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UniProtKB/Swiss-Prot entry P54616


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

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Entry information
Entry name FABI_BACSU
Primary accession number P54616
Secondary accession number O31621
Integrated into Swiss-Prot on October 1, 1996
Sequence was last modified on May 30, 2000 (Sequence version 2)
Annotations were last modified on    November 4, 2008 (Entry version 63)
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
Cold shock-induced protein 15
CSI15
Vegetative protein 241
VEG241
Gene name
Name: fabI
Synonyms: yjbW
OrderedLocusNames: BSU11720
From
Bacillus subtilis [TaxID: 1423] [HAMAP proteome]
Taxonomy Bacteria; Firmicutes; Bacillales; Bacillaceae; Bacillus.
Protein existence 1: Evidence at protein level;
References
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=168;
DOI=10.1038/36786; PubMed=9384377 [NCBI, ExPASy, EBI, Israel, Japan]
Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V., Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R., Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S., Bruschi C.V., Caldwell B., Capuano V., Carter N.M., Choi S.-K., Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., Denizot F., Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., Entian K.-D., Errington J., Fabret C., Ferrari E., Foulger D., Fritz C., Fujita M., Fujita Y., Fuma S., Galizzi A., Galleron N., Ghim S.-Y., Glaser P., Goffeau A., Golightly E.J., Grandi G., Guiseppi G., Guy B.J., Haga K., Haiech J., Harwood C.R., Henaut A., Hilbert H., Holsappel S., Hosono S., Hullo M.-F., Itaya M., Jones L.-M., Joris B., Karamata D., Kasahara Y., Klaerr-Blanchard M., Klein C., Kobayashi Y., Koetter P., Koningstein G., Krogh S., Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J., Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C., Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S., Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B., Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S., Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G., Rey M., Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., Rose M., Sadaie Y., Sato T., Scanlan E., Schleich S., Schroeter R., Scoffone F., Sekiguchi J., Sekowska A., Seror S.J., Serror P., Shin B.-S., Soldo B., Sorokin A., Tacconi E., Takagi T., Takahashi H., Takemaru K., Takeuchi M., Tamakoshi A., Tanaka T., Terpstra P., Tognoni A., Tosato V., Uchiyama S., Vandenbol M., Vannier F., Vassarotti A., Viari A., Wambutt R., Wedler E., Wedler H., Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K., Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E., Yoshikawa H., Danchin A.;
"The complete genome sequence of the Gram-positive bacterium Bacillus subtilis.";
Nature 390:249-256(1997).
[2]
PROTEIN SEQUENCE OF 1-21.
STRAIN=168 / JH642;
PubMed=8755892 [NCBI, ExPASy, EBI, Israel, Japan]
Graumann P., Schroeder K., Schmid R., Marahiel M.A.;
"Cold shock stress-induced proteins in Bacillus subtilis.";
J. Bacteriol. 178:4611-4619(1996).
[3]
PROTEIN SEQUENCE OF 1-15.
STRAIN=168 / IS58;
DOI=10.1002/elps.1150180820; PubMed=9298659 [NCBI, ExPASy, EBI, Israel, Japan]
Antelmann H., Bernhardt J., Schmid R., Mach H., Voelker U., Hecker M.;
"First steps from a two-dimensional protein index towards a response-regulation map for Bacillus subtilis.";
Electrophoresis 18:1451-1463(1997).
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
Z99110; CAB13029.2; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
PIR G69845; G69845.
RefSeq NP_389054.2; -.
3D structure databases
HSSP P29132; 1DFI. [HSSP ENTRY / PDB]
ModBase P54616.
Enzyme and pathway databases
BioCyc BSUB224308:BSU1173-MON; -.
Organism-specific databases
SubtiList BG13152; fabI. [Micado]
Ontologies
GO
GO:0004318; Molecular function: enoyl-[acyl-carrier-protein] reductase (NADH) activity (inferred from electronic annotation from EC).
GO:0006633; Biological process: fatty acid biosynthetic process (inferred from electronic annotation from UniProtKB-KW).
GO:0055114; Biological process: oxidation reduction (inferred from electronic annotation from UniProtKB-KW).
GO:0006950; Biological process: response to stress (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.
BLOCKS P54616.
ProtoNet P54616.
Genome annotation databases
GeneID 939379; -.
GenomeReviews AL009126_GR; BSU11720.
KEGG bsu:BSU11720; -.
NMPDR fig|224308.1.peg.1173; -.
Phylogenomic databases
HOGENOM P54616; -.
Genome annotation databases
CMR P54616; BSU11720.
Other
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
Complete proteome; Direct protein sequencing; Fatty acid biosynthesis; Lipid synthesis; NAD; Oxidoreductase; Stress response.
Features
SEVIEWER logo Feature table viewer
KeyFrom   To Length Description FTId
CHAIN   1   258  258     Enoyl-[acyl-carrier-protein] reductase [NADH]. PRO_0000054895
NP_BIND   11    37  27     NAD (By similarity). 
BINDING   158   158        Substrate (By similarity). 
CONFLICT   20    20        S -> Q (in Ref. 2; AA sequence). 
Sequence information
Length: 258 AA [This is the length of the unprocessed precursor] Molecular weight: 27874 Da [This is the MW of the unprocessed precursor] CRC64: 097667168B3F0470 [This is a checksum on the sequence]
        10         20         30         40         50         60 
MNFSLEGRNI VVMGVANKRS IAWGIARSLH EAGARLIFTY AGERLEKSVH ELAGTLDRND 

        70         80         90        100        110        120 
SIILPCDVTN DAEIETCFAS IKEQVGVIHG IAHCIAFANK EELVGEYLNT NRDGFLLAHN 

       130        140        150        160        170        180 
ISSYSLTAVV KAARPMMTEG GSIVTLTYLG GELVMPNYNV MGVAKASLDA SVKYLAADLG 

       190        200        210        220        230        240 
KENIRVNSIS AGPIRTLSAK GISDFNSILK DIEERAPLRR TTTPEEVGDT AAFLFSDMSR 

       250 
GITGENLHVD SGFHITAR 

P54616 in FASTA format

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