ID Q160B1_ROSDO Unreviewed; 330 AA.
AC Q160B1;
DT 25-JUL-2006, integrated into UniProtKB/TrEMBL.
DT 25-JUL-2006, sequence version 1.
DT 27-MAR-2024, entry version 101.
DE SubName: Full=Glyoxylate reductase {ECO:0000313|EMBL:ABG33682.1};
DE EC=1.1.1.26 {ECO:0000313|EMBL:ABG33682.1};
GN Name=gyaR {ECO:0000313|EMBL:ABG33682.1};
GN OrderedLocusNames=RD1_4247 {ECO:0000313|EMBL:ABG33682.1};
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:ABG33682.1, ECO:0000313|Proteomes:UP000007029};
RN [1] {ECO:0000313|EMBL:ABG33682.1, 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|RuleBase:RU003719}.
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DR EMBL; CP000362; ABG33682.1; -; Genomic_DNA.
DR RefSeq; WP_011570292.1; NZ_FOOO01000027.1.
DR AlphaFoldDB; Q160B1; -.
DR STRING; 375451.RD1_4247; -.
DR KEGG; rde:RD1_4247; -.
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; IPR029753; D-isomer_DH_CS.
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; 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:UP000007029}.
FT DOMAIN 14..329
FT /note="D-isomer specific 2-hydroxyacid dehydrogenase
FT catalytic"
FT /evidence="ECO:0000259|Pfam:PF00389"
FT DOMAIN 118..298
FT /note="D-isomer specific 2-hydroxyacid dehydrogenase NAD-
FT binding"
FT /evidence="ECO:0000259|Pfam:PF02826"
SQ SEQUENCE 330 AA; 35993 MW; ACA832DFCF1B3040 CRC64;
MNAPAILKNR PRVLVTRRWP ESVEAQLAER FDTVFNVDDT PMTPAEFRDA LTRFDAILPT
VTDRLTTEAF DISSPKTRLL ANYGVGFSHI DIAAAKAHGI AVTNTPDVLS ECTADLAMTL
LLMVARRAGE GERELRAGQW TGWRPTHLVG SKVSGKTLGI VGFGRIGQAM AQRAHFGFGM
KILVQNRSRV AQEVLDRYQA VQVDTLDDLL PACDFVSMHC PGGAENRHLI NSRRLDLMKS
DAFLINTARG EVVDENALVQ SLTYECIAGA GLDVFDGEPK VSPALMEFDN LVLLPHLGSA
TAETRTAMGE RVLSNVIAFF EGSTPADRVA
//
