| Identification |
|---|
| HMDB Protein ID
| HMDBP00396 |
| Secondary Accession Numbers
| |
| Name
| Alanine--glyoxylate aminotransferase 2, mitochondrial |
| Synonyms
|
- (R)-3-amino-2-methylpropionate--pyruvate transaminase
- AGT 2
- Beta-ALAAT II
- Beta-alanine-pyruvate aminotransferase
- D-AIBAT
|
| Gene Name
| AGXT2 |
| Protein Type
| Enzyme |
| Biological Properties |
|---|
| General Function
| Involved in transaminase activity |
| Specific Function
| 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.
|
| Pathways
|
- Alanine, aspartate and glutamate metabolism
- Glycine, serine and threonine metabolism
|
| Reactions
|
| L-Alanine + Glyoxylic acid → Pyruvic acid + Glycine |
details
|
| (R)-beta-Aminoisobutyric acid + Pyruvic acid → 2-Methyl-3-oxopropanoic acid + L-Alanine |
details
|
| Glycine + Oxoglutaric acid → Glyoxylic acid + Glutamic acid |
details
|
|
| GO Classification
|
| Biological Process |
| pyrimidine nucleobase metabolic process |
| positive regulation of nitric oxide biosynthetic process |
| L-alanine catabolic process, by transamination |
| glyoxylate catabolic process |
| glycine biosynthetic process, by transamination of glyoxylate |
| pyrimidine nucleoside catabolic process |
| Cellular Component |
| mitochondrial matrix |
| Function |
| transaminase activity |
| binding |
| pyridoxal phosphate binding |
| cofactor binding |
| transferase activity, transferring nitrogenous groups |
| transferase activity |
| catalytic activity |
| Molecular Function |
| pyridoxal phosphate binding |
| (R)-3-amino-2-methylpropionate-pyruvate transaminase activity |
| alanine-glyoxylate transaminase activity |
|
| Cellular Location
|
- Mitochondrion (Potential)
|
| Gene Properties |
|---|
| Chromosome Location
| 5 |
| Locus
| 5p13 |
| SNPs
| AGXT2 |
| Gene Sequence
|
>1545 bp
ATGACTCTAATCTGGAGACATTTGCTGAGACCCTTGTGCCTGGTCACTTCCGCTCCCAGG
ATCCTTGAGATGCATCCTTTCCTGAGCCTAGGTACTTCCCGGACATCAGTAACCAAGCTC
AGTCTTCATACAAAGCCCAGAATGCCTCCATGTGACTTCATGCCTGAAAGATACCAGTCC
CTTGGCTACAACCGTGTCCTGGAAATCCACAAGGAACATCTTTCTCCTGTGGTGACGGCA
TATTTCCAGAAACCCCTGCTGCTCCACCAGGGGCACATGGAGTGGCTCTTTGATGCTGAA
GGAAGCAGATACCTGGATTTCTTTTCCGGGATTGTTACTGTCAGTGTTGGCCATTGCCAC
CCAAAGGTGAATGCAGTGGCACAAAAGCAGCTCGGCCGCCTGTGGCATACAAGCACCGTC
TTCTTCCACCCTCCAATGCATGAATATGCAGAGAAGCTTGCCGCACTTCTTCCTGAGCCT
CTTAAGGTCATTTTCTTGGTGAACAGTGGCTCAGAAGCCAATGAGCTGGCCATGCTGATG
GCCAGGGCGCACTCAAACAACATAGACATCATTTCTTTCAGAGGAGCCTACCATGGATGC
