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Database: UniProt
Entry: W4HK16_9RHOB
LinkDB: W4HK16_9RHOB
Original site: W4HK16_9RHOB 
ID   W4HK16_9RHOB            Unreviewed;       531 AA.
AC   W4HK16;
DT   19-MAR-2014, integrated into UniProtKB/TrEMBL.
DT   19-MAR-2014, sequence version 1.
DT   24-JAN-2024, entry version 43.
DE   RecName: Full=D-3-phosphoglycerate dehydrogenase {ECO:0000256|RuleBase:RU363003};
DE            EC=1.1.1.95 {ECO:0000256|RuleBase:RU363003};
GN   ORFNames=ATO8_12951 {ECO:0000313|EMBL:ETW12461.1};
OS   Roseivivax marinus.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC   Roseobacteraceae; Roseivivax.
OX   NCBI_TaxID=1379903 {ECO:0000313|EMBL:ETW12461.1, ECO:0000313|Proteomes:UP000019063};
RN   [1] {ECO:0000313|EMBL:ETW12461.1, ECO:0000313|Proteomes:UP000019063}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=22II-s10s {ECO:0000313|EMBL:ETW12461.1,
RC   ECO:0000313|Proteomes:UP000019063};
RX   PubMed=24567080; DOI=10.1007/s10482-014-0140-5;
RA   Li G., Lai Q., Liu X., Sun F., Shao Z.;
RT   "Roseivivax atlanticus sp. nov., isolated from surface seawater of the
RT   Atlantic Ocean.";
RL   Antonie Van Leeuwenhoek 105:863-869(2014).
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}.
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:ETW12461.1}.
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DR   EMBL; AQQW01000007; ETW12461.1; -; Genomic_DNA.
DR   RefSeq; WP_043844934.1; NZ_JASHIL010000063.1.
DR   AlphaFoldDB; W4HK16; -.
DR   STRING; 1379903.ATO8_12951; -.
DR   PATRIC; fig|1317118.6.peg.2666; -.
DR   eggNOG; COG0111; Bacteria.
DR   UniPathway; UPA00135; UER00196.
DR   Proteomes; UP000019063; 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; IPR029753; D-isomer_DH_CS.
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; 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|RuleBase:RU363003};
KW   NAD {ECO:0000256|RuleBase:RU363003};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW   ECO:0000256|RuleBase:RU363003};
KW   Reference proteome {ECO:0000313|Proteomes:UP000019063};
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;  56743 MW;  84C838DAFC174FE1 CRC64;
     MAPKVLISDK LSAAAVQIFK DRGIEVDFQP DLGKDKDKLA EVIGQYDGLA IRSATKVTPK
     ILENAPNLKV IGRAGIGVDN IDKEAASKQG VIVMNTPFGN MITTAEHAIA MMFAVARQIP
     EASASTHAGK WEKSKFMGVE LTGKTLGVIG AGNIGGIVCD RARGLKMKVA AYDPYLSQEK
     ADQMGVEKVE LDELLTRADF ITLHVPLTDQ TRNILSRENL AKTKKGVRII NCARGGLVDE
     QALADMLKEG HVAGAAFDVF AEEPATDNPL FGLPNVVCTP HLGAATTEAQ ENVALQVAEQ
     MANYLLTGAV ENALNMPSVS AEEAKVMGPW IKLSDHLGSF IGQMTDEPIK AINILYDGSV
     SEMNLAALNC SVVAGIMKRV NPDVNMVSAP LIAQERGIRI STTNQAQSGA FEGYIKVTVV
     TDKRERSIAG TVFSDGKPRF IQIKGINIDA EIGRHMLYTT NEDVPGIIGT LGQTMGQNGV
     NIANFTLGRS KAKGEAIALL YVDDVVPADV IGALEDTGMF QQVKPLQFDV A
//
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