ID A0A197KEE2_9FUNG Unreviewed; 937 AA.
AC A0A197KEE2;
DT 05-OCT-2016, integrated into UniProtKB/TrEMBL.
DT 05-OCT-2016, sequence version 1.
DT 27-MAR-2024, entry version 33.
DE SubName: Full=FTHFS-domain-containing protein {ECO:0000313|EMBL:OAQ35538.1};
GN ORFNames=K457DRAFT_13453 {ECO:0000313|EMBL:OAQ35538.1};
OS Linnemannia elongata AG-77.
OC Eukaryota; Fungi; Fungi incertae sedis; Mucoromycota; Mortierellomycotina;
OC Mortierellomycetes; Mortierellales; Mortierellaceae; Linnemannia.
OX NCBI_TaxID=1314771 {ECO:0000313|EMBL:OAQ35538.1, ECO:0000313|Proteomes:UP000078512};
RN [1] {ECO:0000313|EMBL:OAQ35538.1, ECO:0000313|Proteomes:UP000078512}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AG-77 {ECO:0000313|EMBL:OAQ35538.1,
RC ECO:0000313|Proteomes:UP000078512};
RG DOE Joint Genome Institute;
RA Uehling J., Gryganskyi A., Hameed K., Tschaplinski T., Misztal P., Wu S.,
RA Desiro A., Vande Pol N., Du Z.-Y., Zienkiewicz A., Zienkiewicz K.,
RA Morin E., Tisserant E., Splivallo R., Hainaut M., Henrissat B., Ohm R.,
RA Kuo A., Yan J., Lipzen A., Nolan M., Labutti K., Barry K., Goldstein A.,
RA Labbe J., Schadt C., Tuskan G., Grigoriev I., Martin F., Vilgalys R.,
RA Bonito G.;
RT "Genome sequencing reveals origins of a unique bacterial endosymbiosis in
RT the earliest lineages of terrestrial Fungi.";
RL Submitted (MAY-2016) to the EMBL/GenBank/DDBJ databases.
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; KV442014; OAQ35538.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A197KEE2; -.
DR STRING; 1314771.A0A197KEE2; -.
DR OrthoDB; 651667at2759; -.
DR UniPathway; UPA00193; -.
DR Proteomes; UP000078512; 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; 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};
KW Reference proteome {ECO:0000313|Proteomes:UP000078512}.
FT DOMAIN 5..121
FT /note="Tetrahydrofolate dehydrogenase/cyclohydrolase
FT catalytic"
FT /evidence="ECO:0000259|Pfam:PF00763"
FT DOMAIN 124..287
FT /note="Tetrahydrofolate dehydrogenase/cyclohydrolase
FT NAD(P)-binding"
FT /evidence="ECO:0000259|Pfam:PF02882"
SQ SEQUENCE 937 AA; 100939 MW; FA10B7C898AAE756 CRC64;
MAKVIDGKAI AQNLRNDIKS QIEEMRKTNP HFNPKLSIIQ VGAREDSSVY VNMKKKAAKE
AGMDFELFHL PPTITQFELL SKVQALNNDP KVHGILVQLP LPDHLDDRIV TEAIDPKKDV
DGFHAINIGH LSKRASEPAF VPCTPKGVIE LIKSTGVTMS GKKAVVVGRS DIVGTPVFSL
LTKNNCTVTL CHSKTTNLAE VVKTADILVV AIGSAEFVKG DWIKEGAVVI DVGTNAVEDA
TKKSGIRWVG DVEYNAASTH ASHITPVPGG VGPMTVAMLM QNTYLSAVRF FNESRQRAIV
PLPLELLEPV PSDIAIALAQ KPKPIKFIAE ELGLLPNELE LYGEYKAKVS LDILERLSHR
QNGRYVVVTG ITPTPLGEGK STTTVGLVQA LGAHLNKIAF GCVRQPSQGP TFGIKGGAAG
GGYSQVIPMD EFNLHLTGDI HAVTAANNLL AAAIDARMFH ENTQTDKALF SRLCPTKKGK
RTFAPVMLGR LERLGINKTD PAELTPEEIT RFARLDIDPA TITWQRVMDT NDRFLRKIEI
GRNDTEAGHE RMTGFDIAVA SEVMAVLALS TDLKDMRERL GKMVIASSKG GEPVTADDIG
IGGALTVLMK DAIKPNVMQT LEGTPMFVHA GPFANIAHGN SSIIADRIAL KLAGIEAGEG
EDKMGYVVTE AGFGADIGME KFFDIKCRTS GLVPDCAVLV ATVKALKMHG GGPEVTPGKP
LPEVYNTENL ELLETGCDNL RKHIENAKKF GVPVVVAINR FTTDSDAEMA LIRKIALEAG
ADDAVACENW AKGGLGAVDL GQAVIQSCSK PTAFKYLYDV GADIESKIET IAKEMYGADG
IELSDLAKEK IATYTRQGFG NLPICMAKTH LSLSHDPKLK NRPTGFKIPI RDIRASVGAG
FLYPLCGAMQ TMPGLPTRPC FYDVDIDFNT GNVVGLF
//
