ID A0A225NNU4_9RHOB Unreviewed; 317 AA.
AC A0A225NNU4;
DT 25-OCT-2017, integrated into UniProtKB/TrEMBL.
DT 25-OCT-2017, sequence version 1.
DT 27-MAR-2024, entry version 13.
DE SubName: Full=Glycerate dehydrogenase {ECO:0000313|EMBL:OWU75610.1};
DE EC=1.1.1.29 {ECO:0000313|EMBL:OWU75610.1};
GN ORFNames=ATO3_05135 {ECO:0000313|EMBL:OWU75610.1};
OS Marinibacterium profundimaris.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Paracoccaceae; Marinibacterium.
OX NCBI_TaxID=1679460 {ECO:0000313|EMBL:OWU75610.1, ECO:0000313|Proteomes:UP000215377};
RN [1] {ECO:0000313|EMBL:OWU75610.1, ECO:0000313|Proteomes:UP000215377}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=22II1-22F33 {ECO:0000313|EMBL:OWU75610.1,
RC ECO:0000313|Proteomes:UP000215377};
RA Lai Q., Li G., Shao Z.;
RT "Oceanicola sp. 22II1-22F33 Genome Sequencing.";
RL Submitted (APR-2013) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the D-isomer specific 2-hydroxyacid
CC dehydrogenase family. {ECO:0000256|RuleBase:RU003719}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:OWU75610.1}.
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DR EMBL; AQQR01000002; OWU75610.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A225NNU4; -.
DR OrthoDB; 9793626at2; -.
DR Proteomes; UP000215377; 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; cd12162; 2-Hacid_dh_4; 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; PTHR43761:SF1; 2-HACID_DH DOMAIN-CONTAINING PROTEIN-RELATED; 1.
DR PANTHER; PTHR43761; D-ISOMER SPECIFIC 2-HYDROXYACID DEHYDROGENASE FAMILY PROTEIN (AFU_ORTHOLOGUE AFUA_1G13630); 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:OWU75610.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000215377}.
FT DOMAIN 20..315
FT /note="D-isomer specific 2-hydroxyacid dehydrogenase
FT catalytic"
FT /evidence="ECO:0000259|Pfam:PF00389"
FT DOMAIN 106..286
FT /note="D-isomer specific 2-hydroxyacid dehydrogenase NAD-
FT binding"
FT /evidence="ECO:0000259|Pfam:PF02826"
SQ SEQUENCE 317 AA; 35179 MW; D39CD9B8B097953E CRC64;
MRIVFLDRGS IGPSVELHRP SFEHDWVVYD QTAPDQVAER LADADIAISN KVPIRRDSIE
KCPKLKMIAI PATGYDAFDL EACRERGIVV SNVRGYAINT VPEHTFALIL ALRRSIVGYR
QDVIDGEWQK SGQFCFFNHP IKDLRGSKLG IIGEGVLGQG VADLARAFGM EIMFAAHKGV
DGLGPLYTPW DQVIETADII TLHSPLMPAT KNMIAEPEFR RMKQKPLLVN CSRGGLVHEG
DLVKALDEGW ISGVGFDVLT SEPPAPDNPL LKVLDRPNVI VTPHVAWASE EAMQTLWNQV
RDHLENFERG EPSNVVT
//