ID D4LRH9_9FIRM Unreviewed; 330 AA.
AC D4LRH9;
DT 18-MAY-2010, integrated into UniProtKB/TrEMBL.
DT 18-MAY-2010, sequence version 1.
DT 27-MAR-2024, entry version 62.
DE SubName: Full=Phosphoglycerate dehydrogenase and related dehydrogenases {ECO:0000313|EMBL:CBL23387.1};
DE EC=1.1.1.95 {ECO:0000313|EMBL:CBL23387.1};
GN ORFNames=CK5_20080 {ECO:0000313|EMBL:CBL23387.1};
OS Blautia obeum A2-162.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Lachnospiraceae; Blautia.
OX NCBI_TaxID=657314 {ECO:0000313|EMBL:CBL23387.1, ECO:0000313|Proteomes:UP000008955};
RN [1] {ECO:0000313|EMBL:CBL23387.1, ECO:0000313|Proteomes:UP000008955}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=A2-162 {ECO:0000313|EMBL:CBL23387.1,
RC ECO:0000313|Proteomes:UP000008955};
RG metaHIT consortium -- http://www.metahit.eu/;
RA Pajon A., Turner K., Parkhill J., Duncan S., Flint H.;
RT "The genome sequence of Ruminococcus obeum A2-162.";
RL Submitted (MAR-2010) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:CBL23387.1, ECO:0000313|Proteomes:UP000008955}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=A2-162 {ECO:0000313|EMBL:CBL23387.1,
RC ECO:0000313|Proteomes:UP000008955};
RA Pajon A.;
RL Submitted (MAR-2010) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the D-isomer specific 2-hydroxyacid
CC dehydrogenase family. {ECO:0000256|RuleBase:RU003719}.
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DR EMBL; FP929054; CBL23387.1; -; Genomic_DNA.
DR AlphaFoldDB; D4LRH9; -.
DR KEGG; rob:CK5_20080; -.
DR PATRIC; fig|657314.3.peg.1869; -.
DR HOGENOM; CLU_019796_1_3_9; -.
DR Proteomes; UP000008955; Chromosome.
DR GO; GO:0051287; F:NAD binding; IEA:InterPro.
DR GO; GO:0004617; F:phosphoglycerate dehydrogenase activity; IEA:UniProtKB-EC.
DR CDD; cd12173; PGDH_4; 1.
DR Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 2.
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 PANTHER; PTHR43761:SF1; 2-HACID_DH DOMAIN-CONTAINING PROTEIN-RELATED; 1.
DR PANTHER; PTHR43761; D-ISOMER SPECIFIC 2-HYDROXYACID DEHYDROGENASE FAMILY PROTEIN (AFU_ORTHOLOGUE AFUA_1G13630); 1.
DR Pfam; PF00389; 2-Hacid_dh; 1.
DR Pfam; PF02826; 2-Hacid_dh_C; 1.
DR SUPFAM; SSF52283; Formate/glycerate dehydrogenase catalytic domain-like; 1.
DR SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 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 Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000256|RuleBase:RU003719}.
FT DOMAIN 4..311
FT /note="D-isomer specific 2-hydroxyacid dehydrogenase
FT catalytic"
FT /evidence="ECO:0000259|Pfam:PF00389"
FT DOMAIN 106..283
FT /note="D-isomer specific 2-hydroxyacid dehydrogenase NAD-
FT binding"
FT /evidence="ECO:0000259|Pfam:PF02826"
SQ SEQUENCE 330 AA; 35622 MW; FEC58C68D6A22CBD CRC64;
MKYVMTEAVA PEGMALLDQS EKVYVAHDAN PANYTEEMKD ADALIVRAAP AKIVNKAVME
AAPQLKVIGR TGVGYDSVDV DAATELGIPV VITPGANNRA VAEHSLTLML ALSKNLVEAQ
VEASKGNWAI RDAHKQFELY GKKAGIIGLG RIGRDTASLC TGIGMKVAGY DPFLTKEQIE
GMGYEYYANY EDLLKDCDVI SIHVPLTKET ENMVSAKQLK EMKNTAIIIN CSRGGIINEA
DLIEALDSGE IAGAGLDVFV GEEIHPGNPL LDAKNLIFSP HSAAQTREAV INMATMCVEG
CKAVCAGKKW KLVANPDVYK HEKWKDAEWA
//
