ID M1NUH8_9CORY Unreviewed; 329 AA.
AC M1NUH8;
DT 01-MAY-2013, integrated into UniProtKB/TrEMBL.
DT 01-MAY-2013, sequence version 1.
DT 27-MAR-2024, entry version 39.
DE SubName: Full=Glyoxylate reductase {ECO:0000313|EMBL:AGF71165.1};
GN ORFNames=A605_00745 {ECO:0000313|EMBL:AGF71165.1};
OS Corynebacterium halotolerans YIM 70093 = DSM 44683.
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales;
OC Corynebacteriaceae; Corynebacterium.
OX NCBI_TaxID=1121362 {ECO:0000313|EMBL:AGF71165.1, ECO:0000313|Proteomes:UP000011723};
RN [1] {ECO:0000313|EMBL:AGF71165.1, ECO:0000313|Proteomes:UP000011723}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=YIM 70093 {ECO:0000313|EMBL:AGF71165.1};
RX PubMed=23408721;
RA Ruckert C., Albersmeier A., Al-Dilaimi A., Niehaus K., Szczepanowski R.,
RA Kalinowski J.;
RT "Genome sequence of the halotolerant bacterium Corynebacterium halotolerans
RT type strain YIM 70093(T) (= DSM 44683(T)).";
RL Stand. Genomic Sci. 7:284-293(2012).
CC -!- SIMILARITY: Belongs to the D-isomer specific 2-hydroxyacid
CC dehydrogenase family. {ECO:0000256|RuleBase:RU003719}.
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DR EMBL; CP003697; AGF71165.1; -; Genomic_DNA.
DR RefSeq; WP_015399589.1; NZ_JIAJ01000002.1.
DR AlphaFoldDB; M1NUH8; -.
DR STRING; 1121362.A605_00745; -.
DR KEGG; chn:A605_00745; -.
DR PATRIC; fig|1121362.3.peg.141; -.
DR eggNOG; COG1052; Bacteria.
DR HOGENOM; CLU_019796_1_2_11; -.
DR OrthoDB; 4324715at2; -.
DR Proteomes; UP000011723; Chromosome.
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; 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; PS00670; D_2_HYDROXYACID_DH_2; 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:UP000011723}.
FT DOMAIN 6..324
FT /note="D-isomer specific 2-hydroxyacid dehydrogenase
FT catalytic"
FT /evidence="ECO:0000259|Pfam:PF00389"
FT DOMAIN 108..292
FT /note="D-isomer specific 2-hydroxyacid dehydrogenase NAD-
FT binding"
FT /evidence="ECO:0000259|Pfam:PF02826"
SQ SEQUENCE 329 AA; 35370 MW; 9ED3A8DF36230B17 CRC64;
MDARFLVTTP IPGPGLPLLE EKGSVTVLPE PPSYSRLREL CSSGDYDVVL TQLRDTVDAD
LLAEAQVKGV SNFAVGYNNI DVKAATSHGI LVGNTPGVLT DATADVAMAL ILGTSRRVIE
ADRMVREGRF RGWEPELLLG RDISGSVLGL AGFGRIARAV ARRALGFGME VLFSPRPPGD
RPVGREELGE FADRVQQVPW DELVTRSDFL SLHVPLTEQT HHLVDADVFK LMKPGAILIN
TARGPVVDEK ALVAALRDGE IAAAGLDVYE DEPRLAEGLT ELPNTMLLPH VGSATVPVRA
EMSRLSALNA VAMVTSQEPP HLVNPEVLK
//
