P30197 (EPID_STAEP) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Epidermin decarboxylase
EC=4.1.1.-

Alternative name(s):
Epidermin-modifying enzyme EpiD

Gene names

Name:

epiD

Encoded on

Plasmid pTu 32

Organism

Staphylococcus epidermidis

Taxonomic identifier

1282 [NCBI]

Taxonomic lineage

cellular organisms › Bacteria › Firmicutes › Bacilli › Bacillales › Staphylococcaceae › Staphylococcus

Protein attributes

Sequence length	181 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	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.
Cofactor	Binds 1 FMN per subunit.
Subunit structure	Homododecamer.
Sequence similarities	Belongs to the HFCD (homooligomeric flavin containing Cys decarboxylase) superfamily.

Ontologies

Keywords
Ligand	FMN Flavoprotein
Molecular function	Lyase
Technical term	3D-structure Plasmid
Gene Ontology (GO)
Biological_process	metabolic process Inferred from electronic annotation. Source: GOC
Molecular_function	lyase activity Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 181

181

Epidermin decarboxylase

PRO_0000182034

Sites

Active site

67

1

Experimental info

Mutagenesis

43

1

F → L: Binds FMN, but activity is significantly decreased. Ref.3

Mutagenesis

67

1

H → N: Retains less than 1% activity, binds FMN. Ref.3

Mutagenesis

75

1

E → D or Q: Binds FMN. Ref.3

Mutagenesis

81

1

P → D: Loss of FMN binding. Ref.3

Mutagenesis

83

1

S → A: Loss of FMN binding. Ref.3

Mutagenesis

83

1

S → T: Binds FMN. Ref.3

Mutagenesis

84

1

A → V: Binds FMN. Ref.3

Mutagenesis

85

1

N → D or H: Loss of FMN binding. Ref.3

Mutagenesis

93

1

G → A or D: Loss of FMN binding. Ref.3

Mutagenesis

95

1

C → A: Binds FMN. Ref.3

Mutagenesis

96

1

D → N: Loss of FMN binding. Ref.3

Mutagenesis

98

1

L → V: Binds FMN. Ref.3

Mutagenesis

103

1

C → A: Binds FMN. Ref.3

Mutagenesis

114

1

P → A: Loss of FMN binding. Ref.3

Mutagenesis

115

1

N → D: Retains less than 1% activity, binds FMN. Ref.3

Mutagenesis

117

1

N → D: Binds FMN. Ref.3

Mutagenesis

120

1

M → L: Retains less than 1% activity, binds FMN. Ref.3

Secondary structure

1

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181

Helix Strand Turn

Details...

Beta strand

5 – 9

5

Helix

13 – 17

5

Helix

18 – 25

8

Turn

26 – 28

3

Beta strand

32 – 36

5

Helix

38 – 42

5

Helix

46 – 51

6

Turn

59 – 61

3

Helix

67 – 72

6

Beta strand

75 – 82

8

Helix

84 – 91

8

Helix

98 – 105

8

Helix

107 – 109

3

Beta strand

110 – 114

5

Helix

118 – 121

4

Helix

124 – 134

11

Turn

135 – 137

3

Beta strand

144 – 150

7

Turn

151 – 154

4

Beta strand

155 – 161

7

Helix

165 – 173

9

Sequences

	Sequence		Length	Mass (Da)
	P30197 [UniParc]. Last modified April 1, 1993. Version 1. Checksum: 126830E0B987CE2C	FASTA	181	20,825
	10 20 30 40 50 60 MYGKLLICAT ASINVININH YIVELKQHFD EVNILFSPSS KNFINTDVLK LFCDNLYDEI 70 80 90 100 110 120 KDPLLNHINI VENHEYILVL PASANTINKI ANGICDNLLT TVCLTGYQKL FIFPNMNIRM 130 140 150 160 170 180 WGNPFLQKNI DLLKNNDVKV YSPDMNKSFE ISSGRYKNNI TMPNIENVLN FVLNNEKRPL D

References

[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).

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

X62386 Genomic DNA. Translation: CAA44255.1.

PIR

S23418.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1G5Q	X-ray	2.57	A/D/G/L	1-181	[»]
1G63	X-ray	2.50	A/B/C/D/E/F/G/H/I/J/K/L	1-181	[»]

ProteinModelPortal

P30197.

SMR

P30197. Positions 1-174.

ModBase

Search...

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Family and domain databases

Gene3D

3.40.50.1950. 1 hit.

InterPro

IPR003382. Flavoprotein.
[Graphical view]

Pfam

PF02441. Flavoprotein. 1 hit.
[Graphical view]

SUPFAM

SSF52507. Flavoprotein. 1 hit.

ProtoNet

Search...

Other

EvolutionaryTrace

P30197.

Entry information

Entry name

EPID_STAEP

Accession

Primary (citable) accession number: P30197

Entry history

Integrated into UniProtKB/Swiss-Prot:	April 1, 1993
Last sequence update:	April 1, 1993
Last modified:	April 3, 2013
This is version 56 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program