ID   A0A3Q3MVW1_9LABR        Unreviewed;       986 AA.
AC   A0A3Q3MVW1;
DT   10-APR-2019, integrated into UniProtKB/TrEMBL.
DT   10-APR-2019, sequence version 1.
DT   27-MAR-2024, entry version 24.
DE   RecName: Full=formate--tetrahydrofolate ligase {ECO:0000256|ARBA:ARBA00012295};
DE            EC=6.3.4.3 {ECO:0000256|ARBA:ARBA00012295};
OS   Labrus bergylta (ballan wrasse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC   Eupercaria; Labriformes; Labridae; Labrus.
OX   NCBI_TaxID=56723 {ECO:0000313|Ensembl:ENSLBEP00000025180.1, ECO:0000313|Proteomes:UP000261660};
RN   [1] {ECO:0000313|Ensembl:ENSLBEP00000025180.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (NOV-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; A0A3Q3MVW1; -.
DR   STRING; 56723.ENSLBEP00000025180; -.
DR   Ensembl; ENSLBET00000026457.1; ENSLBEP00000025180.1; ENSLBEG00000019249.1.
DR   GeneTree; ENSGT00940000157477; -.
DR   InParanoid; A0A3Q3MVW1; -.
DR   UniPathway; UPA00193; -.
DR   Proteomes; UP000261660; 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:0004488; F:methylenetetrahydrofolate dehydrogenase (NADP+) activity; IEA:InterPro.
DR   GO; GO:0035999; P:tetrahydrofolate interconversion; IEA:UniProtKB-UniPathway.
DR   CDD; cd00477; FTHFS; 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   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; 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.
PE   3: Inferred from homology;
KW   One-carbon metabolism {ECO:0000256|ARBA:ARBA00022563};
KW   Reference proteome {ECO:0000313|Proteomes:UP000261660}.
FT   DOMAIN          76..183
FT                   /note="Tetrahydrofolate dehydrogenase/cyclohydrolase
FT                   catalytic"
FT                   /evidence="ECO:0000259|Pfam:PF00763"
FT   DOMAIN          187..294
FT                   /note="Tetrahydrofolate dehydrogenase/cyclohydrolase
FT                   NAD(P)-binding"
FT                   /evidence="ECO:0000259|Pfam:PF02882"
FT   REGION          964..986
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   986 AA;  106276 MW;  81DD4077CBC3327D CRC64;
     MKLSIIRSAC GSLRIHPARS GSGVHGLSRR CVPVGPANSK LSLRPVSGTS GGGTNPKLAV
     NFGKHSPASD GLQIDSSLRE VVQSTKEAMV ALQRRNPAIQ PLLAIIQAGE DDSLLEFNKK
     MAGMIGLNLT QICLAKECSE DEIVEEVLKL NEDPRVRGIY LHLPPAALTS RVLNTLRPDK
     DVDGITDLNV GRLVRGDLSK GFVPPLASAV LDLLEKHSAP LDGKTVLLVG DEGPFSMALQ
     CLIERSGMVA LKNHWSSKSL QRKPDAVVLL GAGNMDVPST WVRPGAAIIR CVTDENDIEM
     PSKSGLGYLT AAYRTQNVVH SCSRWLQDQQ YRPWSLRSLK LQPLTPVPSD IEISRAQTPK
     PVNQLAEEIG LLPEELEAYG RSKAKVRLSL LDRLNTQPDG KYVLVAGITP TPLGEGKSTV
     TIGLVQALSA QLKLNSFACL RQPSQGPTFG VKGGAAGGGY AQVIPMEEFN LHLTGDIHAI
     TAANNLVAAA IDARMLHETT QSDKALFHRL VPSVNGVRRF SPIQISRLRR LGINKTDPAS
     LTPQEVSTFV RLDLDPSKIT WQRVLDTNDR FLRKITVGQA STEKGQIRET GFDIAVASEI
     MAILALADSL EDMKNRLSRM VVGTSRSGQP VTAEDLGVSG ALAVLMKDAI KPTLMQTLEG
     TPVFVHAGPF ANIAHGNSSV LADKLALKLV GRDGFVVTEA GFGADIGMEK FFNIKCQASG
     LRPNVVVLVA TVRALKMHGG GPNVSAGAPL PREYIDENLS LVAGGCHSNL RKQIQIAHLF
     GVPVVVALNV FKTDTQAEID QVCQIAKECG ASDAVPCHHW AQGGRGSIEL AQAVKEASSR
     PSDFKFLYHK EMPIVEKIRT IAQRVYGADD IELSPEAEAK IDYYNQQGYG SLPICMAKTH
     LSLSHMPDKK GVPTGFVLPI RDVRASIGAG FIYPLVGTMS TMPGLPTRPC FYDIDLDPVT
     EEITGSSEHP TLKKNIQDPP LFPDTF
//