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Database: UniProt
Entry: W4QLE8_9BACI
LinkDB: W4QLE8_9BACI
Original site: W4QLE8_9BACI 
ID   W4QLE8_9BACI            Unreviewed;       319 AA.
AC   W4QLE8;
DT   19-MAR-2014, integrated into UniProtKB/TrEMBL.
DT   19-MAR-2014, sequence version 1.
DT   27-MAR-2024, entry version 30.
DE   SubName: Full=Glyoxylate reductase {ECO:0000313|EMBL:GAE32184.1};
GN   ORFNames=JCM9152_3706 {ECO:0000313|EMBL:GAE32184.1};
OS   Halalkalibacter hemicellulosilyticusJCM 9152.
OC   Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Halalkalibacter.
OX   NCBI_TaxID=1236971 {ECO:0000313|EMBL:GAE32184.1, ECO:0000313|Proteomes:UP000018895};
RN   [1] {ECO:0000313|EMBL:GAE32184.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JCM 9152 {ECO:0000313|EMBL:GAE32184.1};
RA   Yuki M., Oshima K., Suda W., Oshida Y., Kitamura K., Iida T., Hattori M.,
RA   Ohkuma M.;
RT   "Draft Genome Sequences of Three Alkaliphilic Bacillus Strains, Bacillus
RT   wakoensis JCM 9140T, Bacillus akibai JCM 9157T, and Bacillus
RT   hemicellulosilyticus JCM 9152T.";
RL   Genome Announc. 2:e01258-13(2014).
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:GAE32184.1}.
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DR   EMBL; BAUU01000030; GAE32184.1; -; Genomic_DNA.
DR   RefSeq; WP_035346501.1; NZ_BAZO01000030.1.
DR   AlphaFoldDB; W4QLE8; -.
DR   STRING; 1236971.JCM9152_3706; -.
DR   OrthoDB; 9805416at2; -.
DR   Proteomes; UP000018895; 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; cd05301; GDH; 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; PTHR10996:SF178; 2-HYDROXYACID DEHYDROGENASE YGL185C-RELATED; 1.
DR   PANTHER; PTHR10996; 2-HYDROXYACID DEHYDROGENASE-RELATED; 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:UP000018895}.
FT   DOMAIN          7..312
FT                   /note="D-isomer specific 2-hydroxyacid dehydrogenase
FT                   catalytic"
FT                   /evidence="ECO:0000259|Pfam:PF00389"
FT   DOMAIN          109..288
FT                   /note="D-isomer specific 2-hydroxyacid dehydrogenase NAD-
FT                   binding"
FT                   /evidence="ECO:0000259|Pfam:PF02826"
SQ   SEQUENCE   319 AA;  35659 MW;  0D8B341A7DCB7603 CRC64;
     MSRPIVFSDK PLPKEIQAYL ANHVKLTMWE EAHKLKREQL FEKLQGVDGF MTSGELINEE
     LLQNAPNLRA VSTISVGYDH FDLNAMRKHQ IIGTHTPYVL DDTVADLVLS LMLATARRIP
     ELDALTKSGC WKKGDSRQLF GVDVHHKKLG IIGMGRIGEK IAKRAKYGFD MDVSYFNRKR
     KKGMEQQLGL HYEELEVLLR ESDFIVLMVP LTNETKHFIG AHEFTLMKPS SIFINASRGQ
     TVDEEAMTEA LLTGEILAAG LDVYEQEPIH PTNPLLNLKN VVTLPHIGSA TSETRDAMAM
     MAAKNIVAAL TGVGSCYKV
//
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