ID A0A177HM86_9ACTN Unreviewed; 450 AA.
AC A0A177HM86;
DT 07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT 07-SEP-2016, sequence version 1.
DT 24-JAN-2024, entry version 24.
DE SubName: Full=Mitomycin radical oxidase {ECO:0000313|EMBL:OAH11729.1};
DE EC=1.5.3.- {ECO:0000313|EMBL:OAH11729.1};
GN Name=mcrA {ECO:0000313|EMBL:OAH11729.1};
GN ORFNames=STSP_48980 {ECO:0000313|EMBL:OAH11729.1};
OS Streptomyces jeddahensis.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=1716141 {ECO:0000313|EMBL:OAH11729.1, ECO:0000313|Proteomes:UP000077381};
RN [1] {ECO:0000313|EMBL:OAH11729.1, ECO:0000313|Proteomes:UP000077381}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=G25(2015) {ECO:0000313|Proteomes:UP000077381};
RA Poehlein A., Roettig A., Hiessl S., Hauschild P., Schauer J., Madkour M.H.,
RA Al-Ansari A.M., Almakishah N.H., Steinbuechel A., Daniel R.;
RT "Genome sequence of Streptomyces sp. G25.";
RL Submitted (DEC-2015) 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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:OAH11729.1}.
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DR EMBL; LOHS01000102; OAH11729.1; -; Genomic_DNA.
DR RefSeq; WP_067281898.1; NZ_LOHS01000102.1.
DR AlphaFoldDB; A0A177HM86; -.
DR STRING; 1716141.STSP_48980; -.
DR PATRIC; fig|1716141.3.peg.5141; -.
DR OrthoDB; 9775082at2; -.
DR Proteomes; UP000077381; Unassembled WGS sequence.
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:OAH11729.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000077381}.
FT DOMAIN 40..211
FT /note="FAD-binding PCMH-type"
FT /evidence="ECO:0000259|PROSITE:PS51387"
SQ SEQUENCE 450 AA; 46766 MW; B8B7E1ECBCB2873F CRC64;
MRTIDSSPPA SRLPLPDSLA AAAIRPGDGD YDNVRHTYTR TGSPAAVIRV RDHEDIAAAL
AHARTAQLPL TVRSGGHGIS GRSTNDGGIV VDLSALNAVK VLDARSGLVR VEAGARWGDV
AAQLAPHGLA LSSGDTGDVG VGGLATTGGI GLMSRLHGLT IDHMRAAELV LADGSPVRTD
ADHDPDLFWA VRGAGANFGV ATAFEFQAKP VGDVIAAVTV FDAGDTAAFL TRWGAAVEAA
PRTVTSFLTL MAGPGGKPVA QAMTVHAGAD REAAREALAP VVASGPVLQN QAFVTPYHQL
LPATHAAQHA QQPLAVSRSG LLEHLTEPAA AAIASLLVAA RAPMVQLRSV GGAVNDTPST
STAYAHRTQN FSLMAATLPA GRKNLDRHWE QLHPHLKGLY LSFETGTGPR QLQDAFPGAV
LDRLMVLKSR YDPDHVFDNN FALPSADLPG
//