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Protein

Epidermin decarboxylase

Gene

epiD

Organism
Staphylococcus epidermidis
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Catalyzes the removal of two reducing equivalents (oxidative decarboxylation) from the cysteine residue of the C-terminal meso-lanthionine of epidermin to form a --C==C-- double bond.

Cofactori

FMNNote: Binds 1 FMN per subunit.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei67 – 671

GO - Molecular functioni

Complete GO annotation...

Keywords - Molecular functioni

Lyase

Keywords - Ligandi

Flavoprotein, FMN

Names & Taxonomyi

Protein namesi
Recommended name:
Epidermin decarboxylase (EC:4.1.1.-)
Alternative name(s):
Epidermin-modifying enzyme EpiD
Gene namesi
Name:epiD
Encoded oniPlasmid pTu 320 Publication
OrganismiStaphylococcus epidermidis
Taxonomic identifieri1282 [NCBI]
Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesStaphylococcaceaeStaphylococcus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi43 – 431F → L: Binds FMN, but activity is significantly decreased. 1 Publication
Mutagenesisi67 – 671H → N: Retains less than 1% activity, binds FMN. 1 Publication
Mutagenesisi75 – 751E → D or Q: Binds FMN. 1 Publication
Mutagenesisi81 – 811P → D: Loss of FMN binding. 1 Publication
Mutagenesisi83 – 831S → A: Loss of FMN binding. 1 Publication
Mutagenesisi83 – 831S → T: Binds FMN. 1 Publication
Mutagenesisi84 – 841A → V: Binds FMN. 1 Publication
Mutagenesisi85 – 851N → D or H: Loss of FMN binding. 1 Publication
Mutagenesisi93 – 931G → A or D: Loss of FMN binding. 1 Publication
Mutagenesisi95 – 951C → A: Binds FMN. 1 Publication
Mutagenesisi96 – 961D → N: Loss of FMN binding. 1 Publication
Mutagenesisi98 – 981L → V: Binds FMN. 1 Publication
Mutagenesisi103 – 1031C → A: Binds FMN. 1 Publication
Mutagenesisi114 – 1141P → A: Loss of FMN binding. 1 Publication
Mutagenesisi115 – 1151N → D: Retains less than 1% activity, binds FMN. 1 Publication
Mutagenesisi117 – 1171N → D: Binds FMN. 1 Publication
Mutagenesisi120 – 1201M → L: Retains less than 1% activity, binds FMN. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 181181Epidermin decarboxylasePRO_0000182034Add
BLAST

Interactioni

Subunit structurei

Homododecamer.

Structurei

Secondary structure

1
181
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi5 – 95Combined sources
Helixi13 – 175Combined sources
Helixi18 – 258Combined sources
Turni26 – 283Combined sources
Beta strandi32 – 365Combined sources
Helixi38 – 425Combined sources
Helixi46 – 516Combined sources
Turni59 – 613Combined sources
Helixi67 – 726Combined sources
Beta strandi75 – 828Combined sources
Helixi84 – 918Combined sources
Helixi98 – 1058Combined sources
Helixi107 – 1093Combined sources
Beta strandi110 – 1145Combined sources
Helixi118 – 1214Combined sources
Helixi124 – 13411Combined sources
Turni135 – 1373Combined sources
Beta strandi144 – 1507Combined sources
Beta strandi151 – 1577Combined sources
Helixi165 – 1739Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1G5QX-ray2.57A/D/G/L1-181[»]
1G63X-ray2.50A/B/C/D/E/F/G/H/I/J/K/L1-181[»]
ProteinModelPortaliP30197.
SMRiP30197. Positions 1-174.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP30197.

Family & Domainsi

Sequence similaritiesi

Family and domain databases

Gene3Di3.40.50.1950. 1 hit.
InterProiIPR003382. Flavoprotein.
[Graphical view]
PfamiPF02441. Flavoprotein. 1 hit.
[Graphical view]
SUPFAMiSSF52507. SSF52507. 1 hit.

Sequencei

Sequence statusi: Complete.

P30197-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MYGKLLICAT ASINVININH YIVELKQHFD EVNILFSPSS KNFINTDVLK
60 70 80 90 100
LFCDNLYDEI KDPLLNHINI VENHEYILVL PASANTINKI ANGICDNLLT
110 120 130 140 150
TVCLTGYQKL FIFPNMNIRM WGNPFLQKNI DLLKNNDVKV YSPDMNKSFE
160 170 180
ISSGRYKNNI TMPNIENVLN FVLNNEKRPL D
Length:181
Mass (Da):20,825
Last modified:April 1, 1993 - v1
Checksum:i126830E0B987CE2C
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X62386 Genomic DNA. Translation: CAA44255.1.
PIRiS23418.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X62386 Genomic DNA. Translation: CAA44255.1.
PIRiS23418.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1G5QX-ray2.57A/D/G/L1-181[»]
1G63X-ray2.50A/B/C/D/E/F/G/H/I/J/K/L1-181[»]
ProteinModelPortaliP30197.
SMRiP30197. Positions 1-174.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Miscellaneous databases

EvolutionaryTraceiP30197.

Family and domain databases

Gene3Di3.40.50.1950. 1 hit.
InterProiIPR003382. Flavoprotein.
[Graphical view]
PfamiPF02441. Flavoprotein. 1 hit.
[Graphical view]
SUPFAMiSSF52507. SSF52507. 1 hit.
ProtoNetiSearch...

Publicationsi

  1. "Analysis of genes involved in the biosynthesis of lantibiotic epidermin."
    Schnell N., Engelke G., Augustin J., Rosenstein R., Ungermann V., Goetz F., Entian K.-D.
    Eur. J. Biochem. 204:57-68(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: TU 3298 / DSM 3095.
  2. "Purification and characterization of EpiD, a flavoprotein involved in the biosynthesis of the lantibiotic epidermin."
    Kupke T., Stevanovic S., Sahl H.G., Goetz F.
    J. Bacteriol. 174:5354-5361(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: CHARACTERIZATION.
    Strain: TU 3298 / DSM 3095.
  3. "Molecular characterization of lantibiotic-synthesizing enzyme EpiD reveals a function for bacterial Dfp proteins in coenzyme A biosynthesis."
    Kupke T., Uebele M., Schmid D., Jung G., Blaesse M., Steinbacher S.
    J. Biol. Chem. 275:31838-31846(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: CHARACTERIZATION OF ACTIVITY, MUTAGENESIS OF PHE-43; HIS-67; GLU-75; PRO-81; SER-83; ALA-84; ASN-85; GLY-93; CYS-95; ASP-96; LEU-98; CYS-103; PRO-114; ASN-115; ASN-117 AND MET-120.
  4. "Crystal structure of the peptidyl-cysteine decarboxylase EpiD complexed with a pentapeptide substrate."
    Blaesse M., Kupke T., Huber R., Steinbacher S.
    EMBO J. 19:6299-6310(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS).

Entry informationi

Entry nameiEPID_STAEP
AccessioniPrimary (citable) accession number: P30197
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 1, 1993
Last sequence update: April 1, 1993
Last modified: March 16, 2016
This is version 67 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, Plasmid

Documents

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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.