ID A0A1Y3TNE5_9FIRM Unreviewed; 312 AA.
AC A0A1Y3TNE5;
DT 30-AUG-2017, integrated into UniProtKB/TrEMBL.
DT 30-AUG-2017, sequence version 1.
DT 27-MAR-2024, entry version 18.
DE SubName: Full=Hydroxyacid dehydrogenase {ECO:0000313|EMBL:OUN34500.1};
GN ORFNames=B5G27_07010 {ECO:0000313|EMBL:OUN34500.1};
OS Lachnoclostridium sp. An76.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Lachnospiraceae.
OX NCBI_TaxID=1965654 {ECO:0000313|EMBL:OUN34500.1, ECO:0000313|Proteomes:UP000199802};
RN [1] {ECO:0000313|Proteomes:UP000199802}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=An76 {ECO:0000313|Proteomes:UP000199802};
RA Medvecky M., Cejkova D., Polansky O., Karasova D., Kubasova T., Cizek A.,
RA Rychlik I.;
RT "Function of individual gut microbiota members based on whole genome
RT sequencing of pure cultures obtained from chicken caecum.";
RL Submitted (APR-2017) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the D-isomer specific 2-hydroxyacid
CC dehydrogenase family. {ECO:0000256|RuleBase:RU003719}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:OUN34500.1}.
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DR EMBL; NFHL01000003; OUN34500.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1Y3TNE5; -.
DR OrthoDB; 9805416at2; -.
DR Proteomes; UP000199802; 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: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; 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:UP000199802}.
FT DOMAIN 20..310
FT /note="D-isomer specific 2-hydroxyacid dehydrogenase
FT catalytic"
FT /evidence="ECO:0000259|Pfam:PF00389"
FT DOMAIN 106..287
FT /note="D-isomer specific 2-hydroxyacid dehydrogenase NAD-
FT binding"
FT /evidence="ECO:0000259|Pfam:PF02826"
SQ SEQUENCE 312 AA; 34704 MW; 57EC3F6D40435996 CRC64;
MKIVFLDAST LGDDIDYSQF EQLGEVVRYP FTSSEEAPAR VTDADVLVVN KVLVNRQTIA
DAKNLKLVCV TATGTNNLDK DYLAERGIEW RNVAGYSTES VAQHTFAMLF YLMENLRYYD
DYVKSGSYIN DRIFTHFART FHELKGMTWG ILGLGAIGRR VADIAGLFGA RVIYYSASGA
PAQEGYHQVD LDTLLSESDI LSIHAPLNEY TEGLMDKDAF CKMKSDAILL NLGRGPIINE
ADLADALNAG EIRAAGLDVL SVEPMAMDSP LLNVKDKDRL FITPHIAWAT IEARQRLMKI
IAGQIEEFME AR
//
