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Database: UniProt
Entry: Q9HSS1_HALSA
LinkDB: Q9HSS1_HALSA
Original site: Q9HSS1_HALSA 
ID   Q9HSS1_HALSA            Unreviewed;       323 AA.
AC   Q9HSS1;
DT   01-MAR-2001, integrated into UniProtKB/TrEMBL.
DT   01-MAR-2001, sequence version 1.
DT   27-MAR-2024, entry version 128.
DE   SubName: Full=Phosphoglycerate dehydrogenase {ECO:0000313|EMBL:AAG18731.1};
DE   SubName: Full=Probable D-2-hydroxyacid dehydrogenase {ECO:0000313|EMBL:DAC77416.1};
DE            EC=1.1.1.- {ECO:0000313|EMBL:DAC77416.1};
GN   Name=serA3 {ECO:0000313|EMBL:AAG18731.1};
GN   OrderedLocusNames=VNG_0104G {ECO:0000313|EMBL:AAG18731.1};
OS   Halobacterium salinarum (strain ATCC 700922 / JCM 11081 / NRC-1)
OS   (Halobacterium halobium).
OC   Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Halobacteriales;
OC   Halobacteriaceae; Halobacterium; Halobacterium salinarum NRC-34001.
OX   NCBI_TaxID=64091 {ECO:0000313|EMBL:AAG18731.1, ECO:0000313|Proteomes:UP000000554};
RN   [1] {ECO:0000313|EMBL:AAG18731.1, ECO:0000313|Proteomes:UP000000554}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700922 / JCM 11081 / NRC-1
RC   {ECO:0000313|Proteomes:UP000000554}, and NRC-1
RC   {ECO:0000313|EMBL:AAG18731.1};
RX   PubMed=11016950; DOI=10.1073/pnas.190337797;
RA   Ng W.V., Kennedy S.P., Mahairas G.G., Berquist B., Pan M., Shukla H.D.,
RA   Lasky S.R., Baliga N.S., Thorsson V., Sbrogna J., Swartzell S., Weir D.,
RA   Hall J., Dahl T.A., Welti R., Goo Y.A., Leithauser B., Keller K., Cruz R.,
RA   Danson M.J., Hough D.W., Maddocks D.G., Jablonski P.E., Krebs M.P.,
RA   Angevine C.M., Dale H., Isenbarger T.A., Peck R.F., Pohlschroder M.,
RA   Spudich J.L., Jung K.W., Alam M., Freitas T., Hou S., Daniels C.J.,
RA   Dennis P.P., Omer A.D., Ebhardt H., Lowe T.M., Liang P., Riley M., Hood L.,
RA   DasSarma S.;
RT   "Genome sequence of Halobacterium species NRC-1.";
RL   Proc. Natl. Acad. Sci. U.S.A. 97:12176-12181(2000).
RN   [2] {ECO:0000313|EMBL:DAC77416.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=NRC-1 {ECO:0000313|EMBL:DAC77416.1};
RX   PubMed=18313895; DOI=.1016/j.ygeno.2008.01.001;
RA   Pfeiffer F., Schuster S.C., Broicher A., Falb M., Palm P., Rodewald K.,
RA   Ruepp A., Soppa J., Tittor J., Oesterhelt D.;
RT   "Evolution in the laboratory: the genome of Halobacterium salinarum strain
RT   R1 compared to that of strain NRC-1.";
RL   Genomics 91:335-346(2008).
RN   [3] {ECO:0000313|EMBL:DAC77416.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=NRC-1 {ECO:0000313|EMBL:DAC77416.1};
RX   PubMed=26042526;
RA   Pfeiffer F., Oesterhelt D.;
RT   "A manual curation strategy to improve genome annotation: application to a
RT   set of haloarchael genomes.";
RL   Life 5:1427-1444(2015).
RN   [4] {ECO:0000313|EMBL:DAC77416.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=NRC-1 {ECO:0000313|EMBL:DAC77416.1};
RA   Pfeiffer F., Marchfelder A., Habermann B.H., Dyall-Smith M.;
RT   "The genome of the Halobacterium salinarum type strain is closely related
RT   to that of the laboratory strains NRC-1 and R1.";
RL   Microbiol. Resour. Announc. 0:0-0(2019).
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
CC   -!- SIMILARITY: Belongs to the D-isomer specific 2-hydroxyacid
CC       dehydrogenase family. {ECO:0000256|RuleBase:RU003719}.
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DR   EMBL; AE004437; AAG18731.1; -; Genomic_DNA.
DR   EMBL; BK010829; DAC77416.1; -; Genomic_DNA.
DR   PIR; G84170; G84170.
DR   RefSeq; WP_010902026.1; NC_002607.1.
DR   AlphaFoldDB; Q9HSS1; -.
DR   STRING; 64091.VNG_0104G; -.
DR   PaxDb; 64091-VNG_0104G; -.
DR   GeneID; 68693080; -.
DR   KEGG; hal:VNG_0104G; -.
DR   PATRIC; fig|64091.14.peg.67; -.
DR   HOGENOM; CLU_019796_1_3_2; -.
DR   OrthoDB; 34275at2157; -.
DR   Proteomes; UP000000554; 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:0003714; F:transcription corepressor activity; IEA:InterPro.
DR   CDD; cd05299; CtBP_dh; 1.
DR   Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 2.
DR   InterPro; IPR043322; CtBP.
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:SF1; 2-HACID_DH DOMAIN-CONTAINING PROTEIN-RELATED; 1.
DR   PANTHER; PTHR43761; 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   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW   ECO:0000256|RuleBase:RU003719};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000554}.
FT   DOMAIN          35..317
FT                   /note="D-isomer specific 2-hydroxyacid dehydrogenase
FT                   catalytic"
FT                   /evidence="ECO:0000259|Pfam:PF00389"
FT   DOMAIN          115..289
FT                   /note="D-isomer specific 2-hydroxyacid dehydrogenase NAD-
FT                   binding"
FT                   /evidence="ECO:0000259|Pfam:PF02826"
SQ   SEQUENCE   323 AA;  32877 MW;  CBDAF95AC756D462 CRC64;
     MFTVLVSDGM GMLGALPDAV ADRATRDVAF EHRRVETGEG LVAAVDDTGA DAVVGGPETP
     VPAETIAEID GDVAAIVRAG VGVDAIDCAA AADHGVAVAN APSYCTREVG EHALSLVFGA
     ARRLHEYDRQ TRRGGWAWND APAPLRLADA TVGFVGFGEI ARGVADTATT VAESVIAYDP
     YVDAATAERH GVAMAEFEAV CAQSDVLVVF APLTEETRGL VDEAACNRLP EGAVVVNVGR
     GAVVDDAALA GALEDGPVSA AALDVLPTEP PVESPLVGRS DVLVTPHCGW YSEAAAESLV
     ASLAGTVAAV ADGDGVPERT RVA
//
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