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Database: UniProt
Entry: H5YAL8_9BRAD
LinkDB: H5YAL8_9BRAD
Original site: H5YAL8_9BRAD 
ID   H5YAL8_9BRAD            Unreviewed;       320 AA.
AC   H5YAL8;
DT   18-APR-2012, integrated into UniProtKB/TrEMBL.
DT   18-APR-2012, sequence version 1.
DT   24-JAN-2024, entry version 37.
DE   SubName: Full=Phosphoglycerate dehydrogenase-like oxidoreductase {ECO:0000313|EMBL:EHR01058.1};
GN   ORFNames=Bra471DRAFT_01722 {ECO:0000313|EMBL:EHR01058.1};
OS   Bradyrhizobium sp. WSM471.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC   Nitrobacteraceae; Bradyrhizobium.
OX   NCBI_TaxID=319017 {ECO:0000313|EMBL:EHR01058.1};
RN   [1] {ECO:0000313|EMBL:EHR01058.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=WSM471 {ECO:0000313|EMBL:EHR01058.1};
RG   US DOE Joint Genome Institute;
RA   Lucas S., Han J., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S.,
RA   Peters L., Lu M., Detter J.C., Han C., Tapia R., Land M., Hauser L.,
RA   Kyrpides N., Ivanova N., Pagani I., Brau L., Yates R., O'Hara G., Rui T.,
RA   Howieson J., Reeve W., Woyke T.;
RT   "The Noncontiguous Finished sequence of Bradyrhizobium sp. WSM471.";
RL   Submitted (NOV-2011) 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; CM001442; EHR01058.1; -; Genomic_DNA.
DR   RefSeq; WP_007606108.1; NZ_CM001442.1.
DR   AlphaFoldDB; H5YAL8; -.
DR   HOGENOM; CLU_019796_1_0_5; -.
DR   OrthoDB; 9793626at2; -.
DR   Proteomes; UP000005774; 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   CDD; cd05300; 2-Hacid_dh_1; 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; IPR006140; D-isomer_DH_NAD-bd.
DR   InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR   PANTHER; PTHR43333; 2-HACID_DH_C DOMAIN-CONTAINING PROTEIN; 1.
DR   PANTHER; PTHR43333:SF1; 2-HACID_DH_C DOMAIN-CONTAINING PROTEIN; 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; PS00671; D_2_HYDROXYACID_DH_3; 1.
PE   3: Inferred from homology;
KW   NAD {ECO:0000256|ARBA:ARBA00023027};
KW   Oxidoreductase {ECO:0000256|RuleBase:RU003719}.
FT   DOMAIN          25..314
FT                   /note="D-isomer specific 2-hydroxyacid dehydrogenase
FT                   catalytic"
FT                   /evidence="ECO:0000259|Pfam:PF00389"
FT   DOMAIN          114..283
FT                   /note="D-isomer specific 2-hydroxyacid dehydrogenase NAD-
FT                   binding"
FT                   /evidence="ECO:0000259|Pfam:PF02826"
SQ   SEQUENCE   320 AA;  34804 MW;  1474C74E7B40EBD8 CRC64;
     MPAERPDITI VLCHPDAELY ARLVADRFPQ VRTIIAPSPD QLARCINEAD ALLASSLPVD
     LFEHAKKLRW IQCPFAGVDS IMPFRETIGE ITITNARGIH GDIIADYVMA GVTMLHWDFR
     KLLRDQAERR WSPRFVAPLA EKTLGVVGLG SIGATIGRRA KSAGMTVVGS KRDASVPVDG
     VDRLFASGAL DEMLPLCDFV VLAVPATATT AALIGAAEIA RMRRNAFLIN IARGQVVVEA
     ELIQALKAGT IAGALLDVFQ REPLPQESPL WDMPNVIATP HVSGSATNYP ERVFSIFADN
     IERFLRGQSL TNVVDLGRGY
//
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