Alanine--glyoxylate aminotransferase 2, mitochondrial

NameAlanine--glyoxylate aminotransferase 2, mitochondrial
Synonyms
  • (R)-3-amino-2-methylpropionate--pyruvate transaminase
  • 2.6.1.44
  • AGT 2
  • AGT2
  • Beta-ALAAT II
  • Beta-alanine-pyruvate aminotransferase
  • D-AIBAT
Gene NameAGXT2
OrganismHuman
Amino acid sequence
>lcl|BSEQ0000204|Alanine--glyoxylate aminotransferase 2, mitochondrial
MTLIWRHLLRPLCLVTSAPRILEMHPFLSLGTSRTSVTKLSLHTKPRMPPCDFMPERYQS
LGYNRVLEIHKEHLSPVVTAYFQKPLLLHQGHMEWLFDAEGSRYLDFFSGIVTVSVGHCH
PKVNAVAQKQLGRLWHTSTVFFHPPMHEYAEKLAALLPEPLKVIFLVNSGSEANELAMLM
ARAHSNNIDIISFRGAYHGCSPYTLGLTNVGTYKMELPGGTGCQPTMCPDVFRGPWGGSH
CRDSPVQTIRKCSCAPDCCQAKDQYIEQFKDTLSTSVAKSIAGFFAEPIQGVNGVVQYPK
GFLKEAFELVRARGGVCIADEVQTGFGRLGSHFWGFQTHDVLPDIVTMAKGIGNGFPMAA
VITTPEIAKSLAKCLQHFNTFGGNPMACAIGSAVLEVIKEENLQENSQEVGTYMLLKFAK
LRDEFEIVGDVRGKGLMIGIEMVQDKISCRPLPREEVNQIHEDCKHMGLLVGRGSIFSQT
FRIAPSMCITKPEVDFAVEVFRSALTQHMERRAK
Number of residues514
Molecular Weight57155.905
Theoretical pI7.91
GO Classification
Functions
  • (R)-3-amino-2-methylpropionate-pyruvate transaminase activity
  • pyridoxal phosphate binding
  • beta-alanine-pyruvate transaminase activity
  • identical protein binding
  • alanine-glyoxylate transaminase activity
Processes
  • glyoxylate catabolic process
  • pyrimidine nucleobase metabolic process
  • positive regulation of nitric oxide biosynthetic process
  • pyrimidine nucleoside catabolic process
  • L-alanine catabolic process, by transamination
  • cellular nitrogen compound metabolic process
  • small molecule metabolic process
  • glyoxylate metabolic process
  • nucleobase-containing small molecule metabolic process
  • glycine biosynthetic process, by transamination of glyoxylate
Components
  • mitochondrion
  • mitochondrial matrix
General FunctionPyridoxal phosphate binding
Specific FunctionCan 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.
Pfam Domain Function
Transmembrane RegionsNot Available
GenBank Protein ID12406973
UniProtKB IDQ9BYV1
UniProtKB Entry NameAGT2_HUMAN
Cellular LocationMitochondrion
Gene sequence
>lcl|BSEQ0016012|Alanine--glyoxylate aminotransferase 2, mitochondrial (AGXT2)
ATGACTCTAATCTGGAGACATTTGCTGAGACCCTTGTGCCTGGTCACTTCCGCTCCCAGG
ATCCTTGAGATGCATCCTTTCCTGAGCCTAGGTACTTCCCGGACATCAGTAACCAAGCTC
AGTCTTCATACAAAGCCCAGAATGCCTCCATGTGACTTCATGCCTGAAAGATACCAGTCC
CTTGGCTACAACCGTGTCCTGGAAATCCACAAGGAACATCTTTCTCCTGTGGTGACGGCA
TATTTCCAGAAACCCCTGCTGCTCCACCAGGGGCACATGGAGTGGCTCTTTGATGCTGAA
GGAAGCAGATACCTGGATTTCTTTTCCGGGATTGTTACTGTCAGTGTTGGCCATTGCCAC
CCAAAGGTGAATGCAGTGGCACAAAAGCAGCTCGGCCGCCTGTGGCATACAAGCACCGTC
