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Database: UniProt
Entry: A0A285EJ75_9ACTN
LinkDB: A0A285EJ75_9ACTN
Original site: A0A285EJ75_9ACTN 
ID   A0A285EJ75_9ACTN        Unreviewed;       319 AA.
AC   A0A285EJ75;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   24-JAN-2024, entry version 17.
DE   SubName: Full=Phosphoglycerate dehydrogenase {ECO:0000313|EMBL:SNX98913.1};
GN   ORFNames=SAMN06893097_1132 {ECO:0000313|EMBL:SNX98913.1};
OS   Geodermatophilus sabuli.
OC   Bacteria; Actinomycetota; Actinomycetes; Geodermatophilales;
OC   Geodermatophilaceae; Geodermatophilus.
OX   NCBI_TaxID=1564158 {ECO:0000313|EMBL:SNX98913.1, ECO:0000313|Proteomes:UP000219514};
RN   [1] {ECO:0000313|EMBL:SNX98913.1, ECO:0000313|Proteomes:UP000219514}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 46844 {ECO:0000313|EMBL:SNX98913.1,
RC   ECO:0000313|Proteomes:UP000219514};
RA   Ehlers B., Leendertz F.H.;
RL   Submitted (SEP-2017) 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; OBDO01000013; SNX98913.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A285EJ75; -.
DR   Proteomes; UP000219514; Unassembled WGS sequence.
DR   GO; GO:0051287; F:NAD binding; IEA:InterPro.
DR   GO; GO:0016614; F:oxidoreductase activity, acting on CH-OH group of donors; IEA:UniProt.
DR   CDD; cd12166; 2-Hacid_dh_7; 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; PTHR43333; 2-HACID_DH_C DOMAIN-CONTAINING PROTEIN; 1.
DR   PANTHER; PTHR43333:SF1; 2-HACID_DH_C DOMAIN-CONTAINING PROTEIN; 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   NAD {ECO:0000256|ARBA:ARBA00023027};
KW   Oxidoreductase {ECO:0000256|RuleBase:RU003719};
KW   Reference proteome {ECO:0000313|Proteomes:UP000219514}.
FT   DOMAIN          72..316
FT                   /note="D-isomer specific 2-hydroxyacid dehydrogenase
FT                   catalytic"
FT                   /evidence="ECO:0000259|Pfam:PF00389"
FT   DOMAIN          119..285
FT                   /note="D-isomer specific 2-hydroxyacid dehydrogenase NAD-
FT                   binding"
FT                   /evidence="ECO:0000259|Pfam:PF02826"
SQ   SEQUENCE   319 AA;  32674 MW;  B5BF8F06599D5B55 CRC64;
     MHVAPQITGS AVVGPDETLH VVVPSRALAA AVEAVSPRVR AHRLDPGDVP AGEAAQAQVW
     VPRGGGGADL GLAAALPRLR LVQLLSAGAE KFAGRLPEGV VLCNARGAHT PSTAEWVVAA
     VLAAQRGLPY FVREQDAGRW SPAAFASLAG SRVLVVGAGD IGRAVGRMLA GFDVELTCVA
     RTARDGVHGT DELPRLLPQA DVVVVIVPVT PETTGLVDAG FLAAMADGAL LVNAARGVVV
     DTDALLAELR SGRLRAALDV TEPEPLPEGH PLWSAPGLLL TPHVAGNVPE TNERAAAAVV
     DQLTRVLAGE PLVNVVGAY
//
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