ID A0A397URI6_9GLOM Unreviewed; 921 AA.
AC A0A397URI6;
DT 05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 1.
DT 24-JAN-2024, entry version 16.
DE SubName: Full=Tetrahydrofolate dehydrogenase/cyclohydrolase {ECO:0000313|EMBL:RIB12221.1};
GN ORFNames=C2G38_2201245 {ECO:0000313|EMBL:RIB12221.1};
OS Gigaspora rosea.
OC Eukaryota; Fungi; Fungi incertae sedis; Mucoromycota; Glomeromycotina;
OC Glomeromycetes; Diversisporales; Gigasporaceae; Gigaspora.
OX NCBI_TaxID=44941 {ECO:0000313|EMBL:RIB12221.1, ECO:0000313|Proteomes:UP000266673};
RN [1] {ECO:0000313|EMBL:RIB12221.1, ECO:0000313|Proteomes:UP000266673}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DAOM 194757 {ECO:0000313|EMBL:RIB12221.1,
RC ECO:0000313|Proteomes:UP000266673};
RA Morin E., San Clemente H., Chen E.C.H., De La Providencia I., Hainaut M.,
RA Kuo A., Kohler A., Murat C., Tang N., Roy S., Loubradou J., Henrissat B.,
RA Grigoriev I.V., Corradi N., Roux C., Martin F.M.;
RT "Comparative genomics reveals the genomic features of Rhizophagus
RT irregularis, R. cerebriforme, R. diaphanum and Gigaspora rosea, and their
RT symbiotic lifestyle signature.";
RL Submitted (JUN-2018) to the EMBL/GenBank/DDBJ databases.
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:RIB12221.1}.
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DR EMBL; QKWP01001046; RIB12221.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A397URI6; -.
DR STRING; 44941.A0A397URI6; -.
DR Proteomes; UP000266673; Unassembled WGS sequence.
DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR GO; GO:0004488; F:methylenetetrahydrofolate dehydrogenase (NADP+) activity; IEA:InterPro.
DR GO; GO:0009058; P:biosynthetic process; IEA:InterPro.
DR GO; GO:0006730; P:one-carbon metabolic process; IEA:UniProtKB-KW.
DR CDD; cd06558; crotonase-like; 1.
DR CDD; cd08650; FMT_core_HypX_N; 1.
DR CDD; cd01080; NAD_bind_m-THF_DH_Cyclohyd; 1.
DR Gene3D; 3.40.50.12230; -; 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 HAMAP; MF_01576; THF_DHG_CYH; 1.
DR InterPro; IPR046346; Aminoacid_DH-like_N_sf.
DR InterPro; IPR029045; ClpP/crotonase-like_dom_sf.
DR InterPro; IPR001753; Enoyl-CoA_hydra/iso.
DR InterPro; IPR005793; Formyl_trans_C.
DR InterPro; IPR002376; Formyl_transf_N.
DR InterPro; IPR036477; Formyl_transf_N_sf.
DR InterPro; IPR011034; Formyl_transferase-like_C_sf.
DR InterPro; IPR047180; HoxX-like.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR InterPro; IPR000672; THF_DH/CycHdrlase.
DR InterPro; IPR020630; THF_DH/CycHdrlase_cat_dom.
DR InterPro; IPR020631; THF_DH/CycHdrlase_NAD-bd_dom.
DR PANTHER; PTHR43388; HYDROGENASE MATURATION FACTOR HOXX; 1.
DR PANTHER; PTHR43388:SF1; HYDROGENASE MATURATION FACTOR HOXX; 1.
DR Pfam; PF00378; ECH_1; 1.
DR Pfam; PF02911; Formyl_trans_C; 1.
DR Pfam; PF00551; Formyl_trans_N; 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; SSF52096; ClpP/crotonase; 1.
DR SUPFAM; SSF50486; FMT C-terminal domain-like; 1.
DR SUPFAM; SSF53328; Formyltransferase; 1.
DR SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000313|EMBL:RIB12221.1};
KW One-carbon metabolism {ECO:0000256|ARBA:ARBA00022563};
KW Reference proteome {ECO:0000313|Proteomes:UP000266673}.
FT DOMAIN 19..133
FT /note="Tetrahydrofolate dehydrogenase/cyclohydrolase
FT catalytic"
FT /evidence="ECO:0000259|Pfam:PF00763"
FT DOMAIN 139..298
FT /note="Tetrahydrofolate dehydrogenase/cyclohydrolase
FT NAD(P)-binding"
FT /evidence="ECO:0000259|Pfam:PF02882"
FT DOMAIN 378..478
FT /note="Formyl transferase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00551"
FT DOMAIN 526..614
FT /note="Formyl transferase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02911"
SQ SEQUENCE 921 AA; 103139 MW; 86DAFC918D90EB7F CRC64;
MLKRLPNNIY YKKILDCFSV ADAIKNTAIE AKKSLNSQPK VTVILPTNSA GKARIDSANY
VAKKRKVFEQ LDIPMQLIKI SPQYNETQIK ELIKNLSNDP NNTGIIVQLP FPSDFSINKN
NILNSIPIHK DIDGLTIGSV GNLFDLDKGL KPAAPLGICS IFDYYNIPTE GKHIVIMGKG
QLVGKPLVCM LMASPYNATV TICDIHTENI KNITKSADIL IVAIGKALYV NDDLVKSGVI
VIDVGINRLP PNIINGNSSI VGDVDYSVYE KCKYYTPVPS GVGLLTVSSL AFNAVNASIL
QQGLPPLNLS KLIRQSYSVE KVEKKIIATS QRHSDQLVKI ENKKNLNLLL FSSAYNGMTQ
RIRNELLRLG HKVTFQTADS DDTMRSAFAQ YKPDLIICPT LMKAIPEDIY TKVKCLIVHP
GIKGDKGPSS LDWAIIDKKD EWGVTVLEAD KEMDAGAIWA SENFLVPKAI TKTHLYNSHV
INTATKLVLE CVENFQLNNF KPEPLNYANT SVKGRLHETI KQSHFNRQIN WKIDNTEIIL
RKIRAADSKP GVKAEINLNG TKIMRFLYDA HNEKTINQDL MAYPGKVLAK RDDAICIATK
DGAFWVSQLR SPKTQMKPYP FKLPATIQLG KLSENIPVIN PKQNFTTPTL DTFQEISFEL
FGSYGILYFN FYNGAMSTSQ CERLLKAIKQ CQKMPIKGLI FAGSANNWSN GINLNVIQHA
DNPSIEGWNN IKAINEVVKE IIKLTNIITV AAVQANAGAG GVYLALATDF SFVKPGVVLN
PHYKNMGLYG SELHTYTASK RINTFMLKQI KENVKPMLAV EAIEIGLFDK LIQQEQVNPE
QSFLDSVKGF MDIAIADTIK FTKFIKNKQD IRMRDELAKS LDEYEKHELE EMHKDFFENR
NNFHEKRWAF ITKSPFTLAN K
//
