ID   AGT2_HUMAN              Reviewed;         514 AA.
AC   Q9BYV1; B7ZM47; E9PDL7; Q53FB4; Q53FY7; Q53G03; Q5W7Q1;
DT   05-DEC-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2001, sequence version 1.
DT   27-MAR-2024, entry version 175.
DE   RecName: Full=Alanine--glyoxylate aminotransferase 2, mitochondrial;
DE            Short=AGT 2;
DE            EC=2.6.1.44 {ECO:0000250|UniProtKB:Q64565};
DE   AltName: Full=(R)-3-amino-2-methylpropionate--pyruvate transaminase;
DE            EC=2.6.1.40 {ECO:0000269|PubMed:24586340};
DE   AltName: Full=Beta-ALAAT II;
DE   AltName: Full=Beta-alanine-pyruvate aminotransferase;
DE            EC=2.6.1.18 {ECO:0000250|UniProtKB:Q64565};
DE   AltName: Full=D-3-aminoisobutyrate-pyruvate aminotransferase {ECO:0000250|UniProtKB:Q64565};
DE   AltName: Full=D-AIBAT {ECO:0000250|UniProtKB:Q64565};
DE   AltName: Full=D-beta-aminoisobutyrate-pyruvate aminotransferase {ECO:0000250|UniProtKB:Q64565};
DE   Flags: Precursor;
GN   Name=AGXT2; Synonyms=AGT2;
OS   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Homo.
OX   NCBI_TaxID=9606;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RA   Jenne D.E.;
RT   "The human ortholog for rat alanine-glyoxylate aminotransferase 2.";
RL   Submitted (JAN-2001) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND VARIANTS ASN-102; ILE-140 AND
RP   ILE-212.
RA   Matsuda K., Horikawa Y., Kaneko M., Sakata S., Tamaki N.;
RT   "Human beta-alanine-pyruvate aminotransferase cDNA.";
RL   Submitted (OCT-2004) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANTS ASN-102;
RP   ILE-140; ILE-212 AND LEU-498.
RC   TISSUE=Kidney;
RA   Suzuki Y., Sugano S., Totoki Y., Toyoda A., Takeda T., Sakaki Y.,
RA   Tanaka A., Yokoyama S.;
RL   Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases.
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=15372022; DOI=10.1038/nature02919;
RA   Schmutz J., Martin J., Terry A., Couronne O., Grimwood J., Lowry S.,
RA   Gordon L.A., Scott D., Xie G., Huang W., Hellsten U., Tran-Gyamfi M.,
RA   She X., Prabhakar S., Aerts A., Altherr M., Bajorek E., Black S.,
RA   Branscomb E., Caoile C., Challacombe J.F., Chan Y.M., Denys M.,
RA   Detter J.C., Escobar J., Flowers D., Fotopulos D., Glavina T., Gomez M.,
RA   Gonzales E., Goodstein D., Grigoriev I., Groza M., Hammon N., Hawkins T.,
RA   Haydu L., Israni S., Jett J., Kadner K., Kimball H., Kobayashi A.,
RA   Lopez F., Lou Y., Martinez D., Medina C., Morgan J., Nandkeshwar R.,
RA   Noonan J.P., Pitluck S., Pollard M., Predki P., Priest J., Ramirez L.,
RA   Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A., Thayer N.,
RA   Tice H., Tsai M., Ustaszewska A., Vo N., Wheeler J., Wu K., Yang J.,
RA   Dickson M., Cheng J.-F., Eichler E.E., Olsen A., Pennacchio L.A.,
RA   Rokhsar D.S., Richardson P., Lucas S.M., Myers R.M., Rubin E.M.;
RT   "The DNA sequence and comparative analysis of human chromosome 5.";
RL   Nature 431:268-274(2004).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), AND VARIANTS ASN-102
RP   AND ILE-212.
RC   TISSUE=Testis;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA project:
RT   the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [6]
RP   PROTEIN SEQUENCE OF N-TERMINUS, FUNCTION, TRANSIT PEPTIDE CLEAVAGE SITE,
RP   AND SUBCELLULAR LOCATION.
