ID A0A0L1JF79_ASPNO Unreviewed; 1042 AA.
AC A0A0L1JF79;
DT 11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT 11-NOV-2015, sequence version 1.
DT 27-MAR-2024, entry version 30.
DE SubName: Full=Formyltetrahydrofolate synthetase {ECO:0000313|EMBL:KNG90008.1};
GN ORFNames=ANOM_001181 {ECO:0000313|EMBL:KNG90008.1};
OS Aspergillus nomiae NRRL 13137.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX NCBI_TaxID=1509407 {ECO:0000313|EMBL:KNG90008.1, ECO:0000313|Proteomes:UP000037505};
RN [1] {ECO:0000313|EMBL:KNG90008.1, ECO:0000313|Proteomes:UP000037505}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NRRL 13137 {ECO:0000313|EMBL:KNG90008.1,
RC ECO:0000313|Proteomes:UP000037505};
RA Moore M.G., Shannon B.M., Brian M.M.;
RT "The Genome of the Aflatoxigenic Filamentous Fungus Aspergillus nomius.";
RL Submitted (JUN-2014) 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:KNG90008.1}.
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DR EMBL; JNOM01000021; KNG90008.1; -; Genomic_DNA.
DR RefSeq; XP_015410931.1; XM_015546438.1.
DR AlphaFoldDB; A0A0L1JF79; -.
DR STRING; 1509407.A0A0L1JF79; -.
DR GeneID; 26802985; -.
DR OrthoDB; 651667at2759; -.
DR UniPathway; UPA00193; -.
DR Proteomes; UP000037505; 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; 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:UP000037505}.
FT DOMAIN 109..225
FT /note="Tetrahydrofolate dehydrogenase/cyclohydrolase
FT catalytic"
FT /evidence="ECO:0000259|Pfam:PF00763"
FT DOMAIN 230..393
FT /note="Tetrahydrofolate dehydrogenase/cyclohydrolase
FT NAD(P)-binding"
FT /evidence="ECO:0000259|Pfam:PF02882"
SQ SEQUENCE 1042 AA; 111842 MW; C7D0FB8DB97676B5 CRC64;
MPFSSPARSA ALPRCHFQHH QGAKAKCFFF NSRHLHTSSP LPLSFPRIAP FFLLRPRESS
AGRGVGSLNY GTLRALQHNP TGYKGFTATP FSIRRSSYST GTTMAATKID GTQIAKDIRA
GLKNEIQQIQ ESNPRFKPSL VIFQVGSRSD SSTYVRMKLK AAEEAGISCK IVNFPETAIE
SELLQDIIKA NNDPSVHGIL VQLPLPQHMS EHTITSAVAD EKDVDGFGAV NIGELAKRGG
HPLFVPCTPQ AVMELLRVSG VNPAGKKAVV LGRSDIVGSP VSYLLNKADA TVTLCHSKTP
DVESIIKTAD ILVAALGKTE FVKGEWLKPG AVVIDVGINY KADPSKKSGQ RLVGDVDFES
AVQVASQITP VPGGVGPMTV AMLMQNVVHS AKAYFEKQKD RHITPLPLKL ARPVPSDIAI
SRAQYPKAIT QVASEVGIAA HELEPYGHTK AKVSLDVLDR LAHRRNGKYI LVCGITPTPL
GEGKSTTTLG LTQAIGAHLN RIVFANVRQP SQGPTFGIKG GAAGGGYSQV IPMDEFNLHL
TGDIHAITAA NNLLAAAIET RMFHEATQKD GPLYKRLVPA KKGKREFQPV MFKRLNKLGI
TKTNPDELTD EEIRRFARLD IDPETITWRR VLDVNDRHLR GITVGQAPTE KGLTRETGFD
ISVASECMAI LALSNSLADM RDRLGRMVVA TSRSGDPVTC DDIGAGGALA ALMKDAIKPN
LMQSLEGTPV LVHAGPFANI SIGASSVIAD KLALKLAGTE PDEDHEDKTG FVVTEAGFDF
TMGGERFFNI KCRSSGLTPD TVVIVATVRA LKVHGGGPEI SPGAPLNEVY RTENVDILRK
GCINLKKHIE NARQYGVPVV VAINRMETDT EAEIAVIREE AIAAGAEDAI PANHWAEGGA
GAVDLAKGVL AASSKPKDFK LLYELEGTIQ ERIERIGKAM YGAEKVELSE LAQKKVDTYT
AQGFGHLPIC IAKTQYSLSH DPALKGAPTG FTVPIRDVRL AVGGGYLYAL AADIQTIPGL
PTAPGYLNVD IDPETGEIDG LF
//
