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Database: UniProt
Entry: B9BVZ5_9BURK
LinkDB: B9BVZ5_9BURK
Original site: B9BVZ5_9BURK 
ID   B9BVZ5_9BURK            Unreviewed;       313 AA.
AC   B9BVZ5;
DT   24-MAR-2009, integrated into UniProtKB/TrEMBL.
DT   24-MAR-2009, sequence version 1.
DT   27-MAR-2024, entry version 43.
DE   SubName: Full=Glyoxylate reductase {ECO:0000313|EMBL:EEE05167.1};
DE            EC=1.1.1.79 {ECO:0000313|EMBL:EEE05167.1};
GN   Name=ghrA {ECO:0000313|EMBL:EEE05167.1};
GN   ORFNames=BURMUCGD2_0455 {ECO:0000313|EMBL:EEE05167.1};
OS   Burkholderia multivorans CGD2.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Burkholderia; Burkholderia cepacia complex.
OX   NCBI_TaxID=513052 {ECO:0000313|EMBL:EEE05167.1, ECO:0000313|Proteomes:UP000004535};
RN   [1] {ECO:0000313|EMBL:EEE05167.1, ECO:0000313|Proteomes:UP000004535}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CGD2 {ECO:0000313|EMBL:EEE05167.1,
RC   ECO:0000313|Proteomes:UP000004535};
RX   PubMed=23105085; DOI=10.1128/JB.01306-12;
RA   Varga J.J., Losada L., Zelazny A.M., Brinkac L., Harkins D., Radune D.,
RA   Hostetler J., Sampaio E.P., Ronning C.M., Nierman W.C., Greenberg D.E.,
RA   Holland S.M., Goldberg J.B.;
RT   "Draft Genome Sequence Determination for Cystic Fibrosis and Chronic
RT   Granulomatous Disease Burkholderia multivorans Isolates.";
RL   J. Bacteriol. 194:6356-6357(2012).
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:EEE05167.1}.
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DR   EMBL; ACFC01000011; EEE05167.1; -; Genomic_DNA.
DR   RefSeq; WP_006407140.1; NZ_ACFC01000011.1.
DR   AlphaFoldDB; B9BVZ5; -.
DR   Proteomes; UP000004535; Unassembled WGS sequence.
DR   GO; GO:0030267; F:glyoxylate reductase (NADP+) activity; IEA:UniProtKB-EC.
DR   GO; GO:0051287; F:NAD binding; IEA:InterPro.
DR   CDD; cd12164; GDH_like_2; 1.
DR   Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 2.
DR   InterPro; IPR029753; D-isomer_DH_CS.
DR   InterPro; IPR006140; D-isomer_DH_NAD-bd.
DR   InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR   PANTHER; PTHR43333; 2-HACID_DH_C DOMAIN-CONTAINING PROTEIN; 1.
DR   PANTHER; PTHR43333:SF1; 2-HACID_DH_C DOMAIN-CONTAINING PROTEIN; 1.
DR   Pfam; PF02826; 2-Hacid_dh_C; 1.
DR   SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
DR   PROSITE; PS00671; D_2_HYDROXYACID_DH_3; 1.
PE   4: Predicted;
KW   NAD {ECO:0000256|ARBA:ARBA00023027};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW   ECO:0000313|EMBL:EEE05167.1}.
FT   DOMAIN          107..277
FT                   /note="D-isomer specific 2-hydroxyacid dehydrogenase NAD-
FT                   binding"
FT                   /evidence="ECO:0000259|Pfam:PF02826"
SQ   SEQUENCE   313 AA;  34164 MW;  161790A353029758 CRC64;
     MKILFHSPHQ DAAAWRDAFA RVLPEAELRA WQPGDTAAAD YALVWRAPPA FFAPRDGLRA
     IFNLGAGVDA LLALERTHPG TLPRHVPLVR LEDSGMAQQM IEYVTHAVLR YLRRFDEYDA
     LQRERRWQVL DAHPRASFVV AVLGLGVLGT QVARALAALG LPVRGYSRSP KRIDGIETFA
     GDDALDACLD GAKVLVNLLP STPATDGLLC ARTFARLAPG AYLINVARGA HLVEADLLDA
     LASGRIAAAT LDVFQHEPLP ADHPFWHTPR ITITPHSSAE TLRDEAVEQI AAKIRAFERG
     EPVGGIVDYA RGY
//
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