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UniProtKB/Swiss-Prot entry O67505

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

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Entry information
Entry name FABI_AQUAE
Primary accession number O67505
Secondary accession numbers None
Integrated into Swiss-Prot on May 30, 2000
Sequence was last modified on May 30, 2000 (Sequence version 2)
Annotations were last modified on    December 16, 2008 (Entry version 59)
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: aq_1552
From
Aquifex aeolicus [TaxID: 63363] [HAMAP proteome]
Taxonomy Bacteria; Aquificae; Aquificales; Aquificaceae; Aquifex.
Protein existence 1: Evidence at protein level;
References
[1]
 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=VF5;
DOI=10.1038/32831; PubMed=9537320 [NCBI, ExPASy, EBI, Israel, Japan]
Deckert G., Warren P.V., Gaasterland T., Young W.G., Lenox A.L., Graham D.E., Overbeek R., Snead M.A., Keller M., Aujay M., Huber R., Feldman R.A., Short J.M., Olsen G.J., Swanson R.V.;
"The complete genome of the hyperthermophilic bacterium Aquifex aeolicus.";
Nature 392:353-358(1998).
[2]
 X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS).
Southeast collaboratory for structural genomics (SECSG);
"Crystal structure of enoyl-[acyl-carrier-protein] reductase (NADH) from Aquifex aeolicus VF5.";
Submitted (APR-2007) to the PDB data bank.
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
AE000657; AAC07465.1; ALT_INIT; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
PIR G70434; G70434.
RefSeq NP_214070.1; -.
3D structure databases
PDB
2P91; X-ray; 2.00 A; A/B/C/D=1-270.[ExPASy / RCSB / EBI]
PDBsum 2P91; -.
ModBase O67505.
Enzyme and pathway databases
BioCyc AAEO224324:AQ_1552-MON; -.
Ontologies
GO
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).
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 1193128; -.
GenomeReviews AE000657_GR; aq_1552.
KEGG aae:aq_1552; -.
NMPDR fig|224324.1.peg.1085; -.
Phylogenomic databases
HOGENOM O67505; -.
Genome annotation databases
CMR O67505; aq_1552.
Other
ProtoNet O67505.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
3D-structure; Complete proteome; Fatty acid biosynthesis; Lipid synthesis; NAD; Oxidoreductase.
Features
SEVIEWER logo Feature table viewer
KeyFrom   To Length Description FTId
CHAIN   1   270  270     Enoyl-[acyl-carrier-protein] reductase [NADH]. PRO_0000054894
NP_BIND   10    36  27     NAD (By similarity). 
BINDING   156   156        Substrate (By similarity). 
TURN   3     6  4      
STRAND   8    11  4      
HELIX   20    30  11      
STRAND   34    41  8      
HELIX   42    44  3      
HELIX   45    54  10      
STRAND   60    62  3      
HELIX   68    81  14      
STRAND   87    90  4      
HELIX   97   100  4      
HELIX   104   106  3      
HELIX   109   119  11      
HELIX   121   130  10      
HELIX   131   134  4      
STRAND   140   145  6      
HELIX   147   149  3      
TURN   154   157  4      
HELIX   158   178  21      
TURN   179   181  3      
STRAND   183   189  7      
HELIX   203   213  11      
HELIX   222   232  11      
HELIX   235   237  3      
STRAND   244   248  5      
HELIX   251   253  3      
Sequence information
Length: 270 AA [This is the length of the unprocessed precursor] Molecular weight: 29725 Da [This is the MW of the unprocessed precursor] CRC64: 2ACD6C85EE16DC68 [This is a checksum on the sequence] 
        10         20         30         40         50         60 
MGLLEGKRAL ITGVANERSI AYGIAKSFHR EGAQLAFTYA TPKLEKRVRE IAKGFGSDLV 

        70         80         90        100        110        120 
VKCDVSLDED IKNLKKFLEE NWGSLDIIVH SIAYAPKEEF KGGVIDTSRE GFKIAMDISV 

       130        140        150        160        170        180 
YSLIALTREL LPLMEGRNGA IVTLSYYGAE KVVPHYNVMG IAKAALESTV RYLAYDIAKH 

       190        200        210        220        230        240 
GHRINAISAG PVKTLAAYSI TGFHLLMEHT TKVNPFGKPI TIEDVGDTAV FLCSDWARAI 

       250        260        270 
TGEVVHVDNG YHIMGVFGRE EEIKKEVYGD
O67505 in FASTA format

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