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Q9K151 (FABI_NEIMB) Reviewed, UniProtKB/Swiss-Prot

Last modified January 22, 2014. Version 92. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | 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
Ordered Locus Names:NMB0336
OrganismNeisseria meningitidis serogroup B (strain MC58) [Reference proteome] [HAMAP]
Taxonomic identifier122586 [NCBI]
Taxonomic lineageBacteriaProteobacteriaBetaproteobacteriaNeisserialesNeisseriaceaeNeisseria

Protein attributes

Sequence length261 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

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

Pathway

Lipid metabolism; fatty acid biosynthesis.

Subunit structure

Homotetramer By similarity.

Miscellaneous

Present in outer membrane vesicle formulations which are used as vaccines in human.

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 – 261261Enoyl-[acyl-carrier-protein] reductase [NADH] FabI
PRO_0000320269

Regions

Nucleotide binding19 – 202NAD By similarity
Nucleotide binding64 – 652NAD By similarity
Nucleotide binding193 – 1975NAD By similarity

Sites

Active site1471Proton acceptor By similarity
Active site1571Proton 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 site1641NAD By similarity
Site2061Involved in acyl-ACP binding By similarity

Sequences

Sequence LengthMass (Da)Tools
Q9K151 [UniParc].

Last modified October 1, 2000. Version 1.
Checksum: AF2D0C70F550253D

FASTA26127,691
        10         20         30         40         50         60 
MGFLQGKKIL ITGMISERSI AYGIAKACRE QGAELAFTYV VDKLEERVRK MAAELDSELV 

        70         80         90        100        110        120 
FRCDVASDDE INQVFADLGK HWDGLDGLVH SIGFAPKEAL SGDFLDSISR EAFNTAHEIS 

       130        140        150        160        170        180 
AYSLPALAKA ARPMMRGRNS AIVALSYLGA VRAIPNYNVM GMAKASLEAG IRFTAACLGK 

       190        200        210        220        230        240 
EGIRCNGISA GPIKTLAASG IADFGKLLGH VAAHNPLRRN VTIEEVGNTA AFLLSDLSSG 

       250        260 
ITGEITYVDG GYSINALSTE G 

« Hide

References

[1]"Complete genome sequence of Neisseria meningitidis serogroup B strain MC58."
Tettelin H., Saunders N.J., Heidelberg J.F., Jeffries A.C., Nelson K.E., Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., Nelson W.C., Gwinn M.L., DeBoy R.T., Peterson J.D., Hickey E.K., Haft D.H., Salzberg S.L., White O. expand/collapse author list , Fleischmann R.D., Dougherty B.A., Mason T.M., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., Cotton M.D., Utterback T.R., Khouri H.M., Qin H., Vamathevan J.J., Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.
Science 287:1809-1815(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: MC58.
[2]"Proteomic analysis of a meningococcal outer membrane vesicle vaccine prepared from the group B strain NZ98/254."
Vipond C., Suker J., Jones C., Tang C., Feavers I.M., Wheeler J.X.
Proteomics 6:3400-3413(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Strain: NZ98/254 / Serogroup B.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AE002098 Genomic DNA. Translation: AAF40779.1.
PIRC81211.
RefSeqNP_273385.1. NC_003112.2.

3D structure databases

ProteinModelPortalQ9K151.
SMRQ9K151. Positions 2-258.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING122586.NMB0336.

Proteomic databases

PRIDEQ9K151.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAF40779; AAF40779; NMB0336.
GeneID902451.
KEGGnme:NMB0336.
PATRIC20355813. VBINeiMen85645_0425.

Phylogenomic databases

eggNOGCOG0623.
KOK00208.
OMAGILDMIH.
OrthoDBEOG6HF644.
ProtClustDBPRK08690.

Enzyme and pathway databases

BioCycNMEN122586:GHGG-357-MONOMER.
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_NEIMB
AccessionPrimary (citable) accession number: Q9K151
Entry history
Integrated into UniProtKB/Swiss-Prot: February 26, 2008
Last sequence update: October 1, 2000
Last modified: January 22, 2014
This is version 92 of the entry and version 1 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