RX   PubMed=20018850; DOI=10.1074/jbc.m109.091280;
RA   Rodionov R.N., Murry D.J., Vaulman S.F., Stevens J.W., Lentz S.R.;
RT   "Human alanine-glyoxylate aminotransferase 2 lowers asymmetric
RT   dimethylarginine and protects from inhibition of nitric oxide production.";
RL   J. Biol. Chem. 285:5385-5391(2010).
RN   [7]
RP   FUNCTION, AND CATALYTIC ACTIVITY.
RX   PubMed=23023372; DOI=10.1161/atvbaha.112.254078;
RA   Caplin B., Wang Z., Slaviero A., Tomlinson J., Dowsett L., Delahaye M.,
RA   Salama A., Wheeler D.C., Leiper J.;
RT   "Alanine-Glyoxylate aminotransferase-2 metabolizes endogenous
RT   methylarginines, regulates NO, and controls blood pressure.";
RL   Arterioscler. Thromb. Vasc. Biol. 32:2892-2900(2012).
RN   [8]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Liver;
RX   PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA   Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA   Ye M., Zou H.;
RT   "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT   phosphoproteome.";
RL   J. Proteomics 96:253-262(2014).
RN   [9]
RP   SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX   PubMed=31818439; DOI=10.1016/j.atherosclerosissup.2019.08.041;
RA   Jarzebska N., Georgi S., Jabs N., Brilloff S., Maas R., Rodionov R.N.,
RA   Zietz C., Montresor S., Hohenstein B., Weiss N.;
RT   "Kidney and liver are the main organs of expression of a key metabolic
RT   enzyme alanine:glyoxylate aminotransferase 2 in humans.";
RL   Atheroscler. Suppl. 40:106-112(2019).
RN   [10]
RP   VARIANT ILE-140.
RX   PubMed=24834905; DOI=10.5551/jat.23077;
RA   Zhou J.P., Bai Y.P., Hu X.L., Kuang D.B., Shi R.Z., Xiong Y., Zhang W.,
RA   Xia J., Chen B.L., Yang T.L., Chen X.P.;
RT   "Association of the AGXT2 V140I polymorphism with risk for coronary heart
RT   disease in a Chinese population.";
RL   J. Atheroscler. Thromb. 21:1022-1030(2014).
RN   [11]
RP   POLYMORPHISM, VARIANTS ILE-140 AND LEU-498, FUNCTION, SUBCELLULAR LOCATION,
RP   CHARACTERIZATION OF VARIANT ILE-140, AND CATALYTIC ACTIVITY.
RX   PubMed=24586340; DOI=10.1371/journal.pone.0088544;
RA   Kittel A., Muller F., Konig J., Mieth M., Sticht H., Zolk O., Kralj A.,
RA   Heinrich M.R., Fromm M.F., Maas R.;
RT   "Alanine-glyoxylate aminotransferase 2 (AGXT2) polymorphisms have
RT   considerable impact on methylarginine and beta-aminoisobutyrate metabolism
RT   in healthy volunteers.";
RL   PLoS ONE 9:E88544-E88544(2014).
CC   -!- FUNCTION: Multifunctional aminotransferase with a broad substrate
CC       specifcity (PubMed:20018850, PubMed:24586340, PubMed:23023372).
CC       Catalyzes the conversion of glyoxylate to glycine using alanine as the
CC       amino donor (By similarity). Catalyzes metabolism of not L- but the D-
CC       isomer of D-beta-aminoisobutyric acid to generate 2-methyl-3-
CC       oxopropanoate and alanine (PubMed:24586340). Catalyzes the transfer of
CC       the amino group from beta-alanine to pyruvate to yield L-alanine and 3-
CC       oxopropanoate (By similarity). Can metabolize NG-monomethyl-L-arginine
CC       (NMMA), asymmetric NG,NG-dimethyl-L-arginine (ADMA) and symmetric
CC       NG,N'G-dimethyl-L-arginine (SDMA) (PubMed:20018850, PubMed:23023372).
CC       ADMA is a potent inhibitor of nitric-oxide (NO) synthase, and this
CC       activity provides mechanism through which the kidney regulates blood
CC       pressure (PubMed:20018850, PubMed:23023372).
