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Database: UniProt
Entry: A0A0U5NQ01_9CLOT
LinkDB: A0A0U5NQ01_9CLOT
Original site: A0A0U5NQ01_9CLOT 
ID   A0A0U5NQ01_9CLOT        Unreviewed;       316 AA.
AC   A0A0U5NQ01;
DT   16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT   16-MAR-2016, sequence version 1.
DT   24-JAN-2024, entry version 19.
DE   SubName: Full=Putative 2-hydroxyacid dehydrogenase {ECO:0000313|EMBL:CUX22715.1};
DE            EC=1.-.-.- {ECO:0000313|EMBL:CUX22715.1};
GN   ORFNames=BN3456_00601 {ECO:0000313|EMBL:CUX22715.1};
OS   Clostridium sp. C105KSO13.
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC   Clostridium.
OX   NCBI_TaxID=1776045 {ECO:0000313|EMBL:CUX22715.1, ECO:0000313|Proteomes:UP000198973};
RN   [1] {ECO:0000313|EMBL:CUX22715.1, ECO:0000313|Proteomes:UP000198973}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C105KSO131 {ECO:0000313|EMBL:CUX22715.1};
RA   McClelland M., Jain A., Saraogi P., Mendelson R., Westerman R.,
RA   SanMiguel P., Csonka L.;
RL   Submitted (JAN-2016) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the D-isomer specific 2-hydroxyacid
CC       dehydrogenase family. {ECO:0000256|RuleBase:RU003719}.
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DR   EMBL; FBWL01000150; CUX22715.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0U5NQ01; -.
DR   STRING; 1776045.BN3456_00601; -.
DR   OrthoDB; 9805416at2; -.
DR   Proteomes; UP000198973; Unassembled WGS sequence.
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   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; PTHR43761; D-ISOMER SPECIFIC 2-HYDROXYACID DEHYDROGENASE FAMILY PROTEIN (AFU_ORTHOLOGUE AFUA_1G13630); 1.
DR   PANTHER; PTHR43761:SF1; 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; 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:UP000198973}.
FT   DOMAIN          27..315
FT                   /note="D-isomer specific 2-hydroxyacid dehydrogenase
FT                   catalytic"
FT                   /evidence="ECO:0000259|Pfam:PF00389"
FT   DOMAIN          110..285
FT                   /note="D-isomer specific 2-hydroxyacid dehydrogenase NAD-
FT                   binding"
FT                   /evidence="ECO:0000259|Pfam:PF02826"
SQ   SEQUENCE   316 AA;  35145 MW;  DB3BD34FEF68426B CRC64;
     MNDKTVVLNA GLVNYDGNVD YSKIASEVVI YDETPEDKIL ERVDGFTIVV TKEMKVSGDI
     IRKFPDSVKM ICEAGTGYNN IDLDAVREKG IVLCNIPAYS TKRVAHTAIL LILNLASSMQ
     KQIRMLSKGN HDNFHKHLMV DHVELNGKIL GVIGYGNIGK EIIKVAQALG MKILVSTRTP
     RKDAENIHFT TNEEVFRQSD FISLNCPLNE ATRHMINKET ITIMKPTAFL INTARGALID
     EKTLIEALQN KVIAGAGLDV QEAEPLDDAS PLYTMDNVII TPHMGWRGLE TRQRLVSLIQ
     DNITAFCKGQ PINRVD
//
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