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Database: UniProt
Entry: A0A161I1C7_9MICO
LinkDB: A0A161I1C7_9MICO
Original site: A0A161I1C7_9MICO 
ID   A0A161I1C7_9MICO        Unreviewed;       481 AA.
AC   A0A161I1C7;
DT   06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT   06-JUL-2016, sequence version 1.
DT   27-MAR-2024, entry version 25.
DE   SubName: Full=Mitomycin radical oxidase {ECO:0000313|EMBL:ANC29989.1};
DE            EC=1.5.3.- {ECO:0000313|EMBL:ANC29989.1};
GN   Name=mcrA {ECO:0000313|EMBL:ANC29989.1};
GN   ORFNames=I598_0401 {ECO:0000313|EMBL:ANC29989.1};
OS   Isoptericola dokdonensis DS-3.
OC   Bacteria; Actinomycetota; Actinomycetes; Micrococcales;
OC   Promicromonosporaceae; Isoptericola.
OX   NCBI_TaxID=1300344 {ECO:0000313|EMBL:ANC29989.1, ECO:0000313|Proteomes:UP000076794};
RN   [1] {ECO:0000313|EMBL:ANC29989.1, ECO:0000313|Proteomes:UP000076794}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DS-3 {ECO:0000313|EMBL:ANC29989.1,
RC   ECO:0000313|Proteomes:UP000076794};
RA   Kwon S.-K., Kim J.F.;
RT   "Complete genome sequence of a soil Actinobacterium, Isoptericola
RT   dokdonensis DS-3.";
RL   Submitted (JAN-2016) to the EMBL/GenBank/DDBJ databases.
CC   -!- COFACTOR:
CC       Name=FAD; Xref=ChEBI:CHEBI:57692;
CC         Evidence={ECO:0000256|ARBA:ARBA00001974};
CC   -!- SIMILARITY: Belongs to the oxygen-dependent FAD-linked oxidoreductase
CC       family. {ECO:0000256|ARBA:ARBA00005466}.
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DR   EMBL; CP014209; ANC29989.1; -; Genomic_DNA.
DR   RefSeq; WP_068200825.1; NZ_CP014209.1.
DR   AlphaFoldDB; A0A161I1C7; -.
DR   STRING; 1300344.I598_0401; -.
DR   KEGG; ido:I598_0401; -.
DR   PATRIC; fig|1300344.3.peg.402; -.
DR   OrthoDB; 9775082at2; -.
DR   Proteomes; UP000076794; Chromosome.
DR   GO; GO:0071949; F:FAD binding; IEA:InterPro.
DR   GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR   Gene3D; 3.30.465.10; -; 1.
DR   Gene3D; 3.40.462.20; -; 1.
DR   Gene3D; 3.30.43.10; Uridine Diphospho-n-acetylenolpyruvylglucosamine Reductase, domain 2; 1.
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   PANTHER; PTHR42973; BINDING OXIDOREDUCTASE, PUTATIVE (AFU_ORTHOLOGUE AFUA_1G17690)-RELATED; 1.
DR   PANTHER; PTHR42973:SF39; FAD-BINDING PCMH-TYPE DOMAIN-CONTAINING PROTEIN; 1.
DR   Pfam; PF01565; FAD_binding_4; 1.
DR   SUPFAM; SSF56176; FAD-binding/transporter-associated domain-like; 1.
DR   PROSITE; PS51387; FAD_PCMH; 1.
DR   PROSITE; PS00862; OX2_COVAL_FAD; 1.
PE   3: Inferred from homology;
KW   Oxidoreductase {ECO:0000313|EMBL:ANC29989.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000076794}.
FT   DOMAIN          56..224
FT                   /note="FAD-binding PCMH-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51387"
SQ   SEQUENCE   481 AA;  49325 MW;  38C88769B57F588F CRC64;
     MSRTTGPTTA LDVPTSEHLA AATDAAAALA RTISGTVLRP DDDGYEEALP GYNLALDHRP
     AFVVRAATPG DVALTVRAAV AHGLGVGVRS TGHSAAATGP ADVLLDTSGL ARLEVDPLSR
     TATVGAGVRW QAVLDAAAPH GLGGLCGSSP QVGVVGYTLG GGLGPSARTF GFAADHVRSI
     DVVTPSGDLV TATPTRHTDL FWALRGAGGA YGVVTAMTFD LIPAAVVRAG ALWFDVGDAP
     AVVHRWRELV TDLPDAVSTS VVRLNLPPLP DLPAPLRGRA VVAVRYVRHG DLDAPDPLVD
     ALRTTAAPVL DTVGDLPYSA LGAVHADPED PMPLLDRGVA LRELPAEAVD AFLAATPADS
     PVVLAELRLL GGAVARPPAV PSAVAGRDAA YTLFVGALGW PAGPPDAAEH LQRVVDALAP
     WSTGGSLLNF AGPRDAASAR QVRTAFGPAA YDRLVTLRRR LDPHGVLDPT SRWAVVSDRV
     G
//
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