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
//