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Q81GI3

- FABI_BACCR

UniProt

Q81GI3 - FABI_BACCR

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Protein

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

Gene
fabI, BC_1216
Organism
Bacillus cereus (strain ATCC 14579 / DSM 31)
Status
Reviewed - Annotation score: 5 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 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 oxygen
Binding sitei94 – 941NAD; via carbonyl oxygen
Binding sitei97 – 971Substrate; via amide nitrogen and carbonyl oxygen
Active sitei147 – 1471Proton acceptor By similarity
Active sitei157 – 1571Proton acceptor
Binding sitei164 – 1641NAD
Sitei205 – 2051Involved in acyl-ACP binding By similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi19 – 202NAD
Nucleotide bindingi66 – 672NAD
Nucleotide bindingi193 – 1975NAD

GO - Molecular functioni

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

GO - Biological processi

  1. fatty acid elongation Source: UniProtKB
  2. protein homotetramerization Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Biological processi

Fatty acid biosynthesis, Fatty acid metabolism, Lipid biosynthesis, Lipid metabolism

Keywords - Ligandi

NAD, NADP, Nucleotide-binding

Enzyme and pathway databases

BioCyciBCER226900:GJEU-1216-MONOMER.
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)
Taxonomic identifieri226900 [NCBI]
Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesBacillaceaeBacillusBacillus cereus group
ProteomesiUP000001417: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 256256Enoyl-[acyl-carrier-protein] reductase [NADH] FabIPRO_0000407976Add
BLAST

Proteomic databases

PRIDEiQ81GI3.

Interactioni

Subunit structurei

Homotetramer.1 Publication

Protein-protein interaction databases

STRINGi226900.BC1216.

Structurei

Secondary structure

1
256
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi8 – 125
Helixi20 – 2910
Turni30 – 323
Beta strandi34 – 396
Helixi45 – 5410
Beta strandi55 – 584
Beta strandi62 – 643
Helixi70 – 8415
Beta strandi89 – 924
Helixi99 – 1013
Beta strandi102 – 1043
Helixi106 – 1083
Helixi111 – 12111
Helixi123 – 13311
Beta strandi140 – 1467
Helixi148 – 1503
Turni155 – 1573
Helixi158 – 17821
Helixi179 – 1813
Beta strandi183 – 1908
Helixi196 – 1983
Helixi204 – 21411
Helixi223 – 23412
Helixi236 – 2383
Beta strandi245 – 2495
Helixi252 – 2543

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3OJEX-ray3.02A1-256[»]
3OJFX-ray2.20A/B/C/D1-256[»]
ProteinModelPortaliQ81GI3.

Miscellaneous databases

EvolutionaryTraceiQ81GI3.

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

eggNOGiCOG0623.
KOiK00208.
OMAiTGEIHHV.
OrthoDBiEOG6HF644.

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.

Q81GI3-1 [UniParc]FASTAAdd to Basket

« Hide

MELLQGKTFV VMGVANQRSI AWGIARSLHN AGAKLIFTYA GERLERNVRE    50
LADTLEGQES LVLPCDVTND EELTACFETI KQEVGTIHGV AHCIAFANRD 100
DLKGEFVDTS RDGFLLAQNI SAFSLTAVAR EAKKVMTEGG NILTLTYLGG 150
ERVVKNYNVM GVAKASLEAS VKYLANDLGQ HGIRVNAISA GPIRTLSAKG 200
VGDFNSILRE IEERAPLRRT TTQEEVGDTA VFLFSDLARG VTGENIHVDS 250
GYHILG 256
Length:256
Mass (Da):27,740
Last modified:June 1, 2003 - v1
Checksum:i66780350F497CA31
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AE016877 Genomic DNA. Translation: AAP08201.1.
RefSeqiNP_831000.1. NC_004722.1.

Genome annotation databases

EnsemblBacteriaiAAP08201; AAP08201; BC_1216.
GeneIDi1203565.
KEGGibce:BC1216.
PATRICi32598149. VBIBacCer54481_1186.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AE016877 Genomic DNA. Translation: AAP08201.1 .
RefSeqi NP_831000.1. NC_004722.1.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
3OJE X-ray 3.02 A 1-256 [» ]
3OJF X-ray 2.20 A/B/C/D 1-256 [» ]
ProteinModelPortali Q81GI3.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 226900.BC1216.

Proteomic databases

PRIDEi Q81GI3.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai AAP08201 ; AAP08201 ; BC_1216 .
GeneIDi 1203565.
KEGGi bce:BC1216.
PATRICi 32598149. VBIBacCer54481_1186.

Phylogenomic databases

eggNOGi COG0623.
KOi K00208.
OMAi TGEIHHV.
OrthoDBi EOG6HF644.

Enzyme and pathway databases

UniPathwayi UPA00094 .
BioCyci BCER226900:GJEU-1216-MONOMER.

Miscellaneous databases

EvolutionaryTracei Q81GI3.

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. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 14579 / DSM 31.
  2. "Dimeric and tetrameric forms of enoyl-acyl carrier protein reductase from Bacillus cereus."
    Kim S.J., Ha B.H., Kim K.H., Hong S.K., Shin K.J., Suh S.W., Kim E.E.
    Biochem. Biophys. Res. Commun. 400:517-522(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.20 ANGSTROMS) IN COMPLEX WITH NAD AND INHIBITOR, SUBUNIT.

Entry informationi

Entry nameiFABI_BACCR
AccessioniPrimary (citable) accession number: Q81GI3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 3, 2011
Last sequence update: June 1, 2003
Last modified: May 14, 2014
This is version 84 of the entry and version 1 of the sequence. [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

External Data

Dasty 3

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