EPID_STAEP
ID EPID_STAEP Reviewed; 181 AA.
AC P30197;
DT 01-APR-1993, integrated into UniProtKB/Swiss-Prot.
DT 01-APR-1993, sequence version 1.
DT 25-MAY-2022, entry version 77.
DE RecName: Full=Epidermin decarboxylase;
DE EC=4.1.1.-;
DE AltName: Full=Epidermin-modifying enzyme EpiD;
GN Name=epiD;
OS Staphylococcus epidermidis.
OG Plasmid pTu 32.
OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC Staphylococcus.
OX NCBI_TaxID=1282;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=TU 3298 / DSM 3095;
RX PubMed=1740156; DOI=10.1111/j.1432-1033.1992.tb16605.x;
RA Schnell N., Engelke G., Augustin J., Rosenstein R., Ungermann V., Goetz F.,
RA Entian K.-D.;
RT "Analysis of genes involved in the biosynthesis of lantibiotic epidermin.";
RL Eur. J. Biochem. 204:57-68(1992).
RN [2]
RP CHARACTERIZATION.
RC STRAIN=TU 3298 / DSM 3095;
RX PubMed=1644762; DOI=10.1128/jb.174.16.5354-5361.1992;
RA Kupke T., Stevanovic S., Sahl H.G., Goetz F.;
RT "Purification and characterization of EpiD, a flavoprotein involved in the
RT biosynthesis of the lantibiotic epidermin.";
RL J. Bacteriol. 174:5354-5361(1992).
RN [3]
RP CHARACTERIZATION OF ACTIVITY, AND MUTAGENESIS OF PHE-43; HIS-67; GLU-75;
RP PRO-81; SER-83; ALA-84; ASN-85; GLY-93; CYS-95; ASP-96; LEU-98; CYS-103;
RP PRO-114; ASN-115; ASN-117 AND MET-120.
RX PubMed=10922366; DOI=10.1074/jbc.m004273200;
RA Kupke T., Uebele M., Schmid D., Jung G., Blaesse M., Steinbacher S.;
RT "Molecular characterization of lantibiotic-synthesizing enzyme EpiD reveals
RT a function for bacterial Dfp proteins in coenzyme A biosynthesis.";
RL J. Biol. Chem. 275:31838-31846(2000).
RN [4]
RP X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS).
RX PubMed=11101502; DOI=10.1093/emboj/19.23.6299;
RA Blaesse M., Kupke T., Huber R., Steinbacher S.;
RT "Crystal structure of the peptidyl-cysteine decarboxylase EpiD complexed
RT with a pentapeptide substrate.";
RL EMBO J. 19:6299-6310(2000).
CC -!- FUNCTION: Catalyzes the removal of two reducing equivalents (oxidative
CC decarboxylation) from the cysteine residue of the C-terminal meso-
CC lanthionine of epidermin to form a --C==C-- double bond.
CC -!- COFACTOR:
CC Name=FMN; Xref=ChEBI:CHEBI:58210;
CC Note=Binds 1 FMN per subunit.;
CC -!- SUBUNIT: Homododecamer.
CC -!- SIMILARITY: Belongs to the HFCD (homooligomeric flavin containing Cys
CC decarboxylase) superfamily. {ECO:0000305}.
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DR EMBL; X62386; CAA44255.1; -; Genomic_DNA.
DR PIR; S23418; S23418.
DR PDB; 1G5Q; X-ray; 2.57 A; A/D/G/L=1-181.
DR PDB; 1G63; X-ray; 2.50 A; A/B/C/D/E/F/G/H/I/J/K/L=1-181.
DR PDBsum; 1G5Q; -.
DR PDBsum; 1G63; -.
DR AlphaFoldDB; P30197; -.
DR SMR; P30197; -.
DR DrugBank; DB03247; Flavin mononucleotide.
DR EvolutionaryTrace; P30197; -.
DR GO; GO:0016829; F:lyase activity; IEA:UniProtKB-KW.
DR Gene3D; 3.40.50.1950; -; 1.
DR InterPro; IPR036551; Flavin_trans-like.
DR InterPro; IPR003382; Flavoprotein.
DR Pfam; PF02441; Flavoprotein; 1.
DR SUPFAM; SSF52507; SSF52507; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Flavoprotein; FMN; Lyase; Plasmid.
FT CHAIN 1..181
FT /note="Epidermin decarboxylase"
FT /id="PRO_0000182034"
FT ACT_SITE 67
FT MUTAGEN 43
FT /note="F->L: Binds FMN, but activity is significantly
FT decreased."
