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Database: UniProt
Entry: A0A0A1YHZ6_9PSED
LinkDB: A0A0A1YHZ6_9PSED
Original site: A0A0A1YHZ6_9PSED 
ID   A0A0A1YHZ6_9PSED        Unreviewed;       321 AA.
AC   A0A0A1YHZ6;
DT   04-FEB-2015, integrated into UniProtKB/TrEMBL.
DT   04-FEB-2015, sequence version 1.
DT   24-JAN-2024, entry version 24.
DE   SubName: Full=Glycerate dehydrogenase {ECO:0000313|EMBL:KFX68269.1};
DE            EC=1.1.1.29 {ECO:0000313|EMBL:KFX68269.1};
GN   ORFNames=TMS3_0118665 {ECO:0000313|EMBL:KFX68269.1};
OS   Pseudomonas taeanensis MS-3.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=1395571 {ECO:0000313|EMBL:KFX68269.1, ECO:0000313|Proteomes:UP000030063};
RN   [1] {ECO:0000313|EMBL:KFX68269.1, ECO:0000313|Proteomes:UP000030063}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MS-3 {ECO:0000313|EMBL:KFX68269.1,
RC   ECO:0000313|Proteomes:UP000030063};
RX   PubMed=24407626;
RA   Lee S.Y., Kim S.H., Lee D.G., Shin S., Yun S.H., Choi C.W., Chung Y.H.,
RA   Choi J.S., Kahng H.Y., Kim S.I.;
RT   "Draft Genome Sequence of Petroleum Oil-Degrading Marine Bacterium
RT   Pseudomonas taeanensis Strain MS-3, Isolated from a Crude Oil-Contaminated
RT   Seashore.";
RL   Genome Announc. 2:0-0(2014).
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:KFX68269.1}.
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DR   EMBL; AWSQ01000006; KFX68269.1; -; Genomic_DNA.
DR   RefSeq; WP_025166718.1; NZ_AWSQ01000006.1.
DR   AlphaFoldDB; A0A0A1YHZ6; -.
DR   STRING; 1395571.TMS3_0118665; -.
DR   eggNOG; COG1052; Bacteria.
DR   OrthoDB; 9805416at2; -.
DR   Proteomes; UP000030063; Unassembled WGS sequence.
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; D-ISOMER SPECIFIC 2-HYDROXYACID DEHYDROGENASE FAMILY PROTEIN (AFU_ORTHOLOGUE AFUA_1G13630); 1.
DR   PANTHER; PTHR43761:SF1; 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:UP000030063}.
FT   DOMAIN          21..318
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;  34213 MW;  C8857E04C249F83B CRC64;
     MSNSSLAVFL DHSSLDLGDL DLTPLKQCFA ELRLHGQSTP GQVIERLQGA HVAISNKVPL
     DAETFAACPE LKLVLVAATG TNNIDLAGAR EHGVTVCNCQ GYGTPSVAQH TLMLLLALAT
     RLPDYQTAVR AGRWQQAQQF CLLDFPIVEL EGKTLGLLGH GELGGAVATL AEAFGMRVLL
     GQLPGRQPRP DRVPLDELLP QVDALTLHCP LNDATRDLIG EDELNLMKPG AFLINTARGG
     LVNEQALAAA LRRGHLGGAA TDVLTQEPPK SGNPLLANDI PRLIVTPHSA WGSREARQRI
     VGQLLENAQA FFSGAPRRVV G
//
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