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Database: UniProt
Entry: A0A2U3WKK0_ODORO
LinkDB: A0A2U3WKK0_ODORO
Original site: A0A2U3WKK0_ODORO 
ID   A0A2U3WKK0_ODORO        Unreviewed;       935 AA.
AC   A0A2U3WKK0;
DT   18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT   18-JUL-2018, sequence version 1.
DT   27-MAR-2024, entry version 25.
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|RefSeq:XP_004409418.1};
OS   Odobenus rosmarus divergens (Pacific walrus).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Carnivora; Caniformia; Pinnipedia; Odobenidae;
OC   Odobenus.
OX   NCBI_TaxID=9708 {ECO:0000313|Proteomes:UP000245340, ECO:0000313|RefSeq:XP_004409418.1};
RN   [1] {ECO:0000313|RefSeq:XP_004409418.1}
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   RefSeq; XP_004409418.1; XM_004409361.1.
DR   AlphaFoldDB; A0A2U3WKK0; -.
DR   STRING; 9708.A0A2U3WKK0; -.
DR   GeneID; 101381197; -.
DR   KEGG; oro:101381197; -.
DR   CTD; 4522; -.
DR   InParanoid; A0A2U3WKK0; -.
DR   OrthoDB; 651667at2759; -.
DR   UniPathway; UPA00193; -.
DR   Proteomes; UP000245340; Unplaced.
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:UP000245340}.
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   935 AA;  101227 MW;  AFD9B24EB384D414 CRC64;
     MAPAEILNGK VVSAQIRERL KNQVTQMKEQ VPGFTPGLAI LQVGNRDDSN LYINVKLKAA
     EEIGIKATHI KLPRTATESE VLKYVTSLNE DLTVHGFIVQ LPLDSENPIN TEAVVNAIIP
     EKDVDGLTSI SAGKLARGDL NDCFIPCTPK GCLELIKETG VQIAGRHAVV VGRSKIVGAP
     MHDLLLWNHA TVTTCHSKTA NLGEEVNKGD ILVVATGQPE MVKGEWIKPG AIVIDCGINY
     IPDDTKPNGK KVVGDVAYDE AKERAGFITP VPGGVGPMTV AMLMQSTVES AKRFLEKFKP
     GKWMIQYNKL NLQVPVPSDI DISRSCKPKP IGSLAREIGL LSEEVELYGE TKAKVLLSAL
     ERLKHQPDGK YVVVTGITPT PLGEGKSTTT IGLVQALGAH LFLNVFACVR QPSQGPTFGI
     KGGAAGGGYS QVIPMEEFNL HLTGDIHAIT AANNLVAAAI DARMFHELTQ TDKALFNRLV
     PSVNGVRKFS NIQIRRLQRL GIEKTDPTTL TDDEINRFAR LDIDPETITW QRVLDTNDRF
     LRKITIGQAP TEKGHTRTAQ FDISVASEIM AVLALTSSLE DMRERLSRMV VASSRKGEPI
     STEDLGVSGA LTVLMKDAIK PNLMQTLEGT PVFVHAGPFA NIAHGNSSII ADRIALKLVG
     PEGFVVTEAG FGADIGMEKF FNIKCRYSGL RPHVVVLVAT VRALKMHGGG PTVTAGLPLP
     KAYIEENLEL VEKGFSNLRK QIENARMFGV PVVVAVNAFK TDSEAELDLV SRLAKDHGAF
     DAVKCTHWAE GGKGALALAQ AVQRAAQAAS SFQLLYDLKL PIEDKIRIIA QKIYGADDIE
     LLPEAQHKAE VYTKQGFGDL PICMAKTHLS LSHNPEQKGV PTGFVLPIRD IRASVGAGFL
     YPLVGTMSTM PGLPTRPCFY DIDLDPETEQ VNGLF
//
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