ID A0A401GIY1_9APHY Unreviewed; 947 AA.
AC A0A401GIY1;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 27-MAR-2024, entry version 19.
DE SubName: Full=C-1-tetrahydrofolate synthase, cytoplasmic {ECO:0000313|EMBL:GBE82083.1};
GN ORFNames=SCP_0404620 {ECO:0000313|EMBL:GBE82083.1};
OS Sparassis crispa.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Polyporales; Sparassidaceae; Sparassis.
OX NCBI_TaxID=139825 {ECO:0000313|EMBL:GBE82083.1, ECO:0000313|Proteomes:UP000287166};
RN [1] {ECO:0000313|EMBL:GBE82083.1, ECO:0000313|Proteomes:UP000287166}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=30375506; DOI=10.1038/s41598-018-34415-6;
RA Kiyama R., Furutani Y., Kawaguchi K., Nakanishi T.;
RT "Genome sequence of the cauliflower mushroom Sparassis crispa
RT (Hanabiratake) and its association with beneficial usage.";
RL Sci. Rep. 8:16053-16053(2018).
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:GBE82083.1}.
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DR EMBL; BFAD01000004; GBE82083.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A401GIY1; -.
DR STRING; 139825.A0A401GIY1; -.
DR InParanoid; A0A401GIY1; -.
DR OrthoDB; 651667at2759; -.
DR UniPathway; UPA00193; -.
DR Proteomes; UP000287166; Unassembled WGS sequence.
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:SF5; 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; 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:UP000287166}.
FT DOMAIN 12..131
FT /note="Tetrahydrofolate dehydrogenase/cyclohydrolase
FT catalytic"
FT /evidence="ECO:0000259|Pfam:PF00763"
FT DOMAIN 134..299
FT /note="Tetrahydrofolate dehydrogenase/cyclohydrolase
FT NAD(P)-binding"
FT /evidence="ECO:0000259|Pfam:PF02882"
SQ SEQUENCE 947 AA; 101249 MW; 3831B8573A6B4556 CRC64;
MSSAATGNAK IIDGTAIAKS IRDDVSQRIK SLQSQHPRFH PQLAIVQAGA RPDSSVYVRM
KAKAAEEVGI KFKHIPLSAE ADVDDVVDVV KQLNDDITVS GILVQLPLGG HVGPEGERTV
TEAVSPEKDV DGFHAYNIGH LSSRASEPLF TPCTPAGVVR LLESTGVPIA GSRAVVLGRS
DIVGSPVAAI LRNRDATVTQ CHSRTKNLPE IVKEGDIVIS AIGQPEFVQG SWLKPGAVVI
DVGTNYIPDA TKKSGRRLVG DVHFSSASSV ASYITPVPGG VGPMTVAMLM SNTLKSAERM
WERMHGVHLK PLKLDIKEKV PSDIEIAMAQ TPKPVVHLAR EIGLVPDELE SYGKYKAKVE
LSVLERLAHR KDGKYIVISG ITPTPLGEGK STTTIGLAQA LGAHLGRPAF ACVRQPSQGP
TFGIKGGAAG GGYSQVIPMD EFNLHLTGDI HAVTAANNLL AAALDARMFH ESTQSDKALY
SRLVPSKKGK REFAPLMLKR LKKLGIDKTN PNDLTPEEIT RFSRLDVDPD TITWNRVIDV
NDRFLRKITI GQGESERGHE RVTGFDISVA SECMAVLALT TGLSDMRERL GEMVVATSKQ
GDPITADDIG VGGALAVLMK DAIKPNLMQT LEGTPVFVHA GPFANIAHGN SSILADRVAL
KLAGTEEGDS PDRVGYVLTE GGFGADMGME KFCNIKCRVS GLTPNAVVIV ATTRALKMHG
GGPDVTPGKP LHETYTKEDL VTLKEGCKNL VKHIENSRKF GLKVIVAINQ FSSDTPAELE
LVRLESLAGG ADAAVVSNHW AEGGAGAKAL AEAVIAACEG PSNFKFLYDL NLPIEEKITI
ICRDIYGADG IELSEQARKQ IETYTRQGYS HLPICMAKTQ YSFSHDPKLK GVPTGFTVPI
RAIRLSAGAG FLYPILGDMQ TMPGLGTRPG FWEVGLDPVT GRVVGLF
//
