ID A1RC54_PAEAT Unreviewed; 329 AA. AC A1RC54; DT 06-FEB-2007, integrated into UniProtKB/TrEMBL. DT 06-FEB-2007, sequence version 1. DT 08-OCT-2025, entry version 120. DE SubName: Full=Glyoxylate reductase {ECO:0000313|EMBL:ABM09365.1}; DE EC=1.1.1.26 {ECO:0000313|EMBL:ABM09365.1}; GN OrderedLocusNames=AAur_4149 {ECO:0000313|EMBL:ABM09365.1}; OS Paenarthrobacter aurescens (strain TC1). OC Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales; OC Micrococcaceae; Paenarthrobacter. OX NCBI_TaxID=290340 {ECO:0000313|EMBL:ABM09365.1, ECO:0000313|Proteomes:UP000000637}; RN [1] {ECO:0000313|EMBL:ABM09365.1, ECO:0000313|Proteomes:UP000000637} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=TC1 {ECO:0000313|EMBL:ABM09365.1, RC ECO:0000313|Proteomes:UP000000637}; RX PubMed=17194220; DOI=10.1371/journal.pgen.0020214; RA Mongodin E.F., Shapir N., Daugherty S.C., DeBoy R.T., Emerson J.B., RA Shvartzbeyn A., Radune D., Vamathevan J., Riggs F., Grinberg V., Khouri H., RA Wackett L.P., Nelson K.E., Sadowsky M.J.; RT "Secrets of soil survival revealed by the genome sequence of Arthrobacter RT aurescens TC1."; RL PLoS Genet. 2:2094-2106(2006). CC -!- SIMILARITY: Belongs to the D-isomer specific 2-hydroxyacid CC dehydrogenase family. {ECO:0000256|ARBA:ARBA00005854, CC ECO:0000256|RuleBase:RU003719}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; CP000474; ABM09365.1; -; Genomic_DNA. DR RefSeq; WP_011776740.1; NC_008711.1. DR AlphaFoldDB; A1RC54; -. DR STRING; 290340.AAur_4149; -. DR KEGG; aau:AAur_4149; -. DR eggNOG; COG1052; Bacteria. DR HOGENOM; CLU_019796_1_2_11; -. DR OrthoDB; 117809at2; -. DR Proteomes; UP000000637; Chromosome. DR GO; GO:0005829; C:cytosol; IEA:TreeGrafter. DR GO; GO:0047964; F:glyoxylate reductase (NADH) activity; IEA:UniProtKB-EC. DR GO; GO:0030267; F:glyoxylate reductase (NADPH) activity; IEA:TreeGrafter. DR GO; GO:0016618; F:hydroxypyruvate reductase [NAD(P)H] activity; IEA:TreeGrafter. DR GO; GO:0051287; F:NAD binding; IEA:InterPro. DR CDD; cd05301; GDH; 1. DR FunFam; 3.40.50.720:FF:000203; D-3-phosphoglycerate dehydrogenase (SerA); 1. DR Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 2. DR InterPro; IPR050223; D-isomer_2-hydroxyacid_DH. 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; 2-HYDROXYACID DEHYDROGENASE-RELATED; 1. DR PANTHER; PTHR10996:SF283; GLYOXYLATE_HYDROXYPYRUVATE REDUCTASE B; 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 NAD {ECO:0000256|ARBA:ARBA00023027}; KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002, KW ECO:0000256|RuleBase:RU003719}; KW Reference proteome {ECO:0000313|Proteomes:UP000000637}. FT DOMAIN 6..324 FT /note="D-isomer specific 2-hydroxyacid dehydrogenase FT catalytic" FT /evidence="ECO:0000259|Pfam:PF00389" FT DOMAIN 109..292 FT /note="D-isomer specific 2-hydroxyacid dehydrogenase NAD- FT binding" FT /evidence="ECO:0000259|Pfam:PF02826" SQ SEQUENCE 329 AA; 34917 MW; E093C6997CF51542 CRC64; MGNHYLVTTA IPEPGLQLLS DAGQVTVLPD PPDYATLAAL CASGDYDVVL TQLRDVIDEP LLANARVKGV SNYAVGYNNI DVDAATRHGI LVGNTPGVLT DATADVAMLL ILGTARRVVE SDRVVRDGKF LGWEPEFMLG RDVSGAVLGL AGFGRIARAV ARRALGFGME ELFSPRPPGD RPVSDEELGE FAGKVRQVPW DSLVERSDFL SLHVPLNEQT RHLVDADVLG RMKSDAILIN TARGPVVDES ALVEALRNGV IGGAGLDVFE DEPRLAAGLA ELPNTVLLPH VGSATVPVRA EMARLSALNA IAIAEGRLPL HPVNPLSRA //