ID A0A2P5I4U3_9PEZI Unreviewed; 1106 AA.
AC A0A2P5I4U3;
DT 23-MAY-2018, integrated into UniProtKB/TrEMBL.
DT 23-MAY-2018, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE SubName: Full=Formate-tetrahydrofolate ligase {ECO:0000313|EMBL:POS77532.1};
GN ORFNames=DHEL01_v204083 {ECO:0000313|EMBL:POS77532.1};
OS Diaporthe helianthi.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Sordariomycetidae; Diaporthales; Diaporthaceae; Diaporthe.
OX NCBI_TaxID=158607 {ECO:0000313|EMBL:POS77532.1, ECO:0000313|Proteomes:UP000094444};
RN [1] {ECO:0000313|EMBL:POS77532.1, ECO:0000313|Proteomes:UP000094444}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=7/96 {ECO:0000313|EMBL:POS77532.1,
RC ECO:0000313|Proteomes:UP000094444};
RA Baroncelli R.;
RT "Polyketide synthases of a Diaporthe helianthi virulent isolate.";
RL Submitted (SEP-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}.
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:POS77532.1}.
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DR EMBL; MAVT02000262; POS77532.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2P5I4U3; -.
DR STRING; 158607.A0A2P5I4U3; -.
DR InParanoid; A0A2P5I4U3; -.
DR OrthoDB; 651667at2759; -.
DR UniPathway; UPA00193; -.
DR Proteomes; UP000094444; 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 Ligase {ECO:0000313|EMBL:POS77532.1};
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:UP000094444}.
FT DOMAIN 172..288
FT /note="Tetrahydrofolate dehydrogenase/cyclohydrolase
FT catalytic"
FT /evidence="ECO:0000259|Pfam:PF00763"
FT DOMAIN 292..455
FT /note="Tetrahydrofolate dehydrogenase/cyclohydrolase
FT NAD(P)-binding"
FT /evidence="ECO:0000259|Pfam:PF02882"
FT REGION 1..39
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1106 AA; 118359 MW; 993513A54CB0137E CRC64;
MASMLSRTSS RGDLAMQPHL SLQRSHQRLQ QAPTRRSGLC TGSSWHVLPI SCRCSHRGLW
ASNSGPDSAC VNDRHRAEAY PDQPSARPAV PPAPPAAPIG ITTTLFSAGP ITPRHFLTST
ASSTSPFPLV LKSRRTTLAS CTLRSLSFGS DSLDPGKASF STSSPVMTAQ KIDGTAIAKS
IRARLHSEIA ERKTANPKYI PSLKIIQVGD RSDSSTYVRM KLKAAEEAGI SCELIHLPTD
ISEAELLQEI YKLNNDTSVH GILVQLPVPD HISEYAVTSA VIAEKDVDGF GPDNTGELAK
RTGHPLFTPC TPKGVMVLLR ESGVDLKGKN AVVVGRSDIV GAPVSYLLRH ADATVTVCHS
KSLDLDSHLK QADVVVAALG KPAFIKGSSL KPGVVVIDVG TNYIPDSTKK SGQRLTGDVE
FESASEVASF ITPVPGGVGP MTVAMLLENV VESCTHYFEK QKNRKIVALP LKLKEPVPSD
IAVSRAQTPK QITRVADEIG IAPGELEPYG AHKAKVDLSL LKRLDHRRNG KYVVVTGITP
TPLGEGKSTT TMGLAQALGA HVGRLTFANV RQPSQGPTFG IKGGAAGGGY SQVIPMDEFN
MHLTGDIHAI TAANNLLAAA IETRIFHENT QKDGPLYKRL VPAKNGKRVF APVMFRRLKK
LGIDKTNPDE LTEDEIHRFA RLDIDPETIT WRRVLDVNDR HLRGITVGTA ATEKGQTRET
GFDISVASEC MAILALSTDL KDMRERLGRM VVATSRNGDP VTCDDLGAGG ALTALMKDAI
KPNLMQSLEG TPVFVHAGPF ANISIGNSSI LADKMALKLV GTEPDEEHEV KAGFVVTEAG
FDFTMGGERF FNIKCRTSGL VPDVVVVVAT VRALKVHGGG PPIAPGAALP QVYREENVDV
LRKGCVNLKK HIENACSYGV PVVVAINKFV TDTDAEIAVI REEAIAAGAE DAILSNHWAE
GGKGAIQLAE GVIAASQKPK DFKLLYELEG NTIQERIEAI AKKMYGADAV QFSELAQKKV
DTYTKQGFGN LPICVAKTQY SLSHDPELKG APTGFTVPIR DVRMAAGAGY LYALAADIQT
IPGLPTAPGY LNVDVDEETG EIDGLF
//
