ID A0A2K6D912_MACNE Unreviewed; 875 AA.
AC A0A2K6D912;
DT 28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT 28-MAR-2018, sequence version 1.
DT 24-JAN-2024, entry version 27.
DE RecName: Full=formate--tetrahydrofolate ligase {ECO:0000256|ARBA:ARBA00012295};
DE EC=6.3.4.3 {ECO:0000256|ARBA:ARBA00012295};
GN Name=MTHFD1L {ECO:0000313|Ensembl:ENSMNEP00000032394.1};
OS Macaca nemestrina (Pig-tailed macaque).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC Cercopithecidae; Cercopithecinae; Macaca.
OX NCBI_TaxID=9545 {ECO:0000313|Ensembl:ENSMNEP00000032394.1, ECO:0000313|Proteomes:UP000233120};
RN [1] {ECO:0000313|Ensembl:ENSMNEP00000032394.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-2023) to UniProtKB.
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; A0A2K6D912; -.
DR Ensembl; ENSMNET00000056828.1; ENSMNEP00000032394.1; ENSMNEG00000039466.1.
DR GeneTree; ENSGT00940000157477; -.
DR OMA; CGEIMTM; -.
DR UniPathway; UPA00193; -.
DR Proteomes; UP000233120; Unplaced.
DR Bgee; ENSMNEG00000039466; Expressed in cerebellum and 11 other cell types or tissues.
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:0004488; F:methylenetetrahydrofolate dehydrogenase (NADP+) activity; IEA:InterPro.
DR GO; GO:0035999; P:tetrahydrofolate interconversion; IEA:UniProtKB-UniPathway.
DR CDD; cd00477; FTHFS; 1.
DR CDD; cd05212; NAD_bind_m-THF_DH_Cyclohyd_like; 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; 3.
DR HAMAP; MF_01543; FTHFS; 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; IPR020631; THF_DH/CycHdrlase_NAD-bd_dom.
DR PANTHER; PTHR48099; C-1-TETRAHYDROFOLATE SYNTHASE, CYTOPLASMIC-RELATED; 1.
DR PANTHER; PTHR48099:SF12; MONOFUNCTIONAL C1-TETRAHYDROFOLATE SYNTHASE, MITOCHONDRIAL; 1.
DR Pfam; PF01268; FTHFS; 2.
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.
PE 3: Inferred from homology;
KW One-carbon metabolism {ECO:0000256|ARBA:ARBA00022563};
KW Reference proteome {ECO:0000313|Proteomes:UP000233120}.
FT DOMAIN 20..112
FT /note="Tetrahydrofolate dehydrogenase/cyclohydrolase
FT catalytic"
FT /evidence="ECO:0000259|Pfam:PF00763"
FT DOMAIN 116..236
FT /note="Tetrahydrofolate dehydrogenase/cyclohydrolase
FT NAD(P)-binding"
FT /evidence="ECO:0000259|Pfam:PF02882"
SQ SEQUENCE 875 AA; 95295 MW; 44730FFD5CAA433E CRC64;
LRQRLALPQV IQNSKEVLSL LQEKNPAFKP VLAIIQAGDD NLMQEINQNL AEETGLNITH
ICLPPDSSEA EIIDEILKIN EDTRVHGLAL QISENLFSNK VLNALKPEKD VDGVTDINLG
KLVRGDAHEC FVSPVAKAAI ELLEKSVGVN LDGKKILVAG AHGSLEAALQ CLFQRKGSMT
MSSQWKTPQL QRKLHEADIV VLGSRKPEEI PLTWIQPGIT VLNCSHDFLS GKVGCGSPRI
HFGGLIEEDD VSLLAAALRI QNMVSSGRRW LREQQHRRWR LHCLKLQPLS PVPSDIEISR
GQTPKVVDVL AKEIGLLADE IEIYGKSKAK VRLSVLERLK NQADGKYVLV AGITPTPLGE
GKSTVTIGLV QALTAHLNVN SFACLRQPSQ GPTFGVKGGA AGGGYAQVIP MEEFNLHLTG
DIHAITAANN LLAAAIDTRI LHENTQTDKA LYNRLVPLVN GVREFSEIQL ARLKKLGINK
TDPSTLTEEE VSKFARLDIN PSTITWQRVL DTNDRFLRKI TIGQGNTEKG YSRQAQFDIA
VASEIMAVLA LTDSLADMKA RLGRMVVASD KSGQPVTADD LGVTGALTVL MKDAIKPNLM
QTLEGTPVFV HAGPFANIAH GNSSVLADKI ALKLVGEEGF VGKLLLLNLV VVTAGVPLKK
EYTEENIQLV ADGCCNLQKQ IQIAQLFGVP VVVALNVFKT DTRAEIDLVC ELAKRAGAFD
AVPCYHWSVG GKGSVDLARA VREAASKRSR FQFLYDVQVR SIVDKIRTIA QAVYGAKDIE
LSPEAQAKID RYTQQGFGNL PICMAKTHLS LSHEPDKKGV PRDFILPISD VRASIGAGFI
YPLVGTMSTM PGLPTRPCFY DIDLDTETEQ VKGLF
//