ID C0ZPG2_RHOE4 Unreviewed; 485 AA.
AC C0ZPG2;
DT 26-MAY-2009, integrated into UniProtKB/TrEMBL.
DT 26-MAY-2009, sequence version 1.
DT 27-MAR-2024, entry version 71.
DE RecName: Full=FAD-dependent oxidoreductase 2 FAD binding domain-containing protein {ECO:0000259|Pfam:PF00890};
GN OrderedLocusNames=RER_49500 {ECO:0000313|EMBL:BAH35658.1};
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:BAH35658.1, 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:BAH35658.1, 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};
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DR EMBL; AP008957; BAH35658.1; -; Genomic_DNA.
DR RefSeq; WP_020909035.1; NC_012490.1.
DR AlphaFoldDB; C0ZPG2; -.
DR GeneID; 57485184; -.
DR KEGG; rer:RER_49500; -.
DR PATRIC; fig|234621.6.peg.5510; -.
DR eggNOG; COG1053; Bacteria.
DR HOGENOM; CLU_011398_4_6_11; -.
DR Proteomes; UP000002204; Chromosome.
DR GO; GO:0033765; F:steroid dehydrogenase activity, acting on the CH-CH group of donors; IEA:UniProt.
DR GO; GO:0008152; P:metabolic process; IEA:UniProt.
DR Gene3D; 3.50.50.60; FAD/NAD(P)-binding domain; 1.
DR Gene3D; 3.90.700.10; Succinate dehydrogenase/fumarate reductase flavoprotein, catalytic domain; 1.
DR InterPro; IPR003953; FAD-binding_2.
DR InterPro; IPR036188; FAD/NAD-bd_sf.
DR InterPro; IPR027477; Succ_DH/fumarate_Rdtase_cat_sf.
DR PANTHER; PTHR43400:SF7; FAD_BINDING_2 DOMAIN-CONTAINING PROTEIN; 1.
DR PANTHER; PTHR43400; FUMARATE REDUCTASE; 1.
DR Pfam; PF00890; FAD_binding_2; 1.
DR PRINTS; PR00368; FADPNR.
DR SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 1.
DR SUPFAM; SSF56425; Succinate dehydrogenase/fumarate reductase flavoprotein, catalytic domain; 1.
PE 4: Predicted;
KW Flavoprotein {ECO:0000256|ARBA:ARBA00022630};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002}.
FT DOMAIN 6..452
FT /note="FAD-dependent oxidoreductase 2 FAD binding"
FT /evidence="ECO:0000259|Pfam:PF00890"
SQ SEQUENCE 485 AA; 51007 MW; FA83C98403B59C3F CRC64;
MTEHWDVVVI GGGGAGLAAA VSAAEEGASV LLFESETELG GSTALSAGIF TAAGTSVQAG
LGVDDSAEKF FQHYMDLNQW MLSPGLIRAF CENAGPTLEW LIGLGVEIPA AISGNAHQPG
LAQAGVEDVW RGHVPKDQGY GLIQVLDKAR RKHGIEVIFG TRVQKLIEED GRVVGVVADD
IEVHAGAVVV ASGGFAQDPG LVARHFPDAN KAGDALFVVA AEGSRGDHLR FAENLGASVA
GDGWGLMLPT VYFQRFHHWQ AGFPPKSRIY VNQDGRRFMD EDSSYAVSTG IIDHQGGYGW
MIFDENARVN LAPGYADWNP ERIEEEVAAG GTIRADTIED LAVATGVPVA TLTQTLRRWN
DQLPSGHDDD FLRHRTLRNK GAVGNPDPIA TAPFYAAKIL PAELVCTHAG MEINTDAAVL
GSTGVPIEGL YAAGEAGAGI LGLRYVGGGN AVANALTMGR VAGRNAANYT RTSAESAPVH
SIAHS
//