CC       {ECO:0000250|UniProtKB:Q64565, ECO:0000269|PubMed:20018850,
CC       ECO:0000269|PubMed:23023372, ECO:0000269|PubMed:24586340}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=glyoxylate + L-alanine = glycine + pyruvate;
CC         Xref=Rhea:RHEA:24248, ChEBI:CHEBI:15361, ChEBI:CHEBI:36655,
CC         ChEBI:CHEBI:57305, ChEBI:CHEBI:57972; EC=2.6.1.44;
CC         Evidence={ECO:0000250|UniProtKB:Q64565};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:24249;
CC         Evidence={ECO:0000305|PubMed:20018850};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(R)-3-amino-2-methylpropanoate + pyruvate = 2-methyl-3-
CC         oxopropanoate + L-alanine; Xref=Rhea:RHEA:18393, ChEBI:CHEBI:15361,
CC         ChEBI:CHEBI:57700, ChEBI:CHEBI:57731, ChEBI:CHEBI:57972; EC=2.6.1.40;
CC         Evidence={ECO:0000269|PubMed:24586340};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:18394;
CC         Evidence={ECO:0000305|PubMed:24586340};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=3-oxopropanoate + L-alanine = beta-alanine + pyruvate;
CC         Xref=Rhea:RHEA:14077, ChEBI:CHEBI:15361, ChEBI:CHEBI:33190,
CC         ChEBI:CHEBI:57966, ChEBI:CHEBI:57972; EC=2.6.1.18;
CC         Evidence={ECO:0000250|UniProtKB:Q64565};
CC       PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:14079;
CC         Evidence={ECO:0000250|UniProtKB:Q64565};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=2-oxobutanoate + L-alanine = (2S)-2-aminobutanoate + pyruvate;
CC         Xref=Rhea:RHEA:77355, ChEBI:CHEBI:15361, ChEBI:CHEBI:16763,
CC         ChEBI:CHEBI:57972, ChEBI:CHEBI:74359; EC=2.6.1.44;
CC         Evidence={ECO:0000250|UniProtKB:Q64565};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=N(omega),N(omega)-dimethyl-L-arginine + pyruvate = 5-(3,3-
CC         dimethylguanidino)-2-oxopentanoate + L-alanine; Xref=Rhea:RHEA:77303,
CC         ChEBI:CHEBI:15361, ChEBI:CHEBI:57972, ChEBI:CHEBI:58326,
CC         ChEBI:CHEBI:197301; Evidence={ECO:0000269|PubMed:23023372};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=N(omega),N('omega)-dimethyl-L-arginine + pyruvate = 5-(3,3'-
CC         dimethylguanidino)-2-oxopentanoate + L-alanine; Xref=Rhea:RHEA:77307,
CC         ChEBI:CHEBI:15361, ChEBI:CHEBI:57972, ChEBI:CHEBI:197308,
CC         ChEBI:CHEBI:197310; Evidence={ECO:0000250|UniProtKB:Q64565};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=glyoxylate + N(omega),N(omega)-dimethyl-L-arginine = 5-(3,3-
CC         dimethylguanidino)-2-oxopentanoate + glycine; Xref=Rhea:RHEA:77311,
CC         ChEBI:CHEBI:36655, ChEBI:CHEBI:57305, ChEBI:CHEBI:58326,
CC         ChEBI:CHEBI:197301; Evidence={ECO:0000250|UniProtKB:Q64565};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=glyoxylate + N(omega),N('omega)-dimethyl-L-arginine = 5-(3,3'-
CC         dimethylguanidino)-2-oxopentanoate + glycine; Xref=Rhea:RHEA:77315,
CC         ChEBI:CHEBI:36655, ChEBI:CHEBI:57305, ChEBI:CHEBI:197308,
CC         ChEBI:CHEBI:197310; Evidence={ECO:0000250|UniProtKB:Q64565};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=N(omega)-methyl-L-arginine + pyruvate = 5-(3-methylguanidino)-
CC         2-oxopentanoate + L-alanine; Xref=Rhea:RHEA:77319, ChEBI:CHEBI:15361,
CC         ChEBI:CHEBI:57972, ChEBI:CHEBI:114953, ChEBI:CHEBI:197314;
CC         Evidence={ECO:0000250|UniProtKB:Q64565};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=glyoxylate + N(omega)-methyl-L-arginine = 5-(3-
