AGT1_MOUSE
ID AGT1_MOUSE Reviewed; 414 AA.
AC O35423; Q8R128;
DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT 03-APR-2013, sequence version 3.
DT 03-AUG-2022, entry version 165.
DE RecName: Full=Alanine--glyoxylate aminotransferase {ECO:0000305};
DE Short=AGT;
DE EC=2.6.1.44 {ECO:0000250|UniProtKB:P21549};
DE AltName: Full=Serine--pyruvate aminotransferase, mitochondrial {ECO:0000250|UniProtKB:P09139};
DE Short=SPT;
DE EC=2.6.1.51 {ECO:0000250|UniProtKB:P09139};
DE Flags: Precursor;
GN Name=Agxt {ECO:0000312|MGI:MGI:1329033}; Synonyms=Agxt1;
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;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS MITOCHONDRIAL AND PEROXISOMAL).
RX PubMed=11225057; DOI=10.1023/b:scam.0000007142.36524.58;
RA Li X.M., Salido E.C., Shapiro L.J.;
RT "The mouse alanine:glyoxylate aminotransferase gene (Agxt1): cloning,
RT expression, and mapping to chromosome 1.";
RL Somat. Cell Mol. Genet. 25:67-77(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM MITOCHONDRIAL).
RC STRAIN=FVB/N; TISSUE=Liver;
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 [5]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
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 [6]
RP SUCCINYLATION [LARGE SCALE ANALYSIS] AT LYS-247 AND LYS-330, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
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 [7]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-247; LYS-256; LYS-330 AND
RP LYS-334, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
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 [8]
RP X-RAY CRYSTALLOGRAPHY (1.65 ANGSTROMS) OF 23-414.
RG Joint center for structural genomics (JCSG);
RT "Crystal structure of putative aminotransferase (AAH25799.1) from Mus
RT musculus at 1.65 A resolution.";
RL Submitted (OCT-2009) to the PDB data bank.
CC -!- FUNCTION: [Isoform Peroxisomal]: Catalyzes the transamination of
CC glyoxylate to glycine and contributes to the glyoxylate detoxification.
CC {ECO:0000250|UniProtKB:P21549}.
CC -!- FUNCTION: [Isoform Mitochondrial]: Catalyzes the transamination between
CC L-serine and pyruvate and weakly contributes to gluconeogenesis from
CC the L-serine metabolism. {ECO:0000250|UniProtKB:P09139}.
CC -!- CATALYTIC ACTIVITY: [Isoform Mitochondrial]:
CC Reaction=L-serine + pyruvate = 3-hydroxypyruvate + L-alanine;
CC Xref=Rhea:RHEA:22852, ChEBI:CHEBI:15361, ChEBI:CHEBI:17180,
CC ChEBI:CHEBI:33384, ChEBI:CHEBI:57972; EC=2.6.1.51;
CC Evidence={ECO:0000250|UniProtKB:P09139};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:22853;
CC Evidence={ECO:0000250|UniProtKB:P09139};
CC -!- CATALYTIC ACTIVITY: [Isoform Peroxisomal]:
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:P21549};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:24249;
CC Evidence={ECO:0000250|UniProtKB:P21549};
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000250|UniProtKB:P21549};
CC -!- SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:P21549}.
CC -!- SUBCELLULAR LOCATION: [Isoform Peroxisomal]: Peroxisome
CC {ECO:0000250|UniProtKB:P21549}.
CC -!- SUBCELLULAR LOCATION: [Isoform Mitochondrial]: Mitochondrion matrix
CC {ECO:0000250|UniProtKB:P09139}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative initiation; Named isoforms=2;
CC Name=Mitochondrial {ECO:0000303|PubMed:11225057};
CC IsoId=O35423-1; Sequence=Displayed;
CC Name=Peroxisomal {ECO:0000303|PubMed:11225057};
CC IsoId=O35423-2; Sequence=VSP_018644;
CC -!- SIMILARITY: Belongs to the class-V pyridoxal-phosphate-dependent
CC aminotransferase family. {ECO:0000305}.
CC -!- CAUTION: The intracellular compartmentalization of AGTX in mammalian
CC hepatocytes is species dependent. In human and rabbit, AGTX is
CC peroxisomal. In new world monkeys (marmoset) and rodents (rat and
CC mouse), it is distributed approximately evenly between peroxisomes and
CC mitochondria. In carnivores, like cat, the great majority of the enzyme
CC is mitochondrial with only a small proportion being peroxisomal.
CC {ECO:0000305}.
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DR EMBL; AF027730; AAB82001.2; -; mRNA.
DR EMBL; AC110247; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH466520; EDL39972.1; -; Genomic_DNA.
DR EMBL; BC025799; AAH25799.1; -; mRNA.
DR CCDS; CCDS15184.1; -. [O35423-1]
DR RefSeq; NP_057911.2; NM_016702.3. [O35423-1]
DR PDB; 3KGW; X-ray; 1.65 A; A/B=23-414.
DR PDB; 3KGX; X-ray; 1.80 A; A/B=23-414.
DR PDBsum; 3KGW; -.
