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P44432 (FABI_HAEIN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 108. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
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
Synonyms:envM
Ordered Locus Names:HI_1734
OrganismHaemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd) [Reference proteome] [HAMAP]
Taxonomic identifier71421 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaPasteurellalesPasteurellaceaeHaemophilus

Protein attributes

Sequence length262 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceInferred from homology

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

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

Enzyme regulation

Inhibited by 1,4-benzodiazepine and naphthyridinone derivatives. Ref.2 Ref.3

Pathway

Lipid metabolism; fatty acid biosynthesis.

Sequence similarities

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

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed By similarity
Chain2 – 262261Enoyl-[acyl-carrier-protein] reductase [NADH] FabI
PRO_0000054901

Regions

Nucleotide binding19 – 202NAD By similarity
Nucleotide binding64 – 652NAD By similarity
Nucleotide binding192 – 1965NAD By similarity

Sites

Active site1461Proton acceptor By similarity
Active site1561Proton acceptor By similarity
Binding site131NAD; via carbonyl oxygen By similarity
Binding site921NAD; via carbonyl oxygen By similarity
Binding site951Substrate; via amide nitrogen and carbonyl oxygen By similarity
Binding site1631NAD By similarity
Site2011Involved in acyl-ACP binding By similarity
Site2041Involved in acyl-ACP binding By similarity
Site2051Involved in acyl-ACP binding By similarity

Sequences

Sequence LengthMass (Da)Tools
P44432 [UniParc].

Last modified January 23, 2007. Version 3.
Checksum: 71CEF6189795388E

FASTA26228,119
        10         20         30         40         50         60 
MGFLTGKRIL VTGLASNRSI AYGIAKSMKE QGAELAFTYL NDKLQPRVEE FAKEFGSDIV 

        70         80         90        100        110        120 
LPLDVATDES IQNCFAELSK RWDKFDGFIH AIAFAPGDQL DGDYVNAATR EGYRIAHDIS 

       130        140        150        160        170        180 
AYSFVAMAQA ARPYLNPNAA LLTLSYLGAE RAIPNYNVMC LAKASLEAAT RVMAADLGKE 

       190        200        210        220        230        240 
GIRVNAISAG PIRTLAASGI KNFKKMLSTF EKTAALRRTV TIEDVGNSAA FLCSDLASGI 

       250        260 
TGEIVHVDAG FSITAMGELG EE 

« Hide

References

« Hide 'large scale' references
[1]"Whole-genome random sequencing and assembly of Haemophilus influenzae Rd."
Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., Scott J.D., Shirley R., Liu L.-I. expand/collapse author list , Glodek A., Kelley J.M., Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., Venter J.C.
Science 269:496-512(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 51907 / DSM 11121 / KW20 / Rd.
[2]"Discovery of aminopyridine-based inhibitors of bacterial enoyl-ACP reductase (FabI)."
Miller W.H., Seefeld M.A., Newlander K.A., Uzinskas I.N., Burgess W.J., Heerding D.A., Yuan C.C., Head M.S., Payne D.J., Rittenhouse S.F., Moore T.D., Pearson S.C., Berry V., DeWolf W.E. Jr., Keller P.M., Polizzi B.J., Qiu X., Janson C.A., Huffman W.F.
J. Med. Chem. 45:3246-3256(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: ENZYME REGULATION.
[3]"Indole naphthyridinones as inhibitors of bacterial enoyl-ACP reductases FabI and FabK."
Seefeld M.A., Miller W.H., Newlander K.A., Burgess W.J., DeWolf W.E. Jr., Elkins P.A., Head M.S., Jakas D.R., Janson C.A., Keller P.M., Manley P.J., Moore T.D., Payne D.J., Pearson S., Polizzi B.J., Qiu X., Rittenhouse S.F., Uzinskas I.N., Wallis N.G., Huffman W.F.
J. Med. Chem. 46:1627-1635(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: ENZYME REGULATION.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
L42023 Genomic DNA. Translation: AAC23379.1.
PIRB64139.
RefSeqNP_439876.2. NC_000907.1.

3D structure databases

ProteinModelPortalP44432.
SMRP44432. Positions 2-259.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING71421.HI1734.

Chemistry

BindingDBP44432.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAC23379; AAC23379; HI_1734.
GeneID950535.
KEGGhin:HI1734.
PATRIC20192225. VBIHaeInf48452_1815.

Phylogenomic databases

eggNOGCOG0623.
KOK00208.
OMAGISGEIM.
OrthoDBEOG6HF644.
PhylomeDBP44432.

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...

Entry information

Entry nameFABI_HAEIN
AccessionPrimary (citable) accession number: P44432
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1995
Last sequence update: January 23, 2007
Last modified: July 9, 2014
This is version 108 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways

Haemophilus influenzae

Haemophilus influenzae (strain Rd): entries and gene names