ID C0ZWC4_RHOE4 Unreviewed; 462 AA.
AC C0ZWC4;
DT 26-MAY-2009, integrated into UniProtKB/TrEMBL.
DT 26-MAY-2009, sequence version 1.
DT 27-MAR-2024, entry version 75.
DE SubName: Full=Putative oxidoreductase {ECO:0000313|EMBL:BAH32659.1};
GN OrderedLocusNames=RER_19510 {ECO:0000313|EMBL:BAH32659.1};
OS Rhodococcus erythropolis (strain PR4 / NBRC 100887).
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Nocardiaceae;
OC Rhodococcus; Rhodococcus erythropolis group.
OX NCBI_TaxID=234621 {ECO:0000313|EMBL:BAH32659.1, ECO:0000313|Proteomes:UP000002204};
RN [1] {ECO:0000313|Proteomes:UP000002204}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PR4 / NBRC 100887 {ECO:0000313|Proteomes:UP000002204};
RA Takarada H., Sekine M., Hosoyama A., Yamada R., Fujisawa T., Omata S.,
RA Shimizu A., Tsukatani N., Tanikawa S., Fujita N., Harayama S.;
RT "Comparison of the complete genome sequences of Rhodococcus erythropolis
RT PR4 and Rhodococcus opacus B4.";
RL Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:BAH32659.1, ECO:0000313|Proteomes:UP000002204}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PR4 / NBRC 100887 {ECO:0000313|Proteomes:UP000002204};
RX PubMed=16423019; DOI=10.1111/j.1462-2920.2005.00899.x;
RA Sekine M., Tanikawa S., Omata S., Saito M., Fujisawa T., Tsukatani N.,
RA Tajima T., Sekigawa T., Kosugi H., Matsuo Y., Nishiko R., Imamura K.,
RA Ito M., Narita H., Tago S., Fujita N., Harayama S.;
RT "Sequence analysis of three plasmids harboured in Rhodococcus erythropolis
RT strain PR4.";
RL Environ. Microbiol. 8:334-346(2006).
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; AP008957; BAH32659.1; -; Genomic_DNA.
DR RefSeq; WP_020906947.1; NC_012490.1.
DR AlphaFoldDB; C0ZWC4; -.
DR KEGG; rer:RER_19510; -.
DR PATRIC; fig|234621.6.peg.2448; -.
DR eggNOG; COG0277; Bacteria.
DR HOGENOM; CLU_018354_10_0_11; -.
DR Proteomes; UP000002204; Chromosome.
DR GO; GO:0071949; F:FAD binding; IEA:InterPro.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:InterPro.
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; 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 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; PF08031; BBE; 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;
FT DOMAIN 36..206
FT /note="FAD-binding PCMH-type"
FT /evidence="ECO:0000259|PROSITE:PS51387"
SQ SEQUENCE 462 AA; 49034 MW; 040E08ED2551B580 CRC64;
MTTVEFAPLK STITGSVFGP RDPEYDDARS IWNGQIDHRP AVIARCRSAS DVAVALAFAR
AHSLEVSVRG GGHSYRGTSV CEGGVMIDLS AINVVSVAPS AKRARVGGGA TIADLDKATQ
EHGLAVTGGV ISDTGVGGLT LGGGMGWLTR TLGLAIDNLV SAEVVLADGS IVRASENDHS
DLFWALRGGG GNFGVVTEFE YRLSEIGPEV HLGLFFWGME DGPAALRLCR EVVPALPRNA
GAMVAVSLSA PPAPFVPDQF HLLPGYALLV AGFGSEEEHS NAIAPIREGL PTLFEFVTPI
PYVGLQSMLD ESEPWGAYAY EKALDLVDFS DDVIDVLTEQ AGKKSSPMSF MPIFPLQGAF
TSVGGDDTAF GGSRTPHYVC NMTATATDAG TLELDRSWVR ETWEALRPFS SNQGGYVNFM
TDVDEDRVRA SYGAGKYARL SAVKAKYDPD NVFHLNANIL PA
//