DR PDBsum; 3KGX; -.
DR AlphaFoldDB; O35423; -.
DR SMR; O35423; -.
DR STRING; 10090.ENSMUSP00000027491; -.
DR iPTMnet; O35423; -.
DR PhosphoSitePlus; O35423; -.
DR SwissPalm; O35423; -.
DR jPOST; O35423; -.
DR PaxDb; O35423; -.
DR PeptideAtlas; O35423; -.
DR PRIDE; O35423; -.
DR ProteomicsDB; 261647; -. [O35423-1]
DR ProteomicsDB; 261648; -. [O35423-2]
DR Antibodypedia; 34535; 320 antibodies from 30 providers.
DR DNASU; 11611; -.
DR Ensembl; ENSMUST00000027491; ENSMUSP00000027491; ENSMUSG00000026272. [O35423-1]
DR GeneID; 11611; -.
DR KEGG; mmu:11611; -.
DR UCSC; uc007cdi.2; mouse. [O35423-1]
DR CTD; 189; -.
DR MGI; MGI:1329033; Agxt.
DR VEuPathDB; HostDB:ENSMUSG00000026272; -.
DR eggNOG; KOG2862; Eukaryota.
DR GeneTree; ENSGT00940000153241; -.
DR HOGENOM; CLU_027686_0_0_1; -.
DR InParanoid; O35423; -.
DR OMA; KNWLPIM; -.
DR PhylomeDB; O35423; -.
DR TreeFam; TF313234; -.
DR Reactome; R-MMU-389661; Glyoxylate metabolism and glycine degradation.
DR Reactome; R-MMU-9033241; Peroxisomal protein import.
DR SABIO-RK; O35423; -.
DR BioGRID-ORCS; 11611; 4 hits in 72 CRISPR screens.
DR ChiTaRS; Agxt; mouse.
DR EvolutionaryTrace; O35423; -.
DR PRO; PR:O35423; -.
DR Proteomes; UP000000589; Chromosome 1.
DR RNAct; O35423; protein.
DR Bgee; ENSMUSG00000026272; Expressed in left lobe of liver and 20 other tissues.
DR Genevisible; O35423; MM.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; ISO:MGI.
DR GO; GO:0005759; C:mitochondrial matrix; ISO:MGI.
DR GO; GO:0005739; C:mitochondrion; ISO:MGI.
DR GO; GO:0005782; C:peroxisomal matrix; ISO:MGI.
DR GO; GO:0005777; C:peroxisome; ISS:UniProtKB.
DR GO; GO:0008453; F:alanine-glyoxylate transaminase activity; IMP:MGI.
DR GO; GO:0016597; F:amino acid binding; ISO:MGI.
DR GO; GO:0042802; F:identical protein binding; ISO:MGI.
DR GO; GO:0042803; F:protein homodimerization activity; ISS:UniProtKB.
DR GO; GO:0043621; F:protein self-association; ISS:UniProtKB.
DR GO; GO:0030170; F:pyridoxal phosphate binding; ISO:MGI.
DR GO; GO:0004760; F:serine-pyruvate transaminase activity; ISO:MGI.
DR GO; GO:0008483; F:transaminase activity; ISO:MGI.
DR GO; GO:0019265; P:glycine biosynthetic process, by transamination of glyoxylate; ISO:MGI.
DR GO; GO:0009436; P:glyoxylate catabolic process; ISO:MGI.
DR GO; GO:0046487; P:glyoxylate metabolic process; IMP:MGI.
DR GO; GO:0042853; P:L-alanine catabolic process; ISO:MGI.
DR GO; GO:0019448; P:L-cysteine catabolic process; ISO:MGI.
DR GO; GO:0006563; P:L-serine metabolic process; ISO:MGI.
DR GO; GO:0007219; P:Notch signaling pathway; IDA:MGI.
DR GO; GO:0046724; P:oxalic acid secretion; IMP:MGI.
DR GO; GO:0042866; P:pyruvate biosynthetic process; ISO:MGI.
DR GO; GO:0051591; P:response to cAMP; ISO:MGI.
DR GO; GO:0051384; P:response to glucocorticoid; ISO:MGI.
DR Gene3D; 3.40.640.10; -; 1.
DR Gene3D; 3.90.1150.10; -; 1.
DR InterPro; IPR000192; Aminotrans_V_dom.
DR InterPro; IPR020578; Aminotrans_V_PyrdxlP_BS.
DR InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
DR InterPro; IPR024169; SP_NH2Trfase/AEP_transaminase.
DR Pfam; PF00266; Aminotran_5; 1.
DR PIRSF; PIRSF000524; SPT; 1.
DR SUPFAM; SSF53383; SSF53383; 1.
DR PROSITE; PS00595; AA_TRANSFER_CLASS_5; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Alternative initiation; Aminotransferase;
KW Mitochondrion; Peroxisome; Pyridoxal phosphate; Reference proteome;
KW Transferase; Transit peptide.
