ID G5JIY1_9STAP Unreviewed; 318 AA.
AC G5JIY1;
DT 25-JAN-2012, integrated into UniProtKB/TrEMBL.
DT 25-JAN-2012, sequence version 1.
DT 27-MAR-2024, entry version 35.
DE SubName: Full=Glycerate dehydrogenase {ECO:0000313|EMBL:EHJ07861.1};
GN ORFNames=SS7213T_07138 {ECO:0000313|EMBL:EHJ07861.1};
OS Staphylococcus simiae CCM 7213 = CCUG 51256.
OC Bacteria; Bacillota; Bacilli; Bacillales; Staphylococcaceae;
OC Staphylococcus.
OX NCBI_TaxID=911238 {ECO:0000313|EMBL:EHJ07861.1, ECO:0000313|Proteomes:UP000005413};
RN [1] {ECO:0000313|EMBL:EHJ07861.1, ECO:0000313|Proteomes:UP000005413}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CCM 7213 {ECO:0000313|EMBL:EHJ07861.1,
RC ECO:0000313|Proteomes:UP000005413};
RX PubMed=22272658; DOI=10.1186/1471-2164-13-38;
RA Suzuki H., Lefebure T., Pavinski Bitar P., Stanhope M.J.;
RT "Comparative genomic analysis of the genus Staphylococcus including
RT Staphylococcus aureus and its newly described sister species Staphylococcus
RT simiae.";
RL BMC Genomics 13:38-38(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:EHJ07861.1}.
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DR EMBL; AEUN01000421; EHJ07861.1; -; Genomic_DNA.
DR RefSeq; WP_002464052.1; NZ_AEUN01000421.1.
DR AlphaFoldDB; G5JIY1; -.
DR PATRIC; fig|911238.3.peg.1224; -.
DR OrthoDB; 9805416at2; -.
DR Proteomes; UP000005413; 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; cd12178; 2-Hacid_dh_13; 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; IPR006140; D-isomer_DH_NAD-bd.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR PANTHER; PTHR42789; D-ISOMER SPECIFIC 2-HYDROXYACID DEHYDROGENASE FAMILY PROTEIN (AFU_ORTHOLOGUE AFUA_6G10090); 1.
DR PANTHER; PTHR42789:SF1; D-ISOMER SPECIFIC 2-HYDROXYACID DEHYDROGENASE FAMILY PROTEIN (AFU_ORTHOLOGUE AFUA_6G10090); 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.
PE 3: Inferred from homology;
KW NAD {ECO:0000256|ARBA:ARBA00023027};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000256|RuleBase:RU003719}.
FT DOMAIN 5..318
FT /note="D-isomer specific 2-hydroxyacid dehydrogenase
FT catalytic"
FT /evidence="ECO:0000259|Pfam:PF00389"
FT DOMAIN 109..286
FT /note="D-isomer specific 2-hydroxyacid dehydrogenase NAD-
FT binding"
FT /evidence="ECO:0000259|Pfam:PF02826"
SQ SEQUENCE 318 AA; 34592 MW; 36783918C3E01DE9 CRC64;
MEKVYVAGTI PEVGLKLLQE HFDVVDVYEG DGLIDKDTLI EGVKDATALI SLLSTNVDQD
VIDAGNKLKV IANYGAGFNN VDIAYARDKG IDVTNTPKAS TNATADLTIG LVLAVARRIV
EGDELSRTKG FDGWAPLFFR GREVSGKTIG VIGLGEIGSA VAKRARAFDM DVLYTGPHRK
EEKEHDIGAK YVDLDTLLKN ADFITINAAY SPKLHHLIDT EQFKMMKPTA YLINAARGPI
VHEEALVQAL KDKEIEGAAL DVYEFEPKIT DELKSFSNVV LTPHIGNATF EARDMMSRIV
ANAAISASKG ETPQFIVN
//
