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Database: UniProt
Entry: A0A285CV08_9RHOB
LinkDB: A0A285CV08_9RHOB
Original site: A0A285CV08_9RHOB 
ID   A0A285CV08_9RHOB        Unreviewed;       328 AA.
AC   A0A285CV08;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   27-MAR-2024, entry version 17.
DE   SubName: Full=Glyoxylate reductase {ECO:0000313|EMBL:SNX71255.1};
GN   ORFNames=SAMN05878503_10952 {ECO:0000313|EMBL:SNX71255.1};
OS   Cereibacter ovatus.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC   Paracoccaceae; Cereibacter.
OX   NCBI_TaxID=439529 {ECO:0000313|EMBL:SNX71255.1, ECO:0000313|Proteomes:UP000219467};
RN   [1] {ECO:0000313|Proteomes:UP000219467}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JA234 {ECO:0000313|Proteomes:UP000219467};
RA   Varghese N., Submissions S.;
RL   Submitted (AUG-2017) 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; OAOQ01000009; SNX71255.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A285CV08; -.
DR   OrthoDB; 9793626at2; -.
DR   Proteomes; UP000219467; 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   CDD; cd05301; GDH; 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; 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.
DR   PROSITE; PS00671; D_2_HYDROXYACID_DH_3; 1.
PE   3: Inferred from homology;
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW   ECO:0000256|RuleBase:RU003719};
KW   Reference proteome {ECO:0000313|Proteomes:UP000219467}.
FT   DOMAIN          8..323
FT                   /note="D-isomer specific 2-hydroxyacid dehydrogenase
FT                   catalytic"
FT                   /evidence="ECO:0000259|Pfam:PF00389"
FT   DOMAIN          113..292
FT                   /note="D-isomer specific 2-hydroxyacid dehydrogenase NAD-
FT                   binding"
FT                   /evidence="ECO:0000259|Pfam:PF02826"
SQ   SEQUENCE   328 AA;  36352 MW;  693082965F88FB2A CRC64;
     MPVERLSVVV TRRLPDVVET RLKELFDVEL RDPDTKMTRD ELVQAMCRAD VLVPCVTDQI
     DATMLAQAGP KLKLIANYGA GVDHIDVATA RQRGILVSNT PDVVTEDTAD MTLALILAVT
     RRIPEGLAEM QGGNWAGWAP MAHLGGRLRG RRLGILGMGR IGQAVARRAR AFGMQIHYHN
     RKRLRPELEA ELEATYWESL DQMVTRMDII SVNCPHTPST FHLMNARRLK LMKPTAVIVN
     TSRGEVIDEN ALTRGLRAGE IAGAGLDVFE HGHEINPRLR ELPNVVLLPH MGSATLEGRI
     EMGEKVILNI KTFADGHRPP DQVLPSML
//
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