ID A0A0G0TKJ2_9BACT Unreviewed; 276 AA.
AC A0A0G0TKJ2;
DT 22-JUL-2015, integrated into UniProtKB/TrEMBL.
DT 22-JUL-2015, sequence version 1.
DT 27-MAR-2024, entry version 27.
DE SubName: Full=Bifunctional protein FolD {ECO:0000313|EMBL:KKR77524.1};
GN ORFNames=UU22_C0042G0003 {ECO:0000313|EMBL:KKR77524.1};
OS Parcubacteria group bacterium GW2011_GWA2_40_8.
OC Bacteria.
OX NCBI_TaxID=1618818 {ECO:0000313|EMBL:KKR77524.1, ECO:0000313|Proteomes:UP000033911};
RN [1] {ECO:0000313|EMBL:KKR77524.1, ECO:0000313|Proteomes:UP000033911}
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: One-carbon metabolism; tetrahydrofolate interconversion.
CC {ECO:0000256|ARBA:ARBA00004777}.
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:KKR77524.1}.
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DR EMBL; LBZU01000042; KKR77524.1; -; Genomic_DNA.
DR Proteomes; UP000033911; Unassembled WGS sequence.
DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR GO; GO:0004488; F:methylenetetrahydrofolate dehydrogenase (NADP+) activity; IEA:InterPro.
DR GO; GO:0009086; P:methionine biosynthetic process; IEA:UniProtKB-KW.
DR GO; GO:0006730; P:one-carbon metabolic process; IEA:UniProtKB-KW.
DR GO; GO:0006164; P:purine nucleotide biosynthetic process; IEA:UniProtKB-KW.
DR CDD; cd01080; NAD_bind_m-THF_DH_Cyclohyd; 1.
DR Gene3D; 3.40.50.10860; Leucine Dehydrogenase, chain A, domain 1; 1.
DR Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR InterPro; IPR046346; Aminoacid_DH-like_N_sf.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR InterPro; IPR000672; THF_DH/CycHdrlase.
DR InterPro; IPR020630; THF_DH/CycHdrlase_cat_dom.
DR InterPro; IPR020631; THF_DH/CycHdrlase_NAD-bd_dom.
DR PANTHER; PTHR48099:SF5; C-1-TETRAHYDROFOLATE SYNTHASE, CYTOPLASMIC; 1.
DR PANTHER; PTHR48099; C-1-TETRAHYDROFOLATE SYNTHASE, CYTOPLASMIC-RELATED; 1.
DR Pfam; PF00763; THF_DHG_CYH; 1.
DR Pfam; PF02882; THF_DHG_CYH_C; 1.
DR PRINTS; PR00085; THFDHDRGNASE.
DR SUPFAM; SSF53223; Aminoacid dehydrogenase-like, N-terminal domain; 1.
DR SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
PE 4: Predicted;
KW Amino-acid biosynthesis {ECO:0000256|ARBA:ARBA00023167};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Methionine biosynthesis {ECO:0000256|ARBA:ARBA00023167};
KW Multifunctional enzyme {ECO:0000256|ARBA:ARBA00023268};
KW NADP {ECO:0000256|ARBA:ARBA00022857};
KW One-carbon metabolism {ECO:0000256|ARBA:ARBA00022563};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Purine biosynthesis {ECO:0000256|ARBA:ARBA00022755}.
FT DOMAIN 21..98
FT /note="Tetrahydrofolate dehydrogenase/cyclohydrolase
FT catalytic"
FT /evidence="ECO:0000259|Pfam:PF00763"
FT DOMAIN 121..265
FT /note="Tetrahydrofolate dehydrogenase/cyclohydrolase
FT NAD(P)-binding"
FT /evidence="ECO:0000259|Pfam:PF02882"
SQ SEQUENCE 276 AA; 29827 MW; 5E38F3AFE64A896D CRC64;
MTIILDGKXX XXXXXXXXXX XSEAFVRNKQ AVAARVGMGC RVFKYPNSIS VKDLSVNLNG
IVRGEKYDGV IIQLPLPGLL DRSRYSLLRI IPEDRDADCL SEKWQGRLLT GRNFVEQKGK
KVELLPPVAS AIFKLADKYN ISFENKNIVL VGWGDLVGKP LLPLLVRKGA TVTVCTSKTK
DISVFTKNAD IVISGVGKAH IIIGSMLKRG AIVFDAGYTE IDGKTTGDID TDSVGGVVEM
LSPSPGGIGP LTVACLLENV VALSELRQNV NSKRSL
//
