ID A0A0A5G6I5_9BACI Unreviewed; 321 AA.
AC A0A0A5G6I5;
DT 04-FEB-2015, integrated into UniProtKB/TrEMBL.
DT 04-FEB-2015, sequence version 1.
DT 27-MAR-2024, entry version 22.
DE SubName: Full=2-ketogluconate reductase {ECO:0000313|EMBL:KGX86705.1};
GN ORFNames=N784_03660 {ECO:0000313|EMBL:KGX86705.1};
OS Pontibacillus litoralis JSM 072002.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Pontibacillus.
OX NCBI_TaxID=1385512 {ECO:0000313|EMBL:KGX86705.1, ECO:0000313|Proteomes:UP000030401};
RN [1] {ECO:0000313|EMBL:KGX86705.1, ECO:0000313|Proteomes:UP000030401}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JSM 072002 {ECO:0000313|EMBL:KGX86705.1,
RC ECO:0000313|Proteomes:UP000030401};
RA Huang J., Wang G.;
RL Submitted (AUG-2013) 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}.
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:KGX86705.1}.
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DR EMBL; AVPG01000011; KGX86705.1; -; Genomic_DNA.
DR RefSeq; WP_036834129.1; NZ_AVPG01000011.1.
DR AlphaFoldDB; A0A0A5G6I5; -.
DR STRING; 1385512.N784_03660; -.
DR eggNOG; COG1052; Bacteria.
DR OrthoDB; 9805416at2; -.
DR Proteomes; UP000030401; 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:UP000030401}.
FT DOMAIN 6..320
FT /note="D-isomer specific 2-hydroxyacid dehydrogenase
FT catalytic"
FT /evidence="ECO:0000259|Pfam:PF00389"
FT DOMAIN 111..289
FT /note="D-isomer specific 2-hydroxyacid dehydrogenase NAD-
FT binding"
FT /evidence="ECO:0000259|Pfam:PF02826"
SQ SEQUENCE 321 AA; 35426 MW; 1EDF5EF2A522826D CRC64;
MKKPYIFITR TLPEEIIAPF RANWDIQMWD SEEKPVDRTI LIQETAKADA LITMLSDRID
EQLLEQGAQL KVIANLAVGF DNIDVKAAQK KGIIVTNTPD VLTETTADLT FGLLMATARR
FIEASDHIRN GNWENWAPLL LAGLDIHHKT IGIVGMGRIG RAVAHRAQGF HMNVLYHNRS
RDTEAESALG ATYVSFEELL QQSDFVVCLA PFTEETAGMF NAKAFQTMKS SAMFINASRG
ANVVEEDLYE ALVAGDIAGA GLDVFTKEPI ANDHPLLTLK QVVALPHIGS ASVETRQAMM
HLCLENINLV LSGQQPKTEV K
//
