ID A0A0C9MDJ2_9FUNG Unreviewed; 935 AA.
AC A0A0C9MDJ2;
DT 29-APR-2015, integrated into UniProtKB/TrEMBL.
DT 29-APR-2015, sequence version 1.
DT 27-MAR-2024, entry version 39.
DE SubName: Full=FTHFS-domain-containing protein {ECO:0000313|EMBL:GAN01047.1};
GN ORFNames=MAM1_0004d00478 {ECO:0000313|EMBL:GAN01047.1};
OS Mucor ambiguus.
OC Eukaryota; Fungi; Fungi incertae sedis; Mucoromycota; Mucoromycotina;
OC Mucoromycetes; Mucorales; Mucorineae; Mucoraceae; Mucor.
OX NCBI_TaxID=91626 {ECO:0000313|EMBL:GAN01047.1};
RN [1] {ECO:0000313|EMBL:GAN01047.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=NBRC 6742 {ECO:0000313|EMBL:GAN01047.1};
RA Takeda I., Yamane N., Morita T., Tamano K., Machida M., Baker S., Koike H.;
RT "Draft genome sequence of an oleaginous Mucoromycotina fungus Mucor
RT ambiguus NBRC6742.";
RL Submitted (SEP-2014) 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}.
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DR EMBL; DF836293; GAN01047.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0C9MDJ2; -.
DR STRING; 91626.A0A0C9MDJ2; -.
DR OrthoDB; 651667at2759; -.
DR UniPathway; UPA00193; -.
DR Proteomes; UP000053815; 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; PS00766; THF_DHG_CYH_1; 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:UP000053815}.
FT DOMAIN 6..122
FT /note="Tetrahydrofolate dehydrogenase/cyclohydrolase
FT catalytic"
FT /evidence="ECO:0000259|Pfam:PF00763"
FT DOMAIN 125..291
FT /note="Tetrahydrofolate dehydrogenase/cyclohydrolase
FT NAD(P)-binding"
FT /evidence="ECO:0000259|Pfam:PF02882"
SQ SEQUENCE 935 AA; 100650 MW; FFDA49722343D717 CRC64;
MTATLIDGKA IAQAVRNETK DKILAIKEKY PHFNPHLAMI QVGAREDSSI YVKMKDKAAK
EVGISITMEK LPETISQSEL LRKVKQLNND YRIHGILVQM PLPSHISEAA VIEAIDYQKD
VDGFHAINIG NMAKKGGEPL FLPCTPKGII HLLKSTGIEI TGKQAAVVGR SDIVGAPVAT
LLTAEHATVT LCHSKTPDIE AIVRAADIVV AAAGKTELIK GDWIKPGAVI IDVGTNAVED
ATKKSGIRWV GDVEFAKAKE VASFITPVPG GVGPMTVAML MQNTAISAER WLTLSRKRDI
SALELDLKEP VPSDIEIAKA QTPKHIDELC REIGLSASEY ELYGTAKAKI NLDVLDRLDH
RKDGRYIVVT GITPTPLGEG KSTTTIGLVQ ALGAHLNKAA FACVRQPSQG PTFGIKGGAA
GGGYSQVIPM DEFNLHMTGD LHAVTAANNL MAAAIDARIF HENTQTDKAL FNRLCPAKKG
VRSFAPVMLK RLQKLGITKT DPAELDQDEI SRFVRLDVDP DTITWQRGVD VNDRFLRKIT
IGQAPTEKGM ERQTGFDITV ASEVMAVLAL ATDLKDMRER LGNMVVASSK AGEPITADDF
GIGGALTVLM KDAIKPNLMQ TLEGTPTIVH AGPFANIAHG NSSILADKIA LKLAGSDGTD
MEPGYVITEA GFGADMGMEK FFDIKCRVSG LQPNAVVIVA TVRALKTHGD GPEIIAGKPL
PEAYVGENLE LLEKGCCNLV KHIQNAKKFG VPVLVAVNRF TNDTDAEMEL VRDLSLKAGA
FDAVACDHWA RGGAGAVDLG KAVIKACEQP TDFKFLYELD LPIEKKIEAI CREIYGADGV
EFSDLAKEKI ETYTRQGFAP LPICMAKTQY SFSHDPALKG VPTGFTVPIR DIRASVGAGF
LYPLVGTMQT MPGLPTRPCF FDVDLDDKGE VIGLF
//
