ID   C1TC_SPOFR              Reviewed;         933 AA.
AC   Q27772;
DT   16-JAN-2004, integrated into UniProtKB/Swiss-Prot.
DT   16-JAN-2004, sequence version 3.
DT   16-JUN-2009, entry version 60.
DE   RecName: Full=C-1-tetrahydrofolate synthase, cytoplasmic;
DE            Short=C1-THF synthase;
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;
DE   Includes:
DE     RecName: Full=Formyltetrahydrofolate synthetase;
DE              EC=6.3.4.3;
OS   Spodoptera frugiperda (Fall armyworm).
OC   Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Lepidoptera; Glossata; Ditrysia; Noctuoidea;
OC   Noctuidae; Amphipyrinae; Spodoptera.
OX   NCBI_TaxID=7108;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Ovary;
RX   MEDLINE=95200961; PubMed=7893749; DOI=10.1016/0167-4781(95)00004-Z;
RA   Tremblay G.B., MacKenzie R.E.;
RT   "Primary structure of a folate-dependent trifunctional enzyme from
RT   Spodoptera frugiperda.";
RL   Biochim. Biophys. Acta 1261:129-133(1995).
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   -!- CATALYTIC ACTIVITY: ATP + formate + tetrahydrofolate = ADP +
CC       phosphate + 10-formyltetrahydrofolate.
CC   -!- PATHWAY: One-carbon metabolism; tetrahydrofolate pathway.
CC   -!- SUBUNIT: Homodimer (By similarity).
CC   -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity).
CC   -!- DOMAIN: This trifunctional enzyme consists of two major domains:
CC       an N-terminal part containing the methylene-THF dehydrogenase and
CC       cyclohydrolase activities and a larger C-terminal part containing
CC       formyl-THF synthetase activity.
CC   -!- SIMILARITY: In the N-terminal section; belongs to the
CC       tetrahydrofolate dehydrogenase/cyclohydrolase family.
CC   -!- SIMILARITY: In the C-terminal section; belongs to the formate--
CC       tetrahydrofolate ligase family.
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DR   EMBL; L36189; AAA74302.1; -; mRNA.
DR   PIR; S53523; S53523.
DR   HSSP; P11586; 1A4I.
DR   BRENDA; 1.5.1.5; 15157.
DR   BRENDA; 3.5.4.9; 15157.
DR   BRENDA; 6.3.4.3; 15157.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0004329; F:formate-tetrahydrofolate ligase activity; IEA:EC.
DR   GO; GO:0004477; F:methenyltetrahydrofolate cyclohydrolase act...; IEA:EC.
DR   GO; GO:0004488; F:methylenetetrahydrofolate dehydrogenase (NA...; IEA:EC.
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   InterPro; IPR000559; For_THF_ligase.
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; PF01268; FTHFS; 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; PS00721; FTHFS_1; 1.
DR   PROSITE; PS00722; FTHFS_2; 1.
DR   PROSITE; PS00766; THF_DHG_CYH_1; 1.
DR   PROSITE; PS00767; THF_DHG_CYH_2; 1.
PE   2: Evidence at transcript level;
KW   Amino-acid biosynthesis; ATP-binding; Cytoplasm;
KW   Histidine biosynthesis; Hydrolase; Ligase; Methionine biosynthesis;
KW   Multifunctional enzyme; NADP; Nucleotide-binding;
KW   One-carbon metabolism; Oxidoreductase; Purine biosynthesis.
FT   CHAIN         1    933       C-1-tetrahydrofolate synthase,
FT                                cytoplasmic.
FT                                /FTId=PRO_0000199325.
FT   NP_BIND     170    172       NADP (By similarity).
FT   NP_BIND     378    385       ATP (By similarity).
FT   REGION        1    303       Methylenetetrahydrofolate dehydrogenase
FT                                and cyclohydrolase.
FT   REGION       51     55       Substrate binding (By similarity).
FT   REGION       98    100       Substrate binding (By similarity).
FT   REGION      270    274       Substrate binding (By similarity).
FT   REGION      304    933       Formyltetrahydrofolate synthetase.
FT   BINDING     195    195       NADP (By similarity).
SQ   SEQUENCE   933 AA;  100618 MW;  55C3FA820C1A55CB CRC64;
     MWEPQGSLDP VLESIENELR DQVAEARSRW AGFDARLAIV QVGGREDSNV YIRMKLRAAE
     NIGITAEHIQ LPRDITETEL LANITSLNES PYVHGIIVQM PLDSVHPIDS HAITDAVSPD
     KDVDGLNTIN EGRVRVGDLS GFIPCTPAGC VELIKRTGVT IAGKNVVVLG RSRIVGTPVS
     ELLKWEHATV TVCHSKTKNL SEITKTADIL VVAIGRGEMV RGSWIKPGAV VIDCGINPIS
     DPTKKSGQRL VGDVAYEEAV QVASHVTPVP GGVGPMTVAM LMRNTVQAAR RQLDRLLAPT
     WPLRPLRITP LSPPPSDIVI ARSQKPKDIS ELAHEIGLFS NEVSQYGRTK AKISLSVLDR
     MRNQQGAKYI VVAGITPTPL GEGKSTTLLG LVQALSAHRG RNSFAVMRQP SQGPTFGVKG
     GAAGGGYSQV IPMEEFNLHL TGDIHAGTAA NNLLAAQMDA RIFHELTQKD GPLFDRLVPK
     IKGVRKFSPI QLRRLKRLGI TKTDPDTLTE GEKSKFARLN IDTSKIMWNR VVDLNDRYLR
     KITVGQSPTE KGFTRETAFD ISVASEIMAI LALGRDVEDI KERLANMVVA LDKSGNPVTA
     DDLGMTGALL VLLRDAFEPT LMQSLEGTPV LVHTGPFANI RHGCSSILAD KIAMKLAGEN
     GYVATEAGFG SDIGMEKFFD IKCRASGDTP HCAVIVSTVR ALKMHGGGPP VSAGMPLNDV
     YVQENLELLS KGLCNLGKHI SNGNKFGVPV VVAINKHGND TPAELNLVKE FAVKNGAFRA
     VLCDHWAKGG LGALELADAV IEACDSKSKF DFLYPLQLSI QEKIQIIAKE MYGAGQVEYT
     DEVLEKIKTF TDMGYDKFPI CMAKTSNSLT GDPAVKGAPT GFTLKINGIF ASVGAGFVVP
     MVGEISKMPG LPTRPSIYDI DLNTKTGEIE GLF
//