ID A0A1Y5S0E9_9RHOB Unreviewed; 318 AA.
AC A0A1Y5S0E9;
DT 30-AUG-2017, integrated into UniProtKB/TrEMBL.
DT 30-AUG-2017, sequence version 1.
DT 27-MAR-2024, entry version 16.
DE SubName: Full=Glyoxylate/hydroxypyruvate reductase B {ECO:0000313|EMBL:SLN29605.1};
DE EC=1.1.1.79 {ECO:0000313|EMBL:SLN29605.1};
GN Name=ghrB {ECO:0000313|EMBL:SLN29605.1};
GN ORFNames=PAM7066_01196 {ECO:0000313|EMBL:SLN29605.1};
OS Palleronia marisminoris.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Roseobacteraceae; Palleronia.
OX NCBI_TaxID=315423 {ECO:0000313|EMBL:SLN29605.1, ECO:0000313|Proteomes:UP000193870};
RN [1] {ECO:0000313|EMBL:SLN29605.1, ECO:0000313|Proteomes:UP000193870}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CECT 7066 {ECO:0000313|EMBL:SLN29605.1,
RC ECO:0000313|Proteomes:UP000193870};
RA Afonso C.L., Miller P.J., Scott M.A., Spackman E., Goraichik I.,
RA Dimitrov K.M., Suarez D.L., Swayne D.E.;
RL Submitted (MAR-2017) 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; FWFV01000002; SLN29605.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1Y5S0E9; -.
DR STRING; 315423.SAMN04488020_10284; -.
DR OrthoDB; 7374922at2; -.
DR Proteomes; UP000193870; Unassembled WGS sequence.
DR GO; GO:0030267; F:glyoxylate reductase (NADP+) activity; IEA:UniProtKB-EC.
DR GO; GO:0051287; F:NAD binding; IEA:InterPro.
DR CDD; cd12175; 2-Hacid_dh_11; 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; 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; PS00670; D_2_HYDROXYACID_DH_2; 1.
PE 3: Inferred from homology;
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000256|RuleBase:RU003719}; Pyruvate {ECO:0000313|EMBL:SLN29605.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000193870}.
FT DOMAIN 6..309
FT /note="D-isomer specific 2-hydroxyacid dehydrogenase
FT catalytic"
FT /evidence="ECO:0000259|Pfam:PF00389"
FT DOMAIN 109..283
FT /note="D-isomer specific 2-hydroxyacid dehydrogenase NAD-
FT binding"
FT /evidence="ECO:0000259|Pfam:PF02826"
SQ SEQUENCE 318 AA; 33454 MW; A6B641B289661AA3 CRC64;
MSGPVVAVLE PASDEMRARM ETLCPDFDLR FAASGDPADF AEALGEARYA VTRGLRFPAA
ALDDAPKLEL IHQWGTGTDG IPIEAARLRG ITIARSPGVN APTVAEATVA LMLATLRRLP
QVHASLRSGQ WEQPDLWREA RDLGSLTVGL VGMGAIGTEV AKRLDGFGCA VIYTRASGPM
ADCALRFAPL DALVAECDVI SLHLPLTDTT RAMIDADALA SMKQGAVLIN TSRGGLVHEA
ALVAALVSGH LSGAGLDVFS SEPVSADNPL LSMPQVVTLP HVAGRTLDNF DRMVSHWADN
IRAHAAGRQI APECLVSA
//
