ID   A0A7C9HDE9_9BACT        Unreviewed;       294 AA.
AC   A0A7C9HDE9;
DT   10-FEB-2021, integrated into UniProtKB/TrEMBL.
DT   10-FEB-2021, sequence version 1.
DT   02-JUN-2021, entry version 3.
DE   RecName: Full=Bifunctional protein FolD {ECO:0000256|HAMAP-Rule:MF_01576};
DE   Includes:
DE     RecName: Full=Methylenetetrahydrofolate dehydrogenase {ECO:0000256|HAMAP-Rule:MF_01576};
DE              EC=1.5.1.5 {ECO:0000256|HAMAP-Rule:MF_01576};
DE   Includes:
DE     RecName: Full=Methenyltetrahydrofolate cyclohydrolase {ECO:0000256|HAMAP-Rule:MF_01576};
DE              EC=3.5.4.9 {ECO:0000256|HAMAP-Rule:MF_01576};
GN   Name=folD {ECO:0000256|HAMAP-Rule:MF_01576,
GN   ECO:0000313|EMBL:MUL27383.1};
GN   ORFNames=F0475_03455 {ECO:0000313|EMBL:MUL27383.1};
OS   Prevotella sp. A2879.
OC   Bacteria; Bacteroidetes; Bacteroidia; Bacteroidales; Prevotellaceae;
OC   Prevotella; unclassified Prevotella.
OX   NCBI_TaxID=2608404 {ECO:0000313|EMBL:MUL27383.1, ECO:0000313|Proteomes:UP000482295};
RN   [1] {ECO:0000313|EMBL:MUL27383.1, ECO:0000313|Proteomes:UP000482295}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=A2879 {ECO:0000313|EMBL:MUL27383.1,
RC   ECO:0000313|Proteomes:UP000482295};
RA   Buhl M., Oberhettinger P.;
RT   "Prevotella A2879 sp. nov., isolated from an abscess of a patient.";
RL   Submitted (SEP-2019) to the EMBL/GenBank/DDBJ databases.
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:0000256|HAMAP-Rule:MF_01576}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(6R)-5,10-methylene-5,6,7,8-tetrahydrofolate + NADP(+) = 5,10-
CC         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:0000256|HAMAP-
CC         Rule:MF_01576};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=5,10-methenyltetrahydrofolate + H2O = (6S)-10-
CC         formyltetrahydrofolate + H(+); Xref=Rhea:RHEA:23700,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:57454,
CC         ChEBI:CHEBI:57455; EC=3.5.4.9;
CC         Evidence={ECO:0000256|ARBA:ARBA00001660, ECO:0000256|HAMAP-
CC         Rule:MF_01576};
CC   -!- PATHWAY: One-carbon metabolism; tetrahydrofolate interconversion.
CC       {ECO:0000256|HAMAP-Rule:MF_01576}.
CC   -!- SUBUNIT: Homodimer. {ECO:0000256|HAMAP-Rule:MF_01576}.
CC   -!- SIMILARITY: Belongs to the tetrahydrofolate
CC       dehydrogenase/cyclohydrolase family. {ECO:0000256|HAMAP-Rule:MF_01576}.
CC   -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC       feature annotation. {ECO:0000256|HAMAP-Rule:MF_01576}.
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:MUL27383.1}.
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DR   EMBL; VVIQ01000003; MUL27383.1; -; Genomic_DNA.
DR   UniPathway; UPA00193; -.
DR   Proteomes; UP000482295; Unassembled WGS sequence.
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:0000105; P:histidine biosynthetic process; IEA:UniProtKB-KW.
DR   GO; GO:0009086; P:methionine biosynthetic process; IEA:UniProtKB-KW.
DR   GO; GO:0006164; P:purine nucleotide biosynthetic process; IEA:UniProtKB-KW.
DR   GO; GO:0035999; P:tetrahydrofolate interconversion; IEA:UniProtKB-UniPathway.
DR   CDD; cd01080; NAD_bind_m-THF_DH_Cyclohyd; 1.
DR   HAMAP; MF_01576; THF_DHG_CYH; 1.
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   Pfam; PF00763; THF_DHG_CYH; 1.
DR   Pfam; PF02882; THF_DHG_CYH_C; 1.
DR   PRINTS; PR00085; THFDHDRGNASE.
DR   SUPFAM; SSF51735; SSF51735; 1.
DR   PROSITE; PS00766; THF_DHG_CYH_1; 1.
DR   PROSITE; PS00767; THF_DHG_CYH_2; 1.
PE   3: Inferred from homology;
KW   Amino-acid biosynthesis {ECO:0000256|HAMAP-Rule:MF_01576};
KW   Histidine biosynthesis {ECO:0000256|HAMAP-Rule:MF_01576};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|HAMAP-Rule:MF_01576};
KW   Methionine biosynthesis {ECO:0000256|ARBA:ARBA00023167, ECO:0000256|HAMAP-
KW   Rule:MF_01576};
KW   Multifunctional enzyme {ECO:0000256|ARBA:ARBA00023268, ECO:0000256|HAMAP-
KW   Rule:MF_01576};
KW   NADP {ECO:0000256|ARBA:ARBA00022857, ECO:0000256|HAMAP-Rule:MF_01576};
KW   One-carbon metabolism {ECO:0000256|ARBA:ARBA00022563, ECO:0000256|HAMAP-
KW   Rule:MF_01576}; Oxidoreductase {ECO:0000256|HAMAP-Rule:MF_01576};
KW   Purine biosynthesis {ECO:0000256|ARBA:ARBA00022755, ECO:0000256|HAMAP-
KW   Rule:MF_01576}.
FT   DOMAIN          5..121
FT                   /note="THF_DHG_CYH"
FT                   /evidence="ECO:0000259|Pfam:PF00763"
FT   DOMAIN          124..290
FT                   /note="THF_DHG_CYH_C"
FT                   /evidence="ECO:0000259|Pfam:PF02882"
FT   NP_BIND         166..168
FT                   /note="NADP"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01576"
FT   BINDING         194
FT                   /note="NADP"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01576"
FT   BINDING         235
FT                   /note="NADP; via amide nitrogen"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01576"
SQ   SEQUENCE   294 AA;  31959 MW;  2C56F169CFDE1F99 CRC64;
     MEYQLIDGKA TATAIKQQIA EEVKAITKAG GKQPHLVAIL VGHDGGSETY VKNKVIACEQ
     CGFKSTLIRY ETDVTEEELL TCVDKLNKDD DVDGFIVQLP LPKHIDEQKI IMAIDYRKDV
     DGFHPVNVGR MAIGLPCFIS ATPLGILTLL QHYHIPTSGK KCVILGRSNI VGKPMAQLMM
     QKQYGDATVT ICHSHSATLK KECQEADIII AAIGRPDFLT ADMVKPGAVV IDVGTTRVPD
     ATRKSGYRLN GDVKFDEVAP LCSFITPVPG GVGPMTICSL MKNTLAAGKK EYYK
//