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Database: UniProt
Entry: A0A089WQQ4_9PSED
LinkDB: A0A089WQQ4_9PSED
Original site: A0A089WQQ4_9PSED 
ID   A0A089WQQ4_9PSED        Unreviewed;       321 AA.
AC   A0A089WQQ4;
DT   26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT   26-NOV-2014, sequence version 1.
DT   27-MAR-2024, entry version 31.
DE   SubName: Full=Glycerate dehydrogenase {ECO:0000313|EMBL:AIR89494.1};
DE            EC=1.1.1.29 {ECO:0000313|EMBL:AIR89494.1};
GN   ORFNames=LK03_09460 {ECO:0000313|EMBL:AIR89494.1};
OS   Pseudomonas cremoricolorata.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=157783 {ECO:0000313|EMBL:AIR89494.1, ECO:0000313|Proteomes:UP000029493};
RN   [1] {ECO:0000313|EMBL:AIR89494.1, ECO:0000313|Proteomes:UP000029493}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ND07 {ECO:0000313|EMBL:AIR89494.1,
RC   ECO:0000313|Proteomes:UP000029493};
RA   Chan K.-G.;
RL   Submitted (SEP-2014) 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; CP009455; AIR89494.1; -; Genomic_DNA.
DR   RefSeq; WP_038412076.1; NZ_CP009455.1.
DR   AlphaFoldDB; A0A089WQQ4; -.
DR   STRING; 157783.LK03_09460; -.
DR   KEGG; psw:LK03_09460; -.
DR   eggNOG; COG1052; Bacteria.
DR   OrthoDB; 9805416at2; -.
DR   Proteomes; UP000029493; Chromosome.
DR   GO; GO:0008465; F:glycerate dehydrogenase activity; IEA:UniProtKB-EC.
DR   GO; GO:0051287; F:NAD binding; IEA:InterPro.
DR   CDD; cd12162; 2-Hacid_dh_4; 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; 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; 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:UP000029493}.
FT   DOMAIN          19..317
FT                   /note="D-isomer specific 2-hydroxyacid dehydrogenase
FT                   catalytic"
FT                   /evidence="ECO:0000259|Pfam:PF00389"
FT   DOMAIN          112..290
FT                   /note="D-isomer specific 2-hydroxyacid dehydrogenase NAD-
FT                   binding"
FT                   /evidence="ECO:0000259|Pfam:PF02826"
SQ   SEQUENCE   321 AA;  33696 MW;  9BB4A9E75500ECDB CRC64;
     MSSLRRVVFL DHASLDLGDL DLSPLHEAFD EVQLHDATEP AQVAQRLQGA VAVISNKVQI
     DAEILAANPQ LKLVLIAATG TNNVDLAAAR AQGVTVCNCQ GYGTASVAQH TLALLLALTT
     RLCDYQRAVS EGRWAAAKQF CLLDFPISEL SGKTLGVLGH GELGGAVARL AEAFGMRVLS
     GQIPGRPARA ERIPLAELLP QVDALTLHCP LNEHTRHLLG AAELAQLKPG ALVVNTARGG
     LIDEQALADA LRSGHLGGAA TDVLSVEPPV DGNPLLAADI PRLIITPHSA WGAVEARQRI
     VGQLAENARG FFAGQALRVV S
//
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