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Database: UniProt
Entry: G4TRI1_SERID
LinkDB: G4TRI1_SERID
Original site: G4TRI1_SERID 
ID   G4TRI1_SERID            Unreviewed;      1011 AA.
AC   G4TRI1;
DT   14-DEC-2011, integrated into UniProtKB/TrEMBL.
DT   14-DEC-2011, sequence version 1.
DT   27-MAR-2024, entry version 50.
DE   SubName: Full=Probable MIS1-C1-tetrahydrofolate synthase, mitochondrial {ECO:0000313|EMBL:CCA73924.1};
GN   ORFNames=PIIN_07877 {ECO:0000313|EMBL:CCA73924.1};
OS   Serendipita indica (strain DSM 11827) (Root endophyte fungus)
OS   (Piriformospora indica).
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC   Sebacinales; Serendipitaceae; Serendipita.
OX   NCBI_TaxID=1109443 {ECO:0000313|EMBL:CCA73924.1, ECO:0000313|Proteomes:UP000007148};
RN   [1] {ECO:0000313|EMBL:CCA73924.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 11827 {ECO:0000313|EMBL:CCA73924.1};
RX   PubMed=22022265; DOI=10.1371/journal.ppat.1002290;
RA   Zuccaro A., Lahrmann U., Guldener U., Langen G., Pfiffi S., Biedenkopf D.,
RA   Wong P., Samans B., Grimm C., Basiewicz M., Murat C., Martin F.,
RA   Kogel K.H.;
RT   "Endophytic Life Strategies Decoded by Genome and Transcriptome Analyses of
RT   the Mutualistic Root Symbiont Piriformospora indica.";
RL   PLoS Pathog. 7:e1002290-e1002290(2011).
RN   [2] {ECO:0000313|EMBL:CCA73924.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=DSM 11827 {ECO:0000313|EMBL:CCA73924.1};
RA   MIPS;
RL   Submitted (MAY-2011) 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}.
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:CCA73924.1}.
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DR   EMBL; CAFZ01000264; CCA73924.1; -; Genomic_DNA.
DR   AlphaFoldDB; G4TRI1; -.
DR   STRING; 1109443.G4TRI1; -.
DR   eggNOG; KOG4230; Eukaryota.
DR   HOGENOM; CLU_003601_2_0_1; -.
DR   InParanoid; G4TRI1; -.
DR   OMA; QPIMFRR; -.
DR   OrthoDB; 651667at2759; -.
DR   UniPathway; UPA00193; -.
DR   Proteomes; UP000007148; 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:UP000007148}.
FT   DOMAIN          76..196
FT                   /note="Tetrahydrofolate dehydrogenase/cyclohydrolase
FT                   catalytic"
FT                   /evidence="ECO:0000259|Pfam:PF00763"
FT   DOMAIN          199..366
FT                   /note="Tetrahydrofolate dehydrogenase/cyclohydrolase
FT                   NAD(P)-binding"
FT                   /evidence="ECO:0000259|Pfam:PF02882"
SQ   SEQUENCE   1011 AA;  108781 MW;  AD8159AD8D539DF4 CRC64;
     MLTLLSLTNS SWVIVRPLYL PSKHAAVLAA AAAAQTIQDD YPLQQFQLGS EEDAYEGDRI
     VEKVVHDMSD SQAKIIDGTA IAKEIRTSVR DRIEALKKTN PTFPTPKLVI IQAGERPDST
     TYVKMKAKAC AEVGIDYAHV AMPADATAAQ IIEEVQKLNH DSSVHGILVQ MPLGENVGLE
     GERQVMESVS PMKDVDGFHA YNIGHLSSRS SEPLFTPCTP SGVIHLLTTT GFNLAGSNVV
     VLGRSDIVGN PVAAMLRKKD ATVTQCHSRT PKETMINALR NADVVVSAIG KPEYVKAEWL
     KPGTIVIDVG TNYIPDSTKK SGQRLVGDVE FSQASGVASH ITPVPGGVGP MTVAMLISNT
     LKSAERLWEK ERARKLVPLK LNVLEKVPRY ALVMDQRQFL TFHSDIEIAV AQTPKPITHL
     ATEIGIRPDE LESYGKYKAK VELSILDRLA KRKDGKYIVI SGITPTPLGE GKSTTTIGLA
     QAIGAHLGRP AFACVRQPSQ GPTFGIKGGA AGGGYSQVIP MDEFNLHLTG DIHAVSAANN
     LLAAALDARM FHESTQTDKA LYNRLVPTVK GKRAFAPLMF KRLKKLGIDK TDPNELTPEE
     INRFARLDVD PATITWNRVV DTNDRFLRKI VVGKGEAEKG FELTDLKDMR ERLGAMVVAT
     SKRGEPITAD DIGVGGALAV LMKDAIKPNL MQTLEGTPVF VHAGPFANIA HGNSSILADR
     IALKLAGTEP GETDSTREGY VLTEGGFGAD MGMEKFCNIK CRVSGLTPDA VVIVATTRAL
     KMHGGGPEVT PGKPLADTYT KEDLETLGVG IGNLERHIEN AKKFGLKVIV GVNQFSSDSS
     AELELICSRA MQAGADAAVV SNHWALGGAG AKDLAEAVVA ACEGESTFKF LYPLDIPIVD
     KISAIAKEIY RADGIELSEL ARSQVELYEK QGYGNLPICM AKTQYSFSHD PKLKGTPTGF
     TVPIRAVRLS AGAGFLYPLL GDMQTMPGLS TRPGFWEVGL DEETGRVVGL F
//
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