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Alanine--glyoxylate aminotransferase 2, mitochondrial (AGT 2) (EC 2.6.1.44) ((R)-3-amino-2-methylpropionate--pyruvate transaminase) (EC 2.6.1.40) (Beta-ALAAT II) (Beta-alanine-pyruvate aminotransferase) (D-AIBAT)

 AGT2_HUMAN              Reviewed;         514 AA.
Q9BYV1; B7ZM47; E9PDL7; Q53FB4; Q53FY7; Q53G03; Q5W7Q1;
05-DEC-2001, integrated into UniProtKB/Swiss-Prot.
01-JUN-2001, sequence version 1.
27-SEP-2017, entry version 141.
RecName: Full=Alanine--glyoxylate aminotransferase 2, mitochondrial;
Short=AGT 2;
EC=2.6.1.44;
AltName: Full=(R)-3-amino-2-methylpropionate--pyruvate transaminase;
EC=2.6.1.40;
AltName: Full=Beta-ALAAT II;
AltName: Full=Beta-alanine-pyruvate aminotransferase;
AltName: Full=D-AIBAT;
Flags: Precursor;
Name=AGXT2; Synonyms=AGT2;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
Jenne D.E.;
"The human ortholog for rat alanine-glyoxylate aminotransferase 2.";
Submitted (JAN-2001) to the EMBL/GenBank/DDBJ databases.
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND VARIANTS ASN-102; ILE-140
AND ILE-212.
Matsuda K., Horikawa Y., Kaneko M., Sakata S., Tamaki N.;
"Human beta-alanine-pyruvate aminotransferase cDNA.";
Submitted (OCT-2004) to the EMBL/GenBank/DDBJ databases.
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANTS
ASN-102; ILE-140; ILE-212 AND LEU-498.
TISSUE=Kidney;
Suzuki Y., Sugano S., Totoki Y., Toyoda A., Takeda T., Sakaki Y.,
Tanaka A., Yokoyama S.;
Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases.
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=15372022; DOI=10.1038/nature02919;
Schmutz J., Martin J., Terry A., Couronne O., Grimwood J., Lowry S.,
Gordon L.A., 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 J.F., Chan Y.M., Denys M.,
Detter J.C., 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 J.P., 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 J.-F., Eichler E.E., Olsen A., Pennacchio L.A., Rokhsar D.S.,
Richardson P., Lucas S.M., Myers R.M., Rubin E.M.;
"The DNA sequence and comparative analysis of human chromosome 5.";
Nature 431:268-274(2004).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), AND VARIANTS
ASN-102 AND ILE-212.
TISSUE=Testis;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[6]
PROTEIN SEQUENCE OF N-TERMINUS, FUNCTION, TRANSIT PEPTIDE CLEAVAGE
SITE, AND SUBCELLULAR LOCATION.
PubMed=20018850; DOI=10.1074/jbc.M109.091280;
Rodionov R.N., Murry D.J., Vaulman S.F., Stevens J.W., Lentz S.R.;
"Human alanine-glyoxylate aminotransferase 2 lowers asymmetric
dimethylarginine and protects from inhibition of nitric oxide
production.";
J. Biol. Chem. 285:5385-5391(2010).
[7]
FUNCTION.
PubMed=23023372; DOI=10.1161/ATVBAHA.112.254078;
Caplin B., Wang Z., Slaviero A., Tomlinson J., Dowsett L.,
Delahaye M., Salama A., Wheeler D.C., Leiper J.;
"Alanine-Glyoxylate aminotransferase-2 metabolizes endogenous
methylarginines, regulates NO, and controls blood pressure.";
Arterioscler. Thromb. Vasc. Biol. 32:2892-2900(2012).
[8]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
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 96:253-262(2014).
[9]
VARIANT ILE-140.
PubMed=24834905;
Zhou J.P., Bai Y.P., Hu X.L., Kuang D.B., Shi R.Z., Xiong Y.,
Zhang W., Xia J., Chen B.L., Yang T.L., Chen X.P.;
"Association of the AGXT2 V140I polymorphism with risk for coronary
heart disease in a Chinese population.";
J. Atheroscler. Thromb. 21:1022-1030(2014).
[10]
POLYMORPHISM, VARIANTS ILE-140 AND LEU-498, FUNCTION, SUBCELLULAR
LOCATION, AND CHARACTERIZATION OF VARIANT ILE-140.
