ID D9QL36_BRESC Unreviewed; 328 AA.
AC D9QL36;
DT 05-OCT-2010, integrated into UniProtKB/TrEMBL.
DT 05-OCT-2010, sequence version 1.
DT 27-MAR-2024, entry version 61.
DE SubName: Full=Glyoxylate reductase {ECO:0000313|EMBL:ADK99891.1};
DE EC=1.1.1.26 {ECO:0000313|EMBL:ADK99891.1};
GN OrderedLocusNames=Bresu_0577 {ECO:0000313|EMBL:ADK99891.1};
OS Brevundimonas subvibrioides (strain ATCC 15264 / DSM 4735 / LMG 14903 /
OS NBRC 16000 / CB 81) (Caulobacter subvibrioides).
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Caulobacterales;
OC Caulobacteraceae; Brevundimonas.
OX NCBI_TaxID=633149 {ECO:0000313|EMBL:ADK99891.1, ECO:0000313|Proteomes:UP000002696};
RN [1] {ECO:0000313|Proteomes:UP000002696}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 15264 / DSM 4735 / LMG 14903 / NBRC 16000 / CB 81
RC {ECO:0000313|Proteomes:UP000002696};
RX PubMed=21705585; DOI=10.1128/JB.05453-11;
RG US DOE Joint Genome Institute;
RA Brown P.J., Kysela D.T., Buechlein A., Hemmerich C., Brun Y.V.;
RT "Genome sequences of eight morphologically diverse alphaproteobacteria.";
RL J. Bacteriol. 193:4567-4568(2011).
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; CP002102; ADK99891.1; -; Genomic_DNA.
DR RefSeq; WP_013267995.1; NC_014375.1.
DR AlphaFoldDB; D9QL36; -.
DR STRING; 633149.Bresu_0577; -.
DR KEGG; bsb:Bresu_0577; -.
DR eggNOG; COG1052; Bacteria.
DR HOGENOM; CLU_019796_1_2_5; -.
DR InParanoid; D9QL36; -.
DR OrthoDB; 9793626at2; -.
DR BioCyc; BSUB633149:G1GM8-576-MONOMER; -.
DR Proteomes; UP000002696; Chromosome.
DR GO; GO:0047964; F:glyoxylate reductase (NAD+) activity; IEA:UniProtKB-EC.
DR GO; GO:0051287; F:NAD binding; 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; 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:ADK99891.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000002696}.
FT DOMAIN 17..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; 35877 MW; B99E462B287D2CDA CRC64;
MSNPRLKVVL TRRLPDAVET RMRELFDAEL NLKDVPFDRA ALEAAVQRAD VLVPTITDEI
DASLIAGAGD QLKMIANFGA GVDHIDIDAA VARQIIVTNT PGVLTEDTAD LAMSLILAVS
RRIVEGAQVV AEGRFEGWTP TWMCGRKLWG KRLGIVGMGR IGQALARRAR AFGLQVHYHN
RKPVSPRIEE ELGATYWDDL DQMLSRMDLI SLNCPATKDT HHLLSAERLA RLQPHAILVN
TARGELIDEA ALSDAVARRG IAGVGLDVYE HEPAIHPGLL GHPNVVLLPH LGSATLEARQ
DMGDRVIANV MTFQNGHRPP DRVIPAML
//
