ID G7EAS1_MIXOS Unreviewed; 1017 AA.
AC G7EAS1;
DT 25-JAN-2012, integrated into UniProtKB/TrEMBL.
DT 25-JAN-2012, sequence version 1.
DT 27-MAR-2024, entry version 51.
DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:GAA99931.1};
GN Name=Mo06634 {ECO:0000313|EMBL:GAA99931.1};
GN ORFNames=E5Q_06634 {ECO:0000313|EMBL:GAA99931.1};
OS Mixia osmundae (strain CBS 9802 / IAM 14324 / JCM 22182 / KY 12970).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Pucciniomycotina; Mixiomycetes;
OC Mixiales; Mixiaceae; Mixia.
OX NCBI_TaxID=764103 {ECO:0000313|EMBL:GAA99931.1, ECO:0000313|Proteomes:UP000009131};
RN [1] {ECO:0000313|Proteomes:UP000009131}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 9802 / IAM 14324 / JCM 22182 / KY 12970
RC {ECO:0000313|Proteomes:UP000009131};
RX PubMed=21478649; DOI=10.2323/jgam.57.63;
RA Nishida H., Nagatsuka Y., Sugiyama J.;
RT "Draft genome sequencing of the enigmatic basidiomycete Mixia osmundae.";
RL J. Gen. Appl. Microbiol. 57:63-67(2011).
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:GAA99931.1}.
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DR EMBL; BABT02000243; GAA99931.1; -; Genomic_DNA.
DR RefSeq; XP_014569488.1; XM_014714002.1.
DR AlphaFoldDB; G7EAS1; -.
DR STRING; 764103.G7EAS1; -.
DR GeneID; 26266926; -.
DR eggNOG; KOG4230; Eukaryota.
DR HOGENOM; CLU_003601_2_0_1; -.
DR InParanoid; G7EAS1; -.
DR OMA; QPIMFRR; -.
DR OrthoDB; 651667at2759; -.
DR UniPathway; UPA00193; -.
DR Proteomes; UP000009131; 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:UP000009131}.
FT DOMAIN 81..202
FT /note="Tetrahydrofolate dehydrogenase/cyclohydrolase
FT catalytic"
FT /evidence="ECO:0000259|Pfam:PF00763"
FT DOMAIN 205..370
FT /note="Tetrahydrofolate dehydrogenase/cyclohydrolase
FT NAD(P)-binding"
FT /evidence="ECO:0000259|Pfam:PF02882"
SQ SEQUENCE 1017 AA; 109126 MW; 664D84EB77653746 CRC64;
MLASGRRLHS IARQIRLASR HNLQTSRTAT LVSTRAIRSS ANFWREKQLR STLHPIVQEA
VSRDTRGMAP NASDSGGAKI IDGTALAKSI REDIAKRIAE IRQTYPRFAP GLAIIQQGDR
PDSSTYVRMK EKAAQEAGIA FQHQILPDEA TTTEEDVIKA VERLNATENI HGLLVQLPLS
ENIGRDGERR ITEAVSPNKD VDGFHAYNIG LLSSRASEPL FPPCTPAGVM LLLESTGVKL
AGLHAVVLGR SDIVGSPVCA LLRRKDVTVT QCHSQTKNLQ GLVQQADIVV AAIGKPHFVK
GEWLKPGAIV IDVGTNFVKD DSKKSGQRLV GDVDFESASK VASHITPVPG GVGPMTVAVL
MKNALTSAER FHAKSLQRTV KPLRLKLLEK VPSDIEIAMA QTPKPVATLA AEIGVSPSEL
ELYGQYKAKV DLGILKRLEH RKNGKYIVVA GITPTPLGEG KSTTTMGLAQ ALGAHLGKVA
FANVRQPSQG PTFGIKGGAA GGGYSQVIPM DEFNLHLTGD IHAVSAANNL LAAAIDARYF
HESTQSDKAL FNRLCPAKKG VRTFAPIMLR RLKKLGIDKT NPDDLTEAEA SKFARLDINP
ESVTWHRVVD TNDRYLRVID TGLAPTEKGF TRRTGFDIAV ASECMAVLAL ANDLQDMKER
LGRMVVADSK SGEPITADDI GVTGSLAILM KDAIKPNLMQ TLEGTPVFVH AGPFANIAHG
NSSIIADKVA LKLAGIEEGE PEENYGYVIT EAGFGADIGM EKFCNIKCRV SGLHPNAVVI
VATIRALKMH GGGPEVSPGK PLSDVYLNEN LDILGAGCVN LAKHISNARK MGVRVIVAIN
RFTNDTEAEI ALVKQKALEA GADAAVPSNH WAEGGKGAVE LANAVIDSCK EPNPFKFLYE
LDIPIKDKIS AIAVEMYGAD GVSYSAEAEK QIEQYTQQGF ANLPICMAKT QYSFSDDPSK
KGAPTGFTLP IREIKLAAGA EFLYPLVGTM QTLPGLSTRP GFFDQDLTAD GQIIGLS
//