CC         methylguanidino)-2-oxopentanoate + glycine; Xref=Rhea:RHEA:77323,
CC         ChEBI:CHEBI:36655, ChEBI:CHEBI:57305, ChEBI:CHEBI:114953,
CC         ChEBI:CHEBI:197314; Evidence={ECO:0000250|UniProtKB:Q64565};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=L-ornithine + pyruvate = 5-amino-2-oxopentanoate + L-alanine;
CC         Xref=Rhea:RHEA:77327, ChEBI:CHEBI:15361, ChEBI:CHEBI:46911,
CC         ChEBI:CHEBI:57972, ChEBI:CHEBI:58802;
CC         Evidence={ECO:0000250|UniProtKB:Q64565};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=glyoxylate + L-ornithine = 5-amino-2-oxopentanoate + glycine;
CC         Xref=Rhea:RHEA:77331, ChEBI:CHEBI:36655, ChEBI:CHEBI:46911,
CC         ChEBI:CHEBI:57305, ChEBI:CHEBI:58802;
CC         Evidence={ECO:0000250|UniProtKB:Q64565};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(2S)-2-aminobutanoate + glyoxylate = 2-oxobutanoate + glycine;
CC         Xref=Rhea:RHEA:77339, ChEBI:CHEBI:16763, ChEBI:CHEBI:36655,
CC         ChEBI:CHEBI:57305, ChEBI:CHEBI:74359;
CC         Evidence={ECO:0000250|UniProtKB:Q64565};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=N(omega),N(omega)-dimethyl-L-arginine + oxaloacetate = 5-(3,3-
CC         dimethylguanidino)-2-oxopentanoate + L-aspartate;
CC         Xref=Rhea:RHEA:77343, ChEBI:CHEBI:16452, ChEBI:CHEBI:29991,
CC         ChEBI:CHEBI:58326, ChEBI:CHEBI:197301;
CC         Evidence={ECO:0000250|UniProtKB:Q64565};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=L-alanine + oxaloacetate = L-aspartate + pyruvate;
CC         Xref=Rhea:RHEA:77347, ChEBI:CHEBI:15361, ChEBI:CHEBI:16452,
CC         ChEBI:CHEBI:29991, ChEBI:CHEBI:57972;
CC         Evidence={ECO:0000250|UniProtKB:Q64565};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=2-oxobutanoate + N(omega),N(omega)-dimethyl-L-arginine = (2S)-
CC         2-aminobutanoate + 5-(3,3-dimethylguanidino)-2-oxopentanoate;
CC         Xref=Rhea:RHEA:77351, ChEBI:CHEBI:16763, ChEBI:CHEBI:58326,
CC         ChEBI:CHEBI:74359, ChEBI:CHEBI:197301;
CC         Evidence={ECO:0000250|UniProtKB:Q64565};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=2-oxopentanoate + N(omega),N(omega)-dimethyl-L-arginine = 5-
CC         (3,3-dimethylguanidino)-2-oxopentanoate + L-2-aminopentanoate;
CC         Xref=Rhea:RHEA:77359, ChEBI:CHEBI:28644, ChEBI:CHEBI:58326,
CC         ChEBI:CHEBI:58441, ChEBI:CHEBI:197301;
CC         Evidence={ECO:0000250|UniProtKB:Q64565};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=2-oxohexanoate + N(omega),N(omega)-dimethyl-L-arginine = 5-
CC         (3,3-dimethylguanidino)-2-oxopentanoate + L-2-aminohexanoate;
CC         Xref=Rhea:RHEA:77363, ChEBI:CHEBI:35177, ChEBI:CHEBI:58326,
CC         ChEBI:CHEBI:58455, ChEBI:CHEBI:197301;
CC         Evidence={ECO:0000250|UniProtKB:Q64565};
CC   -!- COFACTOR:
CC       Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC         Evidence={ECO:0000250|UniProtKB:Q64565};
CC   -!- SUBUNIT: Homotetramer. {ECO:0000250|UniProtKB:Q64565}.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000269|PubMed:20018850,
CC       ECO:0000269|PubMed:24586340, ECO:0000269|PubMed:31818439}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q9BYV1-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q9BYV1-2; Sequence=VSP_055802;
CC   -!- TISSUE SPECIFICITY: Expressed in the convoluted tubule in the kidney
CC       and in the liver hepatocytes (at protein level).