FT /evidence="ECO:0000269|PubMed:10922366"
FT MUTAGEN 67
FT /note="H->N: Retains less than 1% activity, binds FMN."
FT /evidence="ECO:0000269|PubMed:10922366"
FT MUTAGEN 75
FT /note="E->D,Q: Binds FMN."
FT /evidence="ECO:0000269|PubMed:10922366"
FT MUTAGEN 81
FT /note="P->D: Loss of FMN binding."
FT /evidence="ECO:0000269|PubMed:10922366"
FT MUTAGEN 83
FT /note="S->A: Loss of FMN binding."
FT /evidence="ECO:0000269|PubMed:10922366"
FT MUTAGEN 83
FT /note="S->T: Binds FMN."
FT /evidence="ECO:0000269|PubMed:10922366"
FT MUTAGEN 84
FT /note="A->V: Binds FMN."
FT /evidence="ECO:0000269|PubMed:10922366"
FT MUTAGEN 85
FT /note="N->D,H: Loss of FMN binding."
FT /evidence="ECO:0000269|PubMed:10922366"
FT MUTAGEN 93
FT /note="G->A,D: Loss of FMN binding."
FT /evidence="ECO:0000269|PubMed:10922366"
FT MUTAGEN 95
FT /note="C->A: Binds FMN."
FT /evidence="ECO:0000269|PubMed:10922366"
FT MUTAGEN 96
FT /note="D->N: Loss of FMN binding."
FT /evidence="ECO:0000269|PubMed:10922366"
FT MUTAGEN 98
FT /note="L->V: Binds FMN."
FT /evidence="ECO:0000269|PubMed:10922366"
FT MUTAGEN 103
FT /note="C->A: Binds FMN."
FT /evidence="ECO:0000269|PubMed:10922366"
FT MUTAGEN 114
FT /note="P->A: Loss of FMN binding."
FT /evidence="ECO:0000269|PubMed:10922366"
FT MUTAGEN 115
FT /note="N->D: Retains less than 1% activity, binds FMN."
FT /evidence="ECO:0000269|PubMed:10922366"
FT MUTAGEN 117
FT /note="N->D: Binds FMN."
FT /evidence="ECO:0000269|PubMed:10922366"
FT MUTAGEN 120
FT /note="M->L: Retains less than 1% activity, binds FMN."
FT /evidence="ECO:0000269|PubMed:10922366"
FT STRAND 5..9
FT /evidence="ECO:0007829|PDB:1G63"
FT HELIX 13..17
FT /evidence="ECO:0007829|PDB:1G63"
FT HELIX 18..25
FT /evidence="ECO:0007829|PDB:1G63"
FT TURN 26..28
FT /evidence="ECO:0007829|PDB:1G63"
FT STRAND 32..36
FT /evidence="ECO:0007829|PDB:1G63"
FT HELIX 38..42
FT /evidence="ECO:0007829|PDB:1G63"
FT HELIX 46..51
FT /evidence="ECO:0007829|PDB:1G63"
FT TURN 59..61
FT /evidence="ECO:0007829|PDB:1G63"
FT HELIX 67..72
FT /evidence="ECO:0007829|PDB:1G63"
FT STRAND 75..82
FT /evidence="ECO:0007829|PDB:1G63"
FT HELIX 84..91
FT /evidence="ECO:0007829|PDB:1G63"
FT HELIX 98..105
FT /evidence="ECO:0007829|PDB:1G63"
FT HELIX 107..109
FT /evidence="ECO:0007829|PDB:1G63"
FT STRAND 110..114
FT /evidence="ECO:0007829|PDB:1G63"
FT HELIX 118..121
FT /evidence="ECO:0007829|PDB:1G63"
FT HELIX 124..134
FT /evidence="ECO:0007829|PDB:1G63"
FT TURN 135..137
FT /evidence="ECO:0007829|PDB:1G63"
FT STRAND 144..150
FT /evidence="ECO:0007829|PDB:1G5Q"
FT STRAND 151..157
FT /evidence="ECO:0007829|PDB:1G63"
FT HELIX 165..173
FT /evidence="ECO:0007829|PDB:1G63"
SQ SEQUENCE 181 AA; 20825 MW; 126830E0B987CE2C CRC64;
MYGKLLICAT ASINVININH YIVELKQHFD EVNILFSPSS KNFINTDVLK LFCDNLYDEI
KDPLLNHINI VENHEYILVL PASANTINKI ANGICDNLLT TVCLTGYQKL FIFPNMNIRM
WGNPFLQKNI DLLKNNDVKV YSPDMNKSFE ISSGRYKNNI TMPNIENVLN FVLNNEKRPL
D
