ID A0A0D1VTC6_9EURO Unreviewed; 418 AA.
AC A0A0D1VTC6;
DT 29-APR-2015, integrated into UniProtKB/TrEMBL.
DT 29-APR-2015, sequence version 1.
DT 27-MAR-2024, entry version 27.
DE RecName: Full=D-isomer specific 2-hydroxyacid dehydrogenase NAD-binding domain-containing protein {ECO:0008006|Google:ProtNLM};
GN ORFNames=PV11_06948 {ECO:0000313|EMBL:KIV79385.1};
OS Exophiala sideris.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Chaetothyriomycetidae; Chaetothyriales; Herpotrichiellaceae; Exophiala.
OX NCBI_TaxID=1016849 {ECO:0000313|EMBL:KIV79385.1, ECO:0000313|Proteomes:UP000053599};
RN [1] {ECO:0000313|EMBL:KIV79385.1, ECO:0000313|Proteomes:UP000053599}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 121828 {ECO:0000313|EMBL:KIV79385.1,
RC ECO:0000313|Proteomes:UP000053599};
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 sideris CBS121828.";
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|RuleBase:RU003719}.
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DR EMBL; KN846953; KIV79385.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0D1VTC6; -.
DR STRING; 1016849.A0A0D1VTC6; -.
DR HOGENOM; CLU_019796_1_3_1; -.
DR OrthoDB; 1462550at2759; -.
DR Proteomes; UP000053599; 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 Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 2.
DR InterPro; IPR006139; D-isomer_2_OHA_DH_cat_dom.
DR InterPro; IPR006140; D-isomer_DH_NAD-bd.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR PANTHER; PTHR43761:SF1; 2-HACID_DH DOMAIN-CONTAINING PROTEIN-RELATED; 1.
DR PANTHER; PTHR43761; D-ISOMER SPECIFIC 2-HYDROXYACID DEHYDROGENASE FAMILY PROTEIN (AFU_ORTHOLOGUE AFUA_1G13630); 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.
PE 3: Inferred from homology;
KW Oxidoreductase {ECO:0000256|RuleBase:RU003719};
KW Reference proteome {ECO:0000313|Proteomes:UP000053599}.
FT DOMAIN 92..396
FT /note="D-isomer specific 2-hydroxyacid dehydrogenase
FT catalytic"
FT /evidence="ECO:0000259|Pfam:PF00389"
FT DOMAIN 185..372
FT /note="D-isomer specific 2-hydroxyacid dehydrogenase NAD-
FT binding"
FT /evidence="ECO:0000259|Pfam:PF02826"
FT REGION 30..53
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 418 AA; 45582 MW; D2420AF5A67F01A0 CRC64;
MLIATSRGFK RFSACTKTGA LQSPTHIISR SATTPTTARP VKQAGPLSTA RPSQLLHLPQ
ARNYSHTSKM APPPLPAGMS KHHIVVLEGV HAEMPPFDFP HTIDIHQRTR PDQVAERIKN
ATVVIACVVP VTPSDMDAAP HLGILAVMAV GIHWVDKADC MRRGVTVTNC RAGNVDAVSE
HFLGLYFASR KRIVQVHNTV TQTDEWHDKG TLTKLWPSGP PLGCRQETLG IMGYGTLGKR
IAQLCRAVGF GEVLISERKN ATTIREGRVS FDDIIRRASV ICVCVPKEDD TLDLIAQKEL
KAMRPEALVI NVARGGIVNE TDLARALREG WISGAAADVL EIEPAAPGSG PLTPNLTKET
AVPNLTISSH IAWFTQTTIQ TYQRLLKEGI EGWVNGTLQE SKDKVQDVVV VHNGKMWN
//
