ID A0A1E4I1R2_9PSEU Unreviewed; 542 AA.
AC A0A1E4I1R2;
DT 18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT 18-JAN-2017, sequence version 1.
DT 27-MAR-2024, entry version 22.
DE RecName: Full=FAD-dependent oxidoreductase 2 FAD binding domain-containing protein {ECO:0000259|Pfam:PF00890};
GN ORFNames=ABS81_15455 {ECO:0000313|EMBL:ODU03106.1};
OS Pseudonocardia sp. SCN 72-86.
OC Bacteria; Actinomycetota; Actinomycetes; Pseudonocardiales;
OC Pseudonocardiaceae; Pseudonocardia.
OX NCBI_TaxID=1660131 {ECO:0000313|EMBL:ODU03106.1, ECO:0000313|Proteomes:UP000094542};
RN [1] {ECO:0000313|EMBL:ODU03106.1, ECO:0000313|Proteomes:UP000094542}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=26031303; DOI=10.1111/1462-2920.12936;
RA Kantor R.S., van Zyl A.W., van Hille R.P., Thomas B.C., Harrison S.T.,
RA Banfield J.F.;
RT "Bioreactor microbial ecosystems for thiocyanate and cyanide degradation
RT unravelled with genome-resolved metagenomics.";
RL Environ. Microbiol. 17:4929-4941(2015).
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000256|ARBA:ARBA00001974};
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:ODU03106.1}.
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DR EMBL; MEFA01000088; ODU03106.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1E4I1R2; -.
DR Proteomes; UP000094542; Unassembled WGS sequence.
DR GO; GO:0033765; F:steroid dehydrogenase activity, acting on the CH-CH group of donors; IEA:UniProt.
DR GO; GO:0008202; P:steroid metabolic process; IEA:UniProt.
DR Gene3D; 3.50.50.60; FAD/NAD(P)-binding domain; 2.
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 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 3..515
FT /note="FAD-dependent oxidoreductase 2 FAD binding"
FT /evidence="ECO:0000259|Pfam:PF00890"
SQ SEQUENCE 542 AA; 56517 MW; 481605A4C77C0873 CRC64;
MADIVVVGAG IGGMSAAVTA ASRGLDVVLL EKGPRVGGAA AYSGGQVWVG GNHVAAREGI
ADSADDTLAY VAAAASRDEA SLDRHLAAQW IEGAAAAARF FEDAGVISWE VIPGYPDYYH
PDLPGSRAAG RYLTGAPFDG TRLGAERDRL LVSPHFPVGI TYAEMFEWGG MSSKTEWDWD
LVARRRSDDV LTFGTGIAAA FFRGVLDSRV DVRTEHEVVG LVSEGDRVVG VRVRGPQGEE
TILGQVVLTT GAHDWSEDLS AKFTGIPPED GGSVAPGTLS GDAIALVEPV GGAPDSLPAW
AAPVLPGYRL ENPAFDGDTG FRACYEHCLP HTFLVNERAE RFCDDSFHTR IVAAALADGD
RGGNLPFFMI WDSRHHQRYG LGATAPGGEY PPGLVQQAST LAGLADALGL PADSLEATAA
RFNTHAVDGT DPDFGRGTNL SVRRFRGDGK HQPNPNVGPV SEAPFFGMRM RLLNTGIAAA
GVRTGDNGAV LDGAGGVVDG LYAAGECSAR AAAGVGYNSG YSLSRAMAYG FLAANAIADA
RT
//
