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Database: UniProt
Entry: A0A1N7RKK8_9BURK
LinkDB: A0A1N7RKK8_9BURK
Original site: A0A1N7RKK8_9BURK 
ID   A0A1N7RKK8_9BURK        Unreviewed;       358 AA.
AC   A0A1N7RKK8;
DT   15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT   15-MAR-2017, sequence version 1.
DT   27-MAR-2024, entry version 14.
DE   SubName: Full=Phosphoglycerate dehydrogenase-like oxidoreductase {ECO:0000313|EMBL:SIT35227.1};
GN   ORFNames=BN2476_20085 {ECO:0000313|EMBL:SIT35227.1};
OS   Paraburkholderia piptadeniae.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Paraburkholderia.
OX   NCBI_TaxID=1701573 {ECO:0000313|EMBL:SIT35227.1, ECO:0000313|Proteomes:UP000195569};
RN   [1] {ECO:0000313|EMBL:SIT35227.1, ECO:0000313|Proteomes:UP000195569}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=STM 7183 {ECO:0000313|EMBL:SIT35227.1,
RC   ECO:0000313|Proteomes:UP000195569};
RA   Song W.-J., Kurnit D.M.;
RL   Submitted (DEC-2016) 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; CYGY02000002; SIT35227.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1N7RKK8; -.
DR   Proteomes; UP000195569; 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; 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}.
FT   DOMAIN          39..343
FT                   /note="D-isomer specific 2-hydroxyacid dehydrogenase
FT                   catalytic"
FT                   /evidence="ECO:0000259|Pfam:PF00389"
FT   DOMAIN          132..317
FT                   /note="D-isomer specific 2-hydroxyacid dehydrogenase NAD-
FT                   binding"
FT                   /evidence="ECO:0000259|Pfam:PF02826"
SQ   SEQUENCE   358 AA;  39497 MW;  9E6E513A9FEDB3A0 CRC64;
     MGHPNRYSVP HPRGAPQNTY AMKIAILDDY QDAVRKLDCF QLLADHEVKV FNNTVRGLGQ
     LASRLSEVDA LVLIRERTRI SSQLLDKLPH LRMISQTGKA GSHIDMPACT ERGIAVLEGV
     GSPIAPAELT WALIMAAQRR IPQYVANLKQ GAWQQSGLKT SALPPNFGLG QVLRGQTLGI
     WGYGKIGRLV AGYGKAFGMN VLIWGREHTR EAAVADGYAV VESREALFEQ SDVLSLHLRL
     HDDTRGIVKQ DDLLRMKPTA LFVNTSRAEL LEENALIGAL SHNRPGMVAI DVYESEPILQ
     GYSLLRMENV ICSPHIGYVE KESYELYFGA AFRNILAFDQ GDTSSVANPE ALQGGRRK
//
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