ID A0A0S3EZA8_9SPHN Unreviewed; 332 AA.
AC A0A0S3EZA8;
DT 17-FEB-2016, integrated into UniProtKB/TrEMBL.
DT 17-FEB-2016, sequence version 1.
DT 27-MAR-2024, entry version 23.
DE SubName: Full=D-glycerate dehydrogenase {ECO:0000313|EMBL:ALR20709.1};
GN ORFNames=ATN00_10770 {ECO:0000313|EMBL:ALR20709.1};
OS Sphingobium baderi.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC Sphingomonadaceae; Sphingobium.
OX NCBI_TaxID=1332080 {ECO:0000313|EMBL:ALR20709.1, ECO:0000313|Proteomes:UP000056968};
RN [1] {ECO:0000313|EMBL:ALR20709.1, ECO:0000313|Proteomes:UP000056968}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DE-13 {ECO:0000313|EMBL:ALR20709.1,
RC ECO:0000313|Proteomes:UP000056968};
RA Cheng M., Meng Q., Yang Y., Chu C., Yan X., He J., Li S.;
RT "A Two-component Flavoprotein Monooxygenase System MeaXY Responsible for
RT para-Hydroxylation of 2-Methyl-6-ethylaniline and 2,6-Diethylaniline in
RT Sphingobium baderi DE-13.";
RL Submitted (NOV-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the D-isomer specific 2-hydroxyacid
CC dehydrogenase family. {ECO:0000256|RuleBase:RU003719}.
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DR EMBL; CP013264; ALR20709.1; -; Genomic_DNA.
DR RefSeq; WP_062064577.1; NZ_CP013264.1.
DR AlphaFoldDB; A0A0S3EZA8; -.
DR STRING; 1332080.ATN00_10770; -.
DR KEGG; sbd:ATN00_10770; -.
DR OrthoDB; 9793626at2; -.
DR Proteomes; UP000056968; Chromosome.
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; 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; PS00670; D_2_HYDROXYACID_DH_2; 1.
PE 3: Inferred from homology;
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000256|RuleBase:RU003719};
KW Reference proteome {ECO:0000313|Proteomes:UP000056968}.
FT DOMAIN 23..327
FT /note="D-isomer specific 2-hydroxyacid dehydrogenase
FT catalytic"
FT /evidence="ECO:0000259|Pfam:PF00389"
FT DOMAIN 117..296
FT /note="D-isomer specific 2-hydroxyacid dehydrogenase NAD-
FT binding"
FT /evidence="ECO:0000259|Pfam:PF02826"
SQ SEQUENCE 332 AA; 35919 MW; 88D58C73D2C483AE CRC64;
MAKKPRPAKP RVIVTRRLPP NVEARMAELF DASFNVGDVP MDRPALIRAM AQCDVLVPCI
SDQIDGALIE AAPERLQLIA SFGSGVDHID LGAARQKGII VTNTPGVLTE DTADMTMALI
LSVPRRLAEG EKLVRSGEWR GWSPSGMLGH RIGGKKLGII GMGRIGRAVA RRACAFGLTI
AYHNRHRLPF EVEQELEASW CPELDGLLET SDIISINCPL NADSRGMIDA RRIALLTPDA
YLINTSRAEI VDEPALIAAL NEGRIAGAGL DVYMHEPAVD ADLLSLSNVV LLPHMGSATF
EGRDATGARV IANIRSWVDG HRPPNQVLEG WV
//
