ID L0AG38_NATGS Unreviewed; 527 AA.
AC L0AG38;
DT 06-MAR-2013, integrated into UniProtKB/TrEMBL.
DT 06-MAR-2013, sequence version 1.
DT 27-MAR-2024, entry version 66.
DE RecName: Full=D-3-phosphoglycerate dehydrogenase {ECO:0000256|ARBA:ARBA00021582, ECO:0000256|RuleBase:RU363003};
DE EC=1.1.1.95 {ECO:0000256|ARBA:ARBA00013143, ECO:0000256|RuleBase:RU363003};
GN OrderedLocusNames=Natgr_1696 {ECO:0000313|EMBL:AFZ72893.1};
GN ORFNames=C490_07411 {ECO:0000313|EMBL:ELY69680.1}, CYV19_01920
GN {ECO:0000313|EMBL:PLK21879.1};
OS Natronobacterium gregoryi (strain ATCC 43098 / DSM 3393 / CCM 3738 / CIP
OS 104747 / IAM 13177 / JCM 8860 / NBRC 102187 / NCIMB 2189 / SP2).
OC Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Natrialbales;
OC Natrialbaceae; Natronobacterium.
OX NCBI_TaxID=797304 {ECO:0000313|EMBL:AFZ72893.1, ECO:0000313|Proteomes:UP000010468};
RN [1] {ECO:0000313|EMBL:AFZ72893.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=SP2 {ECO:0000313|EMBL:AFZ72893.1};
RG US DOE Joint Genome Institute;
RA Lucas S., Han J., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S.,
RA Peters L., Mikhailova N., Teshima H., Detter J.C., Han C., Tapia R.,
RA Land M., Hauser L., Kyrpides N., Ivanova N., Pagani I., Sproer C.,
RA Anderson I., Woyke T.;
RT "Complete sequence of Natronobacterium gregoryi SP2.";
RL Submitted (MAR-2012) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Proteomes:UP000010468}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 43098 / CCM 3738 / NCIMB 2189 / SP2
RC {ECO:0000313|Proteomes:UP000010468};
RA Lucas S., Han J., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S.,
RA Peters L., Mikhailova N., Teshima H., Detter J.C., Han C., Tapia R.,
RA Land M., Hauser L., Kyrpides N., Ivanova N., Pagani I., Sproer C.,
RA Anderson I., Woyke T.;
RT "Complete sequence of Natronobacterium gregoryi SP2.";
RL Submitted (MAR-2012) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|EMBL:ELY69680.1, ECO:0000313|Proteomes:UP000011613}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SP2 {ECO:0000313|EMBL:ELY69680.1,
RC ECO:0000313|Proteomes:UP000011613};
RX PubMed=25393412; DOI=10.1371/journal.pgen.1004784;
RA Becker E.A., Seitzer P.M., Tritt A., Larsen D., Krusor M., Yao A.I., Wu D.,
RA Madern D., Eisen J.A., Darling A.E., Facciotti M.T.;
RT "Phylogenetically driven sequencing of extremely halophilic archaea reveals
RT strategies for static and dynamic osmo-response.";
RL PLoS Genet. 10:E1004784-E1004784(2014).
RN [4] {ECO:0000313|EMBL:PLK21879.1, ECO:0000313|Proteomes:UP000234484}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SP2 {ECO:0000313|EMBL:PLK21879.1,
RC ECO:0000313|Proteomes:UP000234484};
RC TISSUE=Freeze-dried powder thallus {ECO:0000313|EMBL:PLK21879.1};
RA Jiang L., He B., Kang J., Yu M., Li N., Fang Y., Tang Z., Wu P., Yao P.,
RA Huang J.;
RT "The characterization of oligonucleotides binding to NgAgo.";
RL Submitted (DEC-2017) to the EMBL/GenBank/DDBJ databases.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(2R)-3-phosphoglycerate + NAD(+) = 3-phosphooxypyruvate + H(+)
CC + NADH; Xref=Rhea:RHEA:12641, ChEBI:CHEBI:15378, ChEBI:CHEBI:18110,
CC ChEBI:CHEBI:57540, ChEBI:CHEBI:57945, ChEBI:CHEBI:58272; EC=1.1.1.95;
CC Evidence={ECO:0000256|ARBA:ARBA00001878,
CC ECO:0000256|RuleBase:RU363003};
CC -!- PATHWAY: Amino-acid biosynthesis; L-serine biosynthesis; L-serine from
CC 3-phospho-D-glycerate: step 1/3. {ECO:0000256|ARBA:ARBA00005216,
CC ECO:0000256|RuleBase:RU363003}.
CC -!- SIMILARITY: Belongs to the D-isomer specific 2-hydroxyacid
CC dehydrogenase family. {ECO:0000256|ARBA:ARBA00005854,
CC ECO:0000256|RuleBase:RU363003}.
