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Database: UniProt
Entry: A0A1I5VYD8_9BRAD
LinkDB: A0A1I5VYD8_9BRAD
Original site: A0A1I5VYD8_9BRAD 
ID   A0A1I5VYD8_9BRAD        Unreviewed;       347 AA.
AC   A0A1I5VYD8;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   27-MAR-2024, entry version 23.
DE   SubName: Full=D-3-phosphoglycerate dehydrogenase {ECO:0000313|EMBL:SFQ12471.1};
GN   ORFNames=SAMN05216330_11640 {ECO:0000313|EMBL:SFQ12471.1};
OS   Bradyrhizobium sp. Ghvi.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC   Nitrobacteraceae; Bradyrhizobium.
OX   NCBI_TaxID=1855319 {ECO:0000313|EMBL:SFQ12471.1, ECO:0000313|Proteomes:UP000198509};
RN   [1] {ECO:0000313|EMBL:SFQ12471.1, ECO:0000313|Proteomes:UP000198509}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Ghvi {ECO:0000313|EMBL:SFQ12471.1,
RC   ECO:0000313|Proteomes:UP000198509};
RA   de Groot N.N.;
RL   Submitted (OCT-2016) 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; FOVU01000016; SFQ12471.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1I5VYD8; -.
DR   STRING; 1855319.SAMN05216330_11640; -.
DR   OrthoDB; 9793626at2; -.
DR   Proteomes; UP000198509; 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   GO; GO:0003714; F:transcription corepressor activity; IEA:InterPro.
DR   CDD; cd05299; CtBP_dh; 1.
DR   Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 2.
DR   InterPro; IPR043322; CtBP.
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; PTHR10996:SF178; 2-HYDROXYACID DEHYDROGENASE YGL185C-RELATED; 1.
DR   PANTHER; PTHR10996; 2-HYDROXYACID DEHYDROGENASE-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.
PE   3: Inferred from homology;
KW   Oxidoreductase {ECO:0000256|RuleBase:RU003719}.
FT   DOMAIN          31..113
FT                   /note="D-isomer specific 2-hydroxyacid dehydrogenase
FT                   catalytic"
FT                   /evidence="ECO:0000259|Pfam:PF00389"
FT   DOMAIN          114..292
FT                   /note="D-isomer specific 2-hydroxyacid dehydrogenase NAD-
FT                   binding"
FT                   /evidence="ECO:0000259|Pfam:PF02826"
SQ   SEQUENCE   347 AA;  38134 MW;  ED866B850976B10E CRC64;
     MPKYKVVTPK GASFTVAGSD YSYEREALDP IDAEIVEAPA NEAEFIAAAK HADAIYAKGI
     PITKTIIDAL ENCKVITLGS VGVDSVDVKA ATARGIPVTN IPDTFIEEVA DHAMMLLLSG
     FRRLVEQDRM VRTGRWAEGR PALLKIPRLM GQTLGFISFG RVARAVAKRA APFGLRMMAY
     DPFIQETLMW DHGVIPATLN EVLSQSDFVS MHAPARPEVH HMLTEKHFRQ MKKGSIFINT
     GRGATVDEEG LIKALQEGWI AHAALDVLEK EPPSHNNPIL SMENVTLTAH VASASARFDE
     ARKRRVGYEL SLVLQGMWPV SCVNPSVLQD TALRRWQPVG MDRGPNS
//
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