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Reviewed, UniProtKB/Swiss-Prot Q68X10 (FABI_RICTY)

Last modified June 16, 2009. Version 36. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    Enoyl-[acyl-carrier-protein] reductase [NADH]
    EC=1.3.1.9
Alternative name(s):
    NADH-dependent enoyl-ACP reductase
Gene names
Name: fabI
Ordered Locus Names: RT0353
OrganismRickettsia typhi [Complete proteome] [HAMAP]
Taxonomic identifier785 [NCBI]
Taxonomic lineageBacteriaProteobacteriaAlphaproteobacteriaRickettsialesRickettsiaceaeRickettsieaeRickettsiatyphus group

Protein attributes

Sequence length261 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
Protein existenceInferred from homology.

General annotation (Comments)

Catalytic activity

Acyl-[acyl-carrier-protein] + NAD+ = trans-2,3-dehydroacyl-[acyl-carrier-protein] + NADH.

Pathway

Lipid metabolism; fatty acid biosynthesis.

Subcellular location

Cell inner membrane; Peripheral membrane protein By similarity.

Sequence similarities

Belongs to the short-chain dehydrogenases/reductases (SDR) family. FabI subfamily.

Ontologies

Keywords
   Biological processFatty acid biosynthesis
Lipid synthesis
   Cellular componentCell inner membrane
Cell membrane
Membrane
   LigandNAD
   Molecular functionOxidoreductase
   Technical termComplete proteome
Gene Ontology (GO)
   Biological processfatty acid biosynthetic process

Inferred from electronic annotation. Source: UniProtKB-KW

oxidation reduction

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular componentplasma membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular functionbinding

Inferred from electronic annotation. Source: InterPro

enoyl-[acyl-carrier-protein] reductase (NADH) activity

Inferred from electronic annotation. Source: EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 261261Enoyl-[acyl-carrier-protein] reductase [NADH]
PRO_0000286637

Regions

Nucleotide binding12 – 3827NAD By similarity

Sites

Active site1571Proton acceptor By similarity

Sequences

Sequence LengthMass (Da)Tools
Q68X10-1 [UniParc].

Last modified October 11, 2004. Version 1.
Checksum: 45A3A9D3F0E6DF9F

FASTA26128,713
        10         20         30         40         50         60 
MTTRLLQGKK GLITGIANNM SISWAIAQLA KKHGAELWFT YQSEALEKRV KPLAEEIGCN 

        70         80         90        100        110        120 
FISELDVTDQ KSISNLFNDI KEKWNSFDFL LHGMAFANKN ELKGRYVDTS LENFYNSLHI 

       130        140        150        160        170        180 
SCYSLLELSR SAETLMHDGG SILTLTYYGA EKVIPNYNIM GVAKAALEAS VKYLANDMGE 

       190        200        210        220        230        240 
NNIRVNAISA GPIKTLASSA ISDFSTMLKF HASTAPLKRN ITQEDVGGAA VYLFSELSKG 

       250        260 
VTGEIHYVDC GYNIIGSSKL L 

« Hide

References

[1]"Complete genome sequence of Rickettsia typhi and comparison with sequences of other Rickettsiae."
McLeod M.P., Qin X., Karpathy S.E., Gioia J., Highlander S.K., Fox G.E., McNeill T.Z., Jiang H., Muzny D., Jacob L.S., Hawes A.C., Sodergren E., Gill R., Hume J., Morgan M., Fan G., Amin A.G., Gibbs R.A. expand/collapse author list , Hong C., Yu X.-J., Walker D.H., Weinstock G.M.
J. Bacteriol. 186:5842-5855(2004) [PubMed: 15317790] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC VR-144 / Wilmington.

Cross-references

Sequence databases

AE017197 Genomic DNA. Translation: AAU03832.1.
RefSeqYP_067314.1.

3D structure databases

ModBaseSearch...

Genome annotation databases

GeneID2958632.
GenomeReviewsGene locus RT0353 in contig AE017197_GR.
KEGGrty:RT0353.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMQ68X10.
OMAQ68X10. LVHCLAF.

Enzyme and pathway databases

BioCycRTYP257363:RT0353-MON.
BRENDA1.3.1.9. 281221.

Family and domain databases

InterProIPR002198. DH_sc/Rdtase_SDR.
IPR014358. Enoyl-ACP_Rdtase_NADH.
IPR002347. Glc/ribitol_DH.
IPR016040. NAD(P)-bd_dom.
[Graphical view]
Gene3DG3DSA:3.40.50.720. NAD(P)-bd. 1 hit.
PANTHERPTHR19410. ADH_short_C2. 1 hit.
PTHR19410:SF12. Enoyl-ACP_rdct. 1 hit.
PRINTSPR00081. GDHRDH.
ProtoNetSearch...

Entry information

Entry nameFABI_RICTY
AccessionPrimary (citable) accession number: Q68X10
Entry history
Integrated into UniProtKB/Swiss-Prot: May 15, 2007
Last sequence update: October 11, 2004
Last modified: June 16, 2009
This is version 36 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)

Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

Rickettsia typhi

Rickettsia typhi (strain Wilmington): entries and gene names

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents