ID A5UKD4_METS3 Unreviewed; 524 AA.
AC A5UKD4;
DT 10-JUL-2007, integrated into UniProtKB/TrEMBL.
DT 10-JUL-2007, sequence version 1.
DT 27-MAR-2024, entry version 90.
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 OrderedLocusNames=Msm_0457 {ECO:0000313|EMBL:ABQ86662.1};
OS Methanobrevibacter smithii (strain ATCC 35061 / DSM 861 / OCM 144 / PS).
OC Archaea; Euryarchaeota; Methanomada group; Methanobacteria;
OC Methanobacteriales; Methanobacteriaceae; Methanobrevibacter.
OX NCBI_TaxID=420247 {ECO:0000313|EMBL:ABQ86662.1, ECO:0000313|Proteomes:UP000001992};
RN [1] {ECO:0000313|EMBL:ABQ86662.1, ECO:0000313|Proteomes:UP000001992}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 35061 / DSM 861 / OCM 144 / PS
RC {ECO:0000313|Proteomes:UP000001992};
RX PubMed=17563350; DOI=10.1073/pnas.0704189104;
RA Samuel B.S., Hansen E.E., Manchester J.K., Coutinho P.M., Henrissat B.,
RA Fulton R., Latreille P., Kim K., Wilson R.K., Gordon J.I.;
RT "Genomic and metabolic adaptations of Methanobrevibacter smithii to the
RT human gut.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:10643-10648(2007).
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; CP000678; ABQ86662.1; -; Genomic_DNA.
DR RefSeq; WP_011953898.1; NZ_CP117965.1.
DR AlphaFoldDB; A5UKD4; -.
DR STRING; 420247.Msm_0457; -.
DR EnsemblBacteria; ABQ86662; ABQ86662; Msm_0457.
DR GeneID; 78817084; -.
DR KEGG; msi:Msm_0457; -.
DR PATRIC; fig|420247.28.peg.457; -.
DR eggNOG; arCOG01754; Archaea.
DR HOGENOM; CLU_019796_8_1_2; -.
DR BioCyc; MSMI420247:GHWZ-463-MONOMER; -.
DR UniPathway; UPA00135; UER00196.
DR Proteomes; UP000001992; Chromosome.
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|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 452..524
FT /note="ACT"
FT /evidence="ECO:0000259|PROSITE:PS51671"
SQ SEQUENCE 524 AA; 57167 MW; 5D819172F37B089D CRC64;
MKVLIADAIN EKGIENLKEA AEVVVDTTIT PEELANTIHE YEGIIVRSRT KLTKEVIDKA
DNLKIIARAG VGVDNIDLNA ATEKGIMVVN SPESTSITVA EHTMGLLLSL ARKSAIADKS
VKEGKWEKKK FMGVELRNKT LGVIGMGRIG SQVVNRCKAF EMDAVAYDPY LPEEVAAQMG
VELTDLETVL KKADFITIHV PLTPETKHLI STKEFEIMKD TAFIANCARG GIIDEDALYE
ALSNDKIGGA ALDVYEEEPP AKDCKLFELD NIVLTPHIAA STKEAQRDAA IIVADEIIDL
INGGTPQNVL NLPRIDRNTY QEVTPYLELC EKLGSFISQA VNGKIKEIEV IYSGELSKID
NLEMLTRTVL QGAVNPFLSS PVTAVNASIV AKNRGIIVTE GKTENSKGYD SLIKVTAKSE
DDEFSAEGTT LHDPKILKVN DYWVDVKPEG HMFIAKYEDV PGSIGKIGTA LGEYGINIGI
MQVGRDEKGG RAIMILTLDK EIPKEVIKGI QDLDNVYDAI GLEL
//
