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FOLD_STRA5
ID   FOLD_STRA5              Reviewed;         284 AA.
AC   Q8E168;
DT   12-DEC-2006, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2003, sequence version 1.
DT   03-AUG-2022, entry version 101.
DE   RecName: Full=Bifunctional protein FolD {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=folD {ECO:0000255|HAMAP-Rule:MF_01576}; OrderedLocusNames=SAG0494;
OS   Streptococcus agalactiae serotype V (strain ATCC BAA-611 / 2603 V/R).
OC   Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC   Streptococcus.
OX   NCBI_TaxID=208435;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-611 / 2603 V/R;
RX   PubMed=12200547; DOI=10.1073/pnas.182380799;
RA   Tettelin H., Masignani V., Cieslewicz M.J., Eisen J.A., Peterson S.N.,
RA   Wessels M.R., Paulsen I.T., Nelson K.E., Margarit I., Read T.D.,
RA   Madoff L.C., Wolf A.M., Beanan M.J., Brinkac L.M., Daugherty S.C.,
RA   DeBoy R.T., Durkin A.S., Kolonay J.F., Madupu R., Lewis M.R., Radune D.,
RA   Fedorova N.B., Scanlan D., Khouri H.M., Mulligan S., Carty H.A.,
RA   Cline R.T., Van Aken S.E., Gill J., Scarselli M., Mora M., Iacobini E.T.,
RA   Brettoni C., Galli G., Mariani M., Vegni F., Maione D., Rinaudo D.,
RA   Rappuoli R., Telford J.L., Kasper D.L., Grandi G., Fraser C.M.;
RT   "Complete genome sequence and comparative genomic analysis of an emerging
RT   human pathogen, serotype V Streptococcus agalactiae.";
RL   Proc. Natl. Acad. Sci. U.S.A. 99:12391-12396(2002).
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(+) = 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:0000255|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; 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; AE009948; AAM99396.1; -; Genomic_DNA.
DR   RefSeq; NP_687524.1; NC_004116.1.
DR   RefSeq; WP_000137498.1; NC_004116.1.
DR   AlphaFoldDB; Q8E168; -.
DR   SMR; Q8E168; -.
DR   STRING; 208435.SAG0494; -.
DR   EnsemblBacteria; AAM99396; AAM99396; SAG0494.
DR   GeneID; 66885476; -.
DR   KEGG; sag:SAG0494; -.
DR   PATRIC; fig|208435.3.peg.491; -.
DR   HOGENOM; CLU_034045_2_1_9; -.
DR   OMA; HIVGRPM; -.
DR   UniPathway; UPA00193; -.
DR   Proteomes; UP000000821; Chromosome.
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; IPR046346; Aminiacid_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   Pfam; PF00763; THF_DHG_CYH; 1.
DR   Pfam; PF02882; THF_DHG_CYH_C; 1.
DR   PRINTS; PR00085; THFDHDRGNASE.
DR   SUPFAM; SSF51735; SSF51735; 1.
DR   SUPFAM; SSF53223; SSF53223; 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; Histidine biosynthesis; Hydrolase;
KW   Methionine biosynthesis; Multifunctional enzyme; NADP;
KW   One-carbon metabolism; Oxidoreductase; Purine biosynthesis;
KW   Reference proteome.
FT   CHAIN           1..284
FT                   /note="Bifunctional protein FolD"
FT                   /id="PRO_0000268510"
FT   BINDING         165..167
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01576"
FT   BINDING         190
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01576"
SQ   SEQUENCE   284 AA;  31252 MW;  D832D6D802F6BE6A CRC64;
     MTELIDGKAL SQKMQAELGR KVERLKEQHG IIPGLAVILV GDNPASQVYV RNKERSALEA
     GFKSETLRLS ESISQEELID IIHQYNEDKS IHGILVQLPL PQHINDKKII LAIDPKKDVD
     GFHPMNTGHL WSGRPMMVPC TPAGIMEMFR EYHVDLEGKH AVIIGRSNIV GKPMAQLLLD
     KNATVTLTHS RTRNLSEVTK EADILIVAIG QGHFVTKDFV KEGAVVIDVG MNRDENGKLI
     GDVVFEQVAE VASMITPVPG GVGPMTITML LEQTYQAALR SVSL
 
 
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