ID A0A0D5VNE4_9BURK Unreviewed; 332 AA.
AC A0A0D5VNE4; A0A2T1B0F2;
DT 27-MAY-2015, integrated into UniProtKB/TrEMBL.
DT 27-MAY-2015, sequence version 1.
DT 27-MAR-2024, entry version 39.
DE SubName: Full=Gluconate 2-dehydrogenase {ECO:0000313|EMBL:PRZ54325.1};
GN ORFNames=BX589_107158 {ECO:0000313|EMBL:PRZ54325.1};
OS Paraburkholderia fungorum.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Paraburkholderia.
OX NCBI_TaxID=134537 {ECO:0000313|EMBL:PRZ54325.1, ECO:0000313|Proteomes:UP000238376};
RN [1] {ECO:0000313|EMBL:PRZ54325.1, ECO:0000313|Proteomes:UP000238376}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LMG 28183 {ECO:0000313|EMBL:PRZ54325.1,
RC ECO:0000313|Proteomes:UP000238376};
RA Whitman W.;
RT "Genomic Encyclopedia of Type Strains, Phase III (KMG-III): the genomes of
RT soil and plant-associated and newly described type strains.";
RL Submitted (MAR-2018) 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:PRZ54325.1}.
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DR EMBL; PVZM01000007; PRZ54325.1; -; Genomic_DNA.
DR RefSeq; WP_042273674.1; NZ_QFRC01000002.1.
DR STRING; 134537.OI25_5022; -.
DR GeneID; 66518880; -.
DR KEGG; bfn:OI25_5022; -.
DR OrthoDB; 9805416at2; -.
DR Proteomes; UP000238376; Unassembled WGS sequence.
DR GO; GO:0008873; F:gluconate 2-dehydrogenase activity; IEA:UniProtKB-EC.
DR GO; GO:0030267; F:glyoxylate reductase (NADP+) activity; IEA:UniProtKB-EC.
DR GO; GO:0016618; F:hydroxypyruvate reductase activity; IEA:UniProtKB-EC.
DR GO; GO:0051287; F:NAD binding; 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 4..317
FT /note="D-isomer specific 2-hydroxyacid dehydrogenase
FT catalytic"
FT /evidence="ECO:0000259|Pfam:PF00389"
FT DOMAIN 106..285
FT /note="D-isomer specific 2-hydroxyacid dehydrogenase NAD-
FT binding"
FT /evidence="ECO:0000259|Pfam:PF02826"
SQ SEQUENCE 332 AA; 35582 MW; 93F5F65CF2D9D0BB CRC64;
MKHVVAYRSL PPAVLGLLRE HCSVELVDVS SGDLAPFRRA LGTAHGMVGN NLKITPEILD
AAPLLQVAST ISAGFDAFDV PELSRRGIVL TNTPEEVTET TADLVFSLIL ATARRISELA
DWTRRGQWTR TIGEAQFGVD VHHKTLGIVG LGRIGSAVAK RAALGFGMDV IYSNRSRNPE
AEERYGAQWR PLPELLATAD FVCVLVPLSP ATERLIGSAE LATMKPSAIL INCARGQVVD
EAALIAHLRE GRILGAGLDV FEREPVSPDS PLLQLSNVVA VPHIGSATQQ TRENMAMRAV
RNLIEALDGQ LSSTCVNPEA LHARSSAQQI AG
//
