ID D9SRP6_CLOC7 Unreviewed; 318 AA. AC D9SRP6; DT 05-OCT-2010, integrated into UniProtKB/TrEMBL. DT 05-OCT-2010, sequence version 1. DT 27-MAR-2024, entry version 55. DE SubName: Full=D-isomer specific 2-hydroxyacid dehydrogenase NAD-binding {ECO:0000313|EMBL:ADL50413.1}; GN OrderedLocusNames=Clocel_0642 {ECO:0000313|EMBL:ADL50413.1}; OS Clostridium cellulovorans (strain ATCC 35296 / DSM 3052 / OCM 3 / 743B). OC Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae; OC Clostridium. OX NCBI_TaxID=573061 {ECO:0000313|EMBL:ADL50413.1, ECO:0000313|Proteomes:UP000002730}; RN [1] {ECO:0000313|EMBL:ADL50413.1, ECO:0000313|Proteomes:UP000002730} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 35296 / DSM 3052 / OCM 3 / 743B RC {ECO:0000313|Proteomes:UP000002730}; RG US DOE Joint Genome Institute; RA Lucas S., Copeland A., Lapidus A., Cheng J.-F., Bruce D., Goodwin L., RA Pitluck S., Chertkov O., Detter J.C., Han C., Tapia R., Land M., Hauser L., RA Chang Y.-J., Jeffries C., Kyrpides N., Ivanova N., Mikhailova N., RA Hemme C.L., Woyke T.; RT "Complete sequence of Clostridium cellulovorans 743B."; RL Submitted (AUG-2010) to the EMBL/GenBank/DDBJ databases. 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; CP002160; ADL50413.1; -; Genomic_DNA. DR RefSeq; WP_013291604.1; NC_014393.1. DR AlphaFoldDB; D9SRP6; -. DR STRING; 573061.Clocel_0642; -. DR KEGG; ccb:Clocel_0642; -. DR eggNOG; COG1052; Bacteria. DR HOGENOM; CLU_019796_1_3_9; -. DR OrthoDB; 9805416at2; -. DR Proteomes; UP000002730; 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; cd12162; 2-Hacid_dh_4; 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; PTHR43761:SF1; 2-HACID_DH DOMAIN-CONTAINING PROTEIN-RELATED; 1. DR PANTHER; PTHR43761; D-ISOMER SPECIFIC 2-HYDROXYACID DEHYDROGENASE FAMILY PROTEIN (AFU_ORTHOLOGUE AFUA_1G13630); 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 Reference proteome {ECO:0000313|Proteomes:UP000002730}. FT DOMAIN 22..316 FT /note="D-isomer specific 2-hydroxyacid dehydrogenase FT catalytic" FT /evidence="ECO:0000259|Pfam:PF00389" FT DOMAIN 107..286 FT /note="D-isomer specific 2-hydroxyacid dehydrogenase NAD- FT binding" FT /evidence="ECO:0000259|Pfam:PF02826" SQ SEQUENCE 318 AA; 35260 MW; 1C78DFFDBBDFE68D CRC64; MKIVVLDGKV LNPGDLSWDG LKALGDVTIY DRTSKEEMLT RCESADILIT NKTPIRKEIL EKLPTLKYIG VLATGYNIVD VEYATSKNII VTNIPAYSTD SVVQLIFALL LELCHSVQKH SDLVKEECWV KCSDFAFWRF PLVELAGKTM GIIGFGSIGI ATAKVANAFG MKVMVYTRTI KEEFKELVTF CSKEELFTNS DVISLSAPLT KETEGIVNKK YLSMMKKTAF LINTSRGPLV IEQDLANALN NGDIAAAAVD VLSKEPPTKD NPLLTVKNII ITPHIAWATF EARKRLMNIA IDNVRKFLEG NPVNVVKE //