ID A0A0V0RY12_9BILA Unreviewed; 1133 AA.
AC A0A0V0RY12;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 27-MAR-2024, entry version 29.
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=Mthfd1 {ECO:0000313|EMBL:KRX19247.1};
GN ORFNames=T07_3975 {ECO:0000313|EMBL:KRX19247.1};
OS Trichinella nelsoni.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Enoplea; Dorylaimia;
OC Trichinellida; Trichinellidae; Trichinella.
OX NCBI_TaxID=6336 {ECO:0000313|EMBL:KRX19247.1, ECO:0000313|Proteomes:UP000054630};
RN [1] {ECO:0000313|EMBL:KRX19247.1, ECO:0000313|Proteomes:UP000054630}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ISS37 {ECO:0000313|EMBL:KRX19247.1};
RA Korhonen P.K., Edoardo P., Giuseppe L.R., Gasser R.B.;
RT "Evolution of Trichinella species and genotypes.";
RL Submitted (JAN-2015) to the EMBL/GenBank/DDBJ databases.
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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KRX19247.1}.
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DR EMBL; JYDL01000061; KRX19247.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0V0RY12; -.
DR UniPathway; UPA00193; -.
DR Proteomes; UP000054630; Unassembled WGS sequence.
DR GO; GO:1990904; C:ribonucleoprotein complex; IEA:UniProtKB-KW.
DR GO; GO:0005840; C:ribosome; IEA:UniProtKB-KW.
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; 3.100.10.10; -; 1.
DR Gene3D; 3.30.1510.10; Domain 2, N(10)-formyltetrahydrofolate synthetase; 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; IPR021131; Ribosomal_uL15/eL18.
DR InterPro; IPR036227; Ribosomal_uL15/eL18_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; 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; PF17135; Ribosomal_L18; 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 SUPFAM; SSF52080; Ribosomal proteins L15p and L18e; 1.
DR PROSITE; PS00721; FTHFS_1; 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:UP000054630};
KW Ribonucleoprotein {ECO:0000256|ARBA:ARBA00023274};
KW Ribosomal protein {ECO:0000256|ARBA:ARBA00022980}.
FT DOMAIN 2..165
FT /note="Large ribosomal subunit protein uL15/eL18"
FT /evidence="ECO:0000259|Pfam:PF17135"
FT DOMAIN 212..330
FT /note="Tetrahydrofolate dehydrogenase/cyclohydrolase
FT catalytic"
FT /evidence="ECO:0000259|Pfam:PF00763"
FT DOMAIN 335..494
FT /note="Tetrahydrofolate dehydrogenase/cyclohydrolase
FT NAD(P)-binding"
FT /evidence="ECO:0000259|Pfam:PF02882"
SQ SEQUENCE 1133 AA; 124381 MW; BF06977CF1A806CC CRC64;
MGIDKCHRFL KKSVRRRAHT EDPYHLLLVK LYSFLARRSG SKFNKIILKR LLMARRHKPP
LSLRRLANFM QRKGRNDKIC VIVGTVTNDV RLYRVPKLEV CALHVTEQAR ARILKAGGKI
LTFDQLALRA PKGENTVLVQ GPRKAREAEK HFGPAPGVPH SHSKIAEYCR EKMSSSAVIF
HGRNIPIWRT FRRMLFDGGR QLKTNQEMAV LIDGKKIASQ LRQKIRDHLS TVKSEFPKFN
PKLAIVQVGD RQDSNVYIRN KLKAADEIGI SAQLIKLSSA IGEFELIDRI EKLNTDPDVH
GIIVQLPLDA SAEIDAEKVI NSINFEKDVD GLTLHNAGRL ARGELENTIV PCTPKGCLEL
LKHTGINISG KHCVVVGRSR IVGGPVSALM LWQNATVTTC HSKTANLAEF CQSADILIVA
VGRPNLIQGS WIKPRAVVID CGINIVEDDA KRLVGDVEFE SAKQVASFIT PVPGGVGPMT
VAMLMSNTVD AACRTLKRVK RWPLTPYEPV LKSPVPSDLE ISYSHKPISI DKLANSIGLL
PHEVEQYGKF KAKVSLDVLN RYKEQKNGSY VIVTSMSPPS RGAGKSTIVI GLTQALNVYL
KTNSFACLRQ PSQGPTFGMK GGAAGGGYSQ VVPMDEFNLH LTGDFHAIVA ATNLLAAAVE
TRLFHESTSS TEALYKRLVP VKHGQRVFTD NQLSRLEKLN IRPKHPDQLN PEEREQFSRL
NIDSGTITWN RVIDTNDRFL RLVTVGQSPS EKGHSRQCRF DIAAASEIAA ILALTTGLGD
LRRRLGRIVV ANDFHGRPVC ADDLSVAGAL TALMKDALRP NLMQTLQGTP VFVHGGPFAN
IAHGNSSILA DWIALKLVGQ DGVVVTEAGF GADVGFEKFC NIKCRTSGLC ANVAVVVVTI
EALKLHGGAP EPRPTDDSSP DLLAFVENGC LNMIRHIENI HKFGTPVIVA VNKYSTDTTA
ELDVVRREAL RAGALDVVVC DQWAKGGLGC VELAEAVSKA VRQQKSTHSF KLLYPDQWSI
KEKIETIAKE IYGADGVEFT VDAEKALAKL TDQGFDKLPV CMAKTQKSFS NDPNWKGVPS
GYTLPVRDVQ VCAGAGFLYA LVGEIQTMPG LPIRPAFFDI DVDLETEFVK GLF
//
