Kirkpatrick H.A., Posfai G., Hackett J., Klink S., Boutin A., Shao Y., Miller L., Grotbeck E.J., Davis N.W., Lim A., Dimalanta E.T., Potamousis K., Apodaca J., Anantharaman T.S., Lin J., Yen G., Schwartz D.C., Welch R.A., Blattner F.R.;
"Genome sequence of enterohaemorrhagic Escherichia coli O157:H7.";
Nature 409:529-533(2001).
[2]
 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=O157:H7 / Sakai / RIMD 0509952 / EHEC;
DOI=10.1093/dnares/8.1.11; PubMed=11258796 [NCBI, ExPASy, EBI, Israel, Japan]
Hayashi T., Makino K., Ohnishi M., Kurokawa K., Ishii K., Yokoyama K., Han C.-G., Ohtsubo E., Nakayama K., Murata T., Tanaka M., Tobe T., Iida T., Takami H., Honda T., Sasakawa C., Ogasawara N., Yasunaga T., Kuhara S., Shiba T., Hattori M., Shinagawa H.;
"Complete genome sequence of enterohemorrhagic Escherichia coli O157:H7 and genomic comparison with a laboratory strain K-12.";
DNA Res. 8:11-22(2001).
Comments
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
Sequence databases
EMBL
AE005174; AAG56524.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BA000007; BAB35284.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
PIR E90861; E90861.
H85757; H85757.
RefSeq NP_287908.1; -.
NP_309888.1; -.
3D structure databases
SMR P0AEK5; 2-260.
ModBase P0AEK5.
Enzyme and pathway databases
BioCyc ECOL83334:ECS1861-MON; -.
Ontologies
GO
GO:0005886; Cellular component: plasma membrane (inferred from electronic annotation from UniProtKB-KW).
GO:0005488; Molecular function: binding (inferred from electronic annotation from InterPro).
GO:0004318; Molecular function: enoyl-[acyl-carrier-protein] reductase (NADH) activity (inferred from electronic annotation from InterPro).
GO:0006633; Biological process: fatty acid biosynthetic process (inferred from electronic annotation from InterPro).
GO:0055114; Biological process: oxidation reduction (inferred from electronic annotation from UniProtKB-KW).
GO:0046677; Biological process: response to antibiotic (inferred from electronic annotation from UniProtKB-KW).
QuickGo view.
Family and domain databases
InterPro IPR002198; DHase_sc/Rdtase_SDR.
IPR014358; Enoyl-ACP_rdct.
IPR002347; Glc/ribitol_DHase.
IPR016040; NAD(P)-bd.
Graphical view of domain structure.
Gene3D G3DSA:3.40.50.720; NAD(P)-bd; 1.
PANTHER PTHR19410; ADH_short_C2; 1.
PTHR19410:SF12; Enoyl-ACP_rdct; 1.
Pfam PF00106; adh_short; 1.
Pfam graphical view of domain structure.
PRINTS PR00081; GDHRDH.
Genome annotation databases
GeneID 912787; -.
961367; -.
GenomeReviews AE005174_GR; Z2512.
BA000007_GR; ECs1861.
KEGG ece:Z2512; -.
ecs:ECs1861; -.
Phylogenomic databases
HOGENOM P0AEK5; -.
Other
BindingDB P0AEK5; -.
Genome annotation databases
CMR P0AEK5; Z2512.
Other
ProtoNet P0AEK5.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
Antibiotic resistance; Cell inner membrane; Cell membrane; Complete proteome; Fatty acid biosynthesis; Lipid synthesis; Membrane; NAD; Oxidoreductase.
Features
SEVIEWER logo Feature table viewer
KeyFrom   To Length Description FTId
INIT_MET   1     1        Removed (By similarity). 
CHAIN   2   262  261     Enoyl-[acyl-carrier-protein] reductase [NADH]. PRO_0000054900
NP_BIND   10    36  27     NAD (By similarity). 
BINDING   156   156        Substrate (By similarity). 
Sequence information
Length: 262 AA [This is the length of the unprocessed precursor] Molecular weight: 27864 Da [This is the MW of the unprocessed precursor] CRC64: 436A89AF349D1866 [This is a checksum on the sequence] 
        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
P0AEK5 in FASTA format

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