ID K2MES1_9BACI Unreviewed; 325 AA.
AC K2MES1;
DT 28-NOV-2012, integrated into UniProtKB/TrEMBL.
DT 28-NOV-2012, sequence version 1.
DT 27-MAR-2024, entry version 31.
DE SubName: Full=Gluconate 2-dehydrogenase {ECO:0000313|EMBL:EKF33808.1};
GN ORFNames=BA1_18155 {ECO:0000313|EMBL:EKF33808.1};
OS Bacillus xiamenensis.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX NCBI_TaxID=1178537 {ECO:0000313|EMBL:EKF33808.1, ECO:0000313|Proteomes:UP000010122};
RN [1] {ECO:0000313|EMBL:EKF33808.1, ECO:0000313|Proteomes:UP000010122}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HYC-10 {ECO:0000313|EMBL:EKF33808.1,
RC ECO:0000313|Proteomes:UP000010122};
RX PubMed=23209239; DOI=10.1128/JB.01920-12;
RA Lai Q., Liu Y., Shao Z.;
RT "Genome Sequence of Bacillus sp. Strain HYC-10, Isolated from Intestinal
RT Tract Contents from a Marine Fish (Mugil cephalus).";
RL J. Bacteriol. 194:6991-6991(2012).
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:EKF33808.1}.
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DR EMBL; AMSH01000094; EKF33808.1; -; Genomic_DNA.
DR RefSeq; WP_008361986.1; NZ_JAPDCO010000001.1.
DR AlphaFoldDB; K2MES1; -.
DR PATRIC; fig|1178537.3.peg.3754; -.
DR eggNOG; COG1052; Bacteria.
DR OrthoDB; 9805416at2; -.
DR Proteomes; UP000010122; 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; PS00670; D_2_HYDROXYACID_DH_2; 1.
PE 3: Inferred from homology;
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000256|RuleBase:RU003719}.
FT DOMAIN 5..319
FT /note="D-isomer specific 2-hydroxyacid dehydrogenase
FT catalytic"
FT /evidence="ECO:0000259|Pfam:PF00389"
FT DOMAIN 108..288
FT /note="D-isomer specific 2-hydroxyacid dehydrogenase NAD-
FT binding"
FT /evidence="ECO:0000259|Pfam:PF02826"
SQ SEQUENCE 325 AA; 36705 MW; 4EEFB4C0CF5E1250 CRC64;
MKPHIFVTKP LPASFEDMLK EHCTYEVWQS KDPIPRDVLY EKLQKADGLL TSGTKIDQDL
LDHAPQLKVV SNHSVGYDNF DLEAMRQRGV IGTHTPYTLD HTVADLAFSL ILSSARRIAE
LDRFIREGKW TEFVQEEDMF GIDVHHQTLG IIGMGRIGEQ VAKRAAHGFD MNVLYHNRSR
NEKAESAYGA VYCALDDLLK QADIIVLITP LTDETYHLIG EREFKFMKQT ALFVNISRGK
TVDEKSLIQA LQEGWIKGAG LDVYEQEPLQ KDHPFMEMNN VTLAPHIGSA TETTRDLMLK
RAIHNVIHGI DGKAPVDIVK ELATS
//
