ID A0A0Q8E732_9ACTN Unreviewed; 499 AA.
AC A0A0Q8E732;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 27.
DE RecName: Full=FAD-dependent oxidoreductase 2 FAD binding domain-containing protein {ECO:0000259|Pfam:PF00890};
GN ORFNames=ASD81_09370 {ECO:0000313|EMBL:KRA38789.1};
OS Nocardioides sp. Root614.
OC Bacteria; Actinomycetota; Actinomycetes; Propionibacteriales;
OC Nocardioidaceae; Nocardioides.
OX NCBI_TaxID=1736571 {ECO:0000313|EMBL:KRA38789.1, ECO:0000313|Proteomes:UP000051699};
RN [1] {ECO:0000313|EMBL:KRA38789.1, ECO:0000313|Proteomes:UP000051699}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Root614 {ECO:0000313|EMBL:KRA38789.1,
RC ECO:0000313|Proteomes:UP000051699};
RA Gilbert D.G.;
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KRA38789.1, ECO:0000313|Proteomes:UP000051699}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Root614 {ECO:0000313|EMBL:KRA38789.1,
RC ECO:0000313|Proteomes:UP000051699};
RA Schulze-Lefert P.;
RT "Functional overlap of the Arabidopsis leaf and root microbiotas.";
RL Submitted (NOV-2015) to the EMBL/GenBank/DDBJ databases.
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:KRA38789.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; LMGV01000001; KRA38789.1; -; Genomic_DNA.
DR RefSeq; WP_056709494.1; NZ_LMGV01000001.1.
DR AlphaFoldDB; A0A0Q8E732; -.
DR OrthoDB; 337830at2; -.
DR Proteomes; UP000051699; Unassembled WGS sequence.
DR GO; GO:0033765; F:steroid dehydrogenase activity, acting on the CH-CH group of donors; 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 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};
KW Reference proteome {ECO:0000313|Proteomes:UP000051699}.
FT DOMAIN 28..457
FT /note="FAD-dependent oxidoreductase 2 FAD binding"
FT /evidence="ECO:0000259|Pfam:PF00890"
SQ SEQUENCE 499 AA; 52787 MW; D1ED016B72CACCC1 CRC64;
MSASSPAGLT IPATVPADQL PDDTETFDVV VVGFGIAGGC AALEAARDGV RVLLLERAAV
HGGTSSMSGG HFYLGGGTAV QQATGHDDPV EEMVRYLMAS TKDPDEQKIR AYCEGSVAHF
DWLEALGFEF ERSFFPGKAV IQPGTQGLMY TGNEKVWPFR EDIAPAPRGH KVPVPGDTEG
TRIVMDLLRD QVEKAGVEVR YETGATNLVV DGDRVVGLAW KSFERTGLVR AGGVVVAAGG
FVNNQDMVDR YTPALKSVTF TLGSTYDDGL AIRLGESVGA ALENMEEPFI TAPFYPPSGL
VKGLIVNRDG QRFVAEDSYH ARTSYEVLRQ PGSVAYLIVD SAHFEEQRMG LAPLKDGFET
IEEMESGLGL PEGSLVATMA SYNKHAAVGE DPDLHKHPDW LAPQTEGPWA VLELSLGAAF
YSGFTLGGMA TTVDGEVRRP DGSVIRGLYA AGACASNIAQ DGAGYCSGTQ LGEGSFFGRR
AGAAAARARA RAGVSPAGR
//