ID Q163B5_ROSDO Unreviewed; 328 AA.
AC Q163B5;
DT 25-JUL-2006, integrated into UniProtKB/TrEMBL.
DT 25-JUL-2006, sequence version 1.
DT 27-MAR-2024, entry version 97.
DE SubName: Full=Glyoxylate reductase {ECO:0000313|EMBL:ABG32928.1};
DE EC=1.1.1.26 {ECO:0000313|EMBL:ABG32928.1};
GN Name=gyaR {ECO:0000313|EMBL:ABG32928.1};
GN OrderedLocusNames=RD1_3437 {ECO:0000313|EMBL:ABG32928.1};
OS Roseobacter denitrificans (strain ATCC 33942 / OCh 114) (Erythrobacter sp.
OS (strain OCh 114)) (Roseobacter denitrificans).
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Roseobacteraceae; Roseobacter.
OX NCBI_TaxID=375451 {ECO:0000313|EMBL:ABG32928.1, ECO:0000313|Proteomes:UP000007029};
RN [1] {ECO:0000313|EMBL:ABG32928.1, ECO:0000313|Proteomes:UP000007029}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 33942 / OCh 114 {ECO:0000313|Proteomes:UP000007029};
RX PubMed=17098896; DOI=10.1128/JB.01390-06;
RA Swingley W.D., Sadekar S., Mastrian S.D., Matthies H.J., Hao J., Ramos H.,
RA Acharya C.R., Conrad A.L., Taylor H.L., Dejesa L.C., Shah M.K.,
RA O'huallachain M.E., Lince M.T., Blankenship R.E., Beatty J.T.,
RA Touchman J.W.;
RT "The complete genome sequence of Roseobacter denitrificans reveals a
RT mixotrophic rather than photosynthetic metabolism.";
RL J. Bacteriol. 189:683-690(2007).
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; CP000362; ABG32928.1; -; Genomic_DNA.
DR RefSeq; WP_011569543.1; NZ_FOOO01000019.1.
DR AlphaFoldDB; Q163B5; -.
DR STRING; 375451.RD1_3437; -.
DR KEGG; rde:RD1_3437; -.
DR eggNOG; COG1052; Bacteria.
DR HOGENOM; CLU_019796_1_2_5; -.
DR OrthoDB; 9793626at2; -.
DR Proteomes; UP000007029; 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:ABG32928.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000007029}.
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; 36092 MW; B71B500EF4E6E893 CRC64;
MSKSKLSVVV TRRLPEEVET RLCELFDVQL RQDDKPMERS ELVEAIKTAD VLVPTVTDDI
DSALIANAGD RLKLIANYGA GVDHIDVATA RQRGILVSNT PGVLADDTAD MTMALILAVL
RRVPEGLSVM QSGAWDGWAP NAYLGGRVGG RRLGILGMGR IGQAVARRAV AFGMQVHYHN
RRRLRPEVEA ELQATYWDSL DQMVARMDVI SVNCPATPST FHLMNARRLQ LMKPEAVIVN
TSRGEVIDEN ALTRMLRSDA IAGAGLDVYE RGTQVNPRLR KLNNVVLLPH MGSATREGRA
EMGEKVIINI KTFDDGHRPP DQVVPSML
//