ID M7X4L7_RHOT1 Unreviewed; 1010 AA.
AC M7X4L7;
DT 29-MAY-2013, integrated into UniProtKB/TrEMBL.
DT 29-MAY-2013, sequence version 1.
DT 27-MAR-2024, entry version 44.
DE SubName: Full=C-1-tetrahydrofolate synthase {ECO:0000313|EMBL:EMS25261.1};
GN ORFNames=RHTO_02988 {ECO:0000313|EMBL:EMS25261.1};
OS Rhodotorula toruloides (strain NP11) (Yeast) (Rhodosporidium toruloides).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Pucciniomycotina;
OC Microbotryomycetes; Sporidiobolales; Sporidiobolaceae; Rhodotorula.
OX NCBI_TaxID=1130832 {ECO:0000313|EMBL:EMS25261.1, ECO:0000313|Proteomes:UP000016926};
RN [1] {ECO:0000313|EMBL:EMS25261.1, ECO:0000313|Proteomes:UP000016926}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NP11 {ECO:0000313|EMBL:EMS25261.1,
RC ECO:0000313|Proteomes:UP000016926};
RX PubMed=23047670; DOI=10.1038/ncomms2112;
RA Zhu Z., Zhang S., Liu H., Shen H., Lin X., Yang F., Zhou Y.J., Jin G.,
RA Ye M., Zou H., Zou H., Zhao Z.K.;
RT "A multi-omic map of the lipid-producing yeast Rhodosporidium toruloides.";
RL Nat. Commun. 3:1112-1112(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; KB722643; EMS25261.1; -; Genomic_DNA.
DR RefSeq; XP_016276380.1; XM_016416660.1.
DR AlphaFoldDB; M7X4L7; -.
DR GeneID; 27367001; -.
DR eggNOG; KOG4230; Eukaryota.
DR HOGENOM; CLU_003601_2_0_1; -.
DR OrthoDB; 651667at2759; -.
DR UniPathway; UPA00193; -.
DR Proteomes; UP000016926; 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; 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 73..195
FT /note="Tetrahydrofolate dehydrogenase/cyclohydrolase
FT catalytic"
FT /evidence="ECO:0000259|Pfam:PF00763"
FT DOMAIN 198..363
FT /note="Tetrahydrofolate dehydrogenase/cyclohydrolase
FT NAD(P)-binding"
FT /evidence="ECO:0000259|Pfam:PF02882"
FT REGION 43..63
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 46..63
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1010 AA; 107771 MW; DC14E2676700C033 CRC64;
MLARSHQVAL RAAQSSTRTL ARTAVASLSQ RAFTAGTASL SPLPRRLTPL RSSPSPSRSL
ATMAEQNQGA KLIDGNAIAA SLRQGIAARI AETRARFPRF EPTLVIVQQG ARPDSSTYVK
MKLKAAAEAG IKCTLVQLGG PEDGVGENEV MAEVERLNAD DNVHGIIVQL PLSDEIGRDG
ERRITEAVSP EKDVDGFHAY NIGLLSSRAS EPLFAPCTPA GVMLLLESTG IEISGKNAVV
LGRSDIVGSP VCALLRRKDA TVTQCHSRTK NLADIVRQAD IVVAAIGQAR FVQGDWIKPG
AVVIDVGTNY IADSTRKSGS RLVGDVDFDS ARQVASYITP VPGGVGPMTV AMLMENTVLS
AQRLLEKSQQ RLVKPLKLVC KEKVPSDIEI AKSQVPKPID VLAAEIGIPA KDLELYGRNK
AKVKLEVLDS LRHRKDGKYI VVAGITPTPL GEGKSTTTIG LAQALGAHLG KAAYACVRQP
SQGPTFGIKG GAAGGGYSQV IPMDEFNLHL TGDIHATTAA NNLLAAAISA RYFHESTQSD
KALFSRLCPP KKGVRSFSPV MIKRLEKLGI DKRNPDDLTE EERSAFVRLD IDPEKISWHR
VLDTNDRYLR KVMTGLGPAE QGKTLETGFD IAVASECMAV LALATSLGDM RDRLGRMVVA
ESKSGVPITC DDIGATNSLA ILMKDAIKPN IMQTLEGTPV FVHAGPFANI AHGNSSILAD
KIALKLAGIE EGEEEDKNGY VITEAGFGAD IGMEKFVNIK CRASGLIPNA VVLVATIRAL
KMHGGGPEVT PGKPLPEVYL NEDLEILKSG CANLARHIEN AKKVGVKVIV AVNRFTSDTP
AEIKLVQEQA LAAGADAAVP CNHWAEGGKG AIELGEAVIQ ACKEPNPFKF LYDVNLPIKD
KIEIIAKEFY GAAAVEYSEL AESQIKSFEE TGYGKLPICM AKTHLSFSAD PKLKGAPSGF
TIPIREARLS AGSGFIYPLV GEMSTMPGLA TRPIFFDHRL LDDGEIIGLS
//
