CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-010201
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Glyoxylate/hydroxypyruvate reductase A 
Protein Synonyms/Alias
 2-ketoacid reductase 
Gene Name
 ghrA 
Gene Synonyms/Alias
 ycdW; b1033; JW5146 
Created Date
 July 27, 2013 
Organism
 Escherichia coli (strain K12) 
NCBI Taxa ID
 83333 
Lysine Modification
Position
Peptide
Type
References
298RTIAQLEKGERVCGQacetylation[1]
Reference
 [1] Acetyl-Phosphate Is a Critical Determinant of Lysine Acetylation in E. coli.
 Weinert BT, Iesmantavicius V, Wagner SA, Schölz C, Gummesson B, Beli P, Nyström T, Choudhary C.
 Mol Cell. 2013 Jul 25;51(2):265-72. [PMID: 23830618
Functional Description
 Catalyzes the NADPH-dependent reduction of glyoxylate and hydroxypyruvate into glycolate and glycerate, respectively. Inactive towards 2-oxo-D-gluconate, 2-oxoglutarate, oxaloacetate and pyruvate. Only D- and L-glycerate are involved in the oxidative activity with NADP. Activity with NAD is very low. 
Sequence Annotation
 ACT_SITE 227 227 By similarity.
 ACT_SITE 275 275 Proton donor (By similarity).  
Keyword
 Complete proteome; Cytoplasm; Direct protein sequencing; NAD; NADP; Oxidoreductase; Reference proteome. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 312 AA 
Protein Sequence
MDIIFYHPTF DTQWWIEALR KAIPQARVRA WKSGDNDSAD YALVWHPPVE MLAGRDLKAV 60
FALGAGVDSI LSKLQAHPEM LNPSVPLFRL EDTGMGEQMQ EYAVSQVLHW FRRFDDYRIQ 120
QNSSHWQPLP EYHREDFTIG ILGAGVLGSK VAQSLQTWRF PLRCWSRTRK SWPGVQSFAG 180
REELSAFLSQ CRVLINLLPN TPETVGIINQ QLLEKLPDGA YLLNLARGVH VVEDDLLAAL 240
DSGKVKGAML DVFNREPLPP ESPLWQHPRV TITPHVAAIT RPAEAVEYIS RTIAQLEKGE 300
RVCGQVDRAR GY 312 
Gene Ontology
 GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
 GO:0005886; C:plasma membrane; IEA:HAMAP.
 GO:0048037; F:cofactor binding; IEA:InterPro.
 GO:0030267; F:glyoxylate reductase (NADP) activity; IDA:EcoCyc.
 GO:0016618; F:hydroxypyruvate reductase activity; IDA:EcoCyc. 
Interpro
 IPR006140; D-isomer_2_OHA_DH_NAD-bd.
 IPR023514; GhrA.
 IPR016040; NAD(P)-bd_dom. 
Pfam
 PF02826; 2-Hacid_dh_C 
SMART
  
PROSITE
 PS00065; D_2_HYDROXYACID_DH_1
 PS00670; D_2_HYDROXYACID_DH_2
 PS00671; D_2_HYDROXYACID_DH_3 
PRINTS