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Database: UniProt
Entry: A0A0P7ZKZ6_9GAMM
LinkDB: A0A0P7ZKZ6_9GAMM
Original site: A0A0P7ZKZ6_9GAMM 
ID   A0A0P7ZKZ6_9GAMM        Unreviewed;       315 AA.
AC   A0A0P7ZKZ6;
DT   20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT   20-JAN-2016, sequence version 1.
DT   27-MAR-2024, entry version 22.
DE   SubName: Full=D-3-phosphoglycerate dehydrogenase {ECO:0000313|EMBL:KPQ02771.1};
DE            EC=1.1.1.95 {ECO:0000313|EMBL:KPQ02771.1};
GN   Name=serA {ECO:0000313|EMBL:KPQ02771.1};
GN   ORFNames=HLUCCO02_07865 {ECO:0000313|EMBL:KPQ02771.1};
OS   Idiomarinaceae bacterium HL-53.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Alteromonadales;
OC   Idiomarinaceae.
OX   NCBI_TaxID=1298881 {ECO:0000313|EMBL:KPQ02771.1, ECO:0000313|Proteomes:UP000053932};
RN   [1] {ECO:0000313|EMBL:KPQ02771.1, ECO:0000313|Proteomes:UP000053932}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=HL-53 {ECO:0000313|EMBL:KPQ02771.1};
RA   Nelson W.C., Romine M.F., Lindemann S.R.;
RT   "Identification and resolution of microdiversity through metagenomic
RT   sequencing of parallel consortia.";
RL   Submitted (AUG-2015) to the EMBL/GenBank/DDBJ databases.
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:KPQ02771.1}.
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DR   EMBL; LIHO01000011; KPQ02771.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0P7ZKZ6; -.
DR   STRING; 1298881.Ga0003345_0039; -.
DR   PATRIC; fig|1298881.4.peg.1216; -.
DR   Proteomes; UP000053932; Unassembled WGS sequence.
DR   GO; GO:0051287; F:NAD binding; IEA:InterPro.
DR   GO; GO:0004617; F:phosphoglycerate dehydrogenase activity; IEA:UniProtKB-EC.
DR   CDD; cd12172; PGDH_like_2; 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; 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.
PE   3: Inferred from homology;
KW   NAD {ECO:0000256|ARBA:ARBA00023027};
KW   Oxidoreductase {ECO:0000256|RuleBase:RU003719,
KW   ECO:0000313|EMBL:KPQ02771.1}.
FT   DOMAIN          33..311
FT                   /note="D-isomer specific 2-hydroxyacid dehydrogenase
FT                   catalytic"
FT                   /evidence="ECO:0000259|Pfam:PF00389"
FT   DOMAIN          114..286
FT                   /note="D-isomer specific 2-hydroxyacid dehydrogenase NAD-
FT                   binding"
FT                   /evidence="ECO:0000259|Pfam:PF02826"
SQ   SEQUENCE   315 AA;  34519 MW;  D3BC919CF0EF3148 CRC64;
     MKRVLVTCPP MLGMFEQFIE PAKELGLELV PAQTTQVLSE EELIKLLPDY DGWIIGDDPA
     TRQVFAAAKS GKLVAAVKWG IGVDNVDFEA CKDLGIPIIN TPNMFGTEVA DVAMAYLLGL
     ARQTYFIDRE IRQNHAWPKP AGMSLTGKHI GVVGFGDIGY NVAKRLMGFD VTVTAYDPGV
     EGNRDLQYVQ RKSWPEGLAK LDFLVFTCAL NKHNFHMLNA ETLSQLKAGT HIVNVARGPL
     IDEKALIDAL ESGHITAAGL DVFEVEPLPK ESPLRKMPQC IFGSHNSSNT REGVIRASHK
     ALSEIARFFN EVSAG
//
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