ID W5MMS6_LEPOC Unreviewed; 536 AA.
AC W5MMS6;
DT 16-APR-2014, integrated into UniProtKB/TrEMBL.
DT 16-APR-2014, sequence version 1.
DT 27-MAR-2024, entry version 50.
DE RecName: Full=D-3-phosphoglycerate dehydrogenase {ECO:0000256|RuleBase:RU363003};
DE EC=1.1.1.95 {ECO:0000256|RuleBase:RU363003};
OS Lepisosteus oculatus (Spotted gar).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Holostei; Semionotiformes; Lepisosteidae;
OC Lepisosteus.
OX NCBI_TaxID=7918 {ECO:0000313|Ensembl:ENSLOCP00000009685.1, ECO:0000313|Proteomes:UP000018468};
RN [1] {ECO:0000313|Proteomes:UP000018468}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Di Palma F., Alfoldi J., Johnson J., Berlin A., Gnerre S., Jaffe D.,
RA MacCallum I., Young S., Walker B.J., Lander E.S., Lindblad-Toh K.;
RT "The Draft Genome of Lepisosteus oculatus.";
RL Submitted (DEC-2011) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSLOCP00000009685.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
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; AHAT01020078; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR AlphaFoldDB; W5MMS6; -.
DR STRING; 7918.ENSLOCP00000009685; -.
DR Ensembl; ENSLOCT00000009695.1; ENSLOCP00000009685.1; ENSLOCG00000007973.1.
DR eggNOG; KOG0068; Eukaryota.
DR GeneTree; ENSGT00940000155863; -.
DR HOGENOM; CLU_019796_8_1_1; -.
DR InParanoid; W5MMS6; -.
DR OMA; NIAGMQV; -.
DR UniPathway; UPA00135; UER00196.
DR Proteomes; UP000018468; Linkage group LG12.
DR Bgee; ENSLOCG00000007973; Expressed in larva and 13 other cell types or tissues.
DR GO; GO:0051287; F:NAD binding; IEA:UniProtKB-UniRule.
DR GO; GO:0004617; F:phosphoglycerate dehydrogenase activity; IBA:GO_Central.
DR GO; GO:0006564; P:L-serine biosynthetic process; IEA:UniProtKB-KW.
DR CDD; cd12173; PGDH_4; 1.
DR Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 2.
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; PTHR42938:SF22; D-3-PHOSPHOGLYCERATE DEHYDROGENASE; 1.
DR PANTHER; PTHR42938; 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; 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}; NAD {ECO:0000256|RuleBase:RU363003};
KW Oxidoreductase {ECO:0000256|RuleBase:RU363003};
KW Reference proteome {ECO:0000313|Proteomes:UP000018468};
KW Serine biosynthesis {ECO:0000256|ARBA:ARBA00023299,
KW ECO:0000256|RuleBase:RU363003}.
FT DOMAIN 11..321
FT /note="D-isomer specific 2-hydroxyacid dehydrogenase
FT catalytic"
FT /evidence="ECO:0000259|Pfam:PF00389"
FT DOMAIN 113..289
FT /note="D-isomer specific 2-hydroxyacid dehydrogenase NAD-
FT binding"
FT /evidence="ECO:0000259|Pfam:PF02826"
FT DOMAIN 334..419
FT /note="D-3-phosphoglycerate dehydrogenase ASB"
FT /evidence="ECO:0000259|Pfam:PF19304"
SQ SEQUENCE 536 AA; 56483 MW; C6E3572FC7FD5491 CRC64;
KMALVSIQRL LISESVDPCC KQILQENGID VTAKQNMSKE ELIAEIKDYE GLIVRSATKV
TAEVINAASK LKIIGRAGTG VDNVDVDAAT KKGIIVMNTP SGNTISAAEL TCGMVMCLSR
HIPQAAMSMK SGNWDRKKFM GSELYGKTLG IVGLGRIGKE VALRMQSFGM KTVGYDPIIP
PEVTATFGVE QMSLEQLWPL CDYITVHTPL MPSTTVTRGL LNDTTFARCK KGVKVVNCAR
GGIIDEGALL RALESGQCGG AGLDVFVDEP PKDRSLINHP NVISCPHLGA STKEAQARCG
QDIAVQIVDM LEGKALTGAV NAQVLASTFS PNSQAWIKLG EALGTISKAC TMENQGHCQV
NITALGTRGS LKTSAGYLSS AVAMGWLRDG SNGHVNLVNA LTVAKEAGIK VTSTHSSAVP
SLSRTACLVE TSVNGSCHRA VGSVQEDSPV LLELNGSVFR QPVPLAGNLL FFKAVSNPQL
MPSVAGVLAA AGLQMETFSA SSSTTGEQWC CVGVSSLLSD LNVLKPHVKE VTQLSV
//
