GenomeNet

Database: UniProt
Entry: G7I0A8_9CORY
LinkDB: G7I0A8_9CORY
Original site: G7I0A8_9CORY 
ID   G7I0A8_9CORY            Unreviewed;       528 AA.
AC   G7I0A8;
DT   25-JAN-2012, integrated into UniProtKB/TrEMBL.
DT   25-JAN-2012, sequence version 1.
DT   24-JAN-2024, entry version 50.
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   Name=serA {ECO:0000313|EMBL:CCE55873.1};
GN   ORFNames=CCAS_11990 {ECO:0000313|EMBL:CCE55873.1};
OS   Corynebacterium casei UCMA 3821.
OC   Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales;
OC   Corynebacteriaceae; Corynebacterium.
OX   NCBI_TaxID=1110505 {ECO:0000313|EMBL:CCE55873.1, ECO:0000313|Proteomes:UP000004840};
RN   [1] {ECO:0000313|EMBL:CCE55873.1, ECO:0000313|Proteomes:UP000004840}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=UCMA 3821 {ECO:0000313|EMBL:CCE55873.1,
RC   ECO:0000313|Proteomes:UP000004840};
RX   PubMed=22247534; DOI=10.1128/JB.06496-11;
RA   Monnet C., Loux V., Bento P., Gibrat J.F., Straub C., Bonnarme P.,
RA   Landaud S., Irlinger F.;
RT   "Genome Sequence of Corynebacterium casei UCMA 3821, Isolated from a Smear-
RT   Ripened Cheese.";
RL   J. Bacteriol. 194:738-739(2012).
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:CCE55873.1}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; CAFW01000088; CCE55873.1; -; Genomic_DNA.
DR   RefSeq; WP_006823317.1; NZ_CAFW01000088.1.
DR   AlphaFoldDB; G7I0A8; -.
DR   UniPathway; UPA00135; UER00196.
DR   Proteomes; UP000004840; 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; 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; PTHR42938; FORMATE DEHYDROGENASE 1; 1.
DR   PANTHER; PTHR42938:SF9; FORMATE DEHYDROGENASE 1; 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; PS51671; ACT; 1.
DR   PROSITE; PS00065; D_2_HYDROXYACID_DH_1; 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   Serine biosynthesis {ECO:0000256|ARBA:ARBA00023299,
KW   ECO:0000256|RuleBase:RU363003}.
FT   DOMAIN          455..528
FT                   /note="ACT"
FT                   /evidence="ECO:0000259|PROSITE:PS51671"
SQ   SEQUENCE   528 AA;  55196 MW;  5803CB4C056CE956 CRC64;
     MSKPVVLIAD KLAPSTVEAL GDGVEVRWVD GPNRDELLAA VGEADALLVR SATTVNEEVL
     EAANNLKIVG RAGVGLDNVD VPAATARGVM VVNAPTSNIH SACEHAISLL LSTARQIPQA
     DATLREGEWK RSSFKGVEIY GKTVGIVGFG HIGQLFAHRL KAFETEIIAY DPYANPARAA
     SLGVELVDLE ELMSRSDFVT IHLPKTPETA GMFSAELLAK AKKGQIIINA ARGGLVDEQA
     LADSIKAGHH WGAGFDVYST EPCTDSPLFA LPQVVVTPHL GASTVEAQDR AGTDVAESVL
     KALAGEFVPD AVNVSGGRVG EEVAGWLDLA RKLGLASGKL LRSAPVAIEV TACGQLSTED
     VEVLGLSAVR GLFSGVTSEA VTFVNAMSIA ESRGVTVKVS STEEAKGHNS TVRVKTISAD
     GDTSVLEGAL TGIDGVEKIV RIDGRGVDMR ATGRNLFFSY TDRPGALGVV GSVLGGAGIN
     IQAAALTQGK KDDAAVLILR VEREVNDELI ADIQDKLEAK SLQVNFDA
//
DBGET integrated database retrieval system