CC       {ECO:0000269|PubMed:31818439}.
CC   -!- POLYMORPHISM: Genetic variants in AGXT2 are association with beta-
CC       aminoisobutyric aciduria (BAIBA)[MIM:210100]. Excretion of beta-
CC       aminoisobutyric acid in urine is a common, benign, metabolic trait.
CC       {ECO:0000269|PubMed:24586340}.
CC   -!- SIMILARITY: Belongs to the class-III pyridoxal-phosphate-dependent
CC       aminotransferase family. {ECO:0000305}.
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DR   EMBL; AJ292204; CAC24841.1; -; mRNA.
DR   EMBL; AB193309; BAD66662.1; -; mRNA.
DR   EMBL; AK223128; BAD96848.1; -; mRNA.
DR   EMBL; AK223144; -; NOT_ANNOTATED_CDS; mRNA.
DR   EMBL; AK223375; BAD97095.1; -; mRNA.
DR   EMBL; AC010368; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; BC144268; AAI44269.1; -; mRNA.
DR   EMBL; BC150603; AAI50604.1; -; mRNA.
DR   CCDS; CCDS3908.1; -. [Q9BYV1-1]
DR   CCDS; CCDS78000.1; -. [Q9BYV1-2]
DR   RefSeq; NP_001293102.1; NM_001306173.1. [Q9BYV1-2]
DR   RefSeq; NP_114106.1; NM_031900.3. [Q9BYV1-1]
DR   RefSeq; XP_016865237.1; XM_017009748.1. [Q9BYV1-2]
DR   AlphaFoldDB; Q9BYV1; -.
DR   SMR; Q9BYV1; -.
DR   BioGRID; 122342; 59.
DR   IntAct; Q9BYV1; 2.
DR   STRING; 9606.ENSP00000231420; -.
DR   DrugBank; DB00160; Alanine.
DR   DrugBank; DB00145; Glycine.
DR   DrugBank; DB00114; Pyridoxal phosphate.
DR   DrugBank; DB00119; Pyruvic acid.
DR   iPTMnet; Q9BYV1; -.
DR   PhosphoSitePlus; Q9BYV1; -.
DR   BioMuta; AGXT2; -.
DR   DMDM; 17432913; -.
DR   MassIVE; Q9BYV1; -.
DR   PaxDb; 9606-ENSP00000231420; -.
DR   PeptideAtlas; Q9BYV1; -.
DR   ProteomicsDB; 19698; -.
DR   ProteomicsDB; 79711; -. [Q9BYV1-1]
DR   Antibodypedia; 43482; 155 antibodies from 26 providers.
DR   DNASU; 64902; -.
DR   Ensembl; ENST00000231420.11; ENSP00000231420.6; ENSG00000113492.14. [Q9BYV1-1]
DR   Ensembl; ENST00000510428.1; ENSP00000422799.1; ENSG00000113492.14. [Q9BYV1-2]
DR   Ensembl; ENST00000618015.4; ENSP00000479154.1; ENSG00000113492.14. [Q9BYV1-2]
DR   GeneID; 64902; -.
DR   KEGG; hsa:64902; -.
DR   MANE-Select; ENST00000231420.11; ENSP00000231420.6; NM_031900.4; NP_114106.1.
DR   UCSC; uc003jjf.4; human. [Q9BYV1-1]
DR   AGR; HGNC:14412; -.
DR   CTD; 64902; -.
DR   DisGeNET; 64902; -.
DR   GeneCards; AGXT2; -.
DR   HGNC; HGNC:14412; AGXT2.
DR   HPA; ENSG00000113492; Group enriched (kidney, liver).
