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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
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
//