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Database: UniProt
Entry: A0A1T4YZT3_9ACTN
LinkDB: A0A1T4YZT3_9ACTN
Original site: A0A1T4YZT3_9ACTN 
ID   A0A1T4YZT3_9ACTN        Unreviewed;       419 AA.
AC   A0A1T4YZT3;
DT   10-MAY-2017, integrated into UniProtKB/TrEMBL.
DT   10-MAY-2017, sequence version 1.
DT   08-MAY-2019, entry version 8.
DE   RecName: Full=D-3-phosphoglycerate dehydrogenase {ECO:0000256|RuleBase:RU366013};
DE            EC=1.1.1.399 {ECO:0000256|RuleBase:RU366013};
DE            EC=1.1.1.95 {ECO:0000256|RuleBase:RU366013};
GN   ORFNames=SAMN06295964_1636 {ECO:0000313|EMBL:SKB07284.1};
OS   Aeromicrobium choanae.
OC   Bacteria; Actinobacteria; Propionibacteriales; Nocardioidaceae;
OC   Aeromicrobium.
OX   NCBI_TaxID=1736691 {ECO:0000313|EMBL:SKB07284.1, ECO:0000313|Proteomes:UP000191040};
RN   [1] {ECO:0000313|EMBL:SKB07284.1, ECO:0000313|Proteomes:UP000191040}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=9H-4 {ECO:0000313|EMBL:SKB07284.1,
RC   ECO:0000313|Proteomes:UP000191040};
RA   Peterson S.W.;
RL   Submitted (FEB-2017) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Catalyzes the reversible oxidation of 3-phospho-D-
CC       glycerate to 3-phosphonooxypyruvate, the first step of the
CC       phosphorylated L-serine biosynthesis pathway. Also catalyzes the
CC       reversible oxidation of 2-hydroxyglutarate to 2-oxoglutarate.
CC       {ECO:0000256|RuleBase:RU366013}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(R)-2-hydroxyglutarate + NAD(+) = 2-oxoglutarate + H(+) +
CC         NADH; Xref=Rhea:RHEA:49612, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:15801, ChEBI:CHEBI:16810, ChEBI:CHEBI:57540,
CC         ChEBI:CHEBI:57945; EC=1.1.1.399;
CC         Evidence={ECO:0000256|RuleBase:RU366013};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=3-phospho-D-glycerate + NAD(+) = 3-phosphooxypyruvate +
CC         H(+) + NADH; Xref=Rhea:RHEA:12641, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:18110, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945,
CC         ChEBI:CHEBI:58272; EC=1.1.1.95;
CC         Evidence={ECO:0000256|RuleBase:RU366013};
CC   -!- PATHWAY: Amino-acid biosynthesis; L-serine biosynthesis; L-serine
CC       from 3-phospho-D-glycerate: step 1/3.
CC       {ECO:0000256|RuleBase:RU366013}.
CC   -!- SIMILARITY: Belongs to the D-isomer specific 2-hydroxyacid
CC       dehydrogenase family. {ECO:0000256|RuleBase:RU003719}.
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DR   EMBL; LT796768; SKB07284.1; -; Genomic_DNA.
DR   UniPathway; UPA00135; UER00196.
DR   Proteomes; UP000191040; Chromosome i.
DR   GO; GO:0051287; F:NAD binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0004617; F:phosphoglycerate dehydrogenase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0006564; P:L-serine biosynthetic process; IEA:UniProtKB-UniRule.
DR   InterPro; IPR002912; ACT_dom.
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; IPR029015; PGDH_2.
DR   PANTHER; PTHR10996:SF165; PTHR10996:SF165; 1.
DR   Pfam; PF00389; 2-Hacid_dh; 1.
DR   Pfam; PF02826; 2-Hacid_dh_C; 1.
DR   Pfam; PF01842; ACT; 1.
DR   SUPFAM; SSF51735; SSF51735; 1.
DR   PROSITE; PS51671; ACT; 1.
DR   PROSITE; PS00065; D_2_HYDROXYACID_DH_1; 1.
PE   3: Inferred from homology;
KW   Amino-acid biosynthesis {ECO:0000256|RuleBase:RU366013};
KW   Complete proteome {ECO:0000313|Proteomes:UP000191040};
KW   NAD {ECO:0000256|RuleBase:RU366013};
KW   Oxidoreductase {ECO:0000256|RuleBase:RU003719};
KW   Reference proteome {ECO:0000313|Proteomes:UP000191040};
KW   Serine biosynthesis {ECO:0000256|RuleBase:RU366013}.
FT   DOMAIN      350    419       ACT. {ECO:0000259|PROSITE:PS51671}.
SQ   SEQUENCE   419 AA;  44873 MW;  2711551975BDCFA7 CRC64;
     MTMMSMSFDV HEPMTTIDDQ DVKVLLLENI HADGADFLRN KGYQVETRSA ALTEDELIEA
     IKGVHLLGIR STTYITEKVL ENAPDLLAIG AFCIGTNQID LAATKRHGVA VFNAPYSNTR
     SVVELAIAEI ISLARRLHEK STAMHGGVWN KSAAGSHEVR GRTLGIVGYG NIGSQLSVIA
     EALGLSVVFY DIDDKLALGN AKKCATIDEL LAISDVVSLH VDGRPGNAGL FGDEQMRAMK
     PRSLFLNLSR GIAVDTSALR RHLESGHIAG AALDVFPVEP KAQGDPFESE LRGVPNVILT
     PHVGGSTEEA QQDIGRFVAS KLRAYAKAGT TNLSVTFPEL NLPSDPARHR LAHVHHNAPG
     VLATINTILG DHGVNIEGQQ LATRGELGYV VTDVSAEVGA DVLKELAALP ETVRLRQLS
//
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