PubMed=24586340; DOI=10.1371/journal.pone.0088544;
Kittel A., Muller F., Konig J., Mieth M., Sticht H., Zolk O.,
Kralj A., Heinrich M.R., Fromm M.F., Maas R.;
"Alanine-glyoxylate aminotransferase 2 (AGXT2) polymorphisms have
considerable impact on methylarginine and beta-aminoisobutyrate
metabolism in healthy volunteers.";
PLoS ONE 9:E88544-E88544(2014).
-!- 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. {ECO:0000269|PubMed:20018850,
ECO:0000269|PubMed:23023372, ECO:0000269|PubMed:24586340}.
-!- CATALYTIC ACTIVITY: L-alanine + glyoxylate = pyruvate + glycine.
-!- CATALYTIC ACTIVITY: (R)-3-amino-2-methylpropanoate + pyruvate = 2-
methyl-3-oxopropanoate + L-alanine.
-!- COFACTOR:
Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
-!- SUBUNIT: Homotetramer. {ECO:0000250}.
-!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000269|PubMed:20018850,
ECO:0000269|PubMed:24586340}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1;
IsoId=Q9BYV1-1; Sequence=Displayed;
Name=2;
IsoId=Q9BYV1-2; Sequence=VSP_055802;
Note=No experimental confirmation available.;
-!- POLYMORPHISM: Genetic variants in AGXT2 are association with beta-
aminoisobutyric aciduria (BAIBA)[MIM:210100]. Excretion of beta-
aminoisobutyric acid in urine is a common, benign, metabolic
trait. {ECO:0000269|PubMed:24586340}.
-!- SIMILARITY: Belongs to the class-III pyridoxal-phosphate-dependent
aminotransferase family. {ECO:0000305}.
-----------------------------------------------------------------------
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EMBL; AJ292204; CAC24841.1; -; mRNA.
EMBL; AB193309; BAD66662.1; -; mRNA.
EMBL; AK223128; BAD96848.1; -; mRNA.
EMBL; AK223144; -; NOT_ANNOTATED_CDS; mRNA.
EMBL; AK223375; BAD97095.1; -; mRNA.
EMBL; AC010368; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; BC144268; AAI44269.1; -; mRNA.
EMBL; BC150603; AAI50604.1; -; mRNA.
CCDS; CCDS3908.1; -. [Q9BYV1-1]
CCDS; CCDS78000.1; -. [Q9BYV1-2]
RefSeq; NP_001293102.1; NM_001306173.1. [Q9BYV1-2]
RefSeq; NP_114106.1; NM_031900.3. [Q9BYV1-1]
RefSeq; XP_016865237.1; XM_017009748.1. [Q9BYV1-2]
UniGene; Hs.34494; -.
ProteinModelPortal; Q9BYV1; -.
SMR; Q9BYV1; -.
BioGrid; 122342; 2.
IntAct; Q9BYV1; 2.
STRING; 9606.ENSP00000231420; -.
DrugBank; DB00145; Glycine.
DrugBank; DB00160; L-Alanine.
DrugBank; DB00114; Pyridoxal Phosphate.
DrugBank; DB00119; Pyruvic acid.
iPTMnet; Q9BYV1; -.
PhosphoSitePlus; Q9BYV1; -.
BioMuta; AGXT2; -.
DMDM; 17432913; -.
PaxDb; Q9BYV1; -.
PeptideAtlas; Q9BYV1; -.
PRIDE; Q9BYV1; -.
Ensembl; ENST00000231420; ENSP00000231420; ENSG00000113492. [Q9BYV1-1]
Ensembl; ENST00000510428; ENSP00000422799; ENSG00000113492. [Q9BYV1-2]
Ensembl; ENST00000618015; ENSP00000479154; ENSG00000113492. [Q9BYV1-2]
GeneID; 64902; -.
KEGG; hsa:64902; -.
UCSC; uc003jjf.4; human. [Q9BYV1-1]
CTD; 64902; -.
DisGeNET; 64902; -.
EuPathDB; HostDB:ENSG00000113492.13; -.
