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P16657

- FABI_SALTY

UniProt

P16657 - FABI_SALTY

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Protein

Enoyl-[acyl-carrier-protein] reductase [NADH] FabI

Gene

fabI

Organism
Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at protein leveli

Functioni

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 and in the biotin biosynthesis (By similarity).By similarity

Catalytic activityi

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

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei13 – 131NAD; via carbonyl oxygenBy similarity
Binding sitei40 – 401NADBy similarity
Binding sitei92 – 921NAD; via carbonyl oxygenBy similarity
Binding sitei95 – 951Substrate; via amide nitrogen and carbonyl oxygenBy similarity
Active sitei146 – 1461Proton acceptorBy similarity
Active sitei156 – 1561Proton acceptorBy similarity
Binding sitei163 – 1631NADBy similarity
Sitei201 – 2011Involved in acyl-ACP bindingBy similarity
Sitei204 – 2041Involved in acyl-ACP bindingBy similarity
Sitei205 – 2051Involved in acyl-ACP bindingBy similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi19 – 202NADBy similarity
Nucleotide bindingi64 – 652NADBy similarity
Nucleotide bindingi192 – 1965NADBy similarity

GO - Molecular functioni

  1. enoyl-[acyl-carrier-protein] reductase (NADH) activity Source: UniProtKB

GO - Biological processi

  1. biotin biosynthetic process Source: UniProtKB
  2. fatty acid elongation Source: UniProtKB
  3. protein homotetramerization Source: UniProtKB
  4. response to antibiotic Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Biological processi

Antibiotic resistance, Biotin biosynthesis, Fatty acid biosynthesis, Fatty acid metabolism, Lipid biosynthesis, Lipid metabolism

Keywords - Ligandi

NAD

Enzyme and pathway databases

BioCyciSENT99287:GCTI-1709-MONOMER.
UniPathwayiUPA00078.
UPA00094.

Names & Taxonomyi

Protein namesi
Recommended name:
Enoyl-[acyl-carrier-protein] reductase [NADH] FabI (EC:1.3.1.9)
Short name:
ENR
Alternative name(s):
NADH-dependent enoyl-ACP reductase
Gene namesi
Name:fabI
Synonyms:envM
Ordered Locus Names:STM1700
OrganismiSalmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)
Taxonomic identifieri99287 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeSalmonella
ProteomesiUP000001014: Chromosome

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi93 – 931G → S: Diazaborine resistance. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed1 Publication
Chaini2 – 262261Enoyl-[acyl-carrier-protein] reductase [NADH] FabIPRO_0000054910Add
BLAST

Proteomic databases

PaxDbiP16657.
PRIDEiP16657.

Interactioni

Subunit structurei

Homotetramer.By similarity

Protein-protein interaction databases

STRINGi99287.STM1700.

Structurei

3D structure databases

ProteinModelPortaliP16657.
SMRiP16657. Positions 2-260.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

eggNOGiCOG0623.
KOiK00208.
OMAiKLSIAWA.
OrthoDBiEOG6HF644.
PhylomeDBiP16657.

Family and domain databases

Gene3Di3.40.50.720. 1 hit.
InterProiIPR014358. Enoyl-ACP_Rdtase_NADH.
IPR002347. Glc/ribitol_DH.
IPR016040. NAD(P)-bd_dom.
[Graphical view]
PIRSFiPIRSF000094. Enoyl-ACP_rdct. 1 hit.
PRINTSiPR00081. GDHRDH.

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P16657-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MGFLSGKRIL VTGVASKLSI AYGIAQAMHR EGAELAFTYQ NDKLKGRVEE
60 70 80 90 100
FAAQLGSSIV LPCDVAEDAS IDAMFAELGN VWPKFDGFVH SIGFAPGDQL
110 120 130 140 150
DGDYVNAVTR EGFKVAHDIS SYSFVAMAKA CRTMLNPGSA LLTLSYLGAE
160 170 180 190 200
RAIPNYNVMG LAKASLEANV RYMANAMGPE GVRVNAISAG PIRTLAASGI
210 220 230 240 250
KDFRKMLAHC EAVTPIRRTV TIEDVGNSAA FLCSDLSAGI SGEVVHVDGG
260
FSIAAMNELE LK
Length:262
Mass (Da):27,761
Last modified:January 23, 2007 - v3
Checksum:i185A199EB359F643
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
M31806 Genomic DNA. Translation: AAA27059.1.
AE006468 Genomic DNA. Translation: AAL20618.1.
PIRiB43729.
RefSeqiNP_460659.1. NC_003197.1.

Genome annotation databases

EnsemblBacteriaiAAL20618; AAL20618; STM1700.
GeneIDi1253219.
KEGGistm:STM1700.
PATRICi32381909. VBISalEnt20916_1794.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
M31806 Genomic DNA. Translation: AAA27059.1 .
AE006468 Genomic DNA. Translation: AAL20618.1 .
PIRi B43729.
RefSeqi NP_460659.1. NC_003197.1.

3D structure databases

ProteinModelPortali P16657.
SMRi P16657. Positions 2-260.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 99287.STM1700.

Proteomic databases

PaxDbi P16657.
PRIDEi P16657.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai AAL20618 ; AAL20618 ; STM1700 .
GeneIDi 1253219.
KEGGi stm:STM1700.
PATRICi 32381909. VBISalEnt20916_1794.

Phylogenomic databases

eggNOGi COG0623.
KOi K00208.
OMAi KLSIAWA.
OrthoDBi EOG6HF644.
PhylomeDBi P16657.

Enzyme and pathway databases

UniPathwayi UPA00078 .
UPA00094 .
BioCyci SENT99287:GCTI-1709-MONOMER.

Family and domain databases

Gene3Di 3.40.50.720. 1 hit.
InterProi IPR014358. Enoyl-ACP_Rdtase_NADH.
IPR002347. Glc/ribitol_DH.
IPR016040. NAD(P)-bd_dom.
[Graphical view ]
PIRSFi PIRSF000094. Enoyl-ACP_rdct. 1 hit.
PRINTSi PR00081. GDHRDH.
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "envM genes of Salmonella typhimurium and Escherichia coli."
    Turnowsky F., Fuchs K., Jeschek C., Hoegenauer G.
    J. Bacteriol. 171:6555-6565(1989) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], MUTAGENESIS OF GLY-93.
    Strain: AG701.
  2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: LT2 / SGSC1412 / ATCC 700720.
  3. "Salmonella typhimurium responses to a bactericidal protein from human neutrophils."
    Qi S.Y., Li Y., Szyroki A., Giles I.G., Moir A., O'Connor C.D.
    Mol. Microbiol. 17:523-531(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 2-11.
    Strain: SL1344.

Entry informationi

Entry nameiFABI_SALTY
AccessioniPrimary (citable) accession number: P16657
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 1, 1990
Last sequence update: January 23, 2007
Last modified: October 1, 2014
This is version 120 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Miscellaneous

The antibiotic diazaborine interferes with the activity by binding to the protein.

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3