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Database: UniProt
Entry: A0A0G1TBP1_9BACT
LinkDB: A0A0G1TBP1_9BACT
Original site: A0A0G1TBP1_9BACT 
ID   A0A0G1TBP1_9BACT        Unreviewed;       334 AA.
AC   A0A0G1TBP1;
DT   22-JUL-2015, integrated into UniProtKB/TrEMBL.
DT   22-JUL-2015, sequence version 1.
DT   08-NOV-2023, entry version 24.
DE   RecName: Full=D-glycerate dehydrogenase {ECO:0008006|Google:ProtNLM};
DE   Flags: Fragment;
GN   ORFNames=UY05_C0037G0001 {ECO:0000313|EMBL:KKU79141.1};
OS   Candidatus Peregrinibacteria bacterium GW2011_GWA2_47_7.
OC   Bacteria; Candidatus Peregrinibacteria.
OX   NCBI_TaxID=1619058 {ECO:0000313|EMBL:KKU79141.1, ECO:0000313|Proteomes:UP000034737};
RN   [1] {ECO:0000313|EMBL:KKU79141.1, ECO:0000313|Proteomes:UP000034737}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Brown C.T., Hug L.A., Thomas B.C., Sharon I., Castelle C.J., Singh A.,
RA   Wilkins M.J., Williams K.H., Banfield J.F.;
RT   "rRNA introns, odd ribosomes, and small enigmatic genomes across a large
RT   radiation of phyla.";
RL   Nature 0:0-0(2015).
CC   -!- SIMILARITY: Belongs to the D-isomer specific 2-hydroxyacid
CC       dehydrogenase family. {ECO:0000256|ARBA:ARBA00005854,
CC       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:KKU79141.1}.
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DR   EMBL; LCON01000037; KKU79141.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0G1TBP1; -.
DR   PATRIC; fig|1619058.3.peg.423; -.
DR   Proteomes; UP000034737; Unassembled WGS sequence.
DR   GO; GO:0051287; F:NAD binding; IEA:InterPro.
DR   GO; GO:0016616; F:oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor; IEA:InterPro.
DR   CDD; cd05301; GDH; 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; IPR029752; D-isomer_DH_CS1.
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   PANTHER; PTHR10996:SF257; ZGC:136493; 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; PS00065; D_2_HYDROXYACID_DH_1; 1.
DR   PROSITE; PS00671; D_2_HYDROXYACID_DH_3; 1.
PE   3: Inferred from homology;
KW   Oxidoreductase {ECO:0000256|RuleBase:RU003719}.
FT   DOMAIN          13..328
FT                   /note="D-isomer specific 2-hydroxyacid dehydrogenase
FT                   catalytic"
FT                   /evidence="ECO:0000259|Pfam:PF00389"
FT   DOMAIN          118..296
FT                   /note="D-isomer specific 2-hydroxyacid dehydrogenase NAD-
FT                   binding"
FT                   /evidence="ECO:0000259|Pfam:PF02826"
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:KKU79141.1"
SQ   SEQUENCE   334 AA;  36319 MW;  63A2BC0D43028C95 CRC64;
     AHHLHNIFMA NIYVTRQIPE GGLKMLRDTF GSFEMNTEDR VLSKTELFEK VRGRDAVLCL
     LTDPIDDAIF EAAGPQCRIF SNYAVGYNNI DVAAASKRNI MITNTPGVLT DATADMAVAL
     LFSAARRIAE GDKFTRAGKF KGWGPLLLLG QDITGKTLGI VGAGRIGSAV AERMHKGFNM
     KILYTDLNGN AELEQATGAR KVDLETLLRE SDFISIHVNL TPETTHLLSE KEFKIMKPSA
     VLINTSRGPV MDEVALVNAL KNNIIFAAGL DVYENEPSLA PGLTDLPNVV IPPHTASATF
     ATRTKMATMA AQNLIDALSG KMPEFCVNKD AIRL
//
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