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Database: UniProt
Entry: A0A166ASH4_9EURY
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Original site: A0A166ASH4_9EURY 
ID   A0A166ASH4_9EURY        Unreviewed;       524 AA.
AC   A0A166ASH4;
DT   06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT   06-JUL-2016, sequence version 1.
DT   24-JAN-2024, entry version 29.
DE   RecName: Full=D-3-phosphoglycerate dehydrogenase {ECO:0000256|RuleBase:RU363003};
DE            EC=1.1.1.95 {ECO:0000256|RuleBase:RU363003};
GN   Name=serA {ECO:0000313|EMBL:KZX12419.1};
GN   ORFNames=MBORA_11730 {ECO:0000313|EMBL:KZX12419.1};
OS   Methanobrevibacter oralis.
OC   Archaea; Euryarchaeota; Methanomada group; Methanobacteria;
OC   Methanobacteriales; Methanobacteriaceae; Methanobrevibacter.
OX   NCBI_TaxID=66851 {ECO:0000313|EMBL:KZX12419.1, ECO:0000313|Proteomes:UP000077428};
RN   [1] {ECO:0000313|EMBL:KZX12419.1, ECO:0000313|Proteomes:UP000077428}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 7256 {ECO:0000313|EMBL:KZX12419.1,
RC   ECO:0000313|Proteomes:UP000077428};
RA   Poehlein A., Seedorf H., Daniel R.;
RT   "Genome sequence of Methanobrevibacter oralis DSM 7256.";
RL   Submitted (APR-2016) to the EMBL/GenBank/DDBJ databases.
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:KZX12419.1}.
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DR   EMBL; LWMU01000070; KZX12419.1; -; Genomic_DNA.
DR   RefSeq; WP_063720370.1; NZ_LWMU01000070.1.
DR   AlphaFoldDB; A0A166ASH4; -.
DR   STRING; 66851.MBORA_11730; -.
DR   PATRIC; fig|66851.6.peg.1276; -.
DR   OrthoDB; 7437at2157; -.
DR   UniPathway; UPA00135; UER00196.
DR   Proteomes; UP000077428; 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; 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; PS51671; ACT; 1.
DR   PROSITE; PS00670; D_2_HYDROXYACID_DH_2; 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|RuleBase:RU363003}.
FT   DOMAIN          452..524
FT                   /note="ACT"
FT                   /evidence="ECO:0000259|PROSITE:PS51671"
SQ   SEQUENCE   524 AA;  57316 MW;  DE7C833C35700F44 CRC64;
     MKVLIADAIN EKGIENLKKV AEVVVDTSIT PEKLVNTINE YDGIVVRSRT KVTREVIENA
     SNLKIIARAG VGVDNIDLNA ATEKGIMVVN SPESTSITVA EHTMGLLLNV ARKISIADKS
     VKSGKWEKKR FMGVELRKKT LGIIGMGRIG SQVVNRCKAF EMDAMAYDPY LPKEVAKQMG
     VELTDLESVL KNADFITIHV PLTPETKHLI STDEFEIMKD SAFIANCARG GIIDEEALYV
     ALSENKIGGA ALDVYEEEPP AKDSKLLELD NIVLTPHIAA STKEAQRDAA IIVADEIIDL
     FKGGTPQNVL NMPRIDNNTF QELSPYLELA EKLGSFISQG VNGKLKEIEI IYSGDLAEID
     NLELLTRTVI QGAVNPFLSS PVNTVNATLV AKNRGISITE GRKNNAKGYE SLIKVIAKSD
     ENTFSAEGTT LHEARILKVN GYWVDVVPKG HMFIAKYEDV PGSIGKIGTK LGKHDVNIGI
     MQVGRDKKGG RAIMILTLDK EVPNDVVKEI QNLDNVYEAI RLEL
//
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