ID A0A2U8FRY3_9BURK Unreviewed; 335 AA.
AC A0A2U8FRY3;
DT 12-SEP-2018, integrated into UniProtKB/TrEMBL.
DT 12-SEP-2018, sequence version 1.
DT 27-MAR-2024, entry version 15.
DE SubName: Full=3-phosphoglycerate dehydrogenase {ECO:0000313|EMBL:AWI53637.1};
GN ORFNames=DEH84_09475 {ECO:0000313|EMBL:AWI53637.1};
OS Aquabacterium olei.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Aquabacterium.
OX NCBI_TaxID=1296669 {ECO:0000313|EMBL:AWI53637.1, ECO:0000313|Proteomes:UP000244892};
RN [1] {ECO:0000313|EMBL:AWI53637.1, ECO:0000313|Proteomes:UP000244892}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NBRC 110486 {ECO:0000313|EMBL:AWI53637.1,
RC ECO:0000313|Proteomes:UP000244892};
RA Tang B., Chang J., Zhang L., Yang H.;
RT "complete genome sequence of Aquabacterium olei NBRC 110486.";
RL Submitted (MAY-2018) 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; CP029210; AWI53637.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2U8FRY3; -.
DR KEGG; aon:DEH84_09475; -.
DR OrthoDB; 9805416at2; -.
DR Proteomes; UP000244892; 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; cd12169; PGDH_like_1; 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; PTHR42789; D-ISOMER SPECIFIC 2-HYDROXYACID DEHYDROGENASE FAMILY PROTEIN (AFU_ORTHOLOGUE AFUA_6G10090); 1.
DR PANTHER; PTHR42789:SF1; D-ISOMER SPECIFIC 2-HYDROXYACID DEHYDROGENASE FAMILY PROTEIN (AFU_ORTHOLOGUE AFUA_6G10090); 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 NAD {ECO:0000256|ARBA:ARBA00023027};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000256|RuleBase:RU003719};
KW Reference proteome {ECO:0000313|Proteomes:UP000244892}.
FT DOMAIN 39..327
FT /note="D-isomer specific 2-hydroxyacid dehydrogenase
FT catalytic"
FT /evidence="ECO:0000259|Pfam:PF00389"
FT DOMAIN 111..296
FT /note="D-isomer specific 2-hydroxyacid dehydrogenase NAD-
FT binding"
FT /evidence="ECO:0000259|Pfam:PF02826"
SQ SEQUENCE 335 AA; 36730 MW; E5143858CEF83BD6 CRC64;
MNITILDDYQ DAVRKLKCAS RLDGLSAKVY TNSVKGIGQL SVRLRDVEAL VLIRERTHFP
RALLEKLPKL RLICQTGPVG GHIDVEACTR LGIAVAEGVG DPTAPAELTW ALVMSAMRRL
PQYIGNLKHG AWQQSGLKSA SMPTNFGLGM VLAGKTLGIW GYGRIGKRVA QYGRAFGMHV
TIWGSEASRA QAQADGFIPA PTREAFFEAS DVLSLHLRLT PQTRGLITQD DLHRMKPTAL
LVNTSRAELL QDNALVTALN RGRPGMAAVD VFESEPILQG HPLLRLENAV CTPHIGYVEL
DNYERYFSAA FDNLLNFIAG TPTHIVNPEA LRVHH
//
