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Database: UniProt
Entry: A0A328YCJ5_9BURK
LinkDB: A0A328YCJ5_9BURK
Original site: A0A328YCJ5_9BURK 
ID   A0A328YCJ5_9BURK        Unreviewed;       334 AA.
AC   A0A328YCJ5;
DT   10-OCT-2018, integrated into UniProtKB/TrEMBL.
DT   10-OCT-2018, sequence version 1.
DT   27-MAR-2024, entry version 12.
DE   SubName: Full=D-3-phosphoglycerate dehydrogenase {ECO:0000313|EMBL:RAR71649.1};
GN   ORFNames=AX018_10849 {ECO:0000313|EMBL:RAR71649.1};
OS   Paracidovorax anthurii.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Comamonadaceae; Paracidovorax.
OX   NCBI_TaxID=78229 {ECO:0000313|EMBL:RAR71649.1, ECO:0000313|Proteomes:UP000248856};
RN   [1] {ECO:0000313|EMBL:RAR71649.1, ECO:0000313|Proteomes:UP000248856}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CFPB 3232 {ECO:0000313|EMBL:RAR71649.1,
RC   ECO:0000313|Proteomes:UP000248856};
RA   Goeker M.;
RT   "Genomic Encyclopedia of Archaeal and Bacterial Type Strains, Phase II
RT   (KMG-II): from individual species to whole genera.";
RL   Submitted (JUN-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}.
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:RAR71649.1}.
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DR   EMBL; QLTA01000084; RAR71649.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A328YCJ5; -.
DR   OrthoDB; 9805416at2; -.
DR   Proteomes; UP000248856; Unassembled WGS sequence.
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; cd12173; PGDH_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; 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:UP000248856}.
FT   DOMAIN          29..325
FT                   /note="D-isomer specific 2-hydroxyacid dehydrogenase
FT                   catalytic"
FT                   /evidence="ECO:0000259|Pfam:PF00389"
FT   DOMAIN          127..298
FT                   /note="D-isomer specific 2-hydroxyacid dehydrogenase NAD-
FT                   binding"
FT                   /evidence="ECO:0000259|Pfam:PF02826"
SQ   SEQUENCE   334 AA;  34672 MW;  38D3442509F64BC1 CRC64;
     MNASPDPTHH EAPTPPAPFD VLVTAAHWAE AAQDMVREAG GRVHCMAGPV TEDALAEQLA
     ATGAQALVLR GSPPVTERVL AAAPALRIVA KNGAGVDSVD REAARRRGVA VAVAPGANAD
     AVAEHALALM LALTRQLPEL DRRVRAGGWA GSQWQGRDFR GSTVGIVGYG SIGRATARLA
     AALGAQVLVL RPPGQADGFA TEPDLDRLLA RVDILSLHCP LTERTRGLIG ARELGLMRPG
     SLLVNTARGP VVQEDALIAA LHGGQLAGAG LDTFDTEPLP ERHPLAKLPQ VLLTPHVAGV
     TRDAALRVAT LTARNILDHL RGRALPAGHL LADG
//
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