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DR EMBL; CP003377; AFZ72893.1; -; Genomic_DNA.
DR EMBL; AOIC01000060; ELY69680.1; -; Genomic_DNA.
DR EMBL; PKKI01000004; PLK21879.1; -; Genomic_DNA.
DR RefSeq; WP_005578418.1; NZ_PKKI01000004.1.
DR AlphaFoldDB; L0AG38; -.
DR STRING; 797304.Natgr_1696; -.
DR GeneID; 14208860; -.
DR KEGG; nge:Natgr_1696; -.
DR PATRIC; fig|797304.7.peg.1498; -.
DR eggNOG; arCOG01754; Archaea.
DR HOGENOM; CLU_019796_8_1_2; -.
DR UniPathway; UPA00135; UER00196.
DR Proteomes; UP000010468; Chromosome.
DR Proteomes; UP000011613; Unassembled WGS sequence.
DR Proteomes; UP000234484; Unassembled WGS sequence.
DR GO; GO:0051287; F:NAD binding; IEA:UniProtKB-UniRule.
DR GO; GO:0004617; F:phosphoglycerate dehydrogenase activity; IEA:UniProtKB-EC.
DR GO; GO:0006564; P:L-serine biosynthetic process; IEA:UniProtKB-KW.
DR CDD; cd04902; ACT_3PGDH-xct; 1.
DR CDD; cd12173; PGDH_4; 1.
DR Gene3D; 3.30.70.260; -; 1.
DR Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 2.
DR InterPro; IPR045865; ACT-like_dom_sf.
DR InterPro; IPR029009; ASB_dom_sf.
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 InterPro; IPR006236; PGDH.
DR InterPro; IPR045626; PGDH_ASB_dom.
DR NCBIfam; TIGR01327; PGDH; 1.
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 Pfam; PF19304; PGDH_inter; 1.
DR SUPFAM; SSF55021; ACT-like; 1.
DR SUPFAM; SSF52283; Formate/glycerate dehydrogenase catalytic domain-like; 1.
DR SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
DR SUPFAM; SSF143548; Serine metabolism enzymes domain; 1.
DR PROSITE; PS00065; D_2_HYDROXYACID_DH_1; 1.
PE 3: Inferred from homology;
KW Amino-acid biosynthesis {ECO:0000256|ARBA:ARBA00022605,
KW ECO:0000256|RuleBase:RU363003};
KW NAD {ECO:0000256|ARBA:ARBA00023027, ECO:0000256|RuleBase:RU363003};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000256|RuleBase:RU363003};
KW Reference proteome {ECO:0000313|Proteomes:UP000010468};
KW Serine biosynthesis {ECO:0000256|RuleBase:RU363003}.
FT DOMAIN 3..311
FT /note="D-isomer specific 2-hydroxyacid dehydrogenase
FT catalytic"
FT /evidence="ECO:0000259|Pfam:PF00389"
FT DOMAIN 105..279
FT /note="D-isomer specific 2-hydroxyacid dehydrogenase NAD-
FT binding"
FT /evidence="ECO:0000259|Pfam:PF02826"
FT DOMAIN 323..439
FT /note="D-3-phosphoglycerate dehydrogenase ASB"
FT /evidence="ECO:0000259|Pfam:PF19304"
SQ SEQUENCE 527 AA; 55614 MW; CCBD97C35AE57F48 CRC64;
MKVLVTDPIA DAGLDVLRDA GHEVETGYEL EGEDLLEAVS DAHGLIVRSG TDVTATVLEA
ADELAIVGRA GIGVDNIDID AATDEGVIVA NAPEGNVRAA AEHTVAMTFA TARSIPQAHV
RLKDGEWAKS DYLGAELNGK TLGIVGLGRV GQEVAKKLDS LGMDVVAFDP YISEDRAARL
GAELVEFEAC LERADFLTIH TPLTPETEGM IGEEELDLLE GGHLVNVGRG GIVQEGALAA
KVEDGTLAGA ALDVFAEEPL PENSPLLEYD GVVVTPHLGA STEAAQENVA TSTAEQVNAA
LESEPVTNAL NAPSIDESAF PRVEPYIEIA ETAGKVAAQL LDGRIEAVEI TYEGEIAEED
VEFVTASALK GVFEPLEWQV NAVNAPQIAD DRGVDVTESK TRQAEDFQSL ISVEVSNGDE
QIAVDGTLFA GDDPRIVRID DYRVDAIPHG KMVVTRNADA PGVIGLIGSV MGEHDVNIAG
MFNAREAHGG EALTVYNVDS QVPDEAKAEL NADERIIDVD YITLNGQ
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