ID A0A1H9RAX5_9SPHN Unreviewed; 469 AA.
AC A0A1H9RAX5;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 27-MAR-2024, entry version 23.
DE SubName: Full=Fumarate reductase flavoprotein subunit {ECO:0000313|EMBL:SER69896.1};
GN ORFNames=SAMN05518866_11661 {ECO:0000313|EMBL:SER69896.1};
OS Sphingobium sp. YR768.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC Sphingomonadaceae; Sphingobium.
OX NCBI_TaxID=1884365 {ECO:0000313|EMBL:SER69896.1, ECO:0000313|Proteomes:UP000199142};
RN [1] {ECO:0000313|Proteomes:UP000199142}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=YR768 {ECO:0000313|Proteomes:UP000199142};
RA Varghese N., Submissions S.;
RL Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000256|ARBA:ARBA00001974};
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DR EMBL; FOGE01000016; SER69896.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1H9RAX5; -.
DR STRING; 1884365.SAMN05518866_11661; -.
DR Proteomes; UP000199142; Unassembled WGS sequence.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR GO; GO:0008202; P:steroid 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 PRINTS; PR00411; PNDRDTASEI.
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:UP000199142}.
FT DOMAIN 6..445
FT /note="FAD-dependent oxidoreductase 2 FAD binding"
FT /evidence="ECO:0000259|Pfam:PF00890"
SQ SEQUENCE 469 AA; 49458 MW; 4C142A222256D621 CRC64;
MSTDYDIIVV GGGGAGMTAA LFAQAAGASV MLLEADTKLG GATRLSGGVV YAAGTSVQQA
MGIADSPQAM YDYIMTLNGW QTRPDIIRLF AERSAASVEW LVSLGAEYEW VVKSGVDTVP
RGHCTVGAGD TIGRLLINEV GAKGIETALG TRVDRLLIED GRVVGVHASG MDLRAKAVII
TTGGFGNSPG MRARYFPSAA QHGDIVYSVH NDAPFILGDG IKLGEAIGAQ ITGHDTGLVL
PSAGLVPNSV EAFLPPWCML VNDEGRRFMP ENSPYAVSGY LINEQSGAHA WAIFDEKTLV
EGSADKRFSD PYHTGEVSQT WDEDLIRKHV ESGKIRTADT LEKLADMVGI NRLALAETVA
RYNEDAQDGV DSEWAKQAPK YFPIDAAPYF AVEVRASVIG QTSAGLDIDT KGRVRDRNGI
AIPGLYAAGE ILGCVQGNRY SGGGMGVGNA LTFGRLAGEE AAASLRVNA
//