ID A0A095DIE1_9SPHN Unreviewed; 333 AA.
AC A0A095DIE1;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 27-MAR-2024, entry version 33.
DE SubName: Full=D-3-phosphoglycerate dehydrogenase {ECO:0000313|EMBL:KGB59053.1};
DE EC=1.1.1.95 {ECO:0000313|EMBL:KGB59053.1};
GN ORFNames=FG95_00344 {ECO:0000313|EMBL:KGB59053.1};
OS Sphingopyxis sp. LC363.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC Sphingomonadaceae; Sphingopyxis.
OX NCBI_TaxID=1120705 {ECO:0000313|EMBL:KGB59053.1, ECO:0000313|Proteomes:UP000029625};
RN [1] {ECO:0000313|EMBL:KGB59053.1, ECO:0000313|Proteomes:UP000029625}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LC363 {ECO:0000313|EMBL:KGB59053.1,
RC ECO:0000313|Proteomes:UP000029625};
RA Gan H.M., Gan H.Y., Barton H.A., Savka M.A.;
RT "Genome sequence of acyl-homoserine lactone-producing cave bacterial
RT isolate.";
RL Submitted (MAY-2014) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the D-isomer specific 2-hydroxyacid
CC dehydrogenase family. {ECO:0000256|RuleBase:RU003719}.
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:KGB59053.1}.
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DR EMBL; JNFC01000002; KGB59053.1; -; Genomic_DNA.
DR RefSeq; WP_052181990.1; NZ_JNFC01000002.1.
DR AlphaFoldDB; A0A095DIE1; -.
DR STRING; 1120705.FG95_00344; -.
DR PATRIC; fig|1120705.3.peg.341; -.
DR eggNOG; COG1052; Bacteria.
DR OrthoDB; 7374922at2; -.
DR Proteomes; UP000029625; Unassembled WGS sequence.
DR GO; GO:0051287; F:NAD binding; IEA:InterPro.
DR GO; GO:0004617; F:phosphoglycerate dehydrogenase activity; IEA:UniProtKB-EC.
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; PTHR10996; 2-HYDROXYACID DEHYDROGENASE-RELATED; 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; PS00671; D_2_HYDROXYACID_DH_3; 1.
PE 3: Inferred from homology;
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000256|RuleBase:RU003719};
KW Reference proteome {ECO:0000313|Proteomes:UP000029625}.
FT DOMAIN 76..328
FT /note="D-isomer specific 2-hydroxyacid dehydrogenase
FT catalytic"
FT /evidence="ECO:0000259|Pfam:PF00389"
FT DOMAIN 128..296
FT /note="D-isomer specific 2-hydroxyacid dehydrogenase NAD-
FT binding"
FT /evidence="ECO:0000259|Pfam:PF02826"
SQ SEQUENCE 333 AA; 35257 MW; 813254782E3C3391 CRC64;
MQVGLNLLAN EMSMNTTKLL VAGAPNGRAF LEKLVSTIKS DKIHVDLQIG LDTPAEAPGW
SETQILVSFG VPCGGAEMDA APGLRAIITP SLGYEGIDVD AAHHRGIAFA NGRVAENFES
VAEAAMLFML TSLYAVRDAE ERLRRGETRT GPPRARMLKG KTVGIIGHGN IARALIERLS
GWNTRILLNN RSKVAPSSAF EQCDLDTLLA ESDVVLPLLP LTPDTDNLLS RSRLLAMKPG
AILINLSRGA IVDETALADP EVVAHLGPIA LDVFVTEPLP AASPLRDLPG AILTNHEISH
TQENLGALFA MAVANIQAAI AGTPMPTALV PGR
//
