ID   MCRA_STRLA              Reviewed;         448 AA.
AC   P43485;
DT   01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 2.
DT   25-MAY-2022, entry version 70.
DE   RecName: Full=Mitomycin radical oxidase;
DE            EC=1.5.3.-;
GN   Name=mcrA;
OS   Streptomyces lavendulae.
OC   Bacteria; Actinobacteria; Streptomycetales; Streptomycetaceae;
OC   Streptomyces.
OX   NCBI_TaxID=1914;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROTEIN SEQUENCE OF 2-12.
RC   STRAIN=B619;
RX   PubMed=7517396; DOI=10.1128/jb.176.14.4448-4454.1994;
RA   August P.R., Flickinger M.C., Sherman D.H.;
RT   "Cloning and analysis of a locus (mcr) involved in mitomycin C resistance
RT   in Streptomyces lavendulae.";
RL   J. Bacteriol. 176:4448-4454(1994).
CC   -!- FUNCTION: Involved in mitomycin resistance; oxidizes reduced form of
CC       mitomycins.
CC   -!- COFACTOR:
CC       Name=FAD; Xref=ChEBI:CHEBI:57692; Evidence={ECO:0000305};
CC   -!- INDUCTION: By mitomycin C in concentrations as low as 300 nM.
CC   -!- SIMILARITY: Belongs to the oxygen-dependent FAD-linked oxidoreductase
CC       family. {ECO:0000305}.
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DR   EMBL; L29247; AAA21476.1; -; Genomic_DNA.
DR   PIR; A55519; A55519.
DR   AlphaFoldDB; P43485; -.
DR   SMR; P43485; -.
DR   GO; GO:0071949; F:FAD binding; IEA:InterPro.
DR   GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR   GO; GO:0046677; P:response to antibiotic; IEA:UniProtKB-KW.
DR   Gene3D; 3.30.43.10; -; 1.
DR   Gene3D; 3.30.465.10; -; 1.
DR   InterPro; IPR012951; BBE.
DR   InterPro; IPR016166; FAD-bd_PCMH.
DR   InterPro; IPR036318; FAD-bd_PCMH-like_sf.
DR   InterPro; IPR016167; FAD-bd_PCMH_sub1.
DR   InterPro; IPR016169; FAD-bd_PCMH_sub2.
DR   InterPro; IPR006094; Oxid_FAD_bind_N.
DR   InterPro; IPR006093; Oxy_OxRdtase_FAD_BS.
DR   Pfam; PF08031; BBE; 1.
DR   Pfam; PF01565; FAD_binding_4; 1.
DR   SUPFAM; SSF56176; SSF56176; 1.
DR   PROSITE; PS51387; FAD_PCMH; 1.
DR   PROSITE; PS00862; OX2_COVAL_FAD; 1.
PE   1: Evidence at protein level;
KW   Antibiotic resistance; Direct protein sequencing; FAD; Flavoprotein;
KW   Oxidoreductase.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000269|PubMed:7517396"
FT   CHAIN           2..448
FT                   /note="Mitomycin radical oxidase"
FT                   /id="PRO_0000128158"
FT   DOMAIN          27..195
FT                   /note="FAD-binding PCMH-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00718"
FT   MOD_RES         64
FT                   /note="Pros-8alpha-FAD histidine"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   448 AA;  48351 MW;  23F7EA65E080CB67 CRC64;
     MSTQWGWALE PDQPGYDDAR LGLNRAAESR PAYVVEAADE QEVAAAVRLA AEQKRPVGVM
     ATGHGPSVSA DDAVLVNTRR MEGVSVDAAR ATAWIEAGAR WRKVLEHTAP HGLAPLNGSS
     PNVGAVGYLV GGGAGLLGRR FGYAADHVRR LRLVTADGRL RDVTAGTDPD LFWAVRGGKD
     NFGLVVGMEV DLFPVTRLYG GGLYFAGEAT AEVLHAYAEW VRHVPEEMAS SVLLVHNPDL
     PDVPEPLRGR FITHLRIAYS GEPADGEHLV RPLRELGPIL LDTVRDMPYA EVGTIHHEPT
     SMPYVAYDRN VLLSDLTDDA VDIIVALAGP DAGAPFVTEL RHFGGAYARP PKVPNCVGGR
     DAAFSLFTGA VPEAEGLRRR DDLLDRLRPW STGGTNLNFA GVEDISPASV EAAYTPADFA
     RLRAVKAQYD PDNMFRVNFN IPPAESWT