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Protein

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

Gene

fabI

Organism
Bacillus cereus (strain ATCC 14579 / DSM 31 / JCM 2152 / NBRC 15305 / NCIMB 9373 / NRRL B-3711)
Status
Reviewed-Annotation score: -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 (By similarity).By similarity

Catalytic activityi

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

Pathwayi: fatty acid biosynthesis

This protein is involved in the pathway fatty acid biosynthesis, which is part of Lipid metabolism.
View all proteins of this organism that are known to be involved in the pathway fatty acid biosynthesis and in Lipid metabolism.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Binding sitei13NAD; via carbonyl oxygen1 Publication1
Binding sitei94NAD; via carbonyl oxygen1 Publication1
Binding sitei97Substrate; via amide nitrogen and carbonyl oxygen1
Active sitei147Proton acceptorBy similarity1
Active sitei157Proton acceptor1
Binding sitei164NAD1 Publication1
Sitei205Involved in acyl-ACP bindingBy similarity1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi19 – 20NAD1 Publication2
Nucleotide bindingi66 – 67NAD1 Publication2
Nucleotide bindingi193 – 197NAD1 Publication5

GO - Molecular functioni

GO - Biological processi

  • fatty acid elongation Source: UniProtKB
  • protein homotetramerization Source: UniProtKB

Keywordsi

Molecular functionOxidoreductase
Biological processFatty acid biosynthesis, Fatty acid metabolism, Lipid biosynthesis, Lipid metabolism
LigandNAD, NADP, Nucleotide-binding

Enzyme and pathway databases

BRENDAi1.3.1.10 648
1.3.1.9 648
UniPathwayiUPA00094

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
Ordered Locus Names:BC_1216
OrganismiBacillus cereus (strain ATCC 14579 / DSM 31 / JCM 2152 / NBRC 15305 / NCIMB 9373 / NRRL B-3711)
Taxonomic identifieri226900 [NCBI]
Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesBacillaceaeBacillusBacillus cereus group
Proteomesi
  • UP000001417 Componenti: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00004079761 – 256Enoyl-[acyl-carrier-protein] reductase [NADH] FabIAdd BLAST256

Interactioni

Subunit structurei

Homotetramer.1 Publication

Protein-protein interaction databases

STRINGi226900.BC1216

Structurei

Secondary structure

1256
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Turni3 – 6Combined sources4
Beta strandi8 – 12Combined sources5
Helixi20 – 30Combined sources11
Beta strandi34 – 41Combined sources8
Helixi42 – 53Combined sources12
Beta strandi55 – 58Combined sources4
Beta strandi61 – 64Combined sources4
Helixi70 – 83Combined sources14
Beta strandi88 – 92Combined sources5
Helixi99 – 101Combined sources3
Beta strandi102 – 104Combined sources3
Helixi106 – 108Combined sources3
Helixi113 – 132Combined sources20
Turni133 – 135Combined sources3
Beta strandi140 – 147Combined sources8
Helixi148 – 150Combined sources3
Turni155 – 157Combined sources3
Helixi162 – 178Combined sources17
Helixi179 – 181Combined sources3
Beta strandi183 – 190Combined sources8
Helixi196 – 198Combined sources3
Beta strandi200 – 202Combined sources3
Helixi205 – 214Combined sources10
Helixi223 – 234Combined sources12
Helixi236 – 238Combined sources3
Beta strandi245 – 249Combined sources5
Helixi252 – 255Combined sources4

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
3OJEX-ray3.02A1-256[»]
3OJFX-ray2.20A/B/C/D1-256[»]
5YCRX-ray1.96A/B/C/D1-256[»]
5YCSX-ray1.95A/B/C/D1-256[»]
5YCVX-ray1.85A/B/C/D1-256[»]
5YCXX-ray1.70A1-256[»]
ProteinModelPortaliQ81GI3
SMRiQ81GI3
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ81GI3

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

eggNOGiCOG0623 LUCA
KOiK00208
OMAiGILDMIH

Family and domain databases

InterProiView protein in InterPro
IPR014358 Enoyl-ACP_Rdtase_NADH
IPR036291 NAD(P)-bd_dom_sf
IPR002347 SDR_fam
PANTHERiPTHR43159:SF2 PTHR43159:SF2, 1 hit
PIRSFiPIRSF000094 Enoyl-ACP_rdct, 1 hit
PRINTSiPR00081 GDHRDH
SUPFAMiSSF51735 SSF51735, 1 hit

Sequencei

Sequence statusi: Complete.

Q81GI3-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MELLQGKTFV VMGVANQRSI AWGIARSLHN AGAKLIFTYA GERLERNVRE
60 70 80 90 100
LADTLEGQES LVLPCDVTND EELTACFETI KQEVGTIHGV AHCIAFANRD
110 120 130 140 150
DLKGEFVDTS RDGFLLAQNI SAFSLTAVAR EAKKVMTEGG NILTLTYLGG
160 170 180 190 200
ERVVKNYNVM GVAKASLEAS VKYLANDLGQ HGIRVNAISA GPIRTLSAKG
210 220 230 240 250
VGDFNSILRE IEERAPLRRT TTQEEVGDTA VFLFSDLARG VTGENIHVDS

GYHILG
Length:256
Mass (Da):27,740
Last modified:June 1, 2003 - v1
Checksum:i66780350F497CA31
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE016877 Genomic DNA Translation: AAP08201.1
RefSeqiNP_831000.1, NC_004722.1
WP_000421886.1, NC_004722.1

Genome annotation databases

EnsemblBacteriaiAAP08201; AAP08201; BC_1216
GeneIDi1203565
31631210
KEGGibce:BC1216
PATRICifig|226900.8.peg.1186

Similar proteinsi

Entry informationi

Entry nameiFABI_BACCR
AccessioniPrimary (citable) accession number: Q81GI3
Entry historyiIntegrated into UniProtKB/Swiss-Prot: May 3, 2011
Last sequence update: June 1, 2003
Last modified: May 23, 2018
This is version 102 of the entry and version 1 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

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