ID F8DDT3_HALXS Unreviewed; 325 AA.
AC F8DDT3;
DT 21-SEP-2011, integrated into UniProtKB/TrEMBL.
DT 21-SEP-2011, sequence version 1.
DT 27-MAR-2024, entry version 51.
DE SubName: Full=Phosphoglycerate dehydrogenase {ECO:0000313|EMBL:AEH39186.1};
DE EC=1.1.1.95 {ECO:0000313|EMBL:AEH39186.1};
GN OrderedLocusNames=Halxa_0597 {ECO:0000313|EMBL:AEH39186.1};
OS Halopiger xanaduensis (strain DSM 18323 / JCM 14033 / SH-6).
OG Plasmid pHALXA01 {ECO:0000313|EMBL:AEH39186.1,
OG ECO:0000313|Proteomes:UP000006794}.
OC Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Natrialbales;
OC Natrialbaceae; Halopiger.
OX NCBI_TaxID=797210 {ECO:0000313|EMBL:AEH39186.1, ECO:0000313|Proteomes:UP000006794};
RN [1] {ECO:0000313|Proteomes:UP000006794}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 18323 / JCM 14033 / SH-6
RC {ECO:0000313|Proteomes:UP000006794};
RC PLASMID=Plasmid pHALXA01 {ECO:0000313|Proteomes:UP000006794};
RX PubMed=22675596; DOI=10.4056/sigs.2505605;
RA Anderson I., Tindall B.J., Rohde M., Lucas S., Han J., Lapidus A.,
RA Cheng J.F., Goodwin L., Pitluck S., Peters L., Pati A., Mikhailova N.,
RA Pagani I., Teshima H., Han C., Tapia R., Land M., Woyke T., Klenk H.P.,
RA Kyrpides N., Ivanova N.;
RT "Complete genome sequence of Halopiger xanaduensis type strain (SH-6(T)).";
RL Stand. Genomic Sci. 6:31-42(2012).
CC -!- SIMILARITY: Belongs to the D-isomer specific 2-hydroxyacid
CC dehydrogenase family. {ECO:0000256|RuleBase:RU003719}.
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DR EMBL; CP002840; AEH39186.1; -; Genomic_DNA.
DR RefSeq; WP_013875914.1; NC_015658.1.
DR AlphaFoldDB; F8DDT3; -.
DR GeneID; 10795454; -.
DR KEGG; hxa:Halxa_0597; -.
DR HOGENOM; CLU_019796_1_0_2; -.
DR OrthoDB; 168224at2157; -.
DR Proteomes; UP000006794; Plasmid pHALXA01.
DR GO; GO:0051287; F:NAD binding; IEA:InterPro.
DR GO; GO:0004617; F:phosphoglycerate dehydrogenase activity; IEA:UniProtKB-EC.
DR CDD; cd05300; 2-Hacid_dh_1; 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; 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; PS00671; D_2_HYDROXYACID_DH_3; 1.
PE 3: Inferred from homology;
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000256|RuleBase:RU003719}; Plasmid {ECO:0000313|EMBL:AEH39186.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000006794}.
FT DOMAIN 34..310
FT /note="D-isomer specific 2-hydroxyacid dehydrogenase
FT catalytic"
FT /evidence="ECO:0000259|Pfam:PF00389"
FT DOMAIN 112..286
FT /note="D-isomer specific 2-hydroxyacid dehydrogenase NAD-
FT binding"
FT /evidence="ECO:0000259|Pfam:PF02826"
SQ SEQUENCE 325 AA; 35306 MW; 83DF3B42A7D16B48 CRC64;
MSTNPDIVVL REGTEGLSME SYAETLRDRL PEHTVALART PKEERELVPQ ARVVTGITID
ESLLEAADRL ELFACTFAGT DHVPMDALAE REVAVTNAGG IHAPGIAEQT IANMLVFARN
LHEGWRRKRN GEWRHFQSSE FTDSTVTVVG LGSIGQAVVK RLEGFEVETI GIRYTPEKGG
PTDEVLGFEE ADIHEAFSRS DYVVLACPLN DLTCGLVGEE ELATLPPNAV LVNAARGGLV
DTDALVAALQ SEGIRGAALD VTDPEPLPTD HELWDLENCL LTPHTGGHTP KHWDRLADIV
AANVAALEAD EDEAFENVVY RPESN
//
