ID U5RTJ0_9CLOT Unreviewed; 431 AA.
AC U5RTJ0;
DT 22-JAN-2014, integrated into UniProtKB/TrEMBL.
DT 22-JAN-2014, sequence version 1.
DT 24-JAN-2024, entry version 34.
DE SubName: Full=FAD-dependent oxidoreductase {ECO:0000313|EMBL:AGY76086.1};
GN ORFNames=CAETHG_1867 {ECO:0000313|EMBL:AGY76086.1};
OS Clostridium autoethanogenum DSM 10061.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC Clostridium.
OX NCBI_TaxID=1341692 {ECO:0000313|EMBL:AGY76086.1, ECO:0000313|Proteomes:UP000017590};
RN [1] {ECO:0000313|EMBL:AGY76086.1, ECO:0000313|Proteomes:UP000017590}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 10061 {ECO:0000313|EMBL:AGY76086.1};
RX PubMed=24655715; DOI=10.1186/1754-6834-7-40;
RA Brown S.D., Nagaraju S., Utturkar S., De Tissera S., Segovia S.,
RA Mitchell W., Land M.L., Dassanayake A., Kopke M.;
RT "Comparison of single-molecule sequencing and hybrid approaches for
RT finishing the genome of Clostridium autoethanogenum and analysis of CRISPR
RT systems in industrial relevant Clostridia.";
RL Biotechnol. Biofuels 7:40-40(2014).
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000256|ARBA:ARBA00001974};
CC -!- SIMILARITY: Belongs to the ETF-QO/FixC family.
CC {ECO:0000256|ARBA:ARBA00006796}.
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DR EMBL; CP006763; AGY76086.1; -; Genomic_DNA.
DR RefSeq; WP_013240610.1; NZ_CP012395.1.
DR AlphaFoldDB; U5RTJ0; -.
DR KEGG; cah:CAETHG_1867; -.
DR PATRIC; fig|1341692.11.peg.1887; -.
DR HOGENOM; CLU_050977_0_0_9; -.
DR Proteomes; UP000017590; Chromosome.
DR GO; GO:0004174; F:electron-transferring-flavoprotein dehydrogenase activity; IEA:UniProtKB-EC.
DR Gene3D; 3.50.50.60; FAD/NAD(P)-binding domain; 1.
DR InterPro; IPR036188; FAD/NAD-bd_sf.
DR InterPro; IPR039651; FixC-like.
DR PANTHER; PTHR43624; ELECTRON TRANSFER FLAVOPROTEIN-QUINONE OXIDOREDUCTASE YDIS-RELATED; 1.
DR PANTHER; PTHR43624:SF2; ELECTRON TRANSFER FLAVOPROTEIN-QUINONE OXIDOREDUCTASE YDIS-RELATED; 1.
DR Pfam; PF12831; FAD_oxidored; 1.
DR PRINTS; PR00420; RNGMNOXGNASE.
DR SUPFAM; SSF54373; FAD-linked reductases, C-terminal domain; 1.
DR SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 1.
PE 3: Inferred from homology;
SQ SEQUENCE 431 AA; 47880 MW; 4F74E3AF37B449D3 CRC64;
MAEKFDVIVV GAGVSGLAAT YVMAKEGLKV IVIEKGKYPG SKNVMGGVLY RHMMDEIIPE
FWKEAPLERP IVEQNFWLLG KESAAKTGYR GMEWSKPPYN NFTVFRGKFD QWLSKKCIEA
GALIVNETVV KECIVENNKV VGVRTDRPDG DIYADVVVLA DGVNSLLAKN LGFHKEWRKD
QVALAVMEEL KLPSDKIEDR FNLDKGMGAT VEMFGDGTLG MVGTAFIYTN NEHISIGCGA
LLSQMSERNV KPYELLEYIK QHPVIKPLIA GGEASEYYAH LIPEGGYNSI PKLVGDGVLV
IGDAAQLVNG IHREGSNLGM TSGRFAAETI IQAKKLGKFN EQTLSHYQEL LKESYVMKDL
KKYKNASTTM EENPKFFNHY IPAANKVMSE MFTVDGVSKR DKQKLAIKHM AGGKSILSMG
MDGFKIWRAM K
//
