CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-008762
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Glyoxylate reductase 1 
Protein Synonyms/Alias
  
Gene Name
 GOR1 
Gene Synonyms/Alias
 YNL274C; N0631 
Created Date
 July 27, 2013 
Organism
 Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) 
NCBI Taxa ID
 559292 
Lysine Modification
Position
Peptide
Type
References
183RCILERLKPFGFENFacetylation[1]
Reference
 [1] Proteome-wide analysis of lysine acetylation suggests its broad regulatory scope in Saccharomyces cerevisiae.
 Henriksen P, Wagner SA, Weinert BT, Sharma S, Bacinskaja G, Rehman M, Juffer AH, Walther TC, Lisby M, Choudhary C.
 Mol Cell Proteomics. 2012 Nov;11(11):1510-22. [PMID: 22865919
Functional Description
 Reversibly reduces glyoxylate to glycolate. 
Sequence Annotation
 NP_BIND 173 174 NAD (By similarity).
 NP_BIND 252 254 NAD (By similarity).
 NP_BIND 301 304 NAD (By similarity).
 ACT_SITE 254 254 By similarity.
 ACT_SITE 283 283 By similarity.
 ACT_SITE 301 301 Proton donor (By similarity).
 BINDING 278 278 NAD (By similarity).
 MOD_RES 31 31 Phosphothreonine.  
Keyword
 Complete proteome; Cytoplasm; Mitochondrion; NAD; Nucleus; Oxidoreductase; Phosphoprotein; Reference proteome. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 350 AA 
Protein Sequence
MSKKPIVLKL GKDAFGDQAW GELEKIADVI TIPESTTREQ FLREVKDPQN KLSQVQVITR 60
TARSVKNTGR FDEELALALP SSVVAVCHTG AGYDQIDVEP FKKRHIQVAN VPDLVSNATA 120
DTHVFLLLGA LRNFGIGNRR LIEGNWPEAG PACGSPFGYD PEGKTVGILG LGRIGRCILE 180
RLKPFGFENF IYHNRHQLPS EEEHGCEYVG FEEFLKRSDI VSVNVPLNHN THHLINAETI 240
EKMKDGVVIV NTARGAVIDE QAMTDALRSG KIRSAGLDVF EYEPKISKEL LSMSQVLGLP 300
HMGTHSVETR KKMEELVVEN AKNVILTGKV LTIVPELQNE DWPNESKPLV 350 
Gene Ontology
 GO:0005739; C:mitochondrion; IDA:SGD.
 GO:0005634; C:nucleus; IDA:SGD.
 GO:0047964; F:glyoxylate reductase activity; IMP:SGD.
 GO:0051287; F:NAD binding; IEA:InterPro.
 GO:0009436; P:glyoxylate catabolic process; IMP:SGD. 
Interpro
 IPR006139; D-isomer_2_OHA_DH_cat_dom.
 IPR006140; D-isomer_2_OHA_DH_NAD-bd.
 IPR016040; NAD(P)-bd_dom. 
Pfam
 PF00389; 2-Hacid_dh
 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