ID A0A1X6NA66_9APHY Unreviewed; 945 AA.
AC A0A1X6NA66;
DT 05-JUL-2017, integrated into UniProtKB/TrEMBL.
DT 05-JUL-2017, sequence version 1.
DT 27-MAR-2024, entry version 26.
DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:OSX65539.1};
GN ORFNames=POSPLADRAFT_1134916 {ECO:0000313|EMBL:OSX65539.1};
OS Postia placenta MAD-698-R-SB12.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Polyporales; Postiaceae; Postia.
OX NCBI_TaxID=670580 {ECO:0000313|EMBL:OSX65539.1, ECO:0000313|Proteomes:UP000194127};
RN [1] {ECO:0000313|EMBL:OSX65539.1, ECO:0000313|Proteomes:UP000194127}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MAD-698-R-SB12 {ECO:0000313|EMBL:OSX65539.1,
RC ECO:0000313|Proteomes:UP000194127};
RG DOE Joint Genome Institute;
RA Gaskell J., Kersten P., Larrondo L.F., Canessa P., Martinez D., Hibbett D.,
RA Schmoll M., Kubicek C.P., Martinez A.T., Yadav J., Master E.,
RA Magnuson J.K., James T., Yaver D., Berka R., Labutti K., Lipzen A.,
RA Aerts A., Barry K., Henrissat B., Blanchette R., Grigoriev I., Cullen D.;
RT "Genome Sequence of the Model Brown-Rot Fungus Postia placenta SB12.";
RL Submitted (APR-2017) 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; KZ110593; OSX65539.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1X6NA66; -.
DR STRING; 670580.A0A1X6NA66; -.
DR OrthoDB; 651667at2759; -.
DR UniPathway; UPA00193; -.
DR Proteomes; UP000194127; 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:UP000194127}.
FT DOMAIN 10..129
FT /note="Tetrahydrofolate dehydrogenase/cyclohydrolase
FT catalytic"
FT /evidence="ECO:0000259|Pfam:PF00763"
FT DOMAIN 132..297
FT /note="Tetrahydrofolate dehydrogenase/cyclohydrolase
FT NAD(P)-binding"
FT /evidence="ECO:0000259|Pfam:PF02882"
SQ SEQUENCE 945 AA; 100453 MW; 8FE3A0BA592CB3F8 CRC64;
MATVGCAKII DGNAIAKSIR EEVAARIRSL QAQHSRFQPQ LAIIQAGARP DSAVYVRMKA
KAAEEVGIKF KHVSIPAESD VDEVVELVKK LNDDVSISGI LVQLPLGDHV GADGERTVTE
AVSPEKDVDG FHAYNIGHLS SRASDPLFTP CTPTGVIRLL ESTGVSISGA QAVVLGRSDI
VGSPVAAMLR NRDATVTQCH SRTKNLPEIV KTADIVVSAI GKPEFVQGSW LKPGAVVIDV
GTNYIPDATK KSGQRLVGDV NFASASAVAS HITPVPGGVG PMTVAMLMAN TLRSAERLWE
RARGLKLKPL KLDVKEKVPS DIEIAMAQTP KPVTQLAHEI GLLPDELESY GKYKAKVELS
VLDRLAHRKD GKYIIISGIT PTPLGEGKST TTIGLAQALG AHLGRPAFAC VRQPSQGPTF
GIKGGAAGGG YSQVIPMDEF NLHLTGDIHA VTAANNLLAA ALDARMFHEA TQSDKALYSR
LVPAKKGKRE FAPLMFKRLA KLGIDKTDPN DLTPEEIKRF ARIDVDPATI TWNRVLDVND
RFLRKITVGQ APSEQGHERV AGFDISVASE CMAVLALTTG LEDMRERLGA MVVATSKQGD
PITADDIGVG GALAVLMKDA VKPNLMQTLE GTPVFVHAGP FANIAHGNSS ILADRVALKL
AGTEEGDSAD RVGYVLTEGG FGADMGMEKF CNIKCRVSGL KPDATIIVAT TRALKMHGGG
PDVTPGKPLA DTYTKEDLVT LKEGCKNLVK HIENSRKFGL KVIVAINQFA SDTPAELELV
RQESLAGGAD AAVVSNHWAE GGPGARALAE AVIATCEGES GFKYLYDLDL PIVDKISSIC
KEIYGADGIE LSELAQKQIE TYTRQGFGNL AICMAKTQYS FSHDPKLKGV ATGFTVPIRE
VRLSAGAGFL YPLCGDMQTM PGLGTRPGFW EVGLDPATGR VVGLF
//
