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Database: UniProt
Entry: U5BV96_9BACT
LinkDB: U5BV96_9BACT
Original site: U5BV96_9BACT 
ID   U5BV96_9BACT            Unreviewed;       309 AA.
AC   U5BV96;
DT   11-DEC-2013, integrated into UniProtKB/TrEMBL.
DT   11-DEC-2013, sequence version 1.
DT   27-MAR-2024, entry version 29.
DE   RecName: Full=Phosphoglycerate dehydrogenase {ECO:0008006|Google:ProtNLM};
GN   ORFNames=P872_24460 {ECO:0000313|EMBL:ERM84575.1};
OS   Rhodonellum psychrophilum GCM71 = DSM 17998.
OC   Bacteria; Bacteroidota; Cytophagia; Cytophagales; Cytophagaceae;
OC   Rhodonellum.
OX   NCBI_TaxID=1123057 {ECO:0000313|EMBL:ERM84575.1, ECO:0000313|Proteomes:UP000016843};
RN   [1] {ECO:0000313|EMBL:ERM84575.1, ECO:0000313|Proteomes:UP000016843}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=GCM71 {ECO:0000313|EMBL:ERM84575.1,
RC   ECO:0000313|Proteomes:UP000016843};
RX   PubMed=24309741;
RA   Hauptmann A.L., Glaring M.A., Hallin P.F., Prieme A., Stougaard P.;
RT   "Draft Genome Sequence of the Psychrophilic and Alkaliphilic Rhodonellum
RT   psychrophilum Strain GCM71T.";
RL   Genome Announc. 1:e01014-13(2013).
CC   -!- SIMILARITY: Belongs to the D-isomer specific 2-hydroxyacid
CC       dehydrogenase family. {ECO:0000256|ARBA:ARBA00005854,
CC       ECO:0000256|RuleBase:RU003719}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:ERM84575.1}.
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DR   EMBL; AWXR01000003; ERM84575.1; -; Genomic_DNA.
DR   RefSeq; WP_019597101.1; NZ_KB906675.1.
DR   AlphaFoldDB; U5BV96; -.
DR   PATRIC; fig|1123057.7.peg.419; -.
DR   eggNOG; COG0111; Bacteria.
DR   OrthoDB; 1522997at2; -.
DR   Proteomes; UP000016843; 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; PTHR42789; D-ISOMER SPECIFIC 2-HYDROXYACID DEHYDROGENASE FAMILY PROTEIN (AFU_ORTHOLOGUE AFUA_6G10090); 1.
DR   PANTHER; PTHR42789:SF1; D-ISOMER SPECIFIC 2-HYDROXYACID DEHYDROGENASE FAMILY PROTEIN (AFU_ORTHOLOGUE AFUA_6G10090); 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   NAD {ECO:0000256|ARBA:ARBA00023027};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW   ECO:0000256|RuleBase:RU003719};
KW   Reference proteome {ECO:0000313|Proteomes:UP000016843}.
FT   DOMAIN          3..307
FT                   /note="D-isomer specific 2-hydroxyacid dehydrogenase
FT                   catalytic"
FT                   /evidence="ECO:0000259|Pfam:PF00389"
FT   DOMAIN          105..286
FT                   /note="D-isomer specific 2-hydroxyacid dehydrogenase NAD-
FT                   binding"
FT                   /evidence="ECO:0000259|Pfam:PF02826"
SQ   SEQUENCE   309 AA;  34754 MW;  A6210D0C2D4C07D1 CRC64;
     MKILIIDEMH PSIHSLLEKE GHLVDYRPEI TRKEIEAVIG NYEGMIIRSK TPMDKALLEK
     AVGLKFIGRA GAGLDKIDLE YLEKKGIKLF TAAEGNRDAV GEHAIGMLLG LFNHLSQADV
     QVRKGIWQRE ENRGEELAGK TVGIIGYGNM GESFARKLRG FDVLVLAYDK YKKGFGNEYV
     EEVGFKRLVG EADILSLHVP LTDETRNFIT PEVLEQFAKP IYLINTARGE IISFDTINEG
     FERGILKGAV LDVLENEKFN SFTSAERLAF EKLASRENVM FSPHVAGWTF QSYEKINKVL
     VSKIVKAFK
//
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