DR   MalaCards; AGXT2; -.
DR   MIM; 210100; phenotype.
DR   MIM; 612471; gene.
DR   neXtProt; NX_Q9BYV1; -.
DR   OpenTargets; ENSG00000113492; -.
DR   PharmGKB; PA24634; -.
DR   VEuPathDB; HostDB:ENSG00000113492; -.
DR   eggNOG; KOG1404; Eukaryota.
DR   GeneTree; ENSGT00940000156125; -.
DR   HOGENOM; CLU_016922_8_0_1; -.
DR   InParanoid; Q9BYV1; -.
DR   OMA; MVPGFKY; -.
DR   OrthoDB; 345661at2759; -.
DR   PhylomeDB; Q9BYV1; -.
DR   TreeFam; TF105945; -.
DR   BioCyc; MetaCyc:HS03685-MONOMER; -.
DR   BRENDA; 2.6.1.44; 2681.
DR   PathwayCommons; Q9BYV1; -.
DR   Reactome; R-HSA-389661; Glyoxylate metabolism and glycine degradation.
DR   Reactome; R-HSA-73621; Pyrimidine catabolism.
DR   SignaLink; Q9BYV1; -.
DR   BioGRID-ORCS; 64902; 8 hits in 1153 CRISPR screens.
DR   ChiTaRS; AGXT2; human.
DR   GenomeRNAi; 64902; -.
DR   Pharos; Q9BYV1; Tbio.
DR   PRO; PR:Q9BYV1; -.
DR   Proteomes; UP000005640; Chromosome 5.
DR   RNAct; Q9BYV1; Protein.
DR   Bgee; ENSG00000113492; Expressed in kidney epithelium and 41 other cell types or tissues.
DR   GO; GO:0005759; C:mitochondrial matrix; TAS:Reactome.
DR   GO; GO:0005739; C:mitochondrion; IDA:UniProtKB.
DR   GO; GO:0047305; F:(R)-3-amino-2-methylpropionate-pyruvate transaminase activity; IDA:UniProtKB.
DR   GO; GO:0008453; F:alanine-glyoxylate transaminase activity; IDA:UniProtKB.
DR   GO; GO:0016223; F:beta-alanine-pyruvate transaminase activity; IEA:Ensembl.
DR   GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR   GO; GO:0019265; P:glycine biosynthetic process, by transamination of glyoxylate; IDA:BHF-UCL.
DR   GO; GO:0009436; P:glyoxylate catabolic process; IDA:BHF-UCL.
DR   GO; GO:0019481; P:L-alanine catabolic process, by transamination; IDA:BHF-UCL.
DR   GO; GO:2001299; P:N(omega),N(omega)-dimethyl-L-arginine catabolic process; ISS:UniProtKB.
DR   GO; GO:0045429; P:positive regulation of nitric oxide biosynthetic process; IDA:BHF-UCL.
DR   CDD; cd00610; OAT_like; 1.
DR   Gene3D; 3.90.1150.10; Aspartate Aminotransferase, domain 1; 1.
DR   Gene3D; 3.40.640.10; Type I PLP-dependent aspartate aminotransferase-like (Major domain); 1.
DR   InterPro; IPR005814; Aminotrans_3.
DR   InterPro; IPR049704; Aminotrans_3_PPA_site.
DR   InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR   InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR   InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
DR   PANTHER; PTHR45688; ALANINE--GLYOXYLATE AMINOTRANSFERASE 2, MITOCHONDRIAL; 1.
DR   PANTHER; PTHR45688:SF3; ALANINE--GLYOXYLATE AMINOTRANSFERASE 2, MITOCHONDRIAL; 1.
DR   Pfam; PF00202; Aminotran_3; 1.
DR   PIRSF; PIRSF000521; Transaminase_4ab_Lys_Orn; 1.
DR   SUPFAM; SSF53383; PLP-dependent transferases; 1.
DR   PROSITE; PS00600; AA_TRANSFER_CLASS_3; 1.
DR   Genevisible; Q9BYV1; HS.
