CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-020382
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Alanine--glyoxylate aminotransferase 2, mitochondrial 
Protein Synonyms/Alias
 AGT 2; (R)-3-amino-2-methylpropionate--pyruvate transaminase; Beta-ALAAT II; Beta-alanine-pyruvate aminotransferase; D-AIBAT 
Gene Name
 AGXT2 
Gene Synonyms/Alias
 AGT2 
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
129KVNAVAQKQLGRLWHacetylation[1]
270DQYIEQFKDTLSTSVacetylation[2]
Reference
 [1] Lysine acetylation targets protein complexes and co-regulates major cellular functions.
 Choudhary C, Kumar C, Gnad F, Nielsen ML, Rehman M, Walther TC, Olsen JV, Mann M.
 Science. 2009 Aug 14;325(5942):834-40. [PMID: 19608861]
 [2] Regulation of cellular metabolism by protein lysine acetylation.
 Zhao S, Xu W, Jiang W, Yu W, Lin Y, Zhang T, Yao J, Zhou L, Zeng Y, Li H, Li Y, Shi J, An W, Hancock SM, He F, Qin L, Chin J, Yang P, Chen X, Lei Q, Xiong Y, Guan KL.
 Science. 2010 Feb 19;327(5968):1000-4. [PMID: 20167786
Functional Description
 Can metabolize asymmetric dimethylarginine (ADMA) via transamination to alpha-keto-delta-(NN-dimethylguanidino) valeric acid (DMGV). ADMA is a potent inhibitor of nitric-oxide (NO) synthase, and this activity provides mechanism through which the kidney regulates blood pressure. 
Sequence Annotation
 MOD_RES 350 350 N6-(pyridoxal phosphate)lysine (By  
Keyword
 Aminotransferase; Complete proteome; Direct protein sequencing; Mitochondrion; Polymorphism; Pyridoxal phosphate; Reference proteome; Transferase; Transit peptide. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 514 AA 
Protein Sequence
MTLIWRHLLR PLCLVTSAPR ILEMHPFLSL GTSRTSVTKL SLHTKPRMPP CDFMPERYQS 60
LGYNRVLEIH KEHLSPVVTA YFQKPLLLHQ GHMEWLFDAE GSRYLDFFSG IVTVSVGHCH 120
PKVNAVAQKQ LGRLWHTSTV FFHPPMHEYA EKLAALLPEP LKVIFLVNSG SEANELAMLM 180
ARAHSNNIDI ISFRGAYHGC SPYTLGLTNV GTYKMELPGG TGCQPTMCPD VFRGPWGGSH 240
CRDSPVQTIR KCSCAPDCCQ AKDQYIEQFK DTLSTSVAKS IAGFFAEPIQ GVNGVVQYPK 300
GFLKEAFELV RARGGVCIAD EVQTGFGRLG SHFWGFQTHD VLPDIVTMAK GIGNGFPMAA 360
VITTPEIAKS LAKCLQHFNT FGGNPMACAI GSAVLEVIKE ENLQENSQEV GTYMLLKFAK 420
LRDEFEIVGD VRGKGLMIGI EMVQDKISCR PLPREEVNQI HEDCKHMGLL VGRGSIFSQT 480
FRIAPSMCIT KPEVDFAVEV FRSALTQHME RRAK 514 
Gene Ontology
 GO:0005759; C:mitochondrial matrix; TAS:Reactome.
 GO:0047305; F:(R)-3-amino-2-methylpropionate-pyruvate transaminase activity; IEA:EC.
 GO:0008453; F:alanine-glyoxylate transaminase activity; IDA:BHF-UCL.
 GO:0016223; F:beta-alanine-pyruvate transaminase activity; IEA:Compara.
 GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
 GO:0019265; P:glycine biosynthetic process, by transamination of glyoxylate; IDA:BHF-UCL.
 GO:0009436; P:glyoxylate catabolic process; IDA:BHF-UCL.
 GO:0019481; P:L-alanine catabolic process, by transamination; IDA:BHF-UCL.
 GO:0045429; P:positive regulation of nitric oxide biosynthetic process; IDA:BHF-UCL.
 GO:0006206; P:pyrimidine nucleobase metabolic process; TAS:Reactome.
 GO:0046135; P:pyrimidine nucleoside catabolic process; TAS:Reactome. 
Interpro
 IPR005814; Aminotrans_3.
 IPR015424; PyrdxlP-dep_Trfase.
 IPR015421; PyrdxlP-dep_Trfase_major_sub1.
 IPR015422; PyrdxlP-dep_Trfase_major_sub2. 
Pfam
 PF00202; Aminotran_3 
SMART
  
PROSITE
 PS00600; AA_TRANSFER_CLASS_3 
PRINTS