Q9K151 (FABI_NEIMB) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended 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

Organism

Neisseria meningitidis serogroup B (strain MC58) [Reference proteome] [HAMAP]

Taxonomic identifier

122586 [NCBI]

Taxonomic lineage

cellular organisms › Bacteria › Proteobacteria › Betaproteobacteria › Neisseriales › Neisseriaceae › Neisseria › Neisseria meningitidis › Neisseria meningitidis serogroup B

Protein attributes

Sequence length	261 AA.
Sequence status	Complete.
Protein existence	Evidence 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 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.

Ontologies

Keywords
Biological process	Fatty acid biosynthesis Fatty acid metabolism Lipid biosynthesis Lipid metabolism
Ligand	NAD
Molecular function	Oxidoreductase
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	fatty acid elongation Inferred from sequence or structural similarity. Source: UniProtKB protein homotetramerization Inferred from sequence or structural similarity. Source: UniProtKB
Molecular_function	enoyl-[acyl-carrier-protein] reductase (NADH) activity Inferred from sequence or structural similarity. Source: UniProtKB nucleotide binding Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 261	261	Enoyl-[acyl-carrier-protein] reductase [NADH] FabI		PRO_0000320269
Regions
	Nucleotide binding	19 – 20	2	NAD By similarity
	Nucleotide binding	64 – 65	2	NAD By similarity
	Nucleotide binding	193 – 197	5	NAD By similarity
Sites
	Active site	147	1	Proton acceptor By similarity
	Active site	157	1	Proton acceptor By similarity
	Binding site	13	1	NAD; via carbonyl oxygen By similarity
	Binding site	92	1	NAD; via carbonyl oxygen By similarity
	Binding site	95	1	Substrate; via amide nitrogen and carbonyl oxygen By similarity
	Binding site	164	1	NAD By similarity
	Site	206	1	Involved in acyl-ACP binding By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q9K151 [UniParc]. Last modified October 1, 2000. Version 1. Checksum: AF2D0C70F550253D	FASTA	261	27,691
	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

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. , 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.
PIR	C81211.
RefSeq	NP_273385.1. NC_003112.2.
3D structure databases
HSSP	HSSP built from PDB template 1JW7 based on UniProtKB O24990.
ProteinModelPortal	Q9K151.
SMR	Q9K151. Positions 2-258.
ModBase	Search...
Protein-protein interaction databases
STRING	122586.NMB0336.
Proteomic databases
PRIDE	Q9K151.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	AAF40779; AAF40779; NMB0336.
GeneID	902451.
KEGG	nme:NMB0336.
PATRIC	20355813. VBINeiMen85645_0425.
Phylogenomic databases
eggNOG	COG0623.
KO	K00208.
OMA	LVHCLAF.
ProtClustDB	PRK08690.
Enzyme and pathway databases
BioCyc	NMEN122586:GHGG-337-MONOMER.
UniPathway	UPA00094.
Family and domain databases
Gene3D	3.40.50.720. 1 hit.
InterPro	IPR014358. Enoyl-ACP_Rdtase_NADH. IPR002347. Glc/ribitol_DH. IPR016040. NAD(P)-bd_dom. [Graphical view]
PIRSF	PIRSF000094. Enoyl-ACP_rdct. 1 hit.
PRINTS	PR00081. GDHRDH.
ProtoNet	Search...

Entry information

Entry name

FABI_NEIMB

Accession

Primary (citable) accession number: Q9K151

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 26, 2008
Last sequence update:	October 1, 2000
Last modified:	May 1, 2013
This is version 88 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program