ID H7BWY3_MOUSE Unreviewed; 541 AA.
AC H7BWY3;
DT 18-APR-2012, integrated into UniProtKB/TrEMBL.
DT 18-APR-2012, sequence version 1.
DT 27-MAR-2024, entry version 81.
DE RecName: Full=Alanine--glyoxylate aminotransferase 2, mitochondrial {ECO:0000256|ARBA:ARBA00039862};
DE EC=2.6.1.18 {ECO:0000256|ARBA:ARBA00044055};
DE EC=2.6.1.40 {ECO:0000256|ARBA:ARBA00039130};
DE EC=2.6.1.44 {ECO:0000256|ARBA:ARBA00013049};
DE AltName: Full=(R)-3-amino-2-methylpropionate--pyruvate transaminase {ECO:0000256|ARBA:ARBA00041662};
DE AltName: Full=Beta-ALAAT II {ECO:0000256|ARBA:ARBA00042611};
DE AltName: Full=Beta-alanine-pyruvate aminotransferase {ECO:0000256|ARBA:ARBA00042669};
DE AltName: Full=D-3-aminoisobutyrate-pyruvate aminotransferase {ECO:0000256|ARBA:ARBA00044258};
DE AltName: Full=D-AIBAT {ECO:0000256|ARBA:ARBA00041845};
DE AltName: Full=D-beta-aminoisobutyrate-pyruvate aminotransferase {ECO:0000256|ARBA:ARBA00044257};
GN Name=Agxt2 {ECO:0000313|Ensembl:ENSMUSP00000022858.8,
GN ECO:0000313|MGI:MGI:2146052};
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090 {ECO:0000313|Ensembl:ENSMUSP00000022858.8, ECO:0000313|Proteomes:UP000000589};
RN [1] {ECO:0000313|Ensembl:ENSMUSP00000022858.8, ECO:0000313|Proteomes:UP000000589}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J {ECO:0000313|Ensembl:ENSMUSP00000022858.8,
RC ECO:0000313|Proteomes:UP000000589};
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [2] {ECO:0007829|PubMed:21183079}
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [3] {ECO:0007829|PubMed:23806337}
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=23806337; DOI=10.1016/j.molcel.2013.06.001;
RA Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y.,
RA Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.;
RT "SIRT5-mediated lysine desuccinylation impacts diverse metabolic
RT pathways.";
RL Mol. Cell 50:919-930(2013).
RN [4] {ECO:0007829|PubMed:23576753}
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=23576753; DOI=10.1073/pnas.1302961110;
RA Rardin M.J., Newman J.C., Held J.M., Cusack M.P., Sorensen D.J., Li B.,
RA Schilling B., Mooney S.D., Kahn C.R., Verdin E., Gibson B.W.;
RT "Label-free quantitative proteomics of the lysine acetylome in mitochondria
RT identifies substrates of SIRT3 in metabolic pathways.";
RL Proc. Natl. Acad. Sci. U.S.A. 110:6601-6606(2013).
RN [5] {ECO:0000313|Ensembl:ENSMUSP00000022858.8}
RP IDENTIFICATION.
RC STRAIN=C57BL/6J {ECO:0000313|Ensembl:ENSMUSP00000022858.8};
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
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:0000256|ARBA:ARBA00043679};
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:0000256|ARBA:ARBA00043726};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:18394;
CC Evidence={ECO:0000256|ARBA:ARBA00043726};
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:0000256|ARBA:ARBA00043751};
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:0000256|ARBA:ARBA00043779};
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:0000256|ARBA:ARBA00043837};
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:0000256|ARBA:ARBA00043826};
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:0000256|ARBA:ARBA00043825};
CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:14079;
CC Evidence={ECO:0000256|ARBA:ARBA00043825};
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:0000256|ARBA:ARBA00043764};
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:0000256|ARBA:ARBA00043777};
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:0000256|ARBA:ARBA00043798};
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:0000256|ARBA:ARBA00043749};
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:0000256|ARBA:ARBA00043669};
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:0000256|ARBA:ARBA00043758};
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:0000256|ARBA:ARBA00033660};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:24249;
CC Evidence={ECO:0000256|ARBA:ARBA00033660};
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:0000256|ARBA:ARBA00043808};
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:0000256|ARBA:ARBA00043659};
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:0000256|ARBA:ARBA00043815};
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:0000256|ARBA:ARBA00043652};
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000256|ARBA:ARBA00001933};
CC -!- SIMILARITY: Belongs to the class-III pyridoxal-phosphate-dependent
CC aminotransferase family. {ECO:0000256|ARBA:ARBA00008954,
CC ECO:0000256|RuleBase:RU003560}.
