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Q05069 (FABI_NOSS1) Reviewed, UniProtKB/Swiss-Prot

Last modified January 22, 2014. Version 94. 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:all4391
OrganismNostoc sp. (strain PCC 7120 / UTEX 2576) [Complete proteome] [HAMAP]
Taxonomic identifier103690 [NCBI]
Taxonomic lineageBacteriaCyanobacteriaNostocalesNostocaceaeNostoc

Protein attributes

Sequence length258 AA.
Sequence statusComplete.
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.

Pathway

Lipid metabolism; fatty acid biosynthesis.

Subunit structure

Homotetramer By similarity.

Sequence similarities

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

Sequence caution

The sequence AAD04184.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.

The sequence BAB76090.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 258258Enoyl-[acyl-carrier-protein] reductase [NADH] FabI
PRO_0000054893

Regions

Nucleotide binding19 – 202NAD By similarity
Nucleotide binding67 – 682NAD By similarity
Nucleotide binding194 – 1985NAD By similarity

Sites

Active site1481Proton acceptor By similarity
Active site1581Proton acceptor By similarity
Binding site131NAD; via carbonyl oxygen By similarity
Binding site951NAD; via carbonyl oxygen By similarity
Binding site981Substrate; via amide nitrogen and carbonyl oxygen By similarity
Binding site1651NAD By similarity

Sequences

Sequence LengthMass (Da)Tools
Q05069 [UniParc].

Last modified May 30, 2000. Version 2.
Checksum: 45012CA8497E001B

FASTA25827,421
        10         20         30         40         50         60 
MLNLTGKNAL VTGIANNRSI AWGIAQQLHA AGANLGITYL PDERGKFEKK VSELVEPLNP 

        70         80         90        100        110        120 
SLFLPCNVQN DEQIQSTFDT IRDKWGRLDI LIHCLAFANR DDLTGDFSQT SRAGFATALD 

       130        140        150        160        170        180 
ISTFSLVQLS GAAKPLMTEG GSIITLSYLG GVRAVPNYNV MGVAKAGLEA SVRYLASELG 

       190        200        210        220        230        240 
SQNIRVNAIS AGPIRTLASS AVGGILDMIH HVEQVAPLRR TVTQLEVGNT AAFLASDLAS 

       250 
GITGQVLYVD AGYEIMGM 

« Hide

References

« Hide 'large scale' references
[1]"Anabaena sp. strain PCC 7120 bifA gene encoding a sequence-specific DNA-binding protein cloned by in vivo transcriptional interference selection."
Wei T.-F., Ramasubramanian T.S., Pu F., Golden J.W.
J. Bacteriol. 175:4025-4035(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]"Complete genomic sequence of the filamentous nitrogen-fixing cyanobacterium Anabaena sp. strain PCC 7120."
Kaneko T., Nakamura Y., Wolk C.P., Kuritz T., Sasamoto S., Watanabe A., Iriguchi M., Ishikawa A., Kawashima K., Kimura T., Kishida Y., Kohara M., Matsumoto M., Matsuno A., Muraki A., Nakazaki N., Shimpo S., Sugimoto M. expand/collapse author list , Takazawa M., Yamada M., Yasuda M., Tabata S.
DNA Res. 8:205-213(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: PCC 7120 / UTEX 2576.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
L10036 Genomic DNA. Translation: AAD04184.1. Different initiation.
BA000019 Genomic DNA. Translation: BAB76090.1. Different initiation.
PIRAG2354.
RefSeqNP_488431.1. NC_003272.1.

3D structure databases

ProteinModelPortalQ05069.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING103690.all4391.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaBAB76090; BAB76090; BAB76090.
GeneID1107992.
KEGGana:all4391.
PATRIC22779366. VBINosSp37423_5130.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0623.
KOK00208.
OMAGILDMIH.
OrthoDBEOG6HF644.
ProtClustDBPRK07370.

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_NOSS1
AccessionPrimary (citable) accession number: Q05069
Entry history
Integrated into UniProtKB/Swiss-Prot: February 1, 1994
Last sequence update: May 30, 2000
Last modified: January 22, 2014
This is version 94 of the entry and version 2 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