ID J3S6Y4_CORMI Unreviewed; 1077 AA.
AC J3S6Y4;
DT 31-OCT-2012, integrated into UniProtKB/TrEMBL.
DT 31-OCT-2012, sequence version 1.
DT 27-MAR-2024, entry version 37.
DE SubName: Full=C-1-tetrahydrofolate synthase {ECO:0000313|EMBL:AFK23399.1};
GN Name=CMN3 {ECO:0000313|EMBL:AFK23399.1};
OS Cordyceps militaris (Caterpillar fungus) (Clavaria militaris).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Cordycipitaceae; Cordyceps.
OX NCBI_TaxID=73501 {ECO:0000313|EMBL:AFK23399.1};
RN [1] {ECO:0000313|EMBL:AFK23399.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=HMAS1630 {ECO:0000313|EMBL:AFK23399.1};
RA Aranguren L.F., Tang K.;
RT "Characterization of a highly pathogenic TSV isolate from Colombia.";
RL Submitted (JUN-2011) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:AFK23399.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=HMAS1630 {ECO:0000313|EMBL:AFK23399.1};
RX PubMed=22889355; DOI=10.1111/j.1574-6968.2012.02658.x;
RA Wang W.J., Vogel H., Yao Y.J., Ping L.;
RT "The nonribosomal peptide and polyketide synthetic gene clusters in two
RT strains of entomopathogenic fungi in Cordyceps.";
RL FEMS Microbiol. Lett. 336:89-97(2012).
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 EMBL; JN121123; AFK23399.1; -; Genomic_DNA.
DR AlphaFoldDB; J3S6Y4; -.
DR VEuPathDB; FungiDB:A9K55_008314; -.
DR UniPathway; UPA00193; -.
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; 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; 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 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}.
FT DOMAIN 145..260
FT /note="Tetrahydrofolate dehydrogenase/cyclohydrolase
FT catalytic"
FT /evidence="ECO:0000259|Pfam:PF00763"
FT DOMAIN 265..426
FT /note="Tetrahydrofolate dehydrogenase/cyclohydrolase
FT NAD(P)-binding"
FT /evidence="ECO:0000259|Pfam:PF02882"
FT REGION 78..103
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1077 AA; 114399 MW; 5BE39EAB72B24276 CRC64;
MFRRNQASAA ARAVCRKPGL STGRLMSSCF IKVAPSPTAS SPSSAAIAGR HASYPRALSN
RSCSAAAARQ FSAAATGSTP LFTTKRSSPP AAPPAPHCPA SSTFSSRRPL LLASPSALLP
LPFSAHRGTG RFFSTTSAAM VATKLDGTAI AKSIRERIGR EIAERQKLNP RYRPSLKIVQ
GMNLPPRAEI VLCFGRINDA NIDCELISLP ESITEPEILD LIRRLNHNPS VNGILVQLPI
PAHLSEYAVT SAVADEKDVD GFGTNNIGEL AKRGGTPIFT PCTPKGVMHL LKEAGVNLVG
KYAVVIGRSN IVGSPVSYLL RNADATVTVC HSKTAGLENH IKAADIVIAA IGSPHFVKGE
WIKEGAIVID VGTNFIPDAS KKSGQRLVGD VEYESAAKVA SIITPVPGGV GPMTVAMLLE
NVVEATNVFF ENEKLRKTVP LPLKLLDPVP SDIAISRAQT PKQITRIASE VGIAPHELEP
YGAYKAKVDL GLLERLQHRK NGRYVVVTGI TPTPLGEGKS TTTMGIAQAL GAHLGRVTFA
NVRQPSQGPT FGIKGGAAGG GYSQVIPMDE FNMHLTGDIH AITAANNLLA AGIETRIFHE
NSQKDAALYR RLVPAKNGVR KFAPIMFRRL KKLGIHKTNP DDLTEEEIGR FARLDIDPET
ITWRRVLDVN DRHLRGITIG TAPTEKGQTR ETGFDISVAS ECMAILALST SLADMRERLG
RMVVATSRKG DPVTCDDIGA GGALTALMKD AIKPNLMQTL EGTPVFVHAG PFANISIGQS
SIIADRLALK LAGTEPDEDV SDKAGFVVTE AGFDFTMGGE RFFNIKCRAS GLVPDVVVVV
ATVRALKVHG GGPPIAPGAP LNAIYREENV DILRAGCVNL KKHIANAKSF GVPVVVAINK
FATDTDAEIE VLREEAIAAG AEDAILSDHW AKGGVGAVDL AKGVIAASEK PKKLTLTYDL
DGTVQERIEA IGKKMYGAAA VEFSELAQKK VDTYTKQGYG NLPICIAKTQ YSLSHDPDLK
GAPTGFTIPI RDVRMAAGAG YLYALAADIQ TIPGLPTAPG YLNVDVDLET GEIDGLF
//