GeneCards; AGXT2; -.
HGNC; HGNC:14412; AGXT2.
HPA; HPA037382; -.
MIM; 210100; phenotype.
MIM; 612471; gene.
neXtProt; NX_Q9BYV1; -.
OpenTargets; ENSG00000113492; -.
PharmGKB; PA24634; -.
eggNOG; KOG1404; Eukaryota.
eggNOG; COG0160; LUCA.
GeneTree; ENSGT00530000062907; -.
HOGENOM; HOG000020206; -.
HOVERGEN; HBG004196; -.
InParanoid; Q9BYV1; -.
KO; K00827; -.
OMA; GIATCTL; -.
OrthoDB; EOG091G06LW; -.
PhylomeDB; Q9BYV1; -.
TreeFam; TF105945; -.
BioCyc; MetaCyc:HS03685-MONOMER; -.
Reactome; R-HSA-389661; Glyoxylate metabolism and glycine degradation.
Reactome; R-HSA-73621; Pyrimidine catabolism.
ChiTaRS; AGXT2; human.
GenomeRNAi; 64902; -.
PRO; PR:Q9BYV1; -.
Proteomes; UP000005640; Chromosome 5.
Bgee; ENSG00000113492; -.
CleanEx; HS_AGXT2; -.
Genevisible; Q9BYV1; HS.
GO; GO:0005759; C:mitochondrial matrix; TAS:Reactome.
GO; GO:0005739; C:mitochondrion; IDA:UniProtKB.
GO; GO:0047305; F:(R)-3-amino-2-methylpropionate-pyruvate transaminase activity; IEA:UniProtKB-EC.
GO; GO:0008453; F:alanine-glyoxylate transaminase activity; IDA:UniProtKB.
GO; GO:0042802; F:identical protein binding; IBA:GO_Central.
GO; GO:0030170; F:pyridoxal phosphate binding; IBA:GO_Central.
GO; GO:0019265; P:glycine biosynthetic process, by transamination of glyoxylate; IDA:BHF-UCL.
GO; GO:0009436; P:glyoxylate catabolic process; IDA:BHF-UCL.
GO; GO:0046487; P:glyoxylate metabolic process; TAS:Reactome.
GO; GO:0019481; P:L-alanine catabolic process, by transamination; IDA:BHF-UCL.
GO; GO:0045429; P:positive regulation of nitric oxide biosynthetic process; IDA:BHF-UCL.
CDD; cd00610; OAT_like; 1.
Gene3D; 3.40.640.10; -; 1.
Gene3D; 3.90.1150.10; -; 1.
InterPro; IPR005814; Aminotrans_3.
InterPro; IPR015424; PyrdxlP-dep_Trfase.
InterPro; IPR015421; PyrdxlP-dep_Trfase_major_sub1.
InterPro; IPR015422; PyrdxlP-dep_Trfase_sub2.
Pfam; PF00202; Aminotran_3; 1.
PIRSF; PIRSF000521; Transaminase_4ab_Lys_Orn; 1.
SUPFAM; SSF53383; SSF53383; 1.
PROSITE; PS00600; AA_TRANSFER_CLASS_3; 1.
1: Evidence at protein level;
Acetylation; Alternative splicing; Aminotransferase;
Complete proteome; Direct protein sequencing; Mitochondrion;
Polymorphism; Pyridoxal phosphate; Reference proteome; Transferase;
Transit peptide.
TRANSIT 1 41 Mitochondrion.
{ECO:0000269|PubMed:20018850}.
CHAIN 42 514 Alanine--glyoxylate aminotransferase 2,
mitochondrial.
/FTId=PRO_0000001269.
MOD_RES 71 71 N6-acetyllysine; alternate.
{ECO:0000250|UniProtKB:Q3UEG6}.
MOD_RES 71 71 N6-succinyllysine; alternate.
{ECO:0000250|UniProtKB:Q3UEG6}.
MOD_RES 84 84 N6-acetyllysine.
{ECO:0000250|UniProtKB:Q3UEG6}.
MOD_RES 262 262 N6-acetyllysine; alternate.
{ECO:0000250|UniProtKB:Q3UEG6}.
MOD_RES 262 262 N6-succinyllysine; alternate.
