Overview
| Uniprot ID | Q9BYV1 |
|---|
| Protein Name | Alanine--glyoxylate aminotransferase 2, mitochondrial |
|---|
| Gene Name | AGXT2 |
|---|
| Organism | Homo sapiens |
|---|
Kla Sites from experimental identification
| Position |
Flanking peptide |
| 129 |
KVNAVAQKQLGRLWH |
Function
Multifunctional aminotransferase with a broad substrate specificity (PubMed:20018850, PubMed:23023372, PubMed:24586340). Catalyzes the conversion of glyoxylate to glycine using alanine as the amino donor (By similarity). Catalyzes metabolism of not L- but the D-isomer of D-beta-aminoisobutyric acid to generate 2-methyl-3-oxopropanoate and alanine (PubMed:24586340). Catalyzes the transfer of the amino group from beta-alanine to pyruvate to yield L-alanine and 3-oxopropanoate (By similarity). Can metabolize NG-monomethyl-L-arginine (NMMA), asymmetric NG,NG-dimethyl-L-arginine (ADMA) and symmetric NG,N'G-dimethyl-L-arginine (SDMA) (PubMed:20018850, PubMed:23023372). ADMA is a potent inhibitor of nitric-oxide (NO) synthase, and this activity provides mechanism through which the kidney regulates blood pressure (PubMed:20018850, PubMed:23023372)
Protein Sequence
10
MTLIWRHLLR
20
PLCLVTSAPR
30
ILEMHPFLSL
40
GTSRTSVTKL
50
SLHTKPRMPP
60
CDFMPERYQS
70
LGYNRVLEIH
80
KEHLSPVVTA
90
YFQKPLLLHQ
100
GHMEWLFDAE
110
GSRYLDFFSG
120
IVTVSVGHCH
130
PKVNAVAQKQ
140
LGRLWHTSTV
150
FFHPPMHEYA
160
EKLAALLPEP
170
LKVIFLVNSG
180
SEANELAMLM
190
ARAHSNNIDI
200
ISFRGAYHGC
210
SPYTLGLTNV
220
GTYKMELPGG
230
TGCQPTMCPD
240
VFRGPWGGSH
250
CRDSPVQTIR
260
KCSCAPDCCQ
270
AKDQYIEQFK
280
DTLSTSVAKS
290
IAGFFAEPIQ
300
GVNGVVQYPK
310
GFLKEAFELV
320
RARGGVCIAD
330
EVQTGFGRLG
340
SHFWGFQTHD
350
VLPDIVTMAK
360
GIGNGFPMAA
370
VITTPEIAKS
380
LAKCLQHFNT
390
FGGNPMACAI
400
GSAVLEVIKE
410
ENLQENSQEV
420
GTYMLLKFAK
430
LRDEFEIVGD
440
VRGKGLMIGI
450
EMVQDKISCR
460
PLPREEVNQI
470
HEDCKHMGLL
480
VGRGSIFSQT
490
FRIAPSMCIT
500
KPEVDFAVEV
510
FRSALTQHME
RRAK
Gene Ontology
| Classification |
GO ID |
Description |
| Cellular Component |
GO:0005759 |
mitochondrial matrix |
| Cellular Component |
GO:0005739 |
mitochondrion |
| Molecular Function |
GO:0047305 |
(R)-3-amino-2-methylpropionate-pyruvate transaminase activity |
| Molecular Function |
GO:0008453 |
alanine-glyoxylate transaminase activity |
| Molecular Function |
GO:0016223 |
beta-alanine:pyruvate transaminase activity |
| Molecular Function |
GO:0030170 |
pyridoxal phosphate binding |
| Biological Process |
GO:0019265 |
glycine biosynthetic process, by transamination of glyoxylate |
| Biological Process |
GO:0009436 |
glyoxylate catabolic process |
| Biological Process |
GO:0019481 |
L-alanine catabolic process, by transamination |
| Biological Process |
GO:2001299 |
N(omega),N(omega)-dimethyl-L-arginine catabolic process |
| Biological Process |
GO:0045429 |
positive regulation of nitric oxide biosynthetic process |
Reference
[1] Yang Z, Yan C, Ma J, Peng P, Ren X et al.. Lactylome analysis suggests lactylation-dependent mechanisms of metabolic adaptation in hepatocellular carcinoma.. Nat Metab 5(1):61-79. 2023 Jan. PMID: 36593272.