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Database: UniProt
Entry: A0A142M193_AMIAI
LinkDB: A0A142M193_AMIAI
Original site: A0A142M193_AMIAI 
ID   A0A142M193_AMIAI        Unreviewed;       338 AA.
AC   A0A142M193;
DT   08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT   08-JUN-2016, sequence version 1.
DT   27-MAR-2024, entry version 22.
DE   SubName: Full=Lactate dehydrogenase-like 2-hydroxyacid dehydrogenase {ECO:0000313|EMBL:MBB3710118.1};
GN   ORFNames=FHS67_006478 {ECO:0000313|EMBL:MBB3710118.1};
OS   Aminobacter aminovorans (Chelatobacter heintzii).
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC   Phyllobacteriaceae; Aminobacter.
OX   NCBI_TaxID=83263 {ECO:0000313|EMBL:MBB3710118.1, ECO:0000313|Proteomes:UP000577697};
RN   [1] {ECO:0000313|EMBL:MBB3710118.1, ECO:0000313|Proteomes:UP000577697}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 10368 {ECO:0000313|EMBL:MBB3710118.1,
RC   ECO:0000313|Proteomes:UP000577697};
RA   Goeker M.;
RT   "Genomic Encyclopedia of Type Strains, Phase IV (KMG-IV): sequencing the
RT   most valuable type-strain genomes for metagenomic binning, comparative
RT   biology and taxonomic classification.";
RL   Submitted (AUG-2020) 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:MBB3710118.1}.
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DR   EMBL; JACICB010000043; MBB3710118.1; -; Genomic_DNA.
DR   RefSeq; WP_067956377.1; NZ_JACICB010000043.1.
DR   AlphaFoldDB; A0A142M193; -.
DR   STRING; 83263.AA2016_1177; -.
DR   Proteomes; UP000577697; 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; cd12156; HPPR; 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; 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.
PE   3: Inferred from homology;
KW   Oxidoreductase {ECO:0000256|RuleBase:RU003719}.
FT   DOMAIN          41..327
FT                   /note="D-isomer specific 2-hydroxyacid dehydrogenase
FT                   catalytic"
FT                   /evidence="ECO:0000259|Pfam:PF00389"
FT   DOMAIN          123..296
FT                   /note="D-isomer specific 2-hydroxyacid dehydrogenase NAD-
FT                   binding"
FT                   /evidence="ECO:0000259|Pfam:PF02826"
SQ   SEQUENCE   338 AA;  36773 MW;  A6DF948E6D1300B0 CRC64;
     MNIAAGAETN NGRLADKPVI LQMAELARFP YRSIGDRFEV IRYWQIDEPN AMLARDGAKV
     RGMIAAGSQR IDDVILDKLP NLEVIANIGV GYDRLDIEAV ARRGIIATNT PDVLTEEVAD
     LTVGLLIATV RRMPQAERHI REGRWAKSPF PNSPSLRGRS VGIVGLGRIG KAVARRLQGF
     EVSEICYCGR TRQADVPYRH FKDIREMAAH ISVLILTLPG GPETKGLVDA DVLAKLGSDG
     IIVNVARGAV IEKDALIAAL RDGAILAAGL DVFWNEPEVP QELLALDNVV LLPHVGSASQ
     KTRAEMIELL QDNLFAWFEG RGPLTPVAET PWQGGNGE
//
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