ID A0A239U1R8_9FIRM Unreviewed; 315 AA.
AC A0A239U1R8;
DT 25-OCT-2017, integrated into UniProtKB/TrEMBL.
DT 25-OCT-2017, sequence version 1.
DT 27-MAR-2024, entry version 16.
DE SubName: Full=Glyoxylate/hydroxypyruvate reductase A {ECO:0000313|EMBL:SNV03785.1};
DE EC=1.1.1.79 {ECO:0000313|EMBL:SNV03785.1};
GN Name=ghrA {ECO:0000313|EMBL:SNV03785.1};
GN ORFNames=SAMEA4364220_01867 {ECO:0000313|EMBL:SNV03785.1};
OS Megamonas hypermegale.
OC Bacteria; Bacillota; Negativicutes; Selenomonadales; Selenomonadaceae;
OC Megamonas.
OX NCBI_TaxID=158847 {ECO:0000313|EMBL:SNV03785.1, ECO:0000313|Proteomes:UP000215383};
RN [1] {ECO:0000313|EMBL:SNV03785.1, ECO:0000313|Proteomes:UP000215383}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NCTC10570 {ECO:0000313|EMBL:SNV03785.1,
RC ECO:0000313|Proteomes:UP000215383};
RG Pathogen Informatics;
RL Submitted (JUN-2017) to the EMBL/GenBank/DDBJ databases.
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DR EMBL; LT906446; SNV03785.1; -; Genomic_DNA.
DR RefSeq; WP_027889025.1; NZ_LT906446.1.
DR AlphaFoldDB; A0A239U1R8; -.
DR GeneID; 78507855; -.
DR eggNOG; COG0111; Bacteria.
DR Proteomes; UP000215383; Chromosome 1.
DR GO; GO:0030267; F:glyoxylate reductase (NADP+) activity; IEA:UniProtKB-EC.
DR GO; GO:0051287; F:NAD binding; IEA:InterPro.
DR CDD; cd05300; 2-Hacid_dh_1; 1.
DR Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 2.
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.
PE 4: Predicted;
KW NAD {ECO:0000256|ARBA:ARBA00023027};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000313|EMBL:SNV03785.1}; Pyruvate {ECO:0000313|EMBL:SNV03785.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000215383}.
FT DOMAIN 99..274
FT /note="D-isomer specific 2-hydroxyacid dehydrogenase NAD-
FT binding"
FT /evidence="ECO:0000259|Pfam:PF02826"
SQ SEQUENCE 315 AA; 35074 MW; 17D85DBABDB5F98E CRC64;
MNILVVMPFK QKHKKLMQEN FPNENFIYER NPSKDLVTSA DVIIGNVKTD LLKFATNLKL
LQLNSAGTDG YCDESIFPKN AVLTNATGAY GLALSEYMLA VLMAMQKKLY KYHDNQKQNL
WHDEGEVTSI CNSVILVVGL GDIGGNFAKK VKALGARVIG IKRRIIDKPE YVDELGTLDN
LKEYLPKVDV VVNILPGTKA TYHLFDKDKF ALMKDKAFFV NAGRGNAVVE DDLIEAVESG
HLAGAAVDVT EIEPLPKESR MWQVENIHIT PHTAGQYHLA ATHDNIVNIA KENLSRLLTG
KDLINQVDFT TGYKK
//
