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Database: UniProt
Entry: A4JJ28_BURVG
LinkDB: A4JJ28_BURVG
Original site: A4JJ28_BURVG 
ID   A4JJ28_BURVG            Unreviewed;       337 AA.
AC   A4JJ28;
DT   01-MAY-2007, integrated into UniProtKB/TrEMBL.
DT   01-MAY-2007, sequence version 1.
DT   27-MAR-2024, entry version 97.
DE   SubName: Full=D-isomer specific 2-hydroxyacid dehydrogenase, NAD-binding protein {ECO:0000313|EMBL:ABO56281.1};
GN   OrderedLocusNames=Bcep1808_3291 {ECO:0000313|EMBL:ABO56281.1};
OS   Burkholderia vietnamiensis (strain G4 / LMG 22486) (Burkholderia cepacia
OS   (strain R1808)).
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Burkholderia; Burkholderia cepacia complex.
OX   NCBI_TaxID=269482 {ECO:0000313|EMBL:ABO56281.1, ECO:0000313|Proteomes:UP000002287};
RN   [1] {ECO:0000313|Proteomes:UP000002287}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=G4 / LMG 22486 {ECO:0000313|Proteomes:UP000002287};
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA   Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA   Chain P., Malfatti S., Shin M., Vergez L., Schmutz J., Larimer F., Land M.,
RA   Hauser L., Kyrpides N., Tiedje J., Richardson P.;
RT   "Complete sequence of chromosome 1 of Burkholderia vietnamiensis G4.";
RL   Submitted (MAR-2007) 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; CP000614; ABO56281.1; -; Genomic_DNA.
DR   AlphaFoldDB; A4JJ28; -.
DR   KEGG; bvi:Bcep1808_3291; -.
DR   eggNOG; COG0111; Bacteria.
DR   HOGENOM; CLU_019796_1_3_4; -.
DR   Proteomes; UP000002287; Chromosome 1.
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:UP000002287}.
FT   DOMAIN          20..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   337 AA;  37278 MW;  BB97BD57A8415DC3 CRC64;
     MKIAILDDYQ DAVRKLNCFE MLAEHDVKVF NNTVRGLGQL ASRLAEVEAL VLIRERTPIS
     SQLLAKLPNL RMISQTGRIS SHIDLEACTD RGIAVLEGTG SPVAPAELTW ALVMAAQRRI
     PQYVANLKQG AWQQSGLKTS ALPPNFGLGQ VLRGQTLGIW GYGKIGRLVA GYGKAFGMNV
     LIWGREHSLE AARADGYTAA DSREALFKQS DVLSLHLRLH DDTRGIVKQE DLLRMKPTSL
     LVNTSRAELL EENALVNALS HNRPGMVAID VFESEPILQG YSLLRMENVI CTPHIGYVER
     ESYELYFSAA FRNILAFDQG DLSSVVNPEA LTPRRAR
//
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