ID   FOLD2_PSEMY             Reviewed;         303 AA.
AC   A4XXZ2;
DT   10-JUN-2008, integrated into UniProtKB/Swiss-Prot.
DT   29-MAY-2007, sequence version 1.
DT   16-JUN-2009, entry version 19.
DE   RecName: Full=Bifunctional protein folD 2;
DE   Includes:
DE     RecName: Full=Methylenetetrahydrofolate dehydrogenase;
DE              EC=1.5.1.5;
DE   Includes:
DE     RecName: Full=Methenyltetrahydrofolate cyclohydrolase;
DE              EC=3.5.4.9;
GN   Name=folD2; OrderedLocusNames=Pmen_3458;
OS   Pseudomonas mendocina (strain ymp).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=399739;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T.,
RA   Dalin E., Tice H., Pitluck S., Kiss H., Brettin T., Detter J.C.,
RA   Bruce D., Han C., Schmutz J., Larimer F., Land M., Hauser L.,
RA   Kyrpides N., Mikhailova N., Hersman L., Dubois J., Maurice P.,
RA   Richardson P.;
RT   "Complete sequence of Pseudomonas mendocina ymp.";
RL   Submitted (APR-2007) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Catalyzes the oxidation of 5,10-
CC       methylenetetrahydrofolate to 5,10-methenyltetrahydrofolate and
CC       then the hydrolysis of 5,10-methenyltetrahydrofolate to 10-
CC       formyltetrahydrofolate (By similarity).
CC   -!- CATALYTIC ACTIVITY: 5,10-methylenetetrahydrofolate + NADP(+) =
CC       5,10-methenyltetrahydrofolate + NADPH.
CC   -!- CATALYTIC ACTIVITY: 5,10-methenyltetrahydrofolate + H(2)O = 10-
CC       formyltetrahydrofolate.
CC   -!- PATHWAY: One-carbon metabolism; tetrahydrofolate pathway.
CC   -!- SUBUNIT: Homodimer (By similarity).
CC   -!- SIMILARITY: Belongs to the tetrahydrofolate
CC       dehydrogenase/cyclohydrolase family.
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DR   EMBL; CP000680; ABP86208.1; -; Genomic_DNA.
DR   RefSeq; YP_001188940.1; -.
DR   GeneID; 5105928; -.
DR   GenomeReviews; CP000680_GR; Pmen_3458.
DR   KEGG; pmy:Pmen_3458; -.
DR   OMA; A4XXZ2; MQIIDGK.
DR   GO; GO:0005488; F:binding; IEA:InterPro.
DR   GO; GO:0004477; F:methenyltetrahydrofolate cyclohydrolase act...; IEA:HAMAP.
DR   GO; GO:0004488; F:methylenetetrahydrofolate dehydrogenase (NA...; IEA:HAMAP.
DR   GO; GO:0009396; P:folic acid and derivative biosynthetic process; IEA:InterPro.
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:0006730; P:one-carbon compound metabolic process; IEA:UniProtKB-KW.
DR   GO; GO:0055114; P:oxidation reduction; IEA:UniProtKB-KW.
DR   GO; GO:0006164; P:purine nucleotide biosynthetic process; IEA:UniProtKB-KW.
DR   HAMAP; MF_01576; -; 1.
DR   InterPro; IPR016040; NAD(P)-bd_dom.
DR   InterPro; IPR000672; THF_DH/CycHdrlase.
DR   Gene3D; G3DSA:3.40.50.720; NAD(P)-bd; 1.
DR   Pfam; PF00763; THF_DHG_CYH; 1.
DR   Pfam; PF02882; THF_DHG_CYH_C; 1.
DR   PRINTS; PR00085; THFDHDRGNASE.
DR   ProDom; PD002300; THFDhg/Cyc_hydro; 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; Complete proteome; Histidine biosynthesis;
KW   Hydrolase; Methionine biosynthesis; Multifunctional enzyme; NADP;
KW   One-carbon metabolism; Oxidoreductase; Purine biosynthesis.
FT   CHAIN         1    303       Bifunctional protein folD 2.
FT                                /FTId=PRO_0000340588.
SQ   SEQUENCE   303 AA;  31710 MW;  8AFD9CA49D9C5674 CRC64;
     MSAVLSPKLI DGKAAAARVL AEVTEDVRTL KAAGIKPALA VVLVGDDPAS QVYVRNKVLR
     AEECGIRSLE HKLPADTAEA DLLALIHSLN ADYSVHGILV QLPLPAHIDE TRVLQAINPL
     KDVDGFHAEN VGGLSQGRDV LTPCTPAGCL RLLQDSCGDL TGKHAVVIGR SNIVGKPMAA
     LLLKAHCSVS VVHSKSANLR ELCRQADIVV AAVGKPRLVD ADWLKPGAVV IDVGINRIDE
     GGRSRLVGDV DFDSALTRAA AITPVPGGVG PMTIAFLMKN TLVAARLQHP ATGLPLSTLE
     NPA
//