ID A0A212F741_DANPL Unreviewed; 933 AA.
AC A0A212F741;
DT 27-SEP-2017, integrated into UniProtKB/TrEMBL.
DT 27-SEP-2017, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE RecName: Full=C-1-tetrahydrofolate synthase, cytoplasmic {ECO:0000256|ARBA:ARBA00017592};
DE EC=1.5.1.5 {ECO:0000256|ARBA:ARBA00012859};
DE EC=3.5.4.9 {ECO:0000256|ARBA:ARBA00012776};
DE EC=6.3.4.3 {ECO:0000256|ARBA:ARBA00012295};
GN Name=LOC116773002 {ECO:0000313|RefSeq:XP_032521243.1};
GN ORFNames=KGM_211321 {ECO:0000313|EMBL:OWR49547.1};
OS Danaus plexippus plexippus.
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Lepidoptera; Glossata; Ditrysia; Papilionoidea;
OC Nymphalidae; Danainae; Danaini; Danaina; Danaus; Danaus.
OX NCBI_TaxID=278856 {ECO:0000313|EMBL:OWR49547.1, ECO:0000313|Proteomes:UP000007151};
RN [1] {ECO:0000313|EMBL:OWR49547.1, ECO:0000313|Proteomes:UP000007151}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=F-2 {ECO:0000313|EMBL:OWR49547.1};
RX PubMed=22118469; DOI=10.1016/j.cell.2011.09.052;
RA Zhan S., Merlin C., Boore J.L., Reppert S.M.;
RT "The monarch butterfly genome yields insights into long-distance
RT migration.";
RL Cell 147:1171-1185(2011).
RN [2] {ECO:0000313|EMBL:OWR49547.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=F-2 {ECO:0000313|EMBL:OWR49547.1};
RA Zhan S., Reppert S.M.;
RT "MonarchBase: the monarch butterfly genome database.";
RL Submitted (OCT-2012) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|RefSeq:XP_032521243.1}
RP IDENTIFICATION.
RG RefSeq;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(6R)-5,10-methenyltetrahydrofolate + H2O = (6R)-10-
CC formyltetrahydrofolate + H(+); Xref=Rhea:RHEA:23700,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:57455,
CC ChEBI:CHEBI:195366; EC=3.5.4.9;
CC Evidence={ECO:0000256|ARBA:ARBA00036357};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(6S)-5,6,7,8-tetrahydrofolate + ATP + formate = (6R)-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:195366, ChEBI:CHEBI:456216;
CC EC=6.3.4.3; Evidence={ECO:0000256|ARBA:ARBA00036012};
CC -!- PATHWAY: One-carbon metabolism; tetrahydrofolate interconversion.
CC {ECO:0000256|ARBA:ARBA00004777}.
CC -!- SUBUNIT: Homodimer. {ECO:0000256|ARBA:ARBA00011738}.
CC -!- SIMILARITY: In the C-terminal section; belongs to the
CC formate--tetrahydrofolate ligase family.
CC {ECO:0000256|ARBA:ARBA00006985}.
CC -!- SIMILARITY: In the N-terminal section; belongs to the tetrahydrofolate
CC dehydrogenase/cyclohydrolase family. {ECO:0000256|ARBA:ARBA00005559}.
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DR EMBL; AGBW02009936; OWR49547.1; -; Genomic_DNA.
DR RefSeq; XP_032521243.1; XM_032665352.1.
DR STRING; 278856.A0A212F741; -.
DR EnsemblMetazoa; XM_032665352.1; XP_032521243.1; LOC116773002.
DR KEGG; dpl:KGM_211321; -.
DR eggNOG; KOG4230; Eukaryota.
DR UniPathway; UPA00193; -.
DR Proteomes; UP000007151; Unassembled WGS sequence.
DR Proteomes; UP000596680; Chromosome 19.
DR GO; GO:0005524; F:ATP binding; IEA:InterPro.
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:0035999; P:tetrahydrofolate interconversion; IEA:UniProtKB-UniPathway.
DR CDD; cd00477; FTHFS; 1.