PE   1: Evidence at protein level;
KW   Acetylation; Alternative splicing; Aminotransferase;
KW   Direct protein sequencing; Disease variant; Mitochondrion;
KW   Pyridoxal phosphate; Reference proteome; Transferase; Transit peptide.
FT   TRANSIT         1..41
FT                   /note="Mitochondrion"
FT                   /evidence="ECO:0000269|PubMed:20018850"
FT   CHAIN           42..514
FT                   /note="Alanine--glyoxylate aminotransferase 2,
FT                   mitochondrial"
FT                   /id="PRO_0000001269"
FT   MOD_RES         71
FT                   /note="N6-acetyllysine; alternate"
FT                   /evidence="ECO:0000250|UniProtKB:Q3UEG6"
FT   MOD_RES         71
FT                   /note="N6-succinyllysine; alternate"
FT                   /evidence="ECO:0000250|UniProtKB:Q3UEG6"
FT   MOD_RES         84
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:Q3UEG6"
FT   MOD_RES         262
FT                   /note="N6-acetyllysine; alternate"
FT                   /evidence="ECO:0000250|UniProtKB:Q3UEG6"
FT   MOD_RES         262
FT                   /note="N6-succinyllysine; alternate"
FT                   /evidence="ECO:0000250|UniProtKB:Q3UEG6"
FT   MOD_RES         304
FT                   /note="N6-succinyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:Q3UEG6"
FT   MOD_RES         350
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         417
FT                   /note="N6-acetyllysine; alternate"
FT                   /evidence="ECO:0000250|UniProtKB:Q3UEG6"
FT   MOD_RES         417
FT                   /note="N6-succinyllysine; alternate"
FT                   /evidence="ECO:0000250|UniProtKB:Q3UEG6"
FT   MOD_RES         420
FT                   /note="N6-acetyllysine; alternate"
FT                   /evidence="ECO:0000250|UniProtKB:Q3UEG6"
FT   MOD_RES         420
FT                   /note="N6-succinyllysine; alternate"
FT                   /evidence="ECO:0000250|UniProtKB:Q3UEG6"
FT   VAR_SEQ         321..395
FT                   /note="Missing (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:15489334"
FT                   /id="VSP_055802"
FT   VARIANT         102
FT                   /note="S -> I (in dbSNP:rs37370)"
FT                   /id="VAR_061006"
FT   VARIANT         102
FT                   /note="S -> N (in dbSNP:rs37370)"
FT                   /evidence="ECO:0000269|PubMed:15489334, ECO:0000269|Ref.2,
FT                   ECO:0000269|Ref.3"
FT                   /id="VAR_023483"
FT   VARIANT         102
FT                   /note="S -> T (in dbSNP:rs37370)"
FT                   /id="VAR_061007"
FT   VARIANT         132
FT                   /note="G -> R (in dbSNP:rs16870794)"
FT                   /id="VAR_048231"
FT   VARIANT         140
FT                   /note="V -> I (probable risk factor for
FT                   beta-aminoisobutyric aciduria; probable risk for coronary
FT                   heart disease in smoker and diabetic patients in a Chinese
FT                   population; localized to the mitochondrion as the
FT                   wild-type; reduces alanine-glyoxylate aminotransferase
FT                   activity; dbSNP:rs37369)"
FT                   /evidence="ECO:0000269|PubMed:24586340,
FT                   ECO:0000269|PubMed:24834905, ECO:0000269|Ref.2,
FT                   ECO:0000269|Ref.3"
FT                   /id="VAR_022140"
FT   VARIANT         212
FT                   /note="T -> I (in dbSNP:rs180749)"
FT                   /evidence="ECO:0000269|PubMed:15489334, ECO:0000269|Ref.2,
FT                   ECO:0000269|Ref.3"
FT                   /id="VAR_022141"
FT   VARIANT         492
FT                   /note="P -> R (in dbSNP:rs17245714)"
FT                   /id="VAR_048232"
FT   VARIANT         498
FT                   /note="V -> L (in dbSNP:rs16899974)"
FT                   /evidence="ECO:0000269|PubMed:24586340, ECO:0000269|Ref.3"
FT                   /id="VAR_029513"
SQ   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
//