ID A0A2H3IEW9_9EURO Unreviewed; 939 AA.
AC A0A2H3IEW9;
DT 31-JAN-2018, integrated into UniProtKB/TrEMBL.
DT 31-JAN-2018, sequence version 1.
DT 27-MAR-2024, entry version 23.
DE SubName: Full=Formate-tetrahydrofolate ligase, FTHFS {ECO:0000313|EMBL:PCG96220.1};
GN ORFNames=PENO1_069460 {ECO:0000313|EMBL:PCG96220.1};
OS Penicillium occitanis (nom. inval.).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Penicillium.
OX NCBI_TaxID=290292 {ECO:0000313|EMBL:PCG96220.1, ECO:0000313|Proteomes:UP000218381};
RN [1] {ECO:0000313|EMBL:PCG96220.1, ECO:0000313|Proteomes:UP000218381}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CL100 {ECO:0000313|EMBL:PCG96220.1,
RC ECO:0000313|Proteomes:UP000218381};
RX PubMed=28951729; DOI=10.3389/fmicb.2017.01627;
RA Bravo-Ruiz G., Sassi A.H., Marcet-Houben M., Di Pietro A., Gargouri A.,
RA Gabaldon T., Roncero M.I.G.;
RT "Regulatory Mechanisms of a Highly Pectinolytic Mutant of Penicillium
RT occitanis and Functional Analysis of a Candidate Gene in the Plant Pathogen
RT Fusarium oxysporum.";
RL Front. Microbiol. 8:1627-1627(2017).
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:PCG96220.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; NPFK01000219; PCG96220.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2H3IEW9; -.
DR STRING; 290292.A0A2H3IEW9; -.
DR UniPathway; UPA00193; -.
DR Proteomes; UP000218381; 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 Ligase {ECO:0000313|EMBL:PCG96220.1};
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:UP000218381}.
FT DOMAIN 6..122
FT /note="Tetrahydrofolate dehydrogenase/cyclohydrolase
FT catalytic"
FT /evidence="ECO:0000259|Pfam:PF00763"
FT DOMAIN 127..290
FT /note="Tetrahydrofolate dehydrogenase/cyclohydrolase
FT NAD(P)-binding"
FT /evidence="ECO:0000259|Pfam:PF02882"
SQ SEQUENCE 939 AA; 100800 MW; 5CAAFE94EC5F220C CRC64;
MTGFKIDGTA IAKDIREKLK SEIAELQTKN PRFKPNLVIY QVGDRSDSST YVRMKLKAAE
EANILCSIIK FPETITEAEL LFEIEKSNND AKVHGILVQL PLPSHISEHA ITSAVSDEKD
VDGFGTMSIG ALAKRGGQPL FVPCTPQGVM ELLRVSGVDP AGKEAVVVGR SDIVGSPVSY
LLKNADATVT VCHSKTKNLG EVLKRADIVV AAIGQPEFIK GEQLKAGAVV IDVGTNYIPD
ETKKSGQRLV GDVHFESAVE VASQITPVPG GVGPMTVAML LKNVVSSAKS YFDKQRDRHI
TPLPIKLLNP VPSDIAISRA QKPKAITKIA AEVGIASHEL EPYGHTKAKV DLSVLDRLSH
RRNGRYILVT GITPTPLGEG KSTTTMGLTQ ALGAHLNRIV FANVRQPSQG PTFGIKGGAA
GGGYSQVIPM DEFNLHLTGD IHAITAANNL LAAAIDTRMF HEATQKDGAL YKRLVPTKKG
KREFQPIMFR RLKRLGITKT DPNELTEDEI HRFVRLDIDP ETITWRRVLD VNDRHLRGVT
IGQAPTEKGL SRQTGFDISV ASECMAILAL SNDLADMRER LGRMVVATSK NGDPVTCDDI
GVGGALTALM KDAIKPNMMQ SLEGTPVFVH AGPFANISIG ANSVVADKLA LKLAGTEPDE
DHDAKTGFVV TEAGFDFTMG GERFFNIKCR SSGLVPDVVV VVATVRALKV HGGGPEITPG
APLPDVYRTE NVDILRKGCV NLRKHIQNAR QYGIPVVVAV NKFETDTDAE IAVIREEAIA
AGAEDAVPAN HWAEGGAGAV DLAKSVVTAS SQPKDFKLLY TLEGSVQERI DQIAKVMYGA
DKVEFSELAQ KKVDTYTKQG YGNLPICVAK TQYSLSHDPA LKGAPTGFTV PIRDVRLSAG
AGYLYALAAD IQTIPGLPTA PGYLNVDVDP ITGEIDGLF
//
