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Database: UniProt
Entry: A0A368YY10_9RHOB
LinkDB: A0A368YY10_9RHOB
Original site: A0A368YY10_9RHOB 
ID   A0A368YY10_9RHOB        Unreviewed;       529 AA.
AC   A0A368YY10;
DT   07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT   07-NOV-2018, sequence version 1.
DT   24-JAN-2024, entry version 18.
DE   RecName: Full=D-3-phosphoglycerate dehydrogenase {ECO:0000256|ARBA:ARBA00021582, ECO:0000256|RuleBase:RU363003};
DE            EC=1.1.1.95 {ECO:0000256|RuleBase:RU363003};
GN   ORFNames=DFP89_106120 {ECO:0000313|EMBL:RCW85102.1};
OS   Paracoccus lutimaris.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC   Paracoccaceae; Paracoccus.
OX   NCBI_TaxID=1490030 {ECO:0000313|EMBL:RCW85102.1, ECO:0000313|Proteomes:UP000253345};
RN   [1] {ECO:0000313|EMBL:RCW85102.1, ECO:0000313|Proteomes:UP000253345}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CECT 8525 {ECO:0000313|EMBL:RCW85102.1,
RC   ECO:0000313|Proteomes:UP000253345};
RA   Whitman W.;
RT   "Genomic Encyclopedia of Type Strains, Phase III (KMG-III): the genomes of
RT   soil and plant-associated and newly described type strains.";
RL   Submitted (JUL-2018) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Catalyzes the reversible oxidation of 3-phospho-D-glycerate
CC       to 3-phosphonooxypyruvate, the first step of the phosphorylated L-
CC       serine biosynthesis pathway. Also catalyzes the reversible oxidation of
CC       2-hydroxyglutarate to 2-oxoglutarate. {ECO:0000256|ARBA:ARBA00003800}.
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   -!- CATALYTIC ACTIVITY:
CC       Reaction=(R)-2-hydroxyglutarate + NAD(+) = 2-oxoglutarate + H(+) +
CC         NADH; Xref=Rhea:RHEA:49612, ChEBI:CHEBI:15378, ChEBI:CHEBI:15801,
CC         ChEBI:CHEBI:16810, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945;
CC         EC=1.1.1.399; Evidence={ECO:0000256|ARBA:ARBA00000646};
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}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:RCW85102.1}.
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DR   EMBL; QPJL01000006; RCW85102.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A368YY10; -.
DR   OrthoDB; 9793626at2; -.
DR   UniPathway; UPA00135; UER00196.
DR   Proteomes; UP000253345; 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; IPR002912; ACT_dom.
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; PF01842; ACT; 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}; NAD {ECO:0000256|RuleBase:RU363003};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW   ECO:0000256|RuleBase:RU363003};
KW   Reference proteome {ECO:0000313|Proteomes:UP000253345};
KW   Serine biosynthesis {ECO:0000256|ARBA:ARBA00023299,
KW   ECO:0000256|RuleBase:RU363003}.
FT   DOMAIN          4..314
FT                   /note="D-isomer specific 2-hydroxyacid dehydrogenase
FT                   catalytic"
FT                   /evidence="ECO:0000259|Pfam:PF00389"
FT   DOMAIN          108..282
FT                   /note="D-isomer specific 2-hydroxyacid dehydrogenase NAD-
FT                   binding"
FT                   /evidence="ECO:0000259|Pfam:PF02826"
FT   DOMAIN          326..443
FT                   /note="D-3-phosphoglycerate dehydrogenase ASB"
FT                   /evidence="ECO:0000259|Pfam:PF19304"
FT   DOMAIN          454..515
FT                   /note="ACT"
FT                   /evidence="ECO:0000259|Pfam:PF01842"
SQ   SEQUENCE   529 AA;  56322 MW;  81FE1DA69F764F73 CRC64;
     MPKVLVSDKL SETAVQIFRD RGVEVDYLPD VGKDKDKLAE IIGQYDGLAI RSATKVTAKL
     LESAPNLKVI GRAGIGVDNV EIPAASKKGV IVMNTPFGNS VTTAEHAIAL MFAVARQLPE
     ASVSTHAGKW EKNRFMGVEV FNKTLGIIGA GNIGSIVIDR ALGLRMKVLA YDPFLSEDRA
     VELGVKKVEL DELLAKADFI TLHVPLTDKT RNILSRENLA KTKKGVRIVN AARGGLIDED
     ALADLLKSGH VAGAALDVFA VEPATESPLF NLPNVVVTPH LGASTNEAQE NVALQVAEQM
     ADYLLTGAVQ NALNMPSVTA EEAAVMGPWI KLAGHLGAFI GQMTDEPIKA INVLYDGVAS
     EMNLKALNAA VIAGVMKATN PDVNMVSAPV MAHERGVQVA TTTQAKTGVF DGYIKATVVT
     DTRERSIAGT VFSDGKPRFI QIRGINVDAE IGEHMLYTRN KDVPGVIGAL GMTLGDLGVN
     IANFTLGRTG AGNDAIAILY LDEALRPEVL EALRATGKFL QVRPLHFEV
//
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