ID A0A1A5XSF7_9BACL Unreviewed; 320 AA.
AC A0A1A5XSF7;
DT 05-OCT-2016, integrated into UniProtKB/TrEMBL.
DT 05-OCT-2016, sequence version 1.
DT 27-MAR-2024, entry version 19.
DE SubName: Full=Bifunctional glyoxylate/hydroxypyruvate reductase B {ECO:0000313|EMBL:OBR56080.1};
DE SubName: Full=D-glycerate dehydrogenase {ECO:0000313|EMBL:UYZ15306.1};
GN ORFNames=A6764_04515 {ECO:0000313|EMBL:OBR56080.1}, A6764_10430
GN {ECO:0000313|EMBL:UYZ15306.1};
OS Brevibacillus sp. WF146.
OC Bacteria; Bacillota; Bacilli; Bacillales; Paenibacillaceae; Brevibacillus.
OX NCBI_TaxID=319501 {ECO:0000313|EMBL:OBR56080.1};
RN [1] {ECO:0000313|EMBL:OBR56080.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=WF146 {ECO:0000313|EMBL:OBR56080.1};
RA Evans L.H., Alamgir A., Owens N., Weber N.D., Virtaneva K., Barbian K.,
RA Babar A., Rosenke K.;
RL Submitted (APR-2016) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:UYZ15306.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=WF146 {ECO:0000313|EMBL:UYZ15306.1};
RA Tang B., Tang X.-F., Zhu F., Li Y.;
RT "Complete genome sequence of Brevibacillus thermoruber WF146.";
RL Submitted (OCT-2022) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the D-isomer specific 2-hydroxyacid
CC dehydrogenase family. {ECO:0000256|ARBA:ARBA00005854,
CC ECO:0000256|RuleBase:RU003719}.
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DR EMBL; LXGJ01000063; OBR56080.1; -; Genomic_DNA.
DR EMBL; CP109943; UYZ15306.1; -; Genomic_DNA.
DR RefSeq; WP_065066571.1; NZ_LXGJ01000063.1.
DR AlphaFoldDB; A0A1A5XSF7; -.
DR Proteomes; UP000093585; 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; IPR029752; D-isomer_DH_CS1.
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; PS00065; D_2_HYDROXYACID_DH_1; 1.
PE 3: Inferred from homology;
KW Oxidoreductase {ECO:0000256|RuleBase:RU003719};
KW Pyruvate {ECO:0000313|EMBL:OBR56080.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000093585}.
FT DOMAIN 7..318
FT /note="D-isomer specific 2-hydroxyacid dehydrogenase
FT catalytic"
FT /evidence="ECO:0000259|Pfam:PF00389"
FT DOMAIN 108..287
FT /note="D-isomer specific 2-hydroxyacid dehydrogenase NAD-
FT binding"
FT /evidence="ECO:0000259|Pfam:PF02826"
SQ SEQUENCE 320 AA; 35952 MW; D76858D792C78178 CRC64;
MKPYVYVAAP IPAEVEAYLE EHCEYRKWEG DAPIPRGELL REIADAEGLL TVGGRIDSEL
LDHAPKLKVV SNISVGYNNF DLEAMKRRHV MGTNTPHVLD ETVADLAFAL ILSAARRIPE
LDQHVKAGRW ERKHDEWLFG LDVHGKTLGI IGLGRIGEAI ARRAVYGFRM NVLYHNRRRK
PEAEQTLGIT YRSLEDLLRQ SDFVLLMVPL TEETTRMMGR EQFALMKPTA IFINTSRGKT
VDEAALIEAL QEKRIWGAGL DVFEEEPTPP DNPLLRMPNV VTLPHIGSAT RETRLAMAML
AAQNLVAAVH GKRPPNLVTE
//