AGTCCTTACACACTTGGCTTGACAAACGTAGGGACCTACAAGATGGAACTCCCTGGTGGG
ACAGGTTGCCAACCAACAATGTGTCCAGATGTTTTTCGTGGCCCTTGGGGAGGAAGCCAC
TGTCGAGATTCTCCAGTGCAAACAATCAGGAAGTGCAGCTGTGCACCAGACTGCTGCCAA
GCTAAAGATCAGTATATTGAGCAATTCAAAGATACGCTGAGCACATCTGTGGCCAAGTCA
ATTGCTGGATTTTTCGCAGAACCTATTCAAGGTGTGAATGGAGTTGTCCAGTACCCAAAG
GGGTTTCTAAAGGAAGCCTTTGAGCTGGTGCGAGCAAGGGGAGGCGTGTGCATTGCAGAT
GAAGTGCAGACAGGATTTGGAAGGTTGGGCTCTCACTTCTGGGGCTTCCAAACCCACGAT
GTCCTGCCTGACATTGTCACCATGGCTAAAGGGATTGGGAATGGCTTTCCCATGGCAGCA
GTCATAACCACTCCAGAGATTGCCAAATCTTTGGCGAAATGCCTGCAGCACTTCAACACC
TTTGGAGGGAACCCCATGGCCTGTGCCATTGGATCTGCTGTGCTTGAGGTGATTAAAGAA
GAAAATCTACAGGAAAACAGTCAAGAAGTTGGGACCTACATGTTACTAAAGTTTGCTAAG
CTGCGGGATGAATTTGAAATTGTTGGAGACGTCCGAGGCAAAGGTCTCATGATAGGCATA
GAAATGGTGCAGGATAAGATAAGCTGTCGGCCTCTTCCCCGTGAAGAAGTAAATCAGATC
CATGAGGACTGCAAGCACATGGGACTCCTCGTTGGCAGAGGCAGCATTTTTTCTCAGACA
TTTCGCATTGCGCCCTCAATGTGCATCACTAAACCAGAAGTTGATTTTGCAGTAGAAGTA
TTTCGTTCTGCCTTAACCCAACACATGGAAAGAAGAGCTAAGTAA
|
| Protein Properties |
|---|
| Number of Residues
| 514 |
| Molecular Weight
| 57155.905 |
| Theoretical pI
| 7.864 |
| Pfam Domain Function
|
|
| Signals
|
Not Available
|
|
Transmembrane Regions
|
Not Available
|
| Protein Sequence
|
>Alanine--glyoxylate aminotransferase 2, mitochondrial
MTLIWRHLLRPLCLVTSAPRILEMHPFLSLGTSRTSVTKLSLHTKPRMPPCDFMPERYQS
LGYNRVLEIHKEHLSPVVTAYFQKPLLLHQGHMEWLFDAEGSRYLDFFSGIVTVSVGHCH
PKVNAVAQKQLGRLWHTSTVFFHPPMHEYAEKLAALLPEPLKVIFLVNSGSEANELAMLM
ARAHSNNIDIISFRGAYHGCSPYTLGLTNVGTYKMELPGGTGCQPTMCPDVFRGPWGGSH
CRDSPVQTIRKCSCAPDCCQAKDQYIEQFKDTLSTSVAKSIAGFFAEPIQGVNGVVQYPK
GFLKEAFELVRARGGVCIADEVQTGFGRLGSHFWGFQTHDVLPDIVTMAKGIGNGFPMAA
VITTPEIAKSLAKCLQHFNTFGGNPMACAIGSAVLEVIKEENLQENSQEVGTYMLLKFAK
LRDEFEIVGDVRGKGLMIGIEMVQDKISCRPLPREEVNQIHEDCKHMGLLVGRGSIFSQT
FRIAPSMCITKPEVDFAVEVFRSALTQHMERRAK
|
| External Links |
|---|
| GenBank ID Protein
| 12406973 |
| UniProtKB/Swiss-Prot ID
| Q9BYV1 |
| UniProtKB/Swiss-Prot Entry Name
| AGT2_HUMAN |
| PDB IDs
|
Not Available |
| GenBank Gene ID
| AJ292204 |
| GeneCard ID
| AGXT2 |
| GenAtlas ID
| AGXT2 |
| HGNC ID
| HGNC:14412 |
| References |
|---|
| General References
| - Choudhary C, Kumar C, Gnad F, Nielsen ML, Rehman M, Walther TC, Olsen JV, Mann M: Lysine acetylation targets protein complexes and co-regulates major cellular functions. Science. 2009 Aug 14;325(5942):834-40. doi: 10.1126/science.1175371. Epub 2009 Jul 16. [PubMed:19608861 ]
|
