ID A0A1G6NU33_9BACI Unreviewed; 322 AA.
AC A0A1G6NU33;
DT 05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 1.
DT 27-MAR-2024, entry version 15.
DE SubName: Full=Gluconate 2-dehydrogenase {ECO:0000313|EMBL:SDC70675.1};
GN ORFNames=SAMN05421737_11353 {ECO:0000313|EMBL:SDC70675.1};
OS Shouchella lonarensis.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Shouchella.
OX NCBI_TaxID=1464122 {ECO:0000313|EMBL:SDC70675.1, ECO:0000313|Proteomes:UP000242662};
RN [1] {ECO:0000313|Proteomes:UP000242662}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=25nlg {ECO:0000313|Proteomes:UP000242662};
RA Varghese N., Submissions S.;
RL Submitted (SEP-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; FMYM01000013; SDC70675.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1G6NU33; -.
DR STRING; 1464122.SAMN05421737_11353; -.
DR OrthoDB; 9805416at2; -.
DR Proteomes; UP000242662; 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; 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.
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};
KW Reference proteome {ECO:0000313|Proteomes:UP000242662}.
FT DOMAIN 10..319
FT /note="D-isomer specific 2-hydroxyacid dehydrogenase
FT catalytic"
FT /evidence="ECO:0000259|Pfam:PF00389"
FT DOMAIN 109..288
FT /note="D-isomer specific 2-hydroxyacid dehydrogenase NAD-
FT binding"
FT /evidence="ECO:0000259|Pfam:PF02826"
SQ SEQUENCE 322 AA; 35262 MW; 86132DE29562DB18 CRC64;
MSKPYVFIDE ALPLSVEKYL TKYCTYTMWS KSQPVPTHTL QNELKKAAGA MLTQSRPRAA
DIAHAPHLKV ISTATVGYDH LDVSMLAAHG ITVTNTPYVL DETVADLIFG LILSGCRRIA
ELHTWVRAGS WNQAVPLELY GQDVYNKTLG IIGMGRIGEK IAHRAKHGFN MSILYHNRSR
RPEAEKLYDA KKVDLTTLLE TADVVVIMVP LTKETTHLIG AKELAKMKPT AVLVNGARGA
VIDEDALIAA LKQQQIWGAA LDVFEQEPLP SGHPFLTLEN VTLTPHIGSA TAATREAMAQ
RAAENLVAGL NGQQPQDIVE NE
//
