ID J4HZQ8_9APHY Unreviewed; 342 AA.
AC J4HZQ8;
DT 31-OCT-2012, integrated into UniProtKB/TrEMBL.
DT 31-OCT-2012, sequence version 1.
DT 27-MAR-2024, entry version 38.
DE RecName: Full=D-isomer specific 2-hydroxyacid dehydrogenase NAD-binding domain-containing protein {ECO:0008006|Google:ProtNLM};
GN ORFNames=FIBRA_06836 {ECO:0000313|EMBL:CCM04652.1};
OS Fibroporia radiculosa.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Polyporales; Fibroporiaceae; Fibroporia.
OX NCBI_TaxID=599839 {ECO:0000313|EMBL:CCM04652.1, ECO:0000313|Proteomes:UP000006352};
RN [1] {ECO:0000313|EMBL:CCM04652.1, ECO:0000313|Proteomes:UP000006352}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=TFFH 294 {ECO:0000313|EMBL:CCM04652.1,
RC ECO:0000313|Proteomes:UP000006352};
RX PubMed=22247176; DOI=10.1128/AEM.06745-11;
RA Tang J.D., Perkins A.D., Sonstegard T.S., Schroeder S.G., Burgess S.C.,
RA Diehl S.V.;
RT "Short-read sequencing for genomic analysis of the brown rot fungus
RT Fibroporia radiculosa.";
RL Appl. Environ. Microbiol. 78:2272-2281(2012).
CC -!- SIMILARITY: Belongs to the D-isomer specific 2-hydroxyacid
CC dehydrogenase family. {ECO:0000256|ARBA:ARBA00005854,
CC ECO:0000256|RuleBase:RU003719}.
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DR EMBL; HE797161; CCM04652.1; -; Genomic_DNA.
DR RefSeq; XP_012183935.1; XM_012328545.1.
DR AlphaFoldDB; J4HZQ8; -.
DR STRING; 599839.J4HZQ8; -.
DR GeneID; 24099563; -.
DR HOGENOM; CLU_019796_1_2_1; -.
DR InParanoid; J4HZQ8; -.
DR OrthoDB; 1111153at2759; -.
DR Proteomes; UP000006352; Unassembled WGS sequence.
DR GO; GO:0051287; F:NAD binding; IEA:InterPro.
DR GO; GO:0016616; F:oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor; IEA:InterPro.
DR CDD; cd12168; Mand_dh_like; 1.
DR Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 2.
DR InterPro; IPR006139; D-isomer_2_OHA_DH_cat_dom.
DR InterPro; IPR029753; D-isomer_DH_CS.
DR InterPro; IPR029752; D-isomer_DH_CS1.
DR InterPro; IPR006140; D-isomer_DH_NAD-bd.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR PANTHER; PTHR10996; 2-HYDROXYACID DEHYDROGENASE-RELATED; 1.
DR PANTHER; PTHR10996:SF286; D-3-PHOSPHOGLYCERATE DEHYDROGENASE 1-RELATED; 1.
DR Pfam; PF00389; 2-Hacid_dh; 1.
DR Pfam; PF02826; 2-Hacid_dh_C; 1.
DR SUPFAM; SSF52283; Formate/glycerate dehydrogenase catalytic domain-like; 1.
DR SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
DR PROSITE; PS00065; D_2_HYDROXYACID_DH_1; 1.
DR PROSITE; PS00670; D_2_HYDROXYACID_DH_2; 1.
DR PROSITE; PS00671; D_2_HYDROXYACID_DH_3; 1.
PE 3: Inferred from homology;
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000256|RuleBase:RU003719};
KW Reference proteome {ECO:0000313|Proteomes:UP000006352}.
FT DOMAIN 76..332
FT /note="D-isomer specific 2-hydroxyacid dehydrogenase
FT catalytic"
FT /evidence="ECO:0000259|Pfam:PF00389"
FT DOMAIN 130..306
FT /note="D-isomer specific 2-hydroxyacid dehydrogenase NAD-
FT binding"
FT /evidence="ECO:0000259|Pfam:PF02826"
SQ SEQUENCE 342 AA; 37305 MW; 336B27ADEA1476D8 CRC64;
MSAVRSPFVH LSCHPDQVLW AKDEVPSLFN GIADVFHLDP SVNRTDFLAS FQPGGPFEGA
VGLFRKNHST ARIGLFDKEL INALPSSIAW IAHVGAGYDQ VDAGACKARG IRLSNTPHAV
DDATATTSLY LLISTMRCFS KAERSVRAGL WKSQHSAAHA HDLSGKAVAI LGLGGIGLRF
AELVRAFPMR VLYHSRRKVA HAPEWCEYYD AGRLDEMLAQ ADALSIHVPL NEHTAGMVDE
KMIRKLKKGA VIVNTARGKV TDEEAMMRAL QDGHLSGVGL DVYPDEPNVD PRWLDFPNVT
LLPHIGTGTL ESAKALEVRA LENLRDFLVA GAGKDLVPEF MQ
//
