ID   CYPD_STRSQ              Reviewed;         190 AA.
AC   E5KIB9;
DT   31-MAY-2011, integrated into UniProtKB/Swiss-Prot.
DT   08-FEB-2011, sequence version 1.
DT   03-AUG-2022, entry version 28.
DE   RecName: Full=Cypemycin cysteine dehydrogenase (decarboxylating);
DE            EC=1.3.99.36;
GN   Name=cypD {ECO:0000312|EMBL:ADR72965.1};
OS   Streptomyces sp.
OC   Bacteria; Actinobacteria; Streptomycetales; Streptomycetaceae;
OC   Streptomyces.
OX   NCBI_TaxID=1931;
RN   [1] {ECO:0000305}
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, AND CATALYTIC ACTIVITY.
RC   STRAIN=OH-4156 {ECO:0000269|PubMed:20805503};
RX   PubMed=20805503; DOI=10.1073/pnas.1008608107;
RA   Claesen J., Bibb M.;
RT   "Genome mining and genetic analysis of cypemycin biosynthesis reveal an
RT   unusual class of posttranslationally modified peptides.";
RL   Proc. Natl. Acad. Sci. U.S.A. 107:16297-16302(2010).
CC   -!- FUNCTION: Involved in the biosynthesis of the lanaridin cypemycin.
CC       {ECO:0000269|PubMed:20805503}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=[cypemycin](1-18)-L-Cys-L-Leu-L-Val-L-Cys + A = AH2 +
CC         C(3,19),S(21)-[cypemycin](1-18)-L-Ala-L-Leu-N-thioethenyl-L-
CC         valinamide + CO2 + hydrogen sulfide; Xref=Rhea:RHEA:10904, Rhea:RHEA-
CC         COMP:9797, Rhea:RHEA-COMP:9798, ChEBI:CHEBI:13193, ChEBI:CHEBI:16526,
CC         ChEBI:CHEBI:17499, ChEBI:CHEBI:29919, ChEBI:CHEBI:78612,
CC         ChEBI:CHEBI:78613; EC=1.3.99.36;
CC         Evidence={ECO:0000269|PubMed:20805503};
CC   -!- SIMILARITY: Belongs to the HFCD (homooligomeric flavin containing Cys
CC       decarboxylase) superfamily. {ECO:0000305}.
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DR   EMBL; HQ148718; ADR72965.1; -; Genomic_DNA.
DR   PDB; 6JDD; X-ray; 2.60 A; A=1-190.
DR   PDBsum; 6JDD; -.
DR   AlphaFoldDB; E5KIB9; -.
DR   SMR; E5KIB9; -.
DR   KEGG; ag:ADR72965; -.
DR   BioCyc; MetaCyc:MON-18445; -.
DR   GO; GO:0016831; F:carboxy-lyase activity; IDA:UniProtKB.
DR   GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR   GO; GO:0030651; P:peptide 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; Decarboxylase; Lyase; Oxidoreductase.
FT   CHAIN           1..190
FT                   /note="Cypemycin cysteine dehydrogenase (decarboxylating)"
FT                   /id="PRO_0000408756"
FT   STRAND          7..15
FT                   /evidence="ECO:0007829|PDB:6JDD"
FT   HELIX           19..23
FT                   /evidence="ECO:0007829|PDB:6JDD"
FT   HELIX           24..34
FT                   /evidence="ECO:0007829|PDB:6JDD"
FT   STRAND          39..44
FT                   /evidence="ECO:0007829|PDB:6JDD"
FT   HELIX           48..50
FT                   /evidence="ECO:0007829|PDB:6JDD"
FT   HELIX           54..60
FT                   /evidence="ECO:0007829|PDB:6JDD"
FT   STRAND          65..69
FT                   /evidence="ECO:0007829|PDB:6JDD"
FT   HELIX           77..81
FT                   /evidence="ECO:0007829|PDB:6JDD"
FT   STRAND          90..95
FT                   /evidence="ECO:0007829|PDB:6JDD"
FT   HELIX           97..104
FT                   /evidence="ECO:0007829|PDB:6JDD"
FT   HELIX           111..118
FT                   /evidence="ECO:0007829|PDB:6JDD"
FT   STRAND          123..127
FT                   /evidence="ECO:0007829|PDB:6JDD"
FT   HELIX           134..142
FT                   /evidence="ECO:0007829|PDB:6JDD"
FT   HELIX           143..145
FT                   /evidence="ECO:0007829|PDB:6JDD"
FT   STRAND          149..151
FT                   /evidence="ECO:0007829|PDB:6JDD"
FT   HELIX           172..185
FT                   /evidence="ECO:0007829|PDB:6JDD"
SQ   SEQUENCE   190 AA;  20750 MW;  63BE372B4B73F412 CRC64;
     MNVEKFEGAE LHVHVTGSIS AALVPWWIHW LREFQPELVV NVSVTPAASR FLAVRALRHL
     ANGKVWVDSW DDPDVPPEVN SGKSGASECF LVFPATLDTV MRLAQGRADS PALMMLQLTD
     APLVIADTFP GSNEIVENNV QTLKLRPNVE FAPRVNGVRA SNRQTAEVGF NLPGALAAAN
     RMRKEGRSGE