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Database: UniProt
Entry: A0A101XNC4_9BACL
LinkDB: A0A101XNC4_9BACL
Original site: A0A101XNC4_9BACL 
ID   A0A101XNC4_9BACL        Unreviewed;       321 AA.
AC   A0A101XNC4;
DT   13-APR-2016, integrated into UniProtKB/TrEMBL.
DT   13-APR-2016, sequence version 1.
DT   27-MAR-2024, entry version 24.
DE   RecName: Full=D-glycerate dehydrogenase {ECO:0008006|Google:ProtNLM};
GN   ORFNames=ATW55_04125 {ECO:0000313|EMBL:KUO94607.1};
OS   Ferroacidibacillus organovorans.
OC   Bacteria; Bacillota; Bacilli; Bacillales; Alicyclobacillaceae;
OC   Ferroacidibacillus.
OX   NCBI_TaxID=1765683 {ECO:0000313|EMBL:KUO94607.1, ECO:0000313|Proteomes:UP000053557};
RN   [1] {ECO:0000313|EMBL:KUO94607.1, ECO:0000313|Proteomes:UP000053557}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ITV001 {ECO:0000313|EMBL:KUO94607.1,
RC   ECO:0000313|Proteomes:UP000053557};
RA   Dall'Agnol H., Nancucheo I., Johnson B., Oliveira R., Leite L., Pylro V.,
RA   Nunes G.L., Tzotzos G., Fernandes G.R., Dutra J., Orellana S.C.,
RA   Oliveira G.;
RT   "Draft genome sequence of Acidibacillus ferrooxidans ITV001, isolated from
RT   a chalcopyrite acid mine drainage site in Brazil.";
RL   Submitted (DEC-2015) 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:KUO94607.1}.
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DR   EMBL; LPVJ01000072; KUO94607.1; -; Genomic_DNA.
DR   RefSeq; WP_067720410.1; NZ_LPVJ01000072.1.
DR   AlphaFoldDB; A0A101XNC4; -.
DR   OrthoDB; 9805416at2; -.
DR   Proteomes; UP000053557; 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; IPR006140; D-isomer_DH_NAD-bd.
DR   InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR   PANTHER; PTHR10996:SF178; 2-HYDROXYACID DEHYDROGENASE YGL185C-RELATED; 1.
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}.
FT   DOMAIN          33..319
FT                   /note="D-isomer specific 2-hydroxyacid dehydrogenase
FT                   catalytic"
FT                   /evidence="ECO:0000259|Pfam:PF00389"
FT   DOMAIN          112..290
FT                   /note="D-isomer specific 2-hydroxyacid dehydrogenase NAD-
FT                   binding"
FT                   /evidence="ECO:0000259|Pfam:PF02826"
SQ   SEQUENCE   321 AA;  35143 MW;  8B451B85F4ACF1F8 CRC64;
     MTRLKLFVTR QLPRDVCDAV PADVSLAMYE HEKQAIPREE LLARVAGARG IVTMLTERID
     EEVMNAAGPQ LAVISTMSVG FEHIDRGAAA QRGIVVCHTP DVLTETTADL VFALLLATAR
     QLPQAERALR EGQWGTWQPF QFLGTDVHGK TIGLLGMGGI AQAVARRARG FGMRILYWSR
     SRKSDVEETL GVTYSDLTTL LQASDFVVPL LPGGDATRHL IDQHALSRMK RNAMLINASR
     GSVVDEDALL QALQTRAIAG AGLDVFAREP IALTHPLLRE ERVVLLPHIG SATLETRTSM
     ARRALENALL VMRGEAPFDR V
//
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