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DR RefSeq; NP_001027021.1; NM_001031851.1.
DR AlphaFoldDB; H7BWY3; -.
DR SMR; H7BWY3; -.
DR SwissPalm; H7BWY3; -.
DR jPOST; H7BWY3; -.
DR MaxQB; H7BWY3; -.
DR ProteomicsDB; 350978; -.
DR Antibodypedia; 43482; 155 antibodies from 26 providers.
DR DNASU; 268782; -.
DR Ensembl; ENSMUST00000022858.8; ENSMUSP00000022858.8; ENSMUSG00000089678.9.
DR GeneID; 268782; -.
DR UCSC; uc007vfz.1; mouse.
DR AGR; MGI:2146052; -.
DR CTD; 64902; -.
DR MGI; MGI:2146052; Agxt2.
DR VEuPathDB; HostDB:ENSMUSG00000089678; -.
DR GeneTree; ENSGT00940000156125; -.
DR OMA; MVPGFKY; -.
DR OrthoDB; 345661at2759; -.
DR PhylomeDB; H7BWY3; -.
DR TreeFam; TF105945; -.
DR BioGRID-ORCS; 268782; 2 hits in 63 CRISPR screens.
DR ChiTaRS; Agxt2; mouse.
DR Proteomes; UP000000589; Chromosome 15.
DR Bgee; ENSMUSG00000089678; Expressed in left lobe of liver and 21 other cell types or tissues.
DR ExpressionAtlas; H7BWY3; baseline and differential.
DR GO; GO:0005739; C:mitochondrion; IEA:UniProtKB-KW.
DR GO; GO:0047305; F:(R)-3-amino-2-methylpropionate-pyruvate transaminase activity; IEA:Ensembl.
DR GO; GO:0008453; F:alanine-glyoxylate transaminase activity; IEA:Ensembl.
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; IEA:Ensembl.
DR GO; GO:0009436; P:glyoxylate catabolic process; IEA:Ensembl.
DR GO; GO:0019481; P:L-alanine catabolic process, by transamination; IEA:Ensembl.
DR GO; GO:2001299; P:N(omega),N(omega)-dimethyl-L-arginine catabolic process; IEA:Ensembl.
DR GO; GO:0045429; P:positive regulation of nitric oxide biosynthetic process; IEA:Ensembl.
DR CDD; cd00610; OAT_like; 1.
DR Gene3D; 3.90.1150.10; Aspartate Aminotransferase, domain 1; 2.
DR Gene3D; 3.40.640.10; Type I PLP-dependent aspartate aminotransferase-like (Major domain); 2.
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; 2.
DR SUPFAM; SSF53383; PLP-dependent transferases; 1.
DR PROSITE; PS00600; AA_TRANSFER_CLASS_3; 1.
PE 1: Evidence at protein level;
KW Mitochondrion {ECO:0000256|ARBA:ARBA00023128};
KW Proteomics identification {ECO:0007829|MaxQB:H7BWY3,
KW ECO:0007829|PeptideAtlas:H7BWY3};
KW Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW ECO:0000256|RuleBase:RU003560};
KW Reference proteome {ECO:0000313|Proteomes:UP000000589}.
SQ SEQUENCE 541 AA; 60100 MW; 604604FD9C69DBC7 CRC64;
MSLAWRNLQK PFYLETSLRI LQMRPSLSLG ASRIAVPKLT LHTKHSMPPC DFSPEKYQSL
AYSRVLAIHK QHLSPVDTAY FRKPLLLHQG HMEWLFDSEG NRYLDFFSGI VTVSVGHCHP
KVSAVAKKQI DRLWHTSSVF FHSPMHEYAE KLSALLPEPL KVIFLVNSGS EANDLAMVMA
RAHSNHTDII SFRGAYHGCS PYTLGLTNVG IYKMEVPGGI GCQSTMCPDV FRGPWGGIHC
RDSPVQTVRD CSCAPGPNGQ GGRRECHSNI KCCDLCMCVC FATDCCQAKE RYIEQFKDTL
NTSVATSIAG FFAEPIQGVN GVVQYPKEFL KEAFALVRER GGVCIADEVQ TGFGRLGSHF
WGFQTHDVLP DIVTMAKGIG NGFPMAAVVT TPEIAKSLAK RLLHFSTFGG NPLACAIGSA
VLEVIEEENL QRNSQEVGTY MLLKFAKLRD EFDIVGDVRG KGLMVGIEMV QDKISRQPLP
KTEVNQIHED CKDMGLLVGR GGNFSQTFRI VPPMCVTKME VDFAYEVFRA ALIQHMERRA
K
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