ID A0A1J4RMU8_9BACT Unreviewed; 245 AA.
AC A0A1J4RMU8;
DT 15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT 15-FEB-2017, sequence version 1.
DT 27-MAR-2024, entry version 21.
DE RecName: Full=Methenyltetrahydrofolate cyclohydrolase {ECO:0008006|Google:ProtNLM};
GN ORFNames=AUJ59_03490 {ECO:0000313|EMBL:OIN88729.1};
OS Candidatus Beckwithbacteria bacterium CG1_02_47_37.
OC Bacteria; Candidatus Beckwithbacteria.
OX NCBI_TaxID=1805034 {ECO:0000313|EMBL:OIN88729.1, ECO:0000313|Proteomes:UP000183144};
RN [1] {ECO:0000313|EMBL:OIN88729.1, ECO:0000313|Proteomes:UP000183144}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CG1_02_47_37 {ECO:0000313|EMBL:OIN88729.1};
RX PubMed=27112493;
RA Probst A.J., Castelle C.J., Singh A., Brown C.T., Anantharaman K.,
RA Sharon I., Hug L.A., Burstein D., Emerson J.B., Thomas B.C., Banfield J.F.;
RT "Genomic resolution of a cold subsurface aquifer community provides
RT metabolic insights for novel microbes adapted to high CO concentrations.";
RL Environ. Microbiol. 0:0-0(2016).
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:OIN88729.1}.
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DR EMBL; MNUI01000060; OIN88729.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1J4RMU8; -.
DR STRING; 1805034.AUJ59_03490; -.
DR Proteomes; UP000183144; Unassembled WGS sequence.
DR GO; GO:0004488; F:methylenetetrahydrofolate dehydrogenase (NADP+) activity; IEA:InterPro.
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; 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 SUPFAM; SSF53223; Aminoacid dehydrogenase-like, N-terminal domain; 1.
DR SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
PE 4: Predicted;
FT DOMAIN 4..107
FT /note="Tetrahydrofolate dehydrogenase/cyclohydrolase
FT catalytic"
FT /evidence="ECO:0000259|Pfam:PF00763"
FT DOMAIN 112..242
FT /note="Tetrahydrofolate dehydrogenase/cyclohydrolase
FT NAD(P)-binding"
FT /evidence="ECO:0000259|Pfam:PF02882"
SQ SEQUENCE 245 AA; 26722 MW; B8EFD3520787BCAB CRC64;
MKIIDGAKIA RELEKKLTVK PGTSPCLGII VFADDKAGQV YSRLKSEAAA RVGINIVKSN
SDSVLDEWNR DKSIHGILIQ RPGWRGEAFE KYWQELVGKI APDKDVDGLR ADSKFVPATV
KAVEKILYKF KLDRAGKHIV VVGQGMIGRQ LAARFEVQEL SSKDKNLQEK VKEADVLITA
CGRQGLIKAV KPGAIVIDLG WPKGDVDFAA VKNIAGWITP VPGGVGPVTV ICLLENLVEA
VYNRL
//
