ID A0A448KB20_9ACTO Unreviewed; 324 AA.
AC A0A448KB20;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 27-MAR-2024, entry version 17.
DE SubName: Full=Glyoxylate/hydroxypyruvate reductase B {ECO:0000313|EMBL:VEG74110.1};
DE EC=1.1.1.79 {ECO:0000313|EMBL:VEG74110.1};
GN Name=ghrB {ECO:0000313|EMBL:VEG74110.1};
GN ORFNames=NCTC11923_00730 {ECO:0000313|EMBL:VEG74110.1};
OS Actinomyces slackii.
OC Bacteria; Actinomycetota; Actinomycetes; Actinomycetales; Actinomycetaceae;
OC Actinomyces.
OX NCBI_TaxID=52774 {ECO:0000313|EMBL:VEG74110.1, ECO:0000313|Proteomes:UP000276899};
RN [1] {ECO:0000313|EMBL:VEG74110.1, ECO:0000313|Proteomes:UP000276899}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NCTC11923 {ECO:0000313|EMBL:VEG74110.1,
RC ECO:0000313|Proteomes:UP000276899};
RG Pathogen Informatics;
RL Submitted (DEC-2018) 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; LR134363; VEG74110.1; -; Genomic_DNA.
DR RefSeq; WP_026426401.1; NZ_LR134363.1.
DR AlphaFoldDB; A0A448KB20; -.
DR STRING; 1278298.GCA_000428685_00253; -.
DR KEGG; asla:NCTC11923_00730; -.
DR Proteomes; UP000276899; 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; cd12166; 2-Hacid_dh_7; 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; PTHR43333; 2-HACID_DH_C DOMAIN-CONTAINING PROTEIN; 1.
DR PANTHER; PTHR43333:SF1; 2-HACID_DH_C DOMAIN-CONTAINING PROTEIN; 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.
DR PROSITE; PS00671; D_2_HYDROXYACID_DH_3; 1.
PE 3: Inferred from homology;
KW NAD {ECO:0000256|ARBA:ARBA00023027};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000256|RuleBase:RU003719}; Pyruvate {ECO:0000313|EMBL:VEG74110.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000276899}.
FT DOMAIN 23..307
FT /note="D-isomer specific 2-hydroxyacid dehydrogenase
FT catalytic"
FT /evidence="ECO:0000259|Pfam:PF00389"
FT DOMAIN 109..275
FT /note="D-isomer specific 2-hydroxyacid dehydrogenase NAD-
FT binding"
FT /evidence="ECO:0000259|Pfam:PF02826"
SQ SEQUENCE 324 AA; 35049 MW; 60BF81E4E061A7DB CRC64;
MIVTLPDEEL LDALVAHHPP LGVELRVWDW SRPVREALGE EADEVVGVVL PYLRAASQWR
SLADLPRLRL IQAQSAGYDN LLPIVPDGVA LANARGVHDA STAELALGLI IAAQRELPRW
ARARSWETVQ TRALADSRVL IVGAGEIGEA IRRRLEPFEV DLTRVATRAR DDQHGHIHGI
DELEQLLPSA DIVVLIVPLT ERTRGLIGAE QLALLPDGAL LVNMARGPVV DTRAITAEVV
SGRLRMASDV FDPEPLPEDH PLWQADGALI SPHIGGNTTA MAPRILALLA DQLPRLADGR
PLLHVVNERA DPAAPRAGAA RPAP
//