ID G0HLZ1_THES4 Unreviewed; 304 AA.
AC G0HLZ1;
DT 19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT 19-OCT-2011, sequence version 1.
DT 27-MAR-2024, entry version 58.
DE SubName: Full=Phosphoglycerate dehydrogenase {ECO:0000313|EMBL:AEK73534.1};
GN OrderedLocusNames=GQS_08190 {ECO:0000313|EMBL:AEK73534.1};
OS Thermococcus sp. (strain CGMCC 1.5172 / 4557).
OC Archaea; Euryarchaeota; Thermococci; Thermococcales; Thermococcaceae;
OC Thermococcus.
OX NCBI_TaxID=1042877 {ECO:0000313|EMBL:AEK73534.1, ECO:0000313|Proteomes:UP000000874};
RN [1] {ECO:0000313|EMBL:AEK73534.1, ECO:0000313|Proteomes:UP000000874}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CGMCC 1.5172 / 4557 {ECO:0000313|Proteomes:UP000000874};
RX PubMed=21914870; DOI=10.1128/JB.05851-11;
RA Wang X., Gao Z., Xu X., Ruan L.;
RT "Complete genome sequence of Thermococcus sp. strain 4557, a
RT hyperthermophilic archaeon isolated from a deep-sea hydrothermal vent
RT area.";
RL J. Bacteriol. 193:5544-5545(2011).
CC -!- SIMILARITY: Belongs to the D-isomer specific 2-hydroxyacid
CC dehydrogenase family. {ECO:0000256|ARBA:ARBA00005854,
CC ECO:0000256|RuleBase:RU003719}.
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DR EMBL; CP002920; AEK73534.1; -; Genomic_DNA.
DR RefSeq; WP_014013216.1; NC_015865.1.
DR AlphaFoldDB; G0HLZ1; -.
DR STRING; 1042877.GQS_08190; -.
DR GeneID; 11016314; -.
DR KEGG; the:GQS_08190; -.
DR PATRIC; fig|1042877.9.peg.1591; -.
DR eggNOG; arCOG01754; Archaea.
DR HOGENOM; CLU_019796_1_3_2; -.
DR OrthoDB; 7437at2157; -.
DR Proteomes; UP000000874; Chromosome.
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 GO; GO:0008652; P:amino acid biosynthetic process; IEA:UniProtKB-KW.
DR CDD; cd12173; PGDH_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; IPR029752; D-isomer_DH_CS1.
DR InterPro; IPR006140; D-isomer_DH_NAD-bd.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR PANTHER; PTHR42789; D-ISOMER SPECIFIC 2-HYDROXYACID DEHYDROGENASE FAMILY PROTEIN (AFU_ORTHOLOGUE AFUA_6G10090); 1.
DR PANTHER; PTHR42789:SF1; D-ISOMER SPECIFIC 2-HYDROXYACID DEHYDROGENASE FAMILY PROTEIN (AFU_ORTHOLOGUE AFUA_6G10090); 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.
DR PROSITE; PS00670; D_2_HYDROXYACID_DH_2; 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}.
FT DOMAIN 3..304
FT /note="D-isomer specific 2-hydroxyacid dehydrogenase
FT catalytic"
FT /evidence="ECO:0000259|Pfam:PF00389"
FT DOMAIN 105..280
FT /note="D-isomer specific 2-hydroxyacid dehydrogenase NAD-
FT binding"
FT /evidence="ECO:0000259|Pfam:PF02826"
SQ SEQUENCE 304 AA; 32957 MW; 8199DDD20B7CE2DA CRC64;
MKVLVAAPLH EKAIDVLKNA GFEIVYEEYP DEARLLELVG DVEAIIVRSK PKVTRKVIEA
APKLKVIGRA GVGLDNIDLE AAKERGIKVV NSPGASSRSV AELAVALTFN VARKVAFADR
KMREGTWAKK QAMGIELEGK TLGVVGFGRI GYEVARIAHA LGMKVLLYDP YPNEERAKEV
GGTFVSLEDL LRESDVVTLH VPLIEQTYHL INEERLKLMK PTAILINAAR GAVVDTNALV
RALKEGWIAG AGLDVFEEEP LPADHPLTKL DNVVLTPHIG ASTVEAQMRA GVQVAEQIVE
ALKG
//
