ID A0A0J6WTP2_9FIRM Unreviewed; 343 AA.
AC A0A0J6WTP2;
DT 14-OCT-2015, integrated into UniProtKB/TrEMBL.
DT 14-OCT-2015, sequence version 1.
DT 27-MAR-2024, entry version 29.
DE SubName: Full=Gluconate 2-dehydrogenase {ECO:0000313|EMBL:KMO85909.1};
GN ORFNames=AB840_11025 {ECO:0000313|EMBL:KMO85909.1};
OS Megasphaera cerevisiae DSM 20462.
OC Bacteria; Bacillota; Negativicutes; Veillonellales; Veillonellaceae;
OC Megasphaera.
OX NCBI_TaxID=1122219 {ECO:0000313|EMBL:KMO85909.1, ECO:0000313|Proteomes:UP000036503};
RN [1] {ECO:0000313|EMBL:KMO85909.1, ECO:0000313|Proteomes:UP000036503}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 20462 {ECO:0000313|EMBL:KMO85909.1,
RC ECO:0000313|Proteomes:UP000036503};
RA Kutumbaka K., Pasmowitz J., Mategko J., Reyes D., Friedrich A., Han S.,
RA Martens-Habbena W., Neal-McKinney J., Janagama H.K., Nadala C.,
RA Samadpour M.;
RT "Draft genome sequence of beer spoilage bacterium Megasphaera cerevisiae
RT type strain 20462.";
RL Submitted (JUN-2015) 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:KMO85909.1}.
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DR EMBL; LEKT01000041; KMO85909.1; -; Genomic_DNA.
DR RefSeq; WP_048514903.1; NZ_LEKT01000041.1.
DR AlphaFoldDB; A0A0J6WTP2; -.
DR STRING; 39029.BSR42_13480; -.
DR PATRIC; fig|1122219.3.peg.2157; -.
DR InParanoid; A0A0J6WTP2; -.
DR OrthoDB; 9805416at2; -.
DR Proteomes; UP000036503; 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; cd12171; 2-Hacid_dh_10; 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; PTHR43761:SF1; 2-HACID_DH DOMAIN-CONTAINING PROTEIN-RELATED; 1.
DR PANTHER; PTHR43761; D-ISOMER SPECIFIC 2-HYDROXYACID DEHYDROGENASE FAMILY PROTEIN (AFU_ORTHOLOGUE AFUA_1G13630); 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:UP000036503}.
FT DOMAIN 60..132
FT /note="D-isomer specific 2-hydroxyacid dehydrogenase
FT catalytic"
FT /evidence="ECO:0000259|Pfam:PF00389"
FT DOMAIN 133..308
FT /note="D-isomer specific 2-hydroxyacid dehydrogenase NAD-
FT binding"
FT /evidence="ECO:0000259|Pfam:PF02826"
SQ SEQUENCE 343 AA; 38104 MW; E75582B7938C35FD CRC64;
MKLVGIGDLL IPADYIKKGF QKFADQGVEV KFVDWELQNY EELQNINLKI ETDGCEEYEV
PENLIDKISD ADIIITQFCP INKKVMDACS NLKAIGVLRG GYENINAAYA KRKNILVYNT
PGRNATAVAD FTVGMILSEC RNIAKAHCNL KAGRWVRDYA NAASVPDLAG KIAGIIGLGQ
IGKKVAQRLH GFDMTILGYD PYAATVPEYV QLVSLDILLR KSDFITIHSR LTKDTEELMN
ADAFAKMKPV AYFINTARAG LVDETALYEA LKSKKIMGAA LDVFDKEPLG REYPLVQLNN
VTITPHLAGG TVDAFLKSPF LLEKEMESFL HGKINYQFVI NQK
//
