ID A0A1Y5T9Z6_9PROT Unreviewed; 312 AA.
AC A0A1Y5T9Z6;
DT 30-AUG-2017, integrated into UniProtKB/TrEMBL.
DT 30-AUG-2017, sequence version 1.
DT 27-MAR-2024, entry version 14.
DE SubName: Full=Glyoxylate/hydroxypyruvate reductase B {ECO:0000313|EMBL:SLN58887.1};
DE EC=1.1.1.79 {ECO:0000313|EMBL:SLN58887.1};
GN Name=tkrA {ECO:0000313|EMBL:SLN58887.1};
GN ORFNames=OCH7691_02593 {ECO:0000313|EMBL:SLN58887.1};
OS Oceanibacterium hippocampi.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Sneathiellales;
OC Sneathiellaceae; Oceanibacterium.
OX NCBI_TaxID=745714 {ECO:0000313|EMBL:SLN58887.1, ECO:0000313|Proteomes:UP000193200};
RN [1] {ECO:0000313|EMBL:SLN58887.1, ECO:0000313|Proteomes:UP000193200}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CECT 7691 {ECO:0000313|EMBL:SLN58887.1,
RC ECO:0000313|Proteomes:UP000193200};
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; FWFR01000002; SLN58887.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1Y5T9Z6; -.
DR InParanoid; A0A1Y5T9Z6; -.
DR OrthoDB; 9793626at2; -.
DR Proteomes; UP000193200; 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; cd12156; HPPR; 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; 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.
PE 3: Inferred from homology;
KW Oxidoreductase {ECO:0000256|RuleBase:RU003719,
KW ECO:0000313|EMBL:SLN58887.1}; Pyruvate {ECO:0000313|EMBL:SLN58887.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000193200}.
FT DOMAIN 8..311
FT /note="D-isomer specific 2-hydroxyacid dehydrogenase
FT catalytic"
FT /evidence="ECO:0000259|Pfam:PF00389"
FT DOMAIN 109..281
FT /note="D-isomer specific 2-hydroxyacid dehydrogenase NAD-
FT binding"
FT /evidence="ECO:0000259|Pfam:PF02826"
SQ SEQUENCE 312 AA; 33719 MW; E856F5929A89F4EF CRC64;
MKKPELLLVG PMMPHVMAAM ESDYIVHRLW EAEDREETLD RVAGQIRAIG TGGRSGADAA
LMDRLPNLEI IASFGVGVDT IDVEHAHDRG IIVTNTPDVL NDEVANMALA LLLATTRRLV
AGDRFVREGK WRDGPMPLEH GLRGTRLGIL GLGRIGKDFA RKAGLFGMEI VYNGRREQPD
QPYRFMPDLV EMAAACDHLV VLCPGGPSTD NLVGRAVLDA LGPEGTLINV ARGTVVDEPE
LVAALVEKRL GAAGLDVFAD EPHVPEALLA LDNVVLQPHK ASATIETRHA MGDLVIENLR
AHFAGRRAVT PV
//
