ID K5VA65_PHACS Unreviewed; 362 AA.
AC K5VA65;
DT 09-JAN-2013, integrated into UniProtKB/TrEMBL.
DT 09-JAN-2013, sequence version 1.
DT 24-JAN-2024, entry version 34.
DE RecName: Full=Methylenetetrahydrofolate dehydrogenase {ECO:0008006|Google:ProtNLM};
GN ORFNames=PHACADRAFT_250488 {ECO:0000313|EMBL:EKM59766.1};
OS Phanerochaete carnosa (strain HHB-10118-sp) (White-rot fungus) (Peniophora
OS carnosa).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Polyporales; Phanerochaetaceae; Phanerochaete.
OX NCBI_TaxID=650164 {ECO:0000313|EMBL:EKM59766.1, ECO:0000313|Proteomes:UP000008370};
RN [1] {ECO:0000313|EMBL:EKM59766.1, ECO:0000313|Proteomes:UP000008370}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HHB-10118-sp {ECO:0000313|EMBL:EKM59766.1,
RC ECO:0000313|Proteomes:UP000008370};
RX PubMed=22937793; DOI=10.1186/1471-2164-13-444;
RA Suzuki H., MacDonald J., Syed K., Salamov A., Hori C., Aerts A.,
RA Henrissat B., Wiebenga A., vanKuyk P.A., Barry K., Lindquist E.,
RA LaButti K., Lapidus A., Lucas S., Coutinho P., Gong Y., Samejima M.,
RA Mahadevan R., Abou-Zaid M., de Vries R.P., Igarashi K., Yadav J.S.,
RA Grigoriev I.V., Master E.R.;
RT "Comparative genomics of the white-rot fungi, Phanerochaete carnosa and P.
RT chrysosporium, to elucidate the genetic basis of the distinct wood types
RT they colonize.";
RL BMC Genomics 13:444-444(2012).
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; JH930469; EKM59766.1; -; Genomic_DNA.
DR RefSeq; XP_007392322.1; XM_007392260.1.
DR AlphaFoldDB; K5VA65; -.
DR STRING; 650164.K5VA65; -.
DR GeneID; 18914933; -.
DR KEGG; pco:PHACADRAFT_250488; -.
DR HOGENOM; CLU_031413_0_1_1; -.
DR InParanoid; K5VA65; -.
DR OrthoDB; 2232005at2759; -.
DR Proteomes; UP000008370; Unassembled WGS sequence.
DR GO; GO:0004488; F:methylenetetrahydrofolate dehydrogenase (NADP+) activity; IEA:InterPro.
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 InterPro; IPR046346; Aminoacid_DH-like_N_sf.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR InterPro; IPR020630; THF_DH/CycHdrlase_cat_dom.
DR InterPro; IPR020631; THF_DH/CycHdrlase_NAD-bd_dom.
DR PANTHER; PTHR48099; C-1-TETRAHYDROFOLATE SYNTHASE, CYTOPLASMIC-RELATED; 1.
DR PANTHER; PTHR48099:SF3; METHYLENETETRAHYDROFOLATE DEHYDROGENASE [NAD(+)]; 1.
DR Pfam; PF00763; THF_DHG_CYH; 1.
DR Pfam; PF02882; THF_DHG_CYH_C; 1.
DR SUPFAM; SSF53223; Aminoacid dehydrogenase-like, N-terminal domain; 1.
DR SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
PE 4: Predicted;
KW Reference proteome {ECO:0000313|Proteomes:UP000008370}.
FT DOMAIN 12..127
FT /note="Tetrahydrofolate dehydrogenase/cyclohydrolase
FT catalytic"
FT /evidence="ECO:0000259|Pfam:PF00763"
FT DOMAIN 174..239
FT /note="Tetrahydrofolate dehydrogenase/cyclohydrolase
FT NAD(P)-binding"
FT /evidence="ECO:0000259|Pfam:PF02882"
SQ SEQUENCE 362 AA; 39472 MW; 5D14F7D3D5E2F362 CRC64;
MADHTGKGIL LKADSIAGAF RDEITATIAQ GARVPKLVGI LATSAAPSKF YAEFTRKQCD
ELGVEFVLKN IGAAADPTLA EGEGVEEAII DANNDDSVDG IMVYYPIFGV QQDHYLQQVV
SPLKDVEGLH FKFHYNLYHN IRYLKPESLL SSVAPSEPPP PVVNDTAPPG FVKSILPCTP
LAIVKTLEHI GVYNRILPYG DRAYGKTITV INRSEVVGRP LAALLANDGA RVFSVDIDSI
QEYTKRPPRP SDAATAANDT ARYHPRHVVH PSALSLQACL ALSDVVVSAV PSAAYKVRTE
WLKDGCVCVN VAADKNFDKD VREKASVYMP TIGKVTIMML LRNLLRLRSY REGESRNTPQ
SS
//