DR CDD; cd01080; NAD_bind_m-THF_DH_Cyclohyd; 1.
DR Gene3D; 1.10.8.770; -; 1.
DR Gene3D; 3.10.410.10; Formyltetrahydrofolate synthetase, domain 3; 1.
DR Gene3D; 3.40.50.10860; Leucine Dehydrogenase, chain A, domain 1; 1.
DR Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 2.
DR HAMAP; MF_01543; FTHFS; 1.
DR HAMAP; MF_01576; THF_DHG_CYH; 1.
DR InterPro; IPR046346; Aminoacid_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 PANTHER; PTHR48099:SF5; C-1-TETRAHYDROFOLATE SYNTHASE, CYTOPLASMIC; 1.
DR PANTHER; PTHR48099; C-1-TETRAHYDROFOLATE SYNTHASE, CYTOPLASMIC-RELATED; 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 SUPFAM; SSF53223; Aminoacid dehydrogenase-like, N-terminal domain; 1.
DR SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 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 3: Inferred from homology;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Multifunctional enzyme {ECO:0000256|ARBA:ARBA00023268};
KW NADP {ECO:0000256|ARBA:ARBA00022857};
KW One-carbon metabolism {ECO:0000256|ARBA:ARBA00022563};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Reference proteome {ECO:0000313|Proteomes:UP000007151}.
FT DOMAIN 6..124
FT /note="Tetrahydrofolate dehydrogenase/cyclohydrolase
FT catalytic"
FT /evidence="ECO:0000259|Pfam:PF00763"
FT DOMAIN 128..292
FT /note="Tetrahydrofolate dehydrogenase/cyclohydrolase
FT NAD(P)-binding"
FT /evidence="ECO:0000259|Pfam:PF02882"
SQ SEQUENCE 933 AA; 100235 MW; 538E539EBFCF29D9 CRC64;
MSAQVISGTQ TARSIENDLR QQVAVMGQQH PGFQPKLAIV QVGGREDSNV YIRAKLKAAE
NIGIAAEHIK LPREISQAEL LTKLTALNDS PLVHGIIVQM PLDSVEKIDS HLITDAVSSQ
KDVDGLNTEN EGRVALGDMS GFVSCTPAGC IELIKRTGIS IEGKQAVVIG RSRIVGTPVA
ELLKWENATV TVCHSKTKNL SEITKTADIL VVAIGKAEMV RGSWIKPGAV VIDCGINPIP
DTSKPSGRRL VGDVAYSEAV QVASHVTPVP GGVGPMTVAM LMKNTVLAAS RQLQRISTPV
WPLQPLRLST VSPPPSDIVI ARSQKPKYIS KLAEEIGLFP SEVSQYGNTK AKISLSVLDR
LRDQRGGKYI VVAGITPTPL GEGKSTTLIG LVQALGAHRG RNAFAVMRQP SQGPTFGVKG
GAAGGGYSQV IPMEDFNLHL TGDIHAVSAA NNLLAAHMDA RIFHELTQKD GPLYDRLVPE
IKGVRKFSPI QLRRLKRLGI EKTDPNALTP EERVKFARLN IDPKKVMWNR VVDLNDRYLR
KITIGQSPTE KGFTRETSFD IAVASEIMAV LALGKDVNDI KERLANMVVA LDTNGKPVIA
DDLGITGALM VLLKDAFEPT LMQTLEGTPV LVHTGPFANI AHGCSSILAD KIAMKLAREN
GYVATEAGFG SDIGMEKFFD IKCRSSGDTP HCAVIVSTVR ALKMHGGGPT VSPGQPLHSV
YVQENLELLS KGLCNLGKHI SNGNKFGVPV VIAVNKHGND TEAELNMVRE YALKNGAFRA
VICDHWAKGG AGALELADAV VEACDRPSNF QYLYPLEMTI QDKIKKIAVE MYGAGTVEYT
DVVLEKIKVL NDRGYDKLAI CMAKTSNSLT GDPSIKGAPT GFTLRINDIF VSAGAGFIVP
MVGEISKMPG LPTRPSIYDI DLNTETGEID GLF
//