TTCTTCCACCCTCCAATGCATGAATATGCAGAGAAGCTTGCCGCACTTCTTCCTGAGCCT
CTTAAGGTCATTTTCTTGGTGAACAGTGGCTCAGAAGCCAATGAGCTGGCCATGCTGATG
GCCAGGGCGCACTCAAACAACATAGACATCATTTCTTTCAGAGGAGCCTACCATGGATGC
AGTCCTTACACACTTGGCTTGACAAACGTAGGGACCTACAAGATGGAACTCCCTGGTGGG
ACAGGTTGCCAACCAACAATGTGTCCAGATGTTTTTCGTGGCCCTTGGGGAGGAAGCCAC
TGTCGAGATTCTCCAGTGCAAACAATCAGGAAGTGCAGCTGTGCACCAGACTGCTGCCAA
GCTAAAGATCAGTATATTGAGCAATTCAAAGATACGCTGAGCACATCTGTGGCCAAGTCA
ATTGCTGGATTTTTCGCAGAACCTATTCAAGGTGTGAATGGAGTTGTCCAGTACCCAAAG
GGGTTTCTAAAGGAAGCCTTTGAGCTGGTGCGAGCAAGGGGAGGCGTGTGCATTGCAGAT
GAAGTGATTAAAGAAGAAAATCTACAGGAAAACAGTCAAGAAGTTGGGACCTACATGTTA
CTAAAGTTTGCTAAGCTGCGGGATGAATTTGAAATTGTTGGAGACGTCCGAGGCAAAGGT
CTCATGATAGGCATAGAAATGGTGCAGGATAAGATAAGCTGTCGGCCTCTTCCCCGTGAA
GAAGTAAATCAGATCCATGAGGACTGCAAGCACATGGGACTCCTCGTTGGCAGAGGCAGC
ATTTTTTCTCAGACATTTCGCATTGCGCCCTCAATGTGCATCACTAAACCAGAAGTTGAT
TTTGCAGTAGAAGTATTTCGTTCTGCCTTAACCCAACACATGGAAAGAAGAGCTAAGTAA
GenBank Gene IDAJ292204
GeneCard IDNot Available
GenAtlas IDAGXT2
HGNC IDHGNC:14412
Chromosome Location5
Locus5p13
References
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  3. Rodionov RN, Murry DJ, Vaulman SF, Stevens JW, Lentz SR: Human alanine-glyoxylate aminotransferase 2 lowers asymmetric dimethylarginine and protects from inhibition of nitric oxide production. J Biol Chem. 2010 Feb 19;285(8):5385-91. doi: 10.1074/jbc.M109.091280. Epub 2009 Dec 14. 20018850
  4. Caplin B, Wang Z, Slaviero A, Tomlinson J, Dowsett L, Delahaye M, Salama A, Wheeler DC, Leiper J: Alanine-glyoxylate aminotransferase-2 metabolizes endogenous methylarginines, regulates NO, and controls blood pressure. Arterioscler Thromb Vasc Biol. 2012 Dec;32(12):2892-900. doi: 10.1161/ATVBAHA.112.254078. Epub 2012 Sep 27. 23023372
  5. Bian Y, Song C, Cheng K, Dong M, Wang F, Huang J, Sun D, Wang L, Ye M, Zou H: An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome. J Proteomics. 2014 Jan 16;96:253-62. doi: 10.1016/j.jprot.2013.11.014. Epub 2013 Nov 22. 24275569
  6. Zhou JP, Bai YP, Hu XL, Kuang DB, Shi RZ, Xiong Y, Zhang W, Xia J, Chen BL, Yang TL, Chen XP: Association of the AGXT2 V140I polymorphism with risk for coronary heart disease in a Chinese population. J Atheroscler Thromb. 2014;21(10):1022-30. Epub 2014 May 16. 24834905
  7. Kittel A, Muller F, Konig J, Mieth M, Sticht H, Zolk O, Kralj A, Heinrich MR, Fromm MF, Maas R: Alanine-glyoxylate aminotransferase 2 (AGXT2) polymorphisms have considerable impact on methylarginine and beta-aminoisobutyrate metabolism in healthy volunteers. PLoS One. 2014 Feb 24;9(2):e88544. doi: 10.1371/journal.pone.0088544. eCollection 2014. 24586340