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Database: UniProt
Entry: A0A3P5WXU3_9RHOB
LinkDB: A0A3P5WXU3_9RHOB
Original site: A0A3P5WXU3_9RHOB 
ID   A0A3P5WXU3_9RHOB        Unreviewed;       307 AA.
AC   A0A3P5WXU3;
DT   13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT   13-FEB-2019, sequence version 1.
DT   27-MAR-2024, entry version 13.
DE   SubName: Full=Glyoxylate/hydroxypyruvate reductase B {ECO:0000313|EMBL:VDC20837.1};
DE            EC=1.1.1.79 {ECO:0000313|EMBL:VDC20837.1};
GN   Name=tkrA_2 {ECO:0000313|EMBL:VDC20837.1};
GN   ORFNames=PARPLA_01227 {ECO:0000313|EMBL:VDC20837.1};
OS   Rhodobacteraceae bacterium THAF1.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC   Paracoccaceae.
OX   NCBI_TaxID=2483814 {ECO:0000313|EMBL:VDC20837.1, ECO:0000313|Proteomes:UP000275054};
RN   [1] {ECO:0000313|EMBL:VDC20837.1, ECO:0000313|Proteomes:UP000275054}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATHAF1 {ECO:0000313|EMBL:VDC20837.1};
RA   Criscuolo A.;
RL   Submitted (NOV-2018) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the D-isomer specific 2-hydroxyacid
CC       dehydrogenase family. {ECO:0000256|ARBA:ARBA00005854,
CC       ECO:0000256|RuleBase:RU003719}.
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DR   EMBL; UXAS01000018; VDC20837.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A3P5WXU3; -.
DR   Proteomes; UP000275054; Unassembled WGS sequence.
DR   GO; GO:0030267; F:glyoxylate reductase (NADP+) activity; IEA:UniProtKB-EC.
DR   GO; GO:0051287; F:NAD binding; IEA:InterPro.
DR   CDD; cd12156; HPPR; 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; IPR029752; D-isomer_DH_CS1.
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.
DR   PROSITE; PS00065; D_2_HYDROXYACID_DH_1; 1.
PE   3: Inferred from homology;
KW   Oxidoreductase {ECO:0000256|RuleBase:RU003719,
KW   ECO:0000313|EMBL:VDC20837.1}; Pyruvate {ECO:0000313|EMBL:VDC20837.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000275054}.
FT   DOMAIN          41..307
FT                   /note="D-isomer specific 2-hydroxyacid dehydrogenase
FT                   catalytic"
FT                   /evidence="ECO:0000259|Pfam:PF00389"
FT   DOMAIN          103..275
FT                   /note="D-isomer specific 2-hydroxyacid dehydrogenase NAD-
FT                   binding"
FT                   /evidence="ECO:0000259|Pfam:PF02826"
SQ   SEQUENCE   307 AA;  32583 MW;  1A6C4A8AC21495B9 CRC64;
     MPDIISIGAY PKVDRAALAG MGAVPFATLE EALAMDDRDS VRAIACIAVR LDAATMDAFP
     NLGIIANCMV GYDSIDVKAA RERGIAVTNT PDVLNDDVAD LAVALLFAQA RGMVQADAHV
     RTGAWATEFF PLNRKVSGGT VGILGLGRIG QEIADRLAAF KMDIHYWSRS EKETPGWTYH
     ADPVSLAHAV DFLIVACVGG PETRDIVSSE VIEALGKDGV IVNISRGSTI DEAALLDALE
     NGRLAGAGLD VFENEPAPNP RFTKLDNVVL QPHQASATHA TRAAMGQLQR DNIAAFLKGE
     PLLTQVN
//
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