ID A0A061HDI8_BLUGR Unreviewed; 886 AA.
AC A0A061HDI8;
DT 03-SEP-2014, integrated into UniProtKB/TrEMBL.
DT 03-SEP-2014, sequence version 1.
DT 27-MAR-2024, entry version 34.
DE SubName: Full=Bgt-1197 {ECO:0000313|EMBL:SUZ12616.1};
DE SubName: Full=Mitochondrial C1-tetrahydrofolate synthase {ECO:0000313|EMBL:EPQ62700.1};
DE Flags: Fragment;
GN ORFNames=BGT96224_1197 {ECO:0000313|EMBL:EPQ62700.1},
GN BGT96224V2_LOCUS5779 {ECO:0000313|EMBL:SUZ12616.1};
OS Blumeria graminis f. sp. tritici 96224.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC Erysiphales; Erysiphaceae; Blumeria.
OX NCBI_TaxID=1268274 {ECO:0000313|EMBL:SUZ12616.1};
RN [1] {ECO:0000313|Proteomes:UP000053110}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=96224 {ECO:0000313|Proteomes:UP000053110};
RX PubMed=23852167; DOI=10.1038/ng.2704;
RA Wicker T., Oberhaensli S., Parlange F., Buchmann J.P., Shatalina M.,
RA Roffler S., Ben-David R., Dolezel J., Simkova H., Schulze-Lefert P.,
RA Spanu P.D., Bruggmann R., Amselem J., Quesneville H.,
RA Ver Loren van Themaat E., Paape T., Shimizu K.K., Keller B.;
RT "The wheat powdery mildew genome shows the unique evolution of an obligate
RT biotroph.";
RL Nat. Genet. 45:1092-1096(2013).
RN [2] {ECO:0000313|EMBL:EPQ62700.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=96224 {ECO:0000313|EMBL:EPQ62700.1};
RA Oberhaensli S., Wicker T., Keller B.;
RT "The wheat powdery mildew genome reveals unique evolution of an obligate
RT biotroph.";
RL Submitted (JAN-2013) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|EMBL:SUZ12616.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=96224 {ECO:0000313|EMBL:SUZ12616.1};
RA Quirk P.G., Krulwich T.A.;
RL Submitted (JUL-2018) 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; KE375166; EPQ62700.1; -; Genomic_DNA.
DR EMBL; UIGY01000194; SUZ12616.1; -; Genomic_DNA.
DR HOGENOM; CLU_003601_2_0_1; -.
DR OrthoDB; 651667at2759; -.
DR UniPathway; UPA00193; -.
DR Proteomes; UP000053110; Unassembled WGS sequence.
DR GO; GO:0005739; C:mitochondrion; IEA:EnsemblFungi.
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:0046656; P:folic acid biosynthetic process; IEA:EnsemblFungi.
DR GO; GO:0006139; P:nucleobase-containing compound metabolic process; IEA:EnsemblFungi.
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; 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};
KW Reference proteome {ECO:0000313|Proteomes:UP000053110}.
FT DOMAIN 1..69
FT /note="Tetrahydrofolate dehydrogenase/cyclohydrolase
FT catalytic"
FT /evidence="ECO:0000259|Pfam:PF00763"
FT DOMAIN 74..237
FT /note="Tetrahydrofolate dehydrogenase/cyclohydrolase
FT NAD(P)-binding"
FT /evidence="ECO:0000259|Pfam:PF02882"
FT NON_TER 886
FT /evidence="ECO:0000313|EMBL:SUZ12616.1"
SQ SEQUENCE 886 AA; 94922 MW; 2315724999F0F3BD CRC64;
MKLKAAEEAS IECEIIRFPV TTTETELLNK ISQLNNDFSV HGILVQLPVP EHISEYAVTS
AVSEDKDVDG FGANNIGELA KRGGKPLFTP CTPKGVMVLL QESGINLKGK NAVVLGRSDI
VGNPVSYLLR RADATVTVCH RETQNLEEHL KNADVLVSAV GKPQFVKGEW LKPGVVVIDV
GTNFIPCESK KAGRQLVGDI DFDSASKVAS KITPVPGGVG PMTIAMLLQN VVDAARRSYD
EQISRSIKPL PLILKTPVPS DIAISRSQQP KKINNVAAEI GIAGHELEPY GAHKAKVSLD
VLKRLGHRKN GRFVVVTGIT PTPLGEGKST TTMGIAQALG AHLNRVAFAN VRQPSQGPTF
GIKGGAAGGG YSQVIPMDEF NLHLTGDIHA ITAANNLLAA AIETRMFHEN TQSDAALYKR
LVPSKKGKRQ FTPIMFRRLK KLGINQENPD KLTTDEIRKF ARLDIEPSTI TWRRVLDVND
RHLRGVTVGT AATEKGQSRE TGFDISVASE CMAILALSSD LNDMRERLGR MVIGFSRQGD
PVTCDDIGAG GALTALMKDA IKPNLMQTME GTPVFVHAGP FANISIGASS VLADKIALKL
AGTELDENHN EKAGFVITEA GFDFTMGGER FFNIKCRSSG LVPDVVVIVA TVRALKVHGG
GPPIVPGAAL NKVYAQENVE ILRTGCVNLR KHISNAKIYG VPVVVAINKF ETDTDAEIQV
IREESIAAGA EDAIPANHWA EGGKGAIELS KGIIAACEKE KDFKLLYSLD GSVQSRIEAI
GQKMYGAASV EFSEIAQKKV DMYTSQGFGN LPICIAKTQY SLSHDPDLKG APTGFTVPIR
DVRLAAGAGY LYALAADIQT IPGLPTAPGY LNVDVDTETG EIDGLF
//