FT TRANSIT 1..23
FT /note="Mitochondrion"
FT CHAIN 25..414
FT /note="Alanine--glyoxylate aminotransferase"
FT /id="PRO_0000001288"
FT MOTIF 412..414
FT /note="Microbody targeting signal"
FT /evidence="ECO:0000250"
FT BINDING 382
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT MOD_RES 231
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000250"
FT MOD_RES 247
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0007744|PubMed:23576753"
FT MOD_RES 247
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0007744|PubMed:23806337"
FT MOD_RES 256
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:23576753"
FT MOD_RES 330
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0007744|PubMed:23576753"
FT MOD_RES 330
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0007744|PubMed:23806337"
FT MOD_RES 334
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:23576753"
FT VAR_SEQ 1..22
FT /note="Missing (in isoform Peroxisomal)"
FT /evidence="ECO:0000303|PubMed:11225057"
FT /id="VSP_018644"
FT CONFLICT 304
FT /note="Q -> R (in Ref. 1; AAB82001)"
FT /evidence="ECO:0000305"
FT CONFLICT 348..349
FT /note="VP -> A (in Ref. 1; AAB82001)"
FT /evidence="ECO:0000305"
FT HELIX 34..37
FT /evidence="ECO:0007829|PDB:3KGW"
FT STRAND 49..51
FT /evidence="ECO:0007829|PDB:3KGW"
FT HELIX 57..62
FT /evidence="ECO:0007829|PDB:3KGW"
FT HELIX 73..90
FT /evidence="ECO:0007829|PDB:3KGW"
FT STRAND 95..101
FT /evidence="ECO:0007829|PDB:3KGW"
FT TURN 104..106
FT /evidence="ECO:0007829|PDB:3KGW"
FT HELIX 107..115
FT /evidence="ECO:0007829|PDB:3KGW"
FT STRAND 121..128
FT /evidence="ECO:0007829|PDB:3KGW"
FT HELIX 129..140
FT /evidence="ECO:0007829|PDB:3KGW"
FT STRAND 144..149
FT /evidence="ECO:0007829|PDB:3KGW"
FT HELIX 158..168
FT /evidence="ECO:0007829|PDB:3KGW"
FT STRAND 171..179
FT /evidence="ECO:0007829|PDB:3KGW"
FT TURN 180..183
FT /evidence="ECO:0007829|PDB:3KGW"
FT HELIX 191..197
FT /evidence="ECO:0007829|PDB:3KGW"
FT STRAND 201..205
FT /evidence="ECO:0007829|PDB:3KGW"
FT TURN 207..212
FT /evidence="ECO:0007829|PDB:3KGW"
FT TURN 217..221
FT /evidence="ECO:0007829|PDB:3KGW"
FT STRAND 224..231
FT /evidence="ECO:0007829|PDB:3KGW"
FT STRAND 240..244
FT /evidence="ECO:0007829|PDB:3KGW"
FT HELIX 246..253
FT /evidence="ECO:0007829|PDB:3KGW"
FT HELIX 266..272
FT /evidence="ECO:0007829|PDB:3KGW"
FT STRAND 276..278
FT /evidence="ECO:0007829|PDB:3KGW"
FT HELIX 288..304
FT /evidence="ECO:0007829|PDB:3KGW"
FT HELIX 306..326
FT /evidence="ECO:0007829|PDB:3KGW"
FT STRAND 331..335
FT /evidence="ECO:0007829|PDB:3KGW"
FT HELIX 336..338
FT /evidence="ECO:0007829|PDB:3KGW"
FT STRAND 341..347
FT /evidence="ECO:0007829|PDB:3KGW"
FT HELIX 354..365
FT /evidence="ECO:0007829|PDB:3KGW"
FT HELIX 374..376
FT /evidence="ECO:0007829|PDB:3KGW"
FT TURN 377..379
FT /evidence="ECO:0007829|PDB:3KGW"
FT STRAND 380..384
FT /evidence="ECO:0007829|PDB:3KGW"
FT HELIX 387..389
FT /evidence="ECO:0007829|PDB:3KGW"
FT HELIX 392..408
FT /evidence="ECO:0007829|PDB:3KGW"
SQ SEQUENCE 414 AA; 45912 MW; A2AB28AC48A292E3 CRC64;
MFRMLAKASV TLGSRAAGWV RTMGSYQLLV PPPEALSKPL SVPTRLLLGP GPSNLAPRVL
AAGSLRMIGH MQKEMLQIME EIKQGIQYVF QTRNPLTLVV SGSGHCAMET ALFNLLEPGD
SFLTGTNGIW GMRAAEIADR IGARVHQMIK KPGEHYTLQE VEEGLAQHKP VLLFLVHGES
STGVVQPLDG FGELCHRYQC LLLVDSVASL GGVPIYMDQQ GIDIMYSSSQ KVLNAPPGIS
LISFNDKAKY KVYSRKTKPV SFYTDITYLA KLWGCEGETR VIHHTTPVTS LYCLRESLAL
IAEQGLENCW RRHREATAHL HKHLQEMGLK FFVKDPEIRL PTITTVTVPA GYNWRDIVSY
VLDHFSIEIS GGLGPTEERV LRIGLLGYNA TTENVDRVAE ALREALQHCP KNKL
