ID A0A0D2EF65_9EURO Unreviewed; 338 AA.
AC A0A0D2EF65;
DT 29-APR-2015, integrated into UniProtKB/TrEMBL.
DT 29-APR-2015, sequence version 1.
DT 27-MAR-2024, entry version 29.
DE RecName: Full=Glycerate-and formate-dehydrogenase {ECO:0008006|Google:ProtNLM};
GN ORFNames=PV05_06444 {ECO:0000313|EMBL:KIW54053.1};
OS Exophiala xenobiotica.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Chaetothyriomycetidae; Chaetothyriales; Herpotrichiellaceae; Exophiala.
OX NCBI_TaxID=348802 {ECO:0000313|EMBL:KIW54053.1, ECO:0000313|Proteomes:UP000054342};
RN [1] {ECO:0000313|EMBL:KIW54053.1, ECO:0000313|Proteomes:UP000054342}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 118157 {ECO:0000313|EMBL:KIW54053.1,
RC ECO:0000313|Proteomes:UP000054342};
RG The Broad Institute Genomics Platform;
RA Cuomo C., de Hoog S., Gorbushina A., Stielow B., Teixiera M.,
RA Abouelleil A., Chapman S.B., Priest M., Young S.K., Wortman J., Nusbaum C.,
RA Birren B.;
RT "The Genome Sequence of Exophiala xenobiotica CBS118157.";
RL Submitted (JAN-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the D-isomer specific 2-hydroxyacid
CC dehydrogenase family. {ECO:0000256|ARBA:ARBA00005854,
CC ECO:0000256|RuleBase:RU003719}.
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; KN847320; KIW54053.1; -; Genomic_DNA.
DR RefSeq; XP_013314637.1; XM_013459183.1.
DR AlphaFoldDB; A0A0D2EF65; -.
DR STRING; 348802.A0A0D2EF65; -.
DR GeneID; 25328352; -.
DR HOGENOM; CLU_019796_1_2_1; -.
DR OrthoDB; 1111153at2759; -.
DR Proteomes; UP000054342; 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; 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:UP000054342}.
FT DOMAIN 19..332
FT /note="D-isomer specific 2-hydroxyacid dehydrogenase
FT catalytic"
FT /evidence="ECO:0000259|Pfam:PF00389"
FT DOMAIN 125..300
FT /note="D-isomer specific 2-hydroxyacid dehydrogenase NAD-
FT binding"
FT /evidence="ECO:0000259|Pfam:PF02826"
SQ SEQUENCE 338 AA; 37643 MW; 6AEED487E86A7FDE CRC64;
MATRKPLVVA LGDPKYAGQE FLDEFKKDFD FEILPATNRK ETQDLLPQLI ARRGPVDAFI
IRMGTPPYEP FNEDLLGSLL PHCKIITSAS AGFNEFDVDW MTRNKIWFCN TRNAVAEATA
DMALFLILAV LRDTTRAEKG ARSDSWKAGL VPCRDPTGMT LGIVGMGAIG KYTARKALAF
NMRIHYYNRH RLSPEVEAEY HATYRPTLHS LLAQSDVVSL SCPLNRETTN LISKAEFAAM
KHGSFLVNTS RGAVVDEEAL IDALESGKIT RAGLDVFCNE PNINPYFKTS NKIIAQPHMG
GLTDVAFEKS ERECFENIRS LWRTGRPVAP VNEVVDGL
//
