ID A0A175VYW0_9PEZI Unreviewed; 939 AA.
AC A0A175VYW0;
DT 07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT 07-SEP-2016, sequence version 1.
DT 27-MAR-2024, entry version 30.
DE SubName: Full=C-1-tetrahydrofolate synthase, cytoplasmic {ECO:0000313|EMBL:KXX76371.1};
GN ORFNames=MMYC01_207538 {ECO:0000313|EMBL:KXX76371.1};
OS Madurella mycetomatis.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Sordariomycetidae; Sordariales; Sordariales incertae sedis; Madurella.
OX NCBI_TaxID=100816 {ECO:0000313|EMBL:KXX76371.1, ECO:0000313|Proteomes:UP000078237};
RN [1] {ECO:0000313|Proteomes:UP000078237}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=mm55 {ECO:0000313|Proteomes:UP000078237};
RA van de Sande W.W.J.;
RL Submitted (JUN-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KXX76371.1, ECO:0000313|Proteomes:UP000078237}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=mm55 {ECO:0000313|Proteomes:UP000078237};
RA Van De Sande W.;
RT "Madurella mycetomatis genome sequencing.";
RL Submitted (JAN-2016) 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:KXX76371.1}.
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DR EMBL; LCTW02000214; KXX76371.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A175VYW0; -.
DR STRING; 100816.A0A175VYW0; -.
DR VEuPathDB; FungiDB:MMYC01_207538; -.
DR OrthoDB; 651667at2759; -.
DR UniPathway; UPA00193; -.
DR Proteomes; UP000078237; 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; 3.10.410.10; 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:UP000078237}.
FT DOMAIN 6..122
FT /note="Tetrahydrofolate dehydrogenase/cyclohydrolase
FT catalytic"
FT /evidence="ECO:0000259|Pfam:PF00763"
FT DOMAIN 127..289
FT /note="Tetrahydrofolate dehydrogenase/cyclohydrolase
FT NAD(P)-binding"
FT /evidence="ECO:0000259|Pfam:PF02882"
SQ SEQUENCE 939 AA; 100432 MW; 41CF00847CA7FE98 CRC64;
MAAAKIDGTA IARKVRERLQ AEIAEKKGIN PRFQPCLKII QVGDRSDSST YVRMKLKAAE
EVGISCELIK FNETATESEL VARVHALNND PAVHGILVQL PLPQHVSEYA VTSAVASEKD
VDGFGTHNIG ELAKRGGRPF YIPCTPKGVM VLLSEAGVKL KGKNAVVVGR SDIVGSPVSY
LLKNADATVT VCHSKTQDLE HHLKNADVLV VAIGKPGFIR GEQLKPGVVV IDVGTNYIPD
ATKKSGQRLV GDVDFESASQ VASFITPVPG GVGPMTVAML LQNVVDAATF SFDAEKQRHI
VPLTLTLLDP VPSDIAISRA QAPKHVTQIA KEIGISNSEL EPYGAYKAKV DLSILKRLGH
RRDGRYVVVT GITPTPLGEG KSTTTMGLAQ ALGAHVGRLT FANVRQPSQG PTFGIKGGAA
GGGYSQVIPM DEFNMHLTGD IHAITAANNL LAAAIDTRMF HESTQKDTAL YKRLVPVKNG
KRVFAPVMLR RLKKLGIDKT DPNELTEDEI RRFARLDIDP ATITWRRVLD VNDRHLRGIV
IGNAPTEKGH SRETGFDISV ASECMAILAL STSLADLRER LGRMVVASSR SGDPVTCDDI
GAGGALTALM RDAIKPNLMQ SLEGTPVFVH AGPFANISIG NSSILADKMA LKLAGTEPDE
DYASKAGFVV TEAGFDFTMG GERFFNIKCR TSGLVPDVVV VVATIRALKV HGGGPPISPG
APLDVVYREE NVEVLRKGCV NLAKHIANAK TYGVPVVVAV NKFSTDTQAE IDVVREEAVK
AGAEDAVLAN HWAEGGKGAV DLANAVIAAA EKPKDFKLLY DLEGTVQERL ERIAREMYGA
TAVEFSDLAQ KKIDTYTRQG FGKLPICIAK TQYSLSHDPE LKGAPTGFTV PIRDVRMAAG
AGYLYALAAD IQTIPGLPTA PGYLNVDIDL ETGEIDGLF
//
