ID   FOLD1_MYXXD             Reviewed;         292 AA.
AC   Q1DA76;
DT   12-DEC-2006, integrated into UniProtKB/Swiss-Prot.
DT   11-JUL-2006, sequence version 1.
DT   02-SEP-2026, entry version 118.
DE   RecName: Full=Bifunctional protein FolD 1 {ECO:0000255|HAMAP-Rule:MF_01576};
DE   Includes:
DE     RecName: Full=Methylenetetrahydrofolate dehydrogenase {ECO:0000255|HAMAP-Rule:MF_01576};
DE              EC=1.5.1.5 {ECO:0000255|HAMAP-Rule:MF_01576};
DE   Includes:
DE     RecName: Full=Methenyltetrahydrofolate cyclohydrolase {ECO:0000255|HAMAP-Rule:MF_01576};
DE              EC=3.5.4.9 {ECO:0000255|HAMAP-Rule:MF_01576};
GN   Name=folD1 {ECO:0000255|HAMAP-Rule:MF_01576};
GN   OrderedLocusNames=MXAN_2226;
OS   Myxococcus xanthus (strain DK1622).
OC   Bacteria; Pseudomonadati; Myxococcota; Myxococcia; Myxococcales;
OC   Cystobacterineae; Myxococcaceae; Myxococcus.
OX   NCBI_TaxID=246197;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DK1622;
RX   PubMed=17015832; DOI=10.1073/pnas.0607335103;
RA   Goldman B.S., Nierman W.C., Kaiser D., Slater S.C., Durkin A.S.,
RA   Eisen J.A., Ronning C.M., Barbazuk W.B., Blanchard M., Field C.,
RA   Halling C., Hinkle G., Iartchuk O., Kim H.S., Mackenzie C., Madupu R.,
RA   Miller N., Shvartsbeyn A., Sullivan S.A., Vaudin M., Wiegand R.,
RA   Kaplan H.B.;
RT   "Evolution of sensory complexity recorded in a myxobacterial genome.";
RL   Proc. Natl. Acad. Sci. U.S.A. 103:15200-15205(2006).
CC   -!- FUNCTION: Catalyzes the oxidation of 5,10-methylenetetrahydrofolate to
CC       5,10-methenyltetrahydrofolate and then the hydrolysis of 5,10-
CC       methenyltetrahydrofolate to 10-formyltetrahydrofolate.
CC       {ECO:0000255|HAMAP-Rule:MF_01576}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(6R)-5,10-methylene-5,6,7,8-tetrahydrofolate + NADP(+) = (6R)-
CC         5,10-methenyltetrahydrofolate + NADPH; Xref=Rhea:RHEA:22812,
CC         ChEBI:CHEBI:15636, ChEBI:CHEBI:57455, ChEBI:CHEBI:57783,
CC         ChEBI:CHEBI:58349; EC=1.5.1.5; Evidence={ECO:0000255|HAMAP-
CC         Rule:MF_01576};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(6R)-5,10-methenyltetrahydrofolate + H2O = (6R)-10-
CC         formyltetrahydrofolate + H(+); Xref=Rhea:RHEA:23700,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:57455,
CC         ChEBI:CHEBI:195366; EC=3.5.4.9; Evidence={ECO:0000255|HAMAP-
CC         Rule:MF_01576};
CC   -!- PATHWAY: One-carbon metabolism; tetrahydrofolate interconversion.
CC       {ECO:0000255|HAMAP-Rule:MF_01576}.
CC   -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_01576}.
CC   -!- SIMILARITY: Belongs to the tetrahydrofolate
CC       dehydrogenase/cyclohydrolase family. {ECO:0000255|HAMAP-Rule:MF_01576}.
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DR   EMBL; CP000113; ABF89655.1; -; Genomic_DNA.
DR   RefSeq; WP_011552302.1; NC_008095.1.
DR   AlphaFoldDB; Q1DA76; -.
DR   SMR; Q1DA76; -.
DR   STRING; 246197.MXAN_2226; -.
DR   EnsemblBacteria; ABF89655; ABF89655; MXAN_2226.
DR   GeneID; 41359614; -.
DR   KEGG; mxa:MXAN_2226; -.
DR   eggNOG; COG0190; Bacteria.
DR   HOGENOM; CLU_034045_2_1_7; -.
DR   OrthoDB; 9803580at2; -.
DR   UniPathway; UPA00193; -.
DR   Proteomes; UP000002402; Chromosome.
DR   GO; GO:0005829; C:cytosol; IEA:TreeGrafter.
DR   GO; GO:0004477; F:methenyltetrahydrofolate cyclohydrolase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0004488; F:methylenetetrahydrofolate dehydrogenase (NADP+) activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0035999; P:tetrahydrofolate interconversion; IEA:UniProtKB-UniRule.
DR   CDD; cd01080; NAD_bind_m-THF_DH_Cyclohyd; 1.
DR   FunFam; 3.40.50.720:FF:000189; Bifunctional protein FolD; 1.
DR   FunFam; 3.40.50.10860:FF:000005; C-1-tetrahydrofolate synthase, cytoplasmic, putative; 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   HAMAP; MF_01576; THF_DHG_CYH; 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; IPR020867; THF_DH/CycHdrlase_CS.
DR   InterPro; IPR020631; THF_DH/CycHdrlase_NAD-bd_dom.
DR   NCBIfam; NF010783; PRK14186.1; 1.
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.
DR   PROSITE; PS00767; THF_DHG_CYH_2; 1.
PE   3: Inferred from homology;
KW   Amino-acid biosynthesis; Histidine biosynthesis; Hydrolase;
KW   Methionine biosynthesis; Multifunctional enzyme; NADP;
KW   One-carbon metabolism; Oxidoreductase; Purine biosynthesis;
KW   Reference proteome.
FT   CHAIN           1..292
FT                   /note="Bifunctional protein FolD 1"
FT                   /id="PRO_0000268412"
FT   BINDING         165..167
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01576"
SQ   SEQUENCE   292 AA;  30827 MW;  2DDFC511C5298FB8 CRC64;
     MARTLDGTEI SRVMRAEMAQ DVAALQAAGV TPGLSVVLVG NNPASQAYVA SKTRACESLG
     MRGQTLTLPE DVSKEALFAV IDRLNADPSV HGILVQLPLP AHLPYKAVLE HIHPAKDVDG
     FHPVNAGLAF VGDPRAFVPC TPAGIMEMLR REDIPTRGKH VVIVGRSLIV SKPLASLLMA
     PGPDATVTIT HRHTPDLASF TRQADILIVA VGKQNLITAD MVKPGVVVID VGQNRVSDAS
     SPRGYRMVGD VDFDAIQPIA SAITPVPGGV GPMTITMLLA NTLQAARQTQ AR
//