ID A0A0G0NGX4_9BACT Unreviewed; 161 AA.
AC A0A0G0NGX4;
DT 22-JUL-2015, integrated into UniProtKB/TrEMBL.
DT 22-JUL-2015, sequence version 1.
DT 27-MAR-2024, entry version 19.
DE SubName: Full=Bifunctional deaminase-reductase domain protein {ECO:0000313|EMBL:KKQ85119.1};
GN ORFNames=UT08_C0010G0046 {ECO:0000313|EMBL:KKQ85119.1};
OS Candidatus Woesebacteria bacterium GW2011_GWB1_38_8.
OC Bacteria; Candidatus Woesebacteria.
OX NCBI_TaxID=1618570 {ECO:0000313|EMBL:KKQ85119.1, ECO:0000313|Proteomes:UP000034081};
RN [1] {ECO:0000313|EMBL:KKQ85119.1, ECO:0000313|Proteomes:UP000034081}
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 -!- PATHWAY: Cofactor biosynthesis; riboflavin biosynthesis.
CC {ECO:0000256|ARBA:ARBA00005104}.
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:KKQ85119.1}.
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DR EMBL; LBVL01000010; KKQ85119.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0G0NGX4; -.
DR STRING; 1618570.UT08_C0010G0046; -.
DR Proteomes; UP000034081; Unassembled WGS sequence.
DR GO; GO:0008703; F:5-amino-6-(5-phosphoribosylamino)uracil reductase activity; IEA:InterPro.
DR GO; GO:0004146; F:dihydrofolate reductase activity; IEA:InterPro.
DR GO; GO:0009231; P:riboflavin biosynthetic process; IEA:InterPro.
DR GO; GO:0046654; P:tetrahydrofolate biosynthetic process; IEA:InterPro.
DR Gene3D; 3.40.430.10; Dihydrofolate Reductase, subunit A; 1.
DR InterPro; IPR024072; DHFR-like_dom_sf.
DR InterPro; IPR001796; DHFR_dom.
DR InterPro; IPR002734; RibDG_C.
DR PANTHER; PTHR38011:SF7; 2,5-DIAMINO-6-RIBOSYLAMINO-4(3H)-PYRIMIDINONE 5'-PHOSPHATE REDUCTASE; 1.
DR PANTHER; PTHR38011; DIHYDROFOLATE REDUCTASE FAMILY PROTEIN (AFU_ORTHOLOGUE AFUA_8G06820); 1.
DR Pfam; PF01872; RibD_C; 1.
DR SUPFAM; SSF53597; Dihydrofolate reductase-like; 1.
DR PROSITE; PS51330; DHFR_2; 1.
PE 4: Predicted;
FT DOMAIN 1..161
FT /note="DHFR"
FT /evidence="ECO:0000259|PROSITE:PS51330"
SQ SEQUENCE 161 AA; 18160 MW; 31BC745F597BED6C CRC64;
MDGKIARGVD DPIDWTSKED KKFFAKESKK AGVILMGRKT HAAIGRVLPD RLNIVFTKNP
KKYNSYNYKG NLEFTNKSPE IVLKDLKKRG FKLVILIGGS TLNAEFLKRG LIDEIWITIE
GIIFGEGIPL FAKGKFKVLT ELISCDKLGT SGVLFKYKLK Y
//
