C1TC_SPOFR
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 03-AUG-2022, entry version 107.
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; Ecdysozoa; 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 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:
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;
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;
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(6S)-5,6,7,8-tetrahydrofolate + ATP + formate = (6S)-10-
CC formyltetrahydrofolate + ADP + phosphate; Xref=Rhea:RHEA:20221,
CC ChEBI:CHEBI:15740, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474,
CC ChEBI:CHEBI:57453, ChEBI:CHEBI:57454, ChEBI:CHEBI:456216; EC=6.3.4.3;
CC -!- PATHWAY: One-carbon metabolism; tetrahydrofolate interconversion.
CC -!- SUBUNIT: Homodimer. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC -!- DOMAIN: This trifunctional enzyme consists of two major domains: an N-
CC 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 tetrahydrofolate
CC dehydrogenase/cyclohydrolase family. {ECO:0000305}.
CC -!- SIMILARITY: In the C-terminal section; belongs to the formate--
CC tetrahydrofolate ligase family. {ECO:0000305}.
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DR EMBL; L36189; AAA74302.1; -; mRNA.
DR PIR; S53523; S53523.
DR AlphaFoldDB; Q27772; -.
DR SMR; Q27772; -.
DR UniPathway; UPA00193; -.
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:UniProtKB-EC.
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 CDD; cd00477; FTHFS; 1.
DR CDD; cd01080; NAD_bind_m-THF_DH_Cyclohyd; 1.
DR Gene3D; 3.40.50.300; -; 2.
DR HAMAP; MF_01543; FTHFS; 1.
DR HAMAP; MF_01576; THF_DHG_CYH; 1.
DR InterPro; IPR046346; Aminiacid_DH-like_N_sf.
DR InterPro; IPR000559; Formate_THF_ligase.
DR InterPro; IPR020628; Formate_THF_ligase_CS.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR InterPro; IPR027417; P-loop_NTPase.
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; PF01268; FTHFS; 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 SUPFAM; SSF52540; SSF52540; 1.
DR SUPFAM; SSF53223; SSF53223; 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; Histidine biosynthesis;
KW Hydrolase; Ligase; Methionine biosynthesis; Multifunctional enzyme; NADP;
KW Nucleotide-binding; One-carbon metabolism; Oxidoreductase;
KW Purine biosynthesis.
FT CHAIN 1..933
FT /note="C-1-tetrahydrofolate synthase, cytoplasmic"
FT /id="PRO_0000199325"
FT REGION 1..303
FT /note="Methylenetetrahydrofolate dehydrogenase and
FT cyclohydrolase"
FT REGION 304..933
FT /note="Formyltetrahydrofolate synthetase"
FT BINDING 51..55
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 98..100
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 170..172
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250"
FT BINDING 195
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250"
FT BINDING 270..274
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 378..385
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
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
