ID U3IU85_ANAPP Unreviewed; 925 AA.
AC U3IU85;
DT 13-NOV-2013, integrated into UniProtKB/TrEMBL.
DT 05-JUN-2019, sequence version 2.
DT 27-MAR-2024, entry version 60.
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|Ensembl:ENSAPLP00000010808.2};
OS Anas platyrhynchos platyrhynchos (Northern mallard).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Galloanserae; Anseriformes; Anatidae;
OC Anatinae; Anas.
OX NCBI_TaxID=8840 {ECO:0000313|Ensembl:ENSAPLP00000010808.2, ECO:0000313|Proteomes:UP000016666};
RN [1] {ECO:0000313|Ensembl:ENSAPLP00000010808.2, ECO:0000313|Proteomes:UP000016666}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Hou Z.-C., Zhou Z.-K., Zhu F., Hou S.-S.;
RT "A new Pekin duck reference genome.";
RL Submitted (OCT-2017) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSAPLP00000010808.2}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-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 AlphaFoldDB; U3IU85; -.
DR Ensembl; ENSAPLT00000011526.2; ENSAPLP00000010808.2; ENSAPLG00000010974.2.
DR GeneTree; ENSGT00940000154746; -.
DR HOGENOM; CLU_003601_2_0_1; -.
DR UniPathway; UPA00193; -.
DR Proteomes; UP000016666; Chromosome 5.
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:SF1; 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 One-carbon metabolism {ECO:0000256|ARBA:ARBA00022563};
KW Reference proteome {ECO:0000313|Proteomes:UP000016666}.
FT DOMAIN 7..125
FT /note="Tetrahydrofolate dehydrogenase/cyclohydrolase
FT catalytic"
FT /evidence="ECO:0000259|Pfam:PF00763"
FT DOMAIN 129..293
FT /note="Tetrahydrofolate dehydrogenase/cyclohydrolase
FT NAD(P)-binding"
FT /evidence="ECO:0000259|Pfam:PF02882"
SQ SEQUENCE 925 AA; 99437 MW; 9DCEE8C05A4AA9C7 CRC64;
MAPAEILSGK AVSAQVRERL KKQVAEMKEK FPGFTPGLAI LQVGNRDDSN LYINMKLKAA
AEIGISANHI KLPNTATEAE VLKCIASLNG DPAIHGFIVQ LPLDSDKPIN TEKITNAVSP
EKDVDGLSSI NAGKLSRGDL GDCFIPCTPK GCMELISQTG IQVAGKRAVV IGRSKIVGAP
MHDLLLWNHA TVTTCHSKTS TLAEEVGKAD ILVVAAGKAE MVKGEWIKPG AIVIDCGINH
VPDSTKASGK RVVGDVAYNT AKEKASYITP VPGGVGPMTV AMLMQSTVES AQRFLEKFQP
GKWNIQYNQL TLKMPVPSDI EISRSCIPKP IDQVAKEVGL LPDEMELYGQ TKAKVQLSAL
KRLKNQPDGK YVVVTGITPT PLGEGKSTTT IGLVQALGAH LHQNVFACVR QPSQGPTFGI
KGGAAGGGYS QVIPMEEFNL HLTGDIHAIT AANNLVAAAV DARMFHELTQ NDQALYNRLV
PSVNGVRKFS EIQIRRLQKL GINKTDPTTL TKEEVNMFVR LDIDPATITW QRVLDTNDRF
LRKITIGQSP TEKGFSRTAQ FDITVSSEIM AVLALSDSLD DMKRRLGRMV VASSKRGEPV
TTDDLGVTGA LAVLMKDAVK PNLMQTLEGT PVFVHAGPFA NIAHGNSSVL ADKIALKLVG
KEGFVVTEAG FGADIGMEKF FNIKCRYSGL RPHVVVLVAT VRALKMHGGG PAVTAGVPLP
KEYTEENLQL LAKGCSNLSK QIQNARMFGV PVVVAVNAFK TDTKAELALV VQQAKEAGAF
DAVECTHWAE GGKGAVALAQ AVQRASQTPS NFRFLYNVEL PVIDKIRLIA QQIYGASDIE
LLPEAQEKVT LYTKQGFGNL PICMAKTHLS LSHDPEQKGA PTGFILPIRD IRASVGAGFL
YPLVGTLESP LCYLHKSVMF SWTCS
//
