ID A0A0G1TSQ6_9BACT Unreviewed; 205 AA.
AC A0A0G1TSQ6;
DT 22-JUL-2015, integrated into UniProtKB/TrEMBL.
DT 22-JUL-2015, sequence version 1.
DT 24-JAN-2024, entry version 25.
DE SubName: Full=Putative oxidoreductase FAD/NAD(P)-binding component {ECO:0000313|EMBL:KKU84799.1};
GN ORFNames=UY11_C0003G0010 {ECO:0000313|EMBL:KKU84799.1};
OS Candidatus Amesbacteria bacterium GW2011_GWC2_47_8.
OC Bacteria; Candidatus Amesbacteria.
OX NCBI_TaxID=1618367 {ECO:0000313|EMBL:KKU84799.1, ECO:0000313|Proteomes:UP000034265};
RN [1] {ECO:0000313|EMBL:KKU84799.1, ECO:0000313|Proteomes:UP000034265}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Brown C.T., Hug L.A., Thomas B.C., Sharon I., Castelle C.J., Singh A.,
RA Wilkins M.J., Williams K.H., Banfield J.F.;
RT "rRNA introns, odd ribosomes, and small enigmatic genomes across a large
RT radiation of phyla.";
RL Nature 0:0-0(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:KKU84799.1}.
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DR EMBL; LCOT01000003; KKU84799.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0G1TSQ6; -.
DR PATRIC; fig|1618367.3.peg.73; -.
DR Proteomes; UP000034265; Unassembled WGS sequence.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:InterPro.
DR CDD; cd00322; FNR_like; 1.
DR Gene3D; 3.40.50.80; Nucleotide-binding domain of ferredoxin-NADP reductase (FNR) module; 1.
DR Gene3D; 2.40.30.10; Translation factors; 1.
DR InterPro; IPR008333; Cbr1-like_FAD-bd_dom.
DR InterPro; IPR017927; FAD-bd_FR_type.
DR InterPro; IPR039261; FNR_nucleotide-bd.
DR InterPro; IPR001433; OxRdtase_FAD/NAD-bd.
DR InterPro; IPR017938; Riboflavin_synthase-like_b-brl.
DR PANTHER; PTHR47354; NADH OXIDOREDUCTASE HCR; 1.
DR PANTHER; PTHR47354:SF6; NADH OXIDOREDUCTASE HCR; 1.
DR Pfam; PF00970; FAD_binding_6; 1.
DR Pfam; PF00175; NAD_binding_1; 1.
DR PRINTS; PR00410; PHEHYDRXLASE.
DR SUPFAM; SSF52343; Ferredoxin reductase-like, C-terminal NADP-linked domain; 1.
DR SUPFAM; SSF63380; Riboflavin synthase domain-like; 1.
DR PROSITE; PS51384; FAD_FR; 1.
PE 4: Predicted;
FT DOMAIN 1..92
FT /note="FAD-binding FR-type"
FT /evidence="ECO:0000259|PROSITE:PS51384"
SQ SEQUENCE 205 AA; 23683 MW; 99C574D528D586CE CRC64;
MTAKIIEIID EAKDIRSFRL QAKMDYLPGQ WFYIKLDENL KHHFTISSSP TEDFLQFTTK
FREESDYKKA LWQRKIGDEL EINGPFGNFV LDEKDTTPRL FIAGGIGITP FRSMIKYVSD
KQLTLPIKLL YSVKSKAEAA FAAELSDLRI VETEKEGRLD KEKIEKYCLD WKERSWWVCG
PPAMVEATTS FAPTGKVTSE EFIGY
//
