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
//