ID A0A0U1NMM4_9RHOB Unreviewed; 328 AA.
AC A0A0U1NMM4;
DT 17-FEB-2016, integrated into UniProtKB/TrEMBL.
DT 17-FEB-2016, sequence version 1.
DT 27-MAR-2024, entry version 23.
DE SubName: Full=Glycerate dehydrogenase {ECO:0000313|EMBL:CRK75974.1};
DE EC=1.1.1.29 {ECO:0000313|EMBL:CRK75974.1};
GN ORFNames=NIG5292_02031 {ECO:0000313|EMBL:CRK75974.1};
OS Nereida ignava.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Roseobacteraceae; Nereida.
OX NCBI_TaxID=282199 {ECO:0000313|EMBL:CRK75974.1, ECO:0000313|Proteomes:UP000048949};
RN [1] {ECO:0000313|EMBL:CRK75974.1, ECO:0000313|Proteomes:UP000048949}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CECT 5292 {ECO:0000313|EMBL:CRK75974.1,
RC ECO:0000313|Proteomes:UP000048949};
RA Syromyatnikov M.Y., Popov V.N.;
RL Submitted (APR-2015) 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; CVQV01000011; CRK75974.1; -; Genomic_DNA.
DR RefSeq; WP_048599397.1; NZ_CVQV01000011.1.
DR AlphaFoldDB; A0A0U1NMM4; -.
DR STRING; 282199.GCA_001049735_02030; -.
DR OrthoDB; 9793626at2; -.
DR Proteomes; UP000048949; Unassembled WGS sequence.
DR GO; GO:0008465; F:glycerate dehydrogenase activity; IEA:UniProtKB-EC.
DR GO; GO:0051287; F:NAD binding; 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; IPR029753; D-isomer_DH_CS.
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.
DR PROSITE; PS00671; D_2_HYDROXYACID_DH_3; 1.
PE 3: Inferred from homology;
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000256|RuleBase:RU003719};
KW Reference proteome {ECO:0000313|Proteomes:UP000048949}.
FT DOMAIN 8..323
FT /note="D-isomer specific 2-hydroxyacid dehydrogenase
FT catalytic"
FT /evidence="ECO:0000259|Pfam:PF00389"
FT DOMAIN 113..292
FT /note="D-isomer specific 2-hydroxyacid dehydrogenase NAD-
FT binding"
FT /evidence="ECO:0000259|Pfam:PF02826"
SQ SEQUENCE 328 AA; 35556 MW; D81B27B879D5DA9B CRC64;
MSRKRLSVVV TRRLPAAVEH RMAELFDVTV RDSDAPMSRD ELIAAMQEVD VLVPTVNDRL
DAAVFEQAGE RLKLVANYGA GTDHIDVNAA HANGIMVSNT PGVGAEDTAD MTLALMLSVT
RRIPEGLSVM QTGDWDGWSP TALLGGKIGG RSLGILGMGR IGQAVARRAR AFGMQVHYHN
RNRLRPETEA DLGAKYWSSL NQMLAQVDIL TIHCPHTPST YHIMNARRLA LMKPSAVIVN
TSRGDVIDEN ALTRMLRSGE IAGAGLDVYE GGAEPNPRLR ALKNVVLLPH MASATVEGRE
EMGARVMLNI STHADGFRPP DMVIPSSL
//
