ID   MRSD_BACSY              Reviewed;         194 AA.
AC   Q9RC23;
DT   19-SEP-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-2000, sequence version 1.
DT   25-MAY-2022, entry version 63.
DE   RecName: Full=Mersacidin decarboxylase;
DE            EC=4.1.1.-;
DE   AltName: Full=Mersacidin-modifying enzyme MrsD;
GN   Name=mrsD;
OS   Bacillus sp. (strain HIL-Y85/54728).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX   NCBI_TaxID=69002 {ECO:0000305};
RN   [1] {ECO:0000312|EMBL:CAB60260.1}
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=10831439; DOI=10.1128/aem.66.6.2565-2571.2000;
RA   Altena K., Guder A., Cramer C., Bierbaum G.;
RT   "Biosynthesis of the lantibiotic mersacidin: organization of a type B
RT   lantibiotic gene cluster.";
RL   Appl. Environ. Microbiol. 66:2565-2571(2000).
RN   [2] {ECO:0000305}
RP   FUNCTION, COFACTOR, ACTIVE SITE, AND MUTAGENESIS OF HIS-75.
RX   PubMed=11844751; DOI=10.1128/jb.184.5.1234-1243.2002;
RA   Majer F., Schmid D.G., Altena K., Bierbaum G., Kupke T.;
RT   "The flavoprotein MrsD catalyzes the oxidative decarboxylation reaction
RT   involved in formation of the peptidoglycan biosynthesis inhibitor
RT   mersacidin.";
RL   J. Bacteriol. 184:1234-1243(2002).
RN   [3] {ECO:0000305}
RP   X-RAY CRYSTALLOGRAPHY (2.54 ANGSTROMS).
RX   PubMed=12876343; DOI=10.1107/s0907444903011831;
RA   Blaesse M., Kupke T., Huber R., Steinbacher S.;
RT   "Structure of MrsD, an FAD-binding protein of the HFCD family.";
RL   Acta Crystallogr. D 59:1414-1421(2003).
CC   -!- FUNCTION: Catalyzes the oxidative decarboxylation of the C-terminal
CC       cysteine residue of mersacidin to an aminoenethiol residue.
CC       {ECO:0000269|PubMed:11844751}.
CC   -!- COFACTOR:
CC       Name=FAD; Xref=ChEBI:CHEBI:57692;
CC         Evidence={ECO:0000269|PubMed:11844751};
CC       Note=Binds 1 FAD per subunit. {ECO:0000269|PubMed:11844751};
CC   -!- PATHWAY: Antibiotic biosynthesis; mersacidin biosynthesis.
CC   -!- SUBUNIT: Homododecamer. {ECO:0000269|PubMed:12876343}.
CC   -!- SIMILARITY: Belongs to the HFCD (homooligomeric flavin containing Cys
CC       decarboxylase) superfamily. {ECO:0000305}.
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DR   EMBL; AJ250862; CAB60260.1; -; Genomic_DNA.
DR   PDB; 1P3Y; X-ray; 2.54 A; 1=1-194.
DR   PDBsum; 1P3Y; -.
DR   AlphaFoldDB; Q9RC23; -.
DR   SMR; Q9RC23; -.
DR   DrugBank; DB03147; Flavin adenine dinucleotide.
DR   UniPathway; UPA00166; -.
DR   EvolutionaryTrace; Q9RC23; -.
DR   GO; GO:0016829; F:lyase activity; IEA:UniProtKB-KW.
DR   GO; GO:0016491; F:oxidoreductase activity; IDA:UniProtKB.
DR   GO; GO:0017000; P:antibiotic biosynthetic process; IDA:UniProtKB.
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; FAD; Flavoprotein; Lyase.
FT   CHAIN           1..194
FT                   /note="Mersacidin decarboxylase"
FT                   /id="PRO_0000182035"
FT   ACT_SITE        75
FT                   /evidence="ECO:0000269|PubMed:11844751"
FT   MUTAGEN         75
FT                   /note="H->N: Abolishes enzyme activity."
FT                   /evidence="ECO:0000269|PubMed:11844751"
FT   HELIX           6..8
FT                   /evidence="ECO:0007829|PDB:1P3Y"
FT   STRAND          10..15
FT                   /evidence="ECO:0007829|PDB:1P3Y"
FT   HELIX           19..23
FT                   /evidence="ECO:0007829|PDB:1P3Y"
FT   HELIX           25..31
FT                   /evidence="ECO:0007829|PDB:1P3Y"
FT   TURN            32..34
FT                   /evidence="ECO:0007829|PDB:1P3Y"
FT   STRAND          35..42
FT                   /evidence="ECO:0007829|PDB:1P3Y"
FT   HELIX           44..49
FT                   /evidence="ECO:0007829|PDB:1P3Y"
FT   HELIX           52..55
FT                   /evidence="ECO:0007829|PDB:1P3Y"
FT   HELIX           56..58
FT                   /evidence="ECO:0007829|PDB:1P3Y"
FT   STRAND          59..63
FT                   /evidence="ECO:0007829|PDB:1P3Y"
FT   STRAND          68..70
FT                   /evidence="ECO:0007829|PDB:1P3Y"
FT   HELIX           75..81
FT                   /evidence="ECO:0007829|PDB:1P3Y"
FT   STRAND          83..90
FT                   /evidence="ECO:0007829|PDB:1P3Y"
FT   HELIX           92..99
FT                   /evidence="ECO:0007829|PDB:1P3Y"
FT   HELIX           106..113
FT                   /evidence="ECO:0007829|PDB:1P3Y"
FT   STRAND          114..116
FT                   /evidence="ECO:0007829|PDB:1P3Y"
FT   STRAND          119..122
FT                   /evidence="ECO:0007829|PDB:1P3Y"
FT   HELIX           126..129
FT                   /evidence="ECO:0007829|PDB:1P3Y"
FT   HELIX           132..144
FT                   /evidence="ECO:0007829|PDB:1P3Y"
FT   HELIX           173..183
FT                   /evidence="ECO:0007829|PDB:1P3Y"
SQ   SEQUENCE   194 AA;  21677 MW;  C1C2FE4FA5716878 CRC64;
     MSISILKDKK LLIGICGSIS SVGISSYLLY FKSFFKEIRV VMTKTAEDLI PAHTVSYFCD
     HVYSEHGENG KRHSHVEIGR WADIYCIIPA TANILGQTAN GVAMNLVATT VLAHPHNTIF
     FPNMNDLMWN KTVVSRNIEQ LRKDGHIVIE PVEIMAFEIA TGTRKPNRGL ITPDKALLAI
     EKGFKERTKH PSLT