ID A0A0P7AFD4_9HYPO Unreviewed; 1098 AA.
AC A0A0P7AFD4;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 30.
DE SubName: Full=C-1-tetrahydrofolate synthase, cytoplasmic {ECO:0000313|EMBL:KPM35968.1};
GN ORFNames=AK830_g10592 {ECO:0000313|EMBL:KPM35968.1};
OS Neonectria ditissima.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Nectriaceae; Neonectria.
OX NCBI_TaxID=78410 {ECO:0000313|EMBL:KPM35968.1, ECO:0000313|Proteomes:UP000050424};
RN [1] {ECO:0000313|EMBL:KPM35968.1, ECO:0000313|Proteomes:UP000050424}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=R09/05 {ECO:0000313|EMBL:KPM35968.1,
RC ECO:0000313|Proteomes:UP000050424};
RA Gomez-Cortecero A., Harrison R.J., Armitage A.D.;
RT "Draft genome of a European isolate of the apple canker pathogen Neonectria
RT ditissima.";
RL Submitted (SEP-2015) 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:KPM35968.1}.
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DR EMBL; LKCW01000224; KPM35968.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0P7AFD4; -.
DR STRING; 78410.A0A0P7AFD4; -.
DR OrthoDB; 651667at2759; -.
DR UniPathway; UPA00193; -.
DR Proteomes; UP000050424; 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; 3.30.1510.10; Domain 2, N(10)-formyltetrahydrofolate synthetase; 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:UP000050424}.
FT DOMAIN 172..281
FT /note="Tetrahydrofolate dehydrogenase/cyclohydrolase
FT catalytic"
FT /evidence="ECO:0000259|Pfam:PF00763"
FT DOMAIN 286..447
FT /note="Tetrahydrofolate dehydrogenase/cyclohydrolase
FT NAD(P)-binding"
FT /evidence="ECO:0000259|Pfam:PF02882"
FT REGION 103..141
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1098 AA; 117228 MW; 7CE5FB7EC8EC55CD CRC64;
MSMMPRVYGA LGRSPLFRAP SRYAGRREFW PSTVGGGLRL EATRTVARTQ SARHSHSHTH
AQRDAHALAL AQAGSHAQAG SHALSAALSG DFRLCESPAS AVSAGRRSAA PPPARDCDDF
SDSYRRRPSS SPAATASPAL LSPRRVCTVP SSALTQRRPF TSTTAAMGAI KLDGTAIAKA
IRERLGTEIV ERQKLNPRFK PCLKIIQDTY VRMKTKAAQE AGIACELIHF SESISEPELL
DQIRQLNNDP SVNGLLVQLP LPKHISEYVI TSSVVDEKDV DGFGTKNIGE LAKRGGNPFF
VPCTPKGVMF LLNESGVDLK GKNAVVVGRS DIVGSPVSYL LRNADATVTV CHSKTVGLEN
FLKAADVVVA AIGVPQFIKG EWLKPGAVVI DVGTNFLPDE TKKSGYRLVG DVDFASAVEV
ASAITPVPGG VGPMTVAMLM QNVVDATTLY FESQKLRKTI PLPLKLQDPV PSDIAVSRGQ
TPKQITRIAA EVGIAPHELE PYGAYKAKVD LSLLNRLEHR RDGRYVVVTG ITPTPLGEGK
STTTMGLAQA LGAHIGRLTF ANVRQPSQGP TFGIKGGAAG GGYSQVIPMD EFNLHLTGDI
HAITAANNLL AAAIETRIFH ENTQKNGPLY RRLVPAKNGK RQFSPVMLRR LKKVGIDKTN
PDDLNEDEIN RFARLDIDPE TITWRRVLDV NDRHLRGITV GTAPTEKGQT RETGFDISVA
SECMAILALS TSLGDMRDRL GRMVVAASRS GDTVTCDDIG AGGALTALMK DAIKPNLMQT
LEGTPVFVHA GPFANISIGQ SSILADKLAL KLAGTEPDED YAEKAGFVVT EAGFDFTMGG
ERFFNIKCRT SGLVPDVVVV VATVRALKVH GGGPPIAPGA PLNPIYKEEN VDILRAGCVN
LKKHIANAKS FGIPVVVAIN KFSTDTDAEI AVVREEAIAA GAEDAILANH WAEGGKGAVD
LAHGVIAAST KPKELTLTYD LEGTVQERIE AIGQKMYGAA KVEFSELAQK KVDTYTRQGY
ANLPICIAKT QYSLSHDPDL KGAPTGFTVP IRDVRMAAGA GYLYALAADI QTIPGLPTAP
GYLNVDVDVE TGEIDGLF
//
