ID A0A1V6R5R7_9EURO Unreviewed; 939 AA.
AC A0A1V6R5R7;
DT 07-JUN-2017, integrated into UniProtKB/TrEMBL.
DT 07-JUN-2017, sequence version 1.
DT 27-MAR-2024, entry version 26.
DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:OQD96838.1};
GN ORFNames=PENSOL_c014G03492 {ECO:0000313|EMBL:OQD96838.1};
OS Penicillium solitum.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Penicillium.
OX NCBI_TaxID=60172 {ECO:0000313|EMBL:OQD96838.1, ECO:0000313|Proteomes:UP000191612};
RN [1] {ECO:0000313|Proteomes:UP000191612}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=IBT 29525 {ECO:0000313|Proteomes:UP000191612};
RX PubMed=28368369; DOI=10.1038/nmicrobiol.2017.44;
RA Nielsen J.C., Grijseels S., Prigent S., Ji B., Dainat J., Nielsen K.F.,
RA Frisvad J.C., Workman M., Nielsen J.;
RT "Global analysis of biosynthetic gene clusters reveals vast potential of
RT secondary metabolite production in Penicillium species.";
RL Nat. Microbiol. 2:17044-17044(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:OQD96838.1}.
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DR EMBL; MDYO01000014; OQD96838.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1V6R5R7; -.
DR STRING; 60172.A0A1V6R5R7; -.
DR OrthoDB; 651667at2759; -.
DR UniPathway; UPA00193; -.
DR Proteomes; UP000191612; 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:UP000191612}.
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; 100457 MW; 27D2FCFBAD77CA7E CRC64;
MAAAKIDGTA IAKSIRQGLK SEIEQIQVTN PRFKPNLVIF QVGNRSDSST YVRMKLKAAQ
EANIICTLIN VPESSTELQV IQEITRANND PAIHGILVQL PLPSHMSEHA ITSAVSDEKD
VDGFGAINIG ELAKRGGRPL FTPCTPLAVM ELLKASGVDP AGKEAVVLGR SDIVGSPVSY
LLKNADATVT VCHSKTPDIA RIVKNADIVV AAIGQTELVK GDWLKPGAVV IDVGINYKPD
ATKKSGERLV GDVEFESASQ VASQITPVPG GVGPMTVAML LKNVVHSAKG YFEKQKDRHV
TPLPIRLQTP VPSDIAISRA QYPKPITQVA TEIGIAPHEL EPYGHTKAKI SLSLLDRLSH
RRNGRYILVC GITPTPLGEG KSTTTLGLTQ ALGAHLNRIS FANVRQPSQG PTFGIKGGAA
GGGYSQVIPM DEFNLHLTGD IHAITAANNL LAAAIETRMF HESTQKDGPL YKRLVPASKG
TREFKPIMFR RLKKLGIEKT NPDDLTEEEI TRFARLDIDP DTITWRRVLD VNDRHLRGIT
VGVAPTEKGL SRETGFDISV ASECMAILAL SNDLEDMRER LGRMVVATSR NGDPVTCDDI
GAGGALAALM KDAIKPNLMQ SLEGTPVMVH AGPFANISIG ASSAIADKLA LKLAGTEPDE
DHEAKTGFVV TEAGFDFTMG GERFFNIKCR SSGLVPDTVV IVATVRALKV HGGGPEIKPG
APLQEVYRTE NVDVLRKGCV NLRKHIANAK QYGVPVVVAI NKFETDTDAE IAVIKEEAIA
AGAEDAVPAN HWAEGGAGAV DLAKAVMTAS SKEKDFKLLY GLDGTIQERI ERIGQAMYGA
EKVEFSELAQ KKVDTYTKQG FSNLPICIAK TQYSLSHDPA LKGAPTGFTV PIRDVRLAVG
AGYLYALAAD IQTIPGLPTA PGYLNVDIDT ETGDIDGLF
//
