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Database: UniProt
Entry: A0A0Q6W3E0_9BURK
LinkDB: A0A0Q6W3E0_9BURK
Original site: A0A0Q6W3E0_9BURK 
ID   A0A0Q6W3E0_9BURK        Unreviewed;       328 AA.
AC   A0A0Q6W3E0;
DT   20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT   20-JAN-2016, sequence version 1.
DT   24-JAN-2024, entry version 26.
DE   RecName: Full=Hydroxyacid dehydrogenase {ECO:0008006|Google:ProtNLM};
GN   ORFNames=ASC87_07605 {ECO:0000313|EMBL:KQV85541.1};
OS   Rhizobacter sp. Root1221.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales; Rhizobacter.
OX   NCBI_TaxID=1736433 {ECO:0000313|EMBL:KQV85541.1, ECO:0000313|Proteomes:UP000051465};
RN   [1] {ECO:0000313|EMBL:KQV85541.1, ECO:0000313|Proteomes:UP000051465}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Root1221 {ECO:0000313|EMBL:KQV85541.1,
RC   ECO:0000313|Proteomes:UP000051465};
RA   Gilbert D.G.;
RL   Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:KQV85541.1, ECO:0000313|Proteomes:UP000051465}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Root1221 {ECO:0000313|EMBL:KQV85541.1,
RC   ECO:0000313|Proteomes:UP000051465};
RA   Schulze-Lefert P.;
RT   "Functional overlap of the Arabidopsis leaf and root microbiotas.";
RL   Submitted (NOV-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:KQV85541.1}.
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DR   EMBL; LMDI01000045; KQV85541.1; -; Genomic_DNA.
DR   RefSeq; WP_056669207.1; NZ_LMDI01000045.1.
DR   AlphaFoldDB; A0A0Q6W3E0; -.
DR   STRING; 1736433.ASC87_07605; -.
DR   OrthoDB; 9805416at2; -.
DR   Proteomes; UP000051465; 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; cd05300; 2-Hacid_dh_1; 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; 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:UP000051465}.
FT   DOMAIN          14..322
FT                   /note="D-isomer specific 2-hydroxyacid dehydrogenase
FT                   catalytic"
FT                   /evidence="ECO:0000259|Pfam:PF00389"
FT   DOMAIN          113..291
FT                   /note="D-isomer specific 2-hydroxyacid dehydrogenase NAD-
FT                   binding"
FT                   /evidence="ECO:0000259|Pfam:PF02826"
SQ   SEQUENCE   328 AA;  34621 MW;  CCFA0444D26D0041 CRC64;
     MSQTLTPIRQ LTLLHPLPDA EYARLHAAVP EVRFVRADTA ADWTGAVAHA DAVLLGHQGV
     TIDDLLGAAP GLRWIQTASA GVDRVLTPRL RASPVVVTNA SGVHAVNIAE HVLALLLGFT
     RQLPALRDAQ HRQAWATPPL PGLFEAEGQT LLVVGLGAIG GAVARKAAAL GLKVTAVRRD
     PHGDGVPGVE RTVGLDALDD ELPHADHLVI ALPLTAETRG LFGAERLARL RPGAYLYNIA
     RGGIVDTGAL LAALQSGHLA GAGLDVTDPE PLPPASPLWR LPQVVITSHT AGLTPNSARR
     LVDITLDNLL RVREGRPLRN VVDRARGY
//
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