{ECO:0000250|UniProtKB:Q3UEG6}.
MOD_RES 304 304 N6-succinyllysine.
{ECO:0000250|UniProtKB:Q3UEG6}.
MOD_RES 350 350 N6-(pyridoxal phosphate)lysine.
{ECO:0000250}.
MOD_RES 417 417 N6-acetyllysine; alternate.
{ECO:0000250|UniProtKB:Q3UEG6}.
MOD_RES 417 417 N6-succinyllysine; alternate.
{ECO:0000250|UniProtKB:Q3UEG6}.
MOD_RES 420 420 N6-acetyllysine; alternate.
{ECO:0000250|UniProtKB:Q3UEG6}.
MOD_RES 420 420 N6-succinyllysine; alternate.
{ECO:0000250|UniProtKB:Q3UEG6}.
VAR_SEQ 321 395 Missing (in isoform 2).
{ECO:0000303|PubMed:15489334}.
/FTId=VSP_055802.
VARIANT 102 102 S -> I (in dbSNP:rs37370).
/FTId=VAR_061006.
VARIANT 102 102 S -> N (in dbSNP:rs37370).
{ECO:0000269|PubMed:15489334,
ECO:0000269|Ref.2, ECO:0000269|Ref.3}.
/FTId=VAR_023483.
VARIANT 102 102 S -> T (in dbSNP:rs37370).
/FTId=VAR_061007.
VARIANT 132 132 G -> R (in dbSNP:rs16870794).
/FTId=VAR_048231.
VARIANT 140 140 V -> I (polymorphism; associated with an
increased risk for coronary heart disease
(CHD) in smoker and diabetic mellitus
(DM) patients in a Chinese population;
higher plasma symmetric (SDMA)
dimethylarginine as well as plasma and
urinary beta-aminoisobutyrate (BAIB)
concentrations; localized to the
mitochondrion as the wild-type; reduces
alanine-glyoxylate aminotransferase
activity; dbSNP:rs37369).
{ECO:0000269|PubMed:24586340,
ECO:0000269|PubMed:24834905,
ECO:0000269|Ref.2, ECO:0000269|Ref.3}.
/FTId=VAR_022140.
VARIANT 212 212 T -> I (in dbSNP:rs180749).
{ECO:0000269|PubMed:15489334,
ECO:0000269|Ref.2, ECO:0000269|Ref.3}.
/FTId=VAR_022141.
VARIANT 492 492 P -> R (in dbSNP:rs17245714).
/FTId=VAR_048232.
VARIANT 498 498 V -> L (polymorphism; higher plasma and
urinary beta-aminoisobutyrate (BAIB)
concentrations; dbSNP:rs16899974).
{ECO:0000269|PubMed:24586340,
ECO:0000269|Ref.3}.
/FTId=VAR_029513.
SEQUENCE 514 AA; 57156 MW; CA562F84FF39B5AC CRC64;
MTLIWRHLLR PLCLVTSAPR ILEMHPFLSL GTSRTSVTKL SLHTKPRMPP CDFMPERYQS
LGYNRVLEIH KEHLSPVVTA YFQKPLLLHQ GHMEWLFDAE GSRYLDFFSG IVTVSVGHCH
PKVNAVAQKQ LGRLWHTSTV FFHPPMHEYA EKLAALLPEP LKVIFLVNSG SEANELAMLM
ARAHSNNIDI ISFRGAYHGC SPYTLGLTNV GTYKMELPGG TGCQPTMCPD VFRGPWGGSH
CRDSPVQTIR KCSCAPDCCQ AKDQYIEQFK DTLSTSVAKS IAGFFAEPIQ GVNGVVQYPK
GFLKEAFELV RARGGVCIAD EVQTGFGRLG SHFWGFQTHD VLPDIVTMAK GIGNGFPMAA
VITTPEIAKS LAKCLQHFNT FGGNPMACAI GSAVLEVIKE ENLQENSQEV GTYMLLKFAK
LRDEFEIVGD VRGKGLMIGI EMVQDKISCR PLPREEVNQI HEDCKHMGLL VGRGSIFSQT
FRIAPSMCIT KPEVDFAVEV FRSALTQHME RRAK


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