ID A0A1I3N0S7_9BURK Unreviewed; 324 AA.
AC A0A1I3N0S7;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 27-MAR-2024, entry version 14.
DE SubName: Full=Gluconate 2-dehydrogenase {ECO:0000313|EMBL:SFJ02516.1};
GN ORFNames=SAMN05192543_105179 {ECO:0000313|EMBL:SFJ02516.1};
OS Paraburkholderia megapolitana.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Paraburkholderia.
OX NCBI_TaxID=420953 {ECO:0000313|EMBL:SFJ02516.1, ECO:0000313|Proteomes:UP000199548};
RN [1] {ECO:0000313|EMBL:SFJ02516.1, ECO:0000313|Proteomes:UP000199548}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LMG 23650 {ECO:0000313|EMBL:SFJ02516.1,
RC ECO:0000313|Proteomes:UP000199548};
RA de Groot N.N.;
RL Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the D-isomer specific 2-hydroxyacid
CC dehydrogenase family. {ECO:0000256|ARBA:ARBA00005854,
CC ECO:0000256|RuleBase:RU003719}.
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DR EMBL; FOQU01000005; SFJ02516.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1I3N0S7; -.
DR STRING; 420953.SAMN05192543_105179; -.
DR OrthoDB; 9805416at2; -.
DR Proteomes; UP000199548; 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; IPR029752; D-isomer_DH_CS1.
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; PS00065; D_2_HYDROXYACID_DH_1; 1.
PE 3: Inferred from homology;
KW Oxidoreductase {ECO:0000256|RuleBase:RU003719};
KW Reference proteome {ECO:0000313|Proteomes:UP000199548}.
FT DOMAIN 4..318
FT /note="D-isomer specific 2-hydroxyacid dehydrogenase
FT catalytic"
FT /evidence="ECO:0000259|Pfam:PF00389"
FT DOMAIN 107..286
FT /note="D-isomer specific 2-hydroxyacid dehydrogenase NAD-
FT binding"
FT /evidence="ECO:0000259|Pfam:PF02826"
SQ SEQUENCE 324 AA; 34428 MW; AA6B2D756B185D0E CRC64;
MKKIVAYKPL PDDVLAYLQE HLEVVQIDTS SRDTHDAFVA ALRDADGAIG ASVKIDSSML
EGATRLKALS TISVGFDNFD VADLTRRGIL LANTPDVLTE STADTVFSLI LATARRVVEL
ADWVKAGHWQ RSIGPDHFGV DVQGKTLGIV GLGRIGGAVA RRAALGFNMQ VLYTNRSANQ
AAEETYGARR VELSELLAVS DFVCLQVPLT PETHHLIGAA QLRAMKKSAI LINASRGATV
DEAALIDALQ AGTIHGAGLD VFAHEPLAAD SPLLKLNNVV ALPHIGSATH ETRHAMARCA
AENLVAALAG TLTRNVVNRD VLGR
//
