ID A0A2B7ZCH0_9EURO Unreviewed; 939 AA.
AC A0A2B7ZCH0;
DT 20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT 20-DEC-2017, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:PGH31275.1};
GN ORFNames=GX50_05965 {ECO:0000313|EMBL:PGH31275.1};
OS Emmonsia crescens.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Onygenales; Ajellomycetaceae; Emmonsia.
OX NCBI_TaxID=73230 {ECO:0000313|EMBL:PGH31275.1, ECO:0000313|Proteomes:UP000226031};
RN [1] {ECO:0000313|EMBL:PGH31275.1, ECO:0000313|Proteomes:UP000226031}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=UAMH4076 {ECO:0000313|EMBL:PGH31275.1,
RC ECO:0000313|Proteomes:UP000226031};
RA Munoz J.F., Mcewen J.G., Clay O.K., Cuomo C.A.;
RT "Comparative genomics in systemic dimorphic fungi from Ajellomycetaceae.";
RL Submitted (OCT-2017) 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:PGH31275.1}.
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DR EMBL; PDND01000134; PGH31275.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2B7ZCH0; -.
DR STRING; 73230.A0A2B7ZCH0; -.
DR VEuPathDB; FungiDB:EMCG_07221; -.
DR OrthoDB; 651667at2759; -.
DR UniPathway; UPA00193; -.
DR Proteomes; UP000226031; 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; 3.30.1510.10; Domain 2, N(10)-formyltetrahydrofolate synthetase; 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:UP000226031}.
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; 100585 MW; 61D24D3758789B0E CRC64;
MAGIKIDGTT IAKNIRDRLN AEIQKSQETN PRFKPSLVIF QIGDRSDSST YVRMKLKAAE
EANIHCKLIK FSEDISEPEL LQEIALSNND PSVHGILVQL PIPSHLSEHT VTSAVAAEKD
VDGFGAINIG ELAKRGGKPL FVPCTPQGVM ELLRVTGIEL AGKNAVVLGR SDIVGSPVSY
LLKNADATVT VCHSKTKNLE TIVKEADILV AAIGKPEFVK GSWLKPGAVV IDVGTNYIPD
ETKKSGQRLV GDVEFSSAAE VASHITPVPG GVGPMTVAML LQNVVNSARG YFERQKDRHV
TPLPIKLQTP VPSDIAISRT QRPKPITLVA AEVGIAPHEL EPYGHTKAKV SLDLLDRLSH
RRNGRYIVVC GITPTPLGEG KSTTTMGLTQ ALGAHLNRIA FANVRQPSQG PTFGIKGGAA
GGGYSQVIPM DEFNLHLTGD IHAITAANNL LAAAIETRMF HESTQSDAAL YKRLVPAKKG
KREFQPIFFR RLNKLGITKT NPDDLTPEEI NRFARLDIDP ETITWRRVLD VNDRHLRGIT
VGQAATEKGH TRQTGFDISV ASECMAILAL SNDLGDMRER LGRMVVATSK NGDPVTCDDV
GCGGALAALM RDAIKPNLMQ SLEGTPVFVH AGPFANISIG ANSVVADKLA LKLAGTEPDE
DHEAKTGFVV TEAGFDFTMG GERFFNIKCR SSGLVPDTVV IVATVRAIKT HGGGPPIAPG
AALAAEYTTE NVQLLRNGCV NLKKQIENAK KYGIPVVVAI NKFETDTDAE VAVIREEAIA
AGAEDAIPAN HWAEGGAGAI DLAKGVIIAS SKPKDFKLLY DLEGTVQERI ERIGKEMYGA
AKVEFSELAQ KKVDMYTKQG FGNLPICIAK TQYSLSHDPN LKGAPTGFTV PIRDVRLAVG
AGYLYALAAD IQTIPGLPTA PGYLNVDVDA ETGEIDGLF
//
