ID A0A0F2CAP1_9MICO Unreviewed; 328 AA.
AC A0A0F2CAP1;
DT 24-JUN-2015, integrated into UniProtKB/TrEMBL.
DT 24-JUN-2015, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE SubName: Full=Glycerate dehydrogenase {ECO:0000313|EMBL:KJQ54366.1};
DE EC=1.1.1.29 {ECO:0000313|EMBL:KJQ54366.1};
GN Name=hprA {ECO:0000313|EMBL:KJQ54366.1};
GN ORFNames=RS85_01968 {ECO:0000313|EMBL:KJQ54366.1};
OS Microbacterium sp. SA39.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Microbacteriaceae;
OC Microbacterium.
OX NCBI_TaxID=1263625 {ECO:0000313|EMBL:KJQ54366.1, ECO:0000313|Proteomes:UP000033425};
RN [1] {ECO:0000313|EMBL:KJQ54366.1, ECO:0000313|Proteomes:UP000033425}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SA39 {ECO:0000313|EMBL:KJQ54366.1,
RC ECO:0000313|Proteomes:UP000033425};
RA Corretto E., Antonielli L., Sessitsch A., Kidd P., Weyens N., Brader G.;
RT "Draft genome sequences of ten Microbacterium spp. with emphasis on heavy
RT metal contaminated environments.";
RL Submitted (JAN-2015) to the EMBL/GenBank/DDBJ databases.
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:KJQ54366.1}.
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DR EMBL; JXRU01000033; KJQ54366.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0F2CAP1; -.
DR STRING; 1263625.RS85_01968; -.
DR PATRIC; fig|1263625.4.peg.1979; -.
DR Proteomes; UP000033425; Unassembled WGS sequence.
DR GO; GO:0008465; F:glycerate dehydrogenase activity; IEA:UniProtKB-EC.
DR GO; GO:0051287; F:NAD binding; IEA:InterPro.
DR CDD; cd12165; 2-Hacid_dh_6; 1.
DR Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 2.
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; PTHR43333; 2-HACID_DH_C DOMAIN-CONTAINING PROTEIN; 1.
DR PANTHER; PTHR43333:SF1; 2-HACID_DH_C DOMAIN-CONTAINING PROTEIN; 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; PS00671; D_2_HYDROXYACID_DH_3; 1.
PE 4: Predicted;
KW NAD {ECO:0000256|ARBA:ARBA00023027};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000313|EMBL:KJQ54366.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000033425}.
FT DOMAIN 108..295
FT /note="D-isomer specific 2-hydroxyacid dehydrogenase NAD-
FT binding"
FT /evidence="ECO:0000259|Pfam:PF02826"
SQ SEQUENCE 328 AA; 35122 MW; 42CF9C928878B6C9 CRC64;
MSAPLRIAVT DPIIAEFADE LRRTARPHDW VFADLDVPES VRAAIDGADV VIGSRITVDD
MADADRVRLV HVTGAGVDRV EDGAVPDGVP LCNTGHHGPA IAEHVLVTAL MLRRRVLPVD
AELRRGEWRT VATAPGSIAY HRSLAGSTLG LIGYGEIGRS VAHLAKAFGM RVIAMRRHPD
AAGPGTELLD RVYGEDQLHP LLGESDVVVV TAPLTESTRG LIDADALAQL HPDALIINVA
RGALIDEDAL YAALAEERIG GAGIDVWWDA PDGTQAPASV RRFAALDRVV LTPHYSGHAR
EVFTARAADI ARNIDLLDVG LPLERQVR
//
