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Database: UniProt
Entry: A0A1P8URX8_9RHOB
LinkDB: A0A1P8URX8_9RHOB
Original site: A0A1P8URX8_9RHOB 
ID   A0A1P8URX8_9RHOB        Unreviewed;       531 AA.
AC   A0A1P8URX8;
DT   12-APR-2017, integrated into UniProtKB/TrEMBL.
DT   12-APR-2017, sequence version 1.
DT   27-MAR-2024, entry version 24.
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   ORFNames=Ga0080574_TMP1827 {ECO:0000313|EMBL:APZ52161.1};
OS   Salipiger abyssi.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC   Roseobacteraceae; Salipiger.
OX   NCBI_TaxID=1250539 {ECO:0000313|EMBL:APZ52161.1, ECO:0000313|Proteomes:UP000187059};
RN   [1] {ECO:0000313|EMBL:APZ52161.1, ECO:0000313|Proteomes:UP000187059}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JLT2014 {ECO:0000313|EMBL:APZ52161.1,
RC   ECO:0000313|Proteomes:UP000187059};
RA   Tang K.;
RT   "Deep-sea bacteria in the southern Pacific.";
RL   Submitted (APR-2016) 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; CP015093; APZ52161.1; -; Genomic_DNA.
DR   RefSeq; WP_076697629.1; NZ_JAEKIS010000003.1.
DR   AlphaFoldDB; A0A1P8URX8; -.
DR   STRING; 1250539.Ga0080574_TMP1827; -.
DR   KEGG; paby:Ga0080574_TMP1827; -.
DR   OrthoDB; 9793626at2; -.
DR   UniPathway; UPA00135; UER00196.
DR   Proteomes; UP000187059; Chromosome.
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; 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   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.
DR   PROSITE; PS00670; D_2_HYDROXYACID_DH_2; 1.
DR   PROSITE; PS00671; D_2_HYDROXYACID_DH_3; 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:UP000187059};
KW   Serine biosynthesis {ECO:0000256|RuleBase:RU363003}.
FT   DOMAIN          5..315
FT                   /note="D-isomer specific 2-hydroxyacid dehydrogenase
FT                   catalytic"
FT                   /evidence="ECO:0000259|Pfam:PF00389"
FT   DOMAIN          109..283
FT                   /note="D-isomer specific 2-hydroxyacid dehydrogenase NAD-
FT                   binding"
FT                   /evidence="ECO:0000259|Pfam:PF02826"
FT   DOMAIN          327..444
FT                   /note="D-3-phosphoglycerate dehydrogenase ASB"
FT                   /evidence="ECO:0000259|Pfam:PF19304"
SQ   SEQUENCE   531 AA;  56717 MW;  F2B7AEEF73C645DC CRC64;
     MAPKVLVSDK LSETAVQIFR DRGIDVDFLP DVGKDKEKLA EIIGEYDGLA IRSATKVTPT
     ILEHATKLKV VGRAGIGTDN VDKEAASKKG VIVMNTPFGN MITTAEHAIA LMFAVARQIP
     AADASTQAGK WEKSKFMGTE LTAKTLGVIG AGNIGGIVCD RARGLKMKVV AYDPFLSEEK
     AQQMQVEKVE LDELLKRADF ITLHVPLTDG TRNILSAENL AKTKKGVRII NCARGGLVDE
     AALAELIKSG HVAGAAFDVF KEEPATENPL FGLPNVVCTP HLGASTTEAQ ENVALQVAEQ
     MSDYLLTGAV QNALNMPSVT AEEAKVMGPW IKVAGHLGGF IGQMTDEPIK AINILYDGEA
     ATMNLEALNC ATIAGIMKSI SPEVNMVSAP VIAKERGIQI STTRQEQSGV FEGYIKVTMV
     TAKRERSIAG TVFSDGKPRF IQIKGINIDA EVGEHMLYTT NEDMPGIIGT LGTMLGEHKV
     NLANFTLGRS KQGGQAIAIS YLDEALDPSV VDALKATGLF KQVKPLQFDV A
//
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