ID   A0A0X8CPM8_9BRAD        Unreviewed;       303 AA.
AC   A0A0X8CPM8;
DT   06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT   06-JUL-2016, sequence version 1.
DT   27-MAR-2024, entry version 30.
DE   SubName: Full=3-phosphoglycerate dehydrogenase {ECO:0000313|EMBL:AMA61231.1};
GN   ORFNames=BCCGELA001_13065 {ECO:0000313|EMBL:AMA61231.1};
OS   Bradyrhizobium sp. CCGE-LA001.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC   Nitrobacteraceae; Bradyrhizobium.
OX   NCBI_TaxID=1223566 {ECO:0000313|EMBL:AMA61231.1, ECO:0000313|Proteomes:UP000019052};
RN   [1] {ECO:0000313|EMBL:AMA61231.1, ECO:0000313|Proteomes:UP000019052}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CCGE-LA001 {ECO:0000313|EMBL:AMA61231.1,
RC   ECO:0000313|Proteomes:UP000019052};
RX   PubMed=24952318; DOI=10.1016/j.ympev.2014.06.006;
RA   Servin-Garciduenas L.E., Zayas-Del Moral A., Ormeno-Orrillo E., Rogel M.A.,
RA   Delgado-Salinas A., Sanchez F., Martinez-Romero E.;
RT   "Symbiont shift towards Rhizobium nodulation in a group of phylogenetically
RT   related Phaseolus species.";
RL   Mol. Phylogenet. Evol. 79:1-11(2014).
CC   -!- SIMILARITY: Belongs to the D-isomer specific 2-hydroxyacid
CC       dehydrogenase family. {ECO:0000256|RuleBase:RU003719}.
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DR   EMBL; CP013949; AMA61231.1; -; Genomic_DNA.
DR   RefSeq; WP_008550166.1; NZ_CP013949.1.
DR   AlphaFoldDB; A0A0X8CPM8; -.
DR   STRING; 1223566.BCCGELA001_13065; -.
DR   KEGG; brc:BCCGELA001_13065; -.
DR   Proteomes; UP000019052; Chromosome.
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}.
FT   DOMAIN          15..303
FT                   /note="D-isomer specific 2-hydroxyacid dehydrogenase
FT                   catalytic"
FT                   /evidence="ECO:0000259|Pfam:PF00389"
FT   DOMAIN          110..279
FT                   /note="D-isomer specific 2-hydroxyacid dehydrogenase NAD-
FT                   binding"
FT                   /evidence="ECO:0000259|Pfam:PF02826"
SQ   SEQUENCE   303 AA;  32808 MW;  5B7093B2D7F43F62 CRC64;
     MRGVFVDANE ALAVIMERLE KPGDPKVRIH RDPDIKPEQY PEILDGAEIA IVDHTALPTE
     VAKKCTGLKH VVFLGTGARS YMNPEELAEL GISVHLIKGY GDTAVAESAI ALMWASARVI
     AMMDREMRGG NWLREDGMQL TGKTLGLIGF GGIAAEVARI ASGSGMKVIA WNRSPKSHAG
     VEFTDFDTVL AKSDVVSLHL LLNDETRGMI TREKIFAMKP GVILINTARA AIVDEAAMID
     ALKSGHIRHA GLDVFNIEPL PGDHPLTKLP NVTLSAHSAF RTPEASENLI GAAWEHCRRI
     VKG
//