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
    alanine-glyoxylate transaminase activity
pyridoxal phosphate binding
(R)-3-amino-2-methylpropionate-pyruvate transaminase activity
beta-alanine-pyruvate transaminase activity
identical protein binding
Processes
    glycine biosynthetic process, by transamination of glyoxylate
glyoxylate catabolic process
pyrimidine nucleobase metabolic process
positive regulation of nitric oxide biosynthetic process
pyrimidine nucleoside catabolic process
cellular nitrogen compound metabolic process
small molecule metabolic process
L-alanine catabolic process, by transamination
glyoxylate metabolic process
nucleobase-containing small molecule metabolic process
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.
Transmembrane Regions
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 IDNone
GenAtlas IDAGXT2
HGNC IDHGNC:14412
Chromosome Location5
Locus5p13
References
  1. Schmutz J, Martin J, Terry A, Couronne O, Grimwood J, Lowry S, Gordon LA, Scott D, Xie G, Huang W, Hellsten U, Tran-Gyamfi M, She X, Prabhakar S, Aerts A, Altherr M, Bajorek E, Black S, Branscomb E, Caoile C, Challacombe JF, Chan YM, Denys M, Detter JC, Escobar J, Flowers D, Fotopulos D, Glavina T, Gomez M, Gonzales E, Goodstein D, Grigoriev I, Groza M, Hammon N, Hawkins T, Haydu L, Israni S, Jett J, Kadner K, Kimball H, Kobayashi A, Lopez F, Lou Y, Martinez D, Medina C, Morgan J, Nandkeshwar R, Noonan JP, Pitluck S, Pollard M, Predki P, Priest J, Ramirez L, Retterer J, Rodriguez A, Rogers S, Salamov A, Salazar A, Thayer N, Tice H, Tsai M, Ustaszewska A, Vo N, Wheeler J, Wu K, Yang J, Dickson M, Cheng JF, Eichler EE, Olsen A, Pennacchio LA, Rokhsar DS, Richardson P, Lucas SM, Myers RM, Rubin EM: The DNA sequence and comparative analysis of human chromosome 5. Nature. 2004 Sep 16;431(7006):268-74.[15372022 ]
  2. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7.[15489334 ]
  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 ]

Related FRC

FRCD ID Name Exact Mass Structure




F05337



Glycine


75.067




F05339



L-Alanine


89.094