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Database: UniProt
Entry: A0A1Z5I908_9LACO
LinkDB: A0A1Z5I908_9LACO
Original site: A0A1Z5I908_9LACO 
ID   A0A1Z5I908_9LACO        Unreviewed;       320 AA.
AC   A0A1Z5I908;
DT   27-SEP-2017, integrated into UniProtKB/TrEMBL.
DT   27-SEP-2017, sequence version 1.
DT   24-JAN-2024, entry version 18.
DE   SubName: Full=2-hydroxyacid dehydrogenase {ECO:0000313|EMBL:GAW98242.1};
GN   ORFNames=IWT30_00186 {ECO:0000313|EMBL:GAW98242.1};
OS   Secundilactobacillus mixtipabuli.
OC   Bacteria; Bacillota; Bacilli; Lactobacillales; Lactobacillaceae;
OC   Secundilactobacillus.
OX   NCBI_TaxID=1435342 {ECO:0000313|EMBL:GAW98242.1, ECO:0000313|Proteomes:UP000198374};
RN   [1] {ECO:0000313|EMBL:GAW98242.1, ECO:0000313|Proteomes:UP000198374}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=IWT30 {ECO:0000313|EMBL:GAW98242.1,
RC   ECO:0000313|Proteomes:UP000198374};
RA   Tohno M., Tanizawa Y., Arita M.;
RT   "Draft genome sequences of new species of the genus Lactobacillus isolated
RT   from orchardgrass silage.";
RL   Submitted (NOV-2015) 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   -!- 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:GAW98242.1}.
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DR   EMBL; BCMF01000001; GAW98242.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1Z5I908; -.
DR   OrthoDB; 9805416at2; -.
DR   Proteomes; UP000198374; 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   CDD; cd12178; 2-Hacid_dh_13; 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; IPR029753; D-isomer_DH_CS.
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; PTHR42789; D-ISOMER SPECIFIC 2-HYDROXYACID DEHYDROGENASE FAMILY PROTEIN (AFU_ORTHOLOGUE AFUA_6G10090); 1.
DR   PANTHER; PTHR42789:SF1; D-ISOMER SPECIFIC 2-HYDROXYACID DEHYDROGENASE FAMILY PROTEIN (AFU_ORTHOLOGUE AFUA_6G10090); 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.
DR   PROSITE; PS00671; D_2_HYDROXYACID_DH_3; 1.
PE   3: Inferred from homology;
KW   Amino-acid biosynthesis {ECO:0000256|ARBA:ARBA00022605};
KW   Oxidoreductase {ECO:0000256|RuleBase:RU003719};
KW   Reference proteome {ECO:0000313|Proteomes:UP000198374}.
FT   DOMAIN          8..319
FT                   /note="D-isomer specific 2-hydroxyacid dehydrogenase
FT                   catalytic"
FT                   /evidence="ECO:0000259|Pfam:PF00389"
FT   DOMAIN          109..287
FT                   /note="D-isomer specific 2-hydroxyacid dehydrogenase NAD-
FT                   binding"
FT                   /evidence="ECO:0000259|Pfam:PF02826"
SQ   SEQUENCE   320 AA;  34446 MW;  0D67A1B9B58E037F CRC64;
     MTKVYLSAQL PEVATQQLQK AGLDVSAYEG EGLISHDELL KNVSDIDFLI TPLSTKVDKE
     IIDAAPKLKL IANFGAGFNN IDTAYAKEKG IPVTNTPAVS TNAVAEVTIG LMLALSHRMV
     EGDQKMRNEG FPGWAPLYFL GHEIAGKTLG IFGLGNIGSD VARKANALGM NVQYYKPNRL
     SDPEERSMKV TYKPLDELIK TSDFITINAP QTPETTHKFD AAAFKAMKKT AYIVNVGRGP
     IIDEAALLEA LKSGEIAGAA LDVYEKEPKV DDGFKSLKNV VLTPHVGNAT VEARDAMANI
     VAGNVLLVNS GKDAKFIVNK
//
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