ID B8MTC4_TALSN Unreviewed; 939 AA.
AC B8MTC4;
DT 03-MAR-2009, integrated into UniProtKB/TrEMBL.
DT 03-MAR-2009, sequence version 1.
DT 27-MAR-2024, entry version 67.
DE SubName: Full=C1 tetrahydrofolate synthase, putative {ECO:0000313|EMBL:EED12374.1};
DE EC=1.5.1.5 {ECO:0000313|EMBL:EED12374.1};
DE EC=6.3.4.3 {ECO:0000313|EMBL:EED12374.1};
GN ORFNames=TSTA_004230 {ECO:0000313|EMBL:EED12374.1};
OS Talaromyces stipitatus (strain ATCC 10500 / CBS 375.48 / QM 6759 / NRRL
OS 1006) (Penicillium stipitatum).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Trichocomaceae; Talaromyces;
OC Talaromyces sect. Talaromyces.
OX NCBI_TaxID=441959 {ECO:0000313|EMBL:EED12374.1, ECO:0000313|Proteomes:UP000001745};
RN [1] {ECO:0000313|Proteomes:UP000001745}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 10500 / CBS 375.48 / QM 6759 / NRRL 1006
RC {ECO:0000313|Proteomes:UP000001745};
RX PubMed=25676766; DOI=10.1128/genomea.01559-14;
RA Nierman W.C., Fedorova-Abrams N.D., Andrianopoulos A.;
RT "Genome sequence of the AIDS-associated pathogen Penicillium marneffei
RT (ATCC18224) and its near taxonomic relative Talaromyces stipitatus
RT (ATCC10500).";
RL Genome Announc. 3:E0155914-E0155914(2015).
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; EQ962660; EED12374.1; -; Genomic_DNA.
DR RefSeq; XP_002488028.1; XM_002487983.1.
DR AlphaFoldDB; B8MTC4; -.
DR STRING; 441959.B8MTC4; -.
DR GeneID; 8100134; -.
DR VEuPathDB; FungiDB:TSTA_004230; -.
DR eggNOG; KOG4230; Eukaryota.
DR HOGENOM; CLU_003601_2_0_1; -.
DR InParanoid; B8MTC4; -.
DR OMA; QPIMFRR; -.
DR OrthoDB; 651667at2759; -.
DR PhylomeDB; B8MTC4; -.
DR UniPathway; UPA00193; -.
DR Proteomes; UP000001745; 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; PS00767; THF_DHG_CYH_2; 1.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Ligase {ECO:0000313|EMBL:EED12374.1};
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 ECO:0000313|EMBL:EED12374.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000001745}.
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; 100700 MW; ED88F2FC955A5D12 CRC64;
MTGSKIDGTA IAKDIREKLK GEIAELQAKN PRFKPNLVIY QVGDRSDSST YVRMKLKAAE
EANILCSIIK FPETITEAEL LFEIEKSNND AEVHGILVQL PLPNHISEHA ITSAVSDDKD
VDGFGTMSIG ALAKRGGQPL FVPCTPQGVM ELLRVSGVNP AGKEAVVVGR SDIVGSPVSY
LLKNADATVT VCHSKTKNLG EILKRADMVV AAIGQPEFIK GDQLKPGVVV IDVGTNYIPD
DTKKSGQRLV GDVHFESAVE VASQITPVPG GVGPMTVAML LKNVVSSAKA YFDKQRDRHI
TPLPIKLLNP VPSDIAISRA QKPKAITKIA AEVGIAAHEL EPYGHTKAKV SFSVLDRLSH
RRDGRYVLVT GITPTPLGEG KSTTTMGLTQ ALGAHLNRIV FANVRQPSQG PTFGIKGGAA
GGGYSQVIPM DEFNLHLTGD IHAITAANNL LAAAIDTRMF HEATQKDAAL YKRLVPTKKG
KREFQPIMFR RLKKLGITKT DPNELTEDEI HRFARLDIDP DTITWRRVLD VNDRHLRGVT
IGQAPTEKGL SRQTGFDISV ASECMAILAL CNDLADMRER LGRMVVATSK NGDPVTCDDL
GVGGALTALM KDAIKPNMMQ SLEGTPVFVH AGPFANISIG ANSVVADKLA LKLAGTEPDE
DHDAKTGFVV TEAGFDFTMG GERFFNIKCR SSGLVPDVVV VVATVRALKV HGGGPEISPG
APLPEVYRTE NVDILRKGCV NLRKHIQNAR QYGIPVVVAV NKFETDTDAE IAVIREEAIA
AGAEDAVPAN HWAEGGAGAV DLAKSVITAS SQPKDFKLLY SLEGSVQERI DQIAKVMYGA
DKVEFSELAQ KKVDTYTRQG FGNLPICIAK TQYSLSHDPS LKGAPTGFTV PIRDVRLSAG
AGYLYALAAD IQTIPGLPTA PGYLNVDVDP VTGEIDGLF
//
