ID Q8U3T5_PYRFU Unreviewed; 333 AA.
AC Q8U3T5;
DT 01-JUN-2002, integrated into UniProtKB/TrEMBL.
DT 01-JUN-2002, sequence version 1.
DT 27-MAR-2024, entry version 112.
DE SubName: Full=Phosphoglycerate dehydrogenase {ECO:0000313|EMBL:AAL80494.1};
DE EC=1.1.1.95 {ECO:0000313|EMBL:AAL80494.1};
GN OrderedLocusNames=PF0370 {ECO:0000313|EMBL:AAL80494.1};
OS Pyrococcus furiosus (strain ATCC 43587 / DSM 3638 / JCM 8422 / Vc1).
OC Archaea; Euryarchaeota; Thermococci; Thermococcales; Thermococcaceae;
OC Pyrococcus.
OX NCBI_TaxID=186497 {ECO:0000313|EMBL:AAL80494.1, ECO:0000313|Proteomes:UP000001013};
RN [1] {ECO:0000313|EMBL:AAL80494.1, ECO:0000313|Proteomes:UP000001013}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 43587 / DSM 3638 / JCM 8422 / Vc1
RC {ECO:0000313|Proteomes:UP000001013};
RX PubMed=10430560;
RA Maeder D.L., Weiss R.B., Dunn D.M., Cherry J.L., Gonzalez J.M.,
RA DiRuggiero J., Robb F.T.;
RT "Divergence of the hyperthermophilic archaea Pyrococcus furiosus and P.
RT horikoshii inferred from complete genomic sequences.";
RL Genetics 152:1299-1305(1999).
CC -!- SIMILARITY: Belongs to the D-isomer specific 2-hydroxyacid
CC dehydrogenase family. {ECO:0000256|RuleBase:RU003719}.
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DR EMBL; AE009950; AAL80494.1; -; Genomic_DNA.
DR RefSeq; WP_011011484.1; NZ_CP023154.1.
DR AlphaFoldDB; Q8U3T5; -.
DR STRING; 186497.PF0370; -.
DR PaxDb; 186497-PF0370; -.
DR GeneID; 41712164; -.
DR KEGG; pfu:PF0370; -.
DR PATRIC; fig|186497.12.peg.385; -.
DR eggNOG; arCOG01755; Archaea.
DR HOGENOM; CLU_019796_1_0_2; -.
DR OrthoDB; 34275at2157; -.
DR PhylomeDB; Q8U3T5; -.
DR Proteomes; UP000001013; Chromosome.
DR GO; GO:0051287; F:NAD binding; IEA:InterPro.
DR GO; GO:0004617; F:phosphoglycerate dehydrogenase activity; IEA:UniProtKB-EC.
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; IPR029752; D-isomer_DH_CS1.
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.
DR PROSITE; PS00065; D_2_HYDROXYACID_DH_1; 1.
PE 3: Inferred from homology;
KW Oxidoreductase {ECO:0000256|RuleBase:RU003719,
KW ECO:0000313|EMBL:AAL80494.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000001013}.
FT DOMAIN 10..318
FT /note="D-isomer specific 2-hydroxyacid dehydrogenase
FT catalytic"
FT /evidence="ECO:0000259|Pfam:PF00389"
FT DOMAIN 106..286
FT /note="D-isomer specific 2-hydroxyacid dehydrogenase NAD-
FT binding"
FT /evidence="ECO:0000259|Pfam:PF02826"
SQ SEQUENCE 333 AA; 37966 MW; FAC7D2694121F61C CRC64;
MRPKVGVLLK MKREALEELE KYAEVEVIPY PSEEELKNKI HEFDGIIVSP VTKITKDVLE
KAERLKVISC HSAGYDHIDV EEATRKGIYV TKVSGLLSEA VAEFAVGLLI NLMRKIHYAD
KLIRRGEWES HVKIWTGFKG IESLYGKKVG ILGMGAIGKA IARRLIPFGV ELYYWSRHRK
VDVESELHAT YMDIDELLEK SDIVILALPL TKDTYHIINE ERVKKLEGKY LVNIGRGALV
DERAITEAIK QGKLKGYATD VFENEPVREH ELFKYEWETV LTPHYAGLAV EAQEDVGFRA
VENLISIFRG IVPEDLVNKE VLKIRPIESV KML
//
