ID N6V3A5_9EURY Unreviewed; 523 AA.
AC N6V3A5;
DT 26-JUN-2013, integrated into UniProtKB/TrEMBL.
DT 26-JUN-2013, sequence version 1.
DT 27-MAR-2024, entry version 41.
DE RecName: Full=D-3-phosphoglycerate dehydrogenase {ECO:0000256|ARBA:ARBA00021582, ECO:0000256|RuleBase:RU363003};
DE EC=1.1.1.95 {ECO:0000256|ARBA:ARBA00013143, ECO:0000256|RuleBase:RU363003};
GN ORFNames=J422_00841 {ECO:0000313|EMBL:ENN96738.1};
OS Methanocaldococcus villosus KIN24-T80.
OC Archaea; Euryarchaeota; Methanomada group; Methanococci; Methanococcales;
OC Methanocaldococcaceae; Methanocaldococcus.
OX NCBI_TaxID=1069083 {ECO:0000313|EMBL:ENN96738.1, ECO:0000313|Proteomes:UP000053695};
RN [1] {ECO:0000313|EMBL:ENN96738.1, ECO:0000313|Proteomes:UP000053695}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=KIN24-T80 {ECO:0000313|EMBL:ENN96738.1,
RC ECO:0000313|Proteomes:UP000053695};
RX PubMed=23846275;
RA Thennarasu S., Polireddy D., Antony A., Yada M.R., Algarawi S.,
RA Sivakumar N.;
RT "Draft Genome Sequence of a Highly Flagellated, Fast-Swimming Archaeon,
RT Methanocaldococcus villosus Strain KIN24-T80 (DSM 22612).";
RL Genome Announc. 1:E00481-13(2013).
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:ENN96738.1}.
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DR EMBL; APMM01000004; ENN96738.1; -; Genomic_DNA.
DR RefSeq; WP_004589838.1; NZ_AQUK01000001.1.
DR AlphaFoldDB; N6V3A5; -.
DR STRING; 1069083.GCA_000371805_00866; -.
DR PATRIC; fig|1069083.5.peg.166; -.
DR OrthoDB; 7437at2157; -.
DR UniPathway; UPA00135; UER00196.
DR Proteomes; UP000053695; 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; 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; 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; PS00065; D_2_HYDROXYACID_DH_1; 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|ARBA:ARBA00022605,
KW ECO:0000256|RuleBase:RU363003};
KW NAD {ECO:0000256|ARBA:ARBA00023027, 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 450..522
FT /note="ACT"
FT /evidence="ECO:0000259|PROSITE:PS51671"
SQ SEQUENCE 523 AA; 57492 MW; A5C9E0EA8BDBDEDD CRC64;
MVKILITDPI HEEAIKILKE LGEVEIATDL SKEELLNKIK DVNILIVRSG TYVDREIIDA
GKNLKIIARA GVGVDNIDVD YATEKGIIVV NAPDASSISV AELTMGLILA AARNIPQANN
SVKSGKWERK KFKGIELYGK ILGVVGLGRI GQQVVKRAKA FGMEVIAYDP YIPKEVAENL
GVKLLNDLNE LCKMADIITL HVPLTPKTKH MIGEEQINLM KKNAIIVNCA RGGLIDEKAL
YKALKEKRIK AAALDVFEKE PPKDNPLLKL DNLICTPHLG ASTEEAQKAA GIIIAEQIKK
ILNGELAENV VNFPSLPKEK LGKLKPYMLL AETLGNIVMQ VLNRVDRVEI IYMGSLTKEN
TDLITRAFLK GLLYPILLAG VNLINAPIIA KSRNINVIES YTTEKKYGDA IKIIAEGDRR
FSIVGGIINN KFVILEVDGY EVNFIPEGVL AIIKHIDRPG MIGKVGMILG EYGINIASMQ
VGRREPGGEA VMLINLDHPI SEEVIKKIKE IPNIKDVAVI NLW
//
