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Database: UniProt
Entry: P57557
LinkDB: P57557
Original site: P57557 
ID   FOLD_BUCAI              Reviewed;         285 AA.
AC   P57557;
DT   01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-DEC-2000, sequence version 1.
DT   25-OCT-2017, entry version 95.
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=BU486;
OS   Buchnera aphidicola subsp. Acyrthosiphon pisum (strain APS)
OS   (Acyrthosiphon pisum symbiotic bacterium).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Erwiniaceae; Buchnera.
OX   NCBI_TaxID=107806;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=APS;
RX   PubMed=10993077; DOI=10.1038/35024074;
RA   Shigenobu S., Watanabe H., Hattori M., Sakaki Y., Ishikawa H.;
RT   "Genome sequence of the endocellular bacterial symbiont of aphids
RT   Buchnera sp. APS.";
RL   Nature 407:81-86(2000).
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. {ECO:0000255|HAMAP-Rule:MF_01576}.
CC   -!- CATALYTIC ACTIVITY: 5,10-methylenetetrahydrofolate + NADP(+) =
CC       5,10-methenyltetrahydrofolate + NADPH. {ECO:0000255|HAMAP-
CC       Rule:MF_01576}.
CC   -!- CATALYTIC ACTIVITY: 5,10-methenyltetrahydrofolate + H(2)O = 10-
CC       formyltetrahydrofolate. {ECO:0000255|HAMAP-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-
CC       Rule:MF_01576}.
DR   EMBL; BA000003; BAB13182.1; -; Genomic_DNA.
DR   RefSeq; NP_240296.1; NC_002528.1.
DR   RefSeq; WP_010896140.1; NC_002528.1.
DR   ProteinModelPortal; P57557; -.
DR   SMR; P57557; -.
DR   STRING; 107806.BU486; -.
DR   PRIDE; P57557; -.
DR   EnsemblBacteria; BAB13182; BAB13182; BAB13182.
DR   GeneID; 1109832; -.
DR   KEGG; buc:BU486; -.
DR   PATRIC; fig|107806.10.peg.494; -.
DR   eggNOG; ENOG4105CN0; Bacteria.
DR   eggNOG; COG0190; LUCA.
DR   HOGENOM; HOG000218242; -.
DR   KO; K01491; -.
DR   OMA; AGKLCGD; -.
DR   UniPathway; UPA00193; -.
DR   Proteomes; UP000001806; Chromosome.
DR   GO; GO:0004477; F:methenyltetrahydrofolate cyclohydrolase activity; IEA:UniProtKB-EC.
DR   GO; GO:0004488; F:methylenetetrahydrofolate dehydrogenase (NADP+) activity; IEA:UniProtKB-EC.
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   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   PANTHER; PTHR10025; PTHR10025; 1.
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; Complete proteome; Histidine biosynthesis;
KW   Hydrolase; Methionine biosynthesis; Multifunctional enzyme; NADP;
KW   One-carbon metabolism; Oxidoreductase; Purine biosynthesis;
KW   Reference proteome.
FT   CHAIN         1    285       Bifunctional protein FolD.
FT                                /FTId=PRO_0000199300.
FT   NP_BIND     166    168       NADP. {ECO:0000255|HAMAP-Rule:MF_01576}.
FT   BINDING     232    232       NADP; via amide nitrogen.
FT                                {ECO:0000255|HAMAP-Rule:MF_01576}.
SQ   SEQUENCE   285 AA;  31353 MW;  6571E83A748CC26C CRC64;
     MPAIIIDGNK IAKKIELKIL KKVKQRKKNG ERIPGLAMIL VGNHIPSQIY VNKKKISCKN
     VGFFSECWNL PSNINEKEIL NIISKLNENK NIDGILIQLP LPPQINHMKI LSSIVPDKDV
     DGFHPYNTGS LCQRTPKLRA CTPKGIITML KYNKIKTHGL HAVMVGASNI VGRPMSLELL
     LAGCTTTVTH RFTKNLKDHV QNADLLIVAV GKANFLKGSW IKTGSIVIDV GINRLKNGKV
     VGDVEFKTAY LRASYITPVP GGVGPMTVAT LLQNTLEACE NHDDI
//
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