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O24990 (FABI_HELPY) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 96. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
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to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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:HP_0195
OrganismHelicobacter pylori (strain ATCC 700392 / 26695) (Campylobacter pylori) [Reference proteome] [HAMAP]
Taxonomic identifier85962 [NCBI]
Taxonomic lineageBacteria › Proteobacteria › Epsilonproteobacteria › Campylobacterales › Helicobacteraceae › Helicobacter ›

Protein attributes

Sequence length275 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

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 By similarity.

Catalytic activity

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

Pathway

Lipid metabolism; fatty acid biosynthesis.

Subunit structure

Homotetramer. Ref.2

Sequence similarities

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

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 275275Enoyl-[acyl-carrier-protein] reductase [NADH] FabI
PRO_0000054902

Regions

Nucleotide binding19 – 202NAD
Nucleotide binding64 – 652NAD
Nucleotide binding191 – 1955NAD

Sites

Active site1451Proton acceptor By similarity
Active site1551Proton acceptor
Binding site131NAD; via carbonyl oxygen
Binding site921NAD; via carbonyl oxygen
Binding site951Substrate; via amide nitrogen and carbonyl oxygen
Binding site1621NAD
Site2031Involved in acyl-ACP binding By similarity

Secondary structure

1 .................................................... 275
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
O24990 [UniParc].

Last modified January 1, 1998. Version 1.
Checksum: 1894A5AA2105895A

FASTA27529,981
        10         20         30         40         50         60 
MGFLKGKKGL IVGVANNKSI AYGIAQSCFN QGATLAFTYL NESLEKRVRP IAQELNSPYV 

        70         80         90        100        110        120 
YELDVSKEEH FKSLYNSVKK DLGSLDFIVH SVAFAPKEAL EGSLLETSKS AFNTAMEISV 

       130        140        150        160        170        180 
YSLIELTNTL KPLLNNGASV LTLSYLGSTK YMAHYNVMGL AKAALESAVR YLAVDLGKHH 

       190        200        210        220        230        240 
IRVNALSAGP IRTLASSGIA DFRMILKWNE INAPLRKNVS LEEVGNAGMY LLSSLSSGVS 

       250        260        270 
GEVHFVDAGY HVMGMGAVEE KDNKATLLWD LHKEQ

« Hide

References

« Hide 'large scale' references
[1]"The complete genome sequence of the gastric pathogen Helicobacter pylori."
Tomb J.-F., White O., Kerlavage A.R., Clayton R.A., Sutton G.G., Fleischmann R.D., Ketchum K.A., Klenk H.-P., Gill S.R., Dougherty B.A., Nelson K.E., Quackenbush J., Zhou L., Kirkness E.F., Peterson S.N., Loftus B.J., Richardson D.L., Dodson R.J. expand/collapse author list , Khalak H.G., Glodek A., McKenney K., FitzGerald L.M., Lee N., Adams M.D., Hickey E.K., Berg D.E., Gocayne J.D., Utterback T.R., Peterson J.D., Kelley J.M., Cotton M.D., Weidman J.F., Fujii C., Bowman C., Watthey L., Wallin E., Hayes W.S., Borodovsky M., Karp P.D., Smith H.O., Fraser C.M., Venter J.C.
Nature 388:539-547(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 700392 / 26695.
[2]"Crystal structure of the Helicobacter pylori enoyl-acyl carrier protein reductase in complex with hydroxydiphenyl ether compounds, triclosan and diclosan."
Lee H.H., Moon J., Suh S.W.
Proteins 69:691-694(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) IN COMPLEX WITH NAD AND INHIBITORS, SUBUNIT.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		AE000511 Genomic DNA. Translation: AAD07262.1.
PIRC64544.
RefSeqNP_206994.1. NC_000915.1.
YP_006934118.1. NC_018939.1.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2PD3X-ray2.50A/B/C/D1-275[»]
2PD4X-ray2.30A/B/C/D1-275[»]
ProteinModelPortalO24990.
SMRO24990. Positions 2-275.
ModBaseSearch...

Protein-protein interaction databases

STRING85962.HP0195.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAD07262; AAD07262; HP_0195.
GeneID13869374.
899156.
KEGGheo:C694_00970.
hpy:HP0195.
PATRIC20591611. VBIHelPyl33062_0205.

Phylogenomic databases

eggNOGCOG0623.
KOK00208.
OMALVHCLAF.
ProtClustDBPRK08415.

Enzyme and pathway databases

UniPathwayUPA00094.

Family and domain databases

Gene3D3.40.50.720. 1 hit.
InterProIPR014358. Enoyl-ACP_Rdtase_NADH.
IPR002347. Glc/ribitol_DH.
IPR016040. NAD(P)-bd_dom.
[Graphical view]
PIRSFPIRSF000094. Enoyl-ACP_rdct. 1 hit.
PRINTSPR00081. GDHRDH.
ProtoNetSearch...

Other

EvolutionaryTraceO24990.

Entry information

Entry nameFABI_HELPY
AccessionPrimary (citable) accession number: O24990
Entry history
Integrated into UniProtKB/Swiss-Prot: May 30, 2000
Last sequence update: January 1, 1998
Last modified: May 1, 2013
This is version 96 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

Helicobacter pylori

Helicobacter pylori (strain 26695): entries and gene names

PATHWAY comments

Index of metabolic and biosynthesis pathways

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents