ID   FOLD1_SILPO             Reviewed;         296 AA.
AC   Q5LNV2;
DT   12-DEC-2006, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-2005, sequence version 1.
DT   25-NOV-2008, entry version 28.
DE   RecName: Full=Bifunctional protein folD 1/3;
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=folD1; OrderedLocusNames=SPO1559;
GN   and
GN   Name=folD3; OrderedLocusNames=SPO3101;
OS   Silicibacter pomeroyi.
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales;
OC   Rhodobacteraceae; Silicibacter.
OX   NCBI_TaxID=89184;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700808 / DSM 15171 / DSS-3;
RX   PubMed=15602564; DOI=10.1038/nature03170;
RA   Moran M.A., Buchan A., Gonzalez J.M., Heidelberg J.F., Whitman W.B.,
RA   Kiene R.P., Henriksen J.R., King G.M., Belas R., Fuqua C.,
RA   Brinkac L.M., Lewis M., Johri S., Weaver B., Pai G., Eisen J.A.,
RA   Rahe E., Sheldon W.M., Ye W., Miller T.R., Carlton J., Rasko D.A.,
RA   Paulsen I.T., Ren Q., Daugherty S.C., DeBoy R.T., Dodson R.J.,
RA   Durkin A.S., Madupu R., Nelson W.C., Sullivan S.A., Rosovitz M.J.,
RA   Haft D.H., Selengut J., Ward N.;
RT   "Genome sequence of Silicibacter pomeroyi reveals adaptations to the
RT   marine environment.";
RL   Nature 432:910-913(2004).
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; CP000031; AAV96336.1; -; Genomic_DNA.
DR   EMBL; CP000031; AAV94846.1; -; Genomic_DNA.
DR   RefSeq; YP_166800.1; -.
DR   RefSeq; YP_168304.1; -.
DR   GeneID; 3193798; -.
DR   GeneID; 3194901; -.
DR   GenomeReviews; CP000031_GR; SPO1559.
DR   GenomeReviews; CP000031_GR; SPO3101.
DR   KEGG; sil:SPO1559; -.
DR   KEGG; sil:SPO3101; -.
DR   HOGENOM; Q5LNV2; -.
DR   BioCyc; SPOM246200:SPO_1559-MON; -.
DR   BioCyc; SPOM246200:SPO_3101-MON; -.
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.
DR   InterPro; IPR000672; THF_DHase/CycOHase.
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    296       Bifunctional protein folD 1/3.
FT                                /FTId=PRO_0000268501.
SQ   SEQUENCE   296 AA;  30926 MW;  E8331BCC13CE786C CRC64;
     MAATVIDGKA FAARIRGQVA EHVAELKAGH GITPGLAVVL VGEDPASQVY VRSKGKQTVE
     VGMNSYEHKL DADTSEADLL ALIDRLNGDP DVHGILVQLP LPGHLDEDLV INAIDPAKDV
     DGFHISNVGL LGTGQKSMVP CTPLGCLMML RDHHGSLSGM DAVVIGRSNI VGKPMAQLLL
     GDSCTVTIAH SRTKDLADVV RRADIVVAAV GRPEMVPGDW IKPGATVIDV GINRIERDGK
     TRLVGDVHYD SCAQVAGAIT PVPGGVGPMT IACLLANTLT ACTRANKLTE PDGLTP
//