AGT1_RAT
ID AGT1_RAT Reviewed; 414 AA.
AC P09139; Q9R2C7;
DT 01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-1989, sequence version 1.
DT 03-AUG-2022, entry version 171.
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:0000305};
DE Short=SPT;
DE EC=2.6.1.51 {ECO:0000269|PubMed:10347151};
DE Flags: Precursor;
GN Name=Agxt {ECO:0000312|RGD:2073}; Synonyms=Agt1;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM MITOCHONDRIAL), AND PARTIAL PROTEIN
RP SEQUENCE.
RC TISSUE=Liver;
RX PubMed=2822418; DOI=10.1111/j.1432-1033.1987.tb13451.x;
RA Oda T., Miyajima H., Suzuki Y., Ichiyama A.;
RT "Nucleotide sequence of the cDNA encoding the precursor for mitochondrial
RT serine:pyruvate aminotransferase of rat liver.";
RL Eur. J. Biochem. 168:537-542(1987).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM PEROXISOMAL), ALTERNATIVE INITIATION,
RP AND INDUCTION.
RX PubMed=2332438; DOI=10.1016/s0021-9258(19)39143-4;
RA Oda T., Funai T., Ichiyama A.;
RT "Generation from a single gene of two mRNAs that encode the mitochondrial
RT and peroxisomal serine:pyruvate aminotransferase of rat liver.";
RL J. Biol. Chem. 265:7513-7519(1990).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-141.
RC STRAIN=Wistar;
RX PubMed=8406472; DOI=10.1006/geno.1993.1283;
RA Oda T., Nishiyama K., Ichiyama A.;
RT "Characterization and sequence analysis of rat
RT serine:pyruvate/alanine:glyoxylate aminotransferase gene.";
RL Genomics 17:59-65(1993).
RN [4]
RP SUBCELLULAR LOCATION.
RX PubMed=6725236; DOI=10.1093/oxfordjournals.jbchem.a134673;
RA Oda T., Ichiyama A., Miura S., Mori M.;
RT "Uptake and processing of serine: pyruvate aminotransferase precursor by
RT rat liver mitochondria in vitro and in vivo.";
RL J. Biochem. 95:815-824(1984).
RN [5]
RP FUNCTION (ISOFORM MITOCHONDRIAL), AND CATALYTIC ACTIVITY(ISOFORM
RP MITOCHONDRIAL).
RX PubMed=10347151; DOI=10.1074/jbc.274.23.16020;
RA Xue H.H., Fujie M., Sakaguchi T., Oda T., Ogawa H., Kneer N.M., Lardy H.A.,
RA Ichiyama A.;
RT "Flux of the L-serine metabolism in rat liver. The predominant contribution
RT of serine dehydratase.";
RL J. Biol. Chem. 274:16020-16027(1999).
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:0000269|PubMed:10347151}.
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:0000269|PubMed:10347151};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:22853;
CC Evidence={ECO:0000305|PubMed:10347151};
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:0000269|PubMed:6725236}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative initiation; Named isoforms=2;
CC Name=Mitochondrial {ECO:0000303|PubMed:2822418};
CC IsoId=P09139-1; Sequence=Displayed;
CC Name=Peroxisomal {ECO:0000303|PubMed:2332438};
CC IsoId=P09139-2; Sequence=VSP_018645;
CC -!- INDUCTION: [Isoform Mitochondrial]: Induced by glucagon and insulin.
CC {ECO:0000269|PubMed:2332438}.
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; X06357; CAA29656.1; -; mRNA.
DR EMBL; D13667; BAA02838.1; -; Genomic_DNA.
DR EMBL; M35270; AAA42169.1; -; mRNA.
DR PIR; S00164; XNRTSP.
DR RefSeq; NP_001263635.1; NM_001276706.1. [P09139-2]
DR RefSeq; NP_085914.2; NM_030656.2. [P09139-1]
DR AlphaFoldDB; P09139; -.
DR SMR; P09139; -.
DR STRING; 10116.ENSRNOP00000030340; -.
DR iPTMnet; P09139; -.
DR PhosphoSitePlus; P09139; -.
DR PaxDb; P09139; -.
DR PRIDE; P09139; -.
DR Ensembl; ENSRNOT00000029127; ENSRNOP00000030340; ENSRNOG00000023856. [P09139-1]
DR GeneID; 24792; -.
DR KEGG; rno:24792; -.
DR UCSC; RGD:2073; rat. [P09139-1]
DR CTD; 189; -.
DR RGD; 2073; Agxt.
DR eggNOG; KOG2862; Eukaryota.
DR GeneTree; ENSGT00940000153241; -.
DR HOGENOM; CLU_027686_0_0_1; -.
DR InParanoid; P09139; -.
DR OMA; KNWLPIM; -.
DR PhylomeDB; P09139; -.
DR TreeFam; TF313234; -.
DR BioCyc; MetaCyc:MON-13151; -.
DR Reactome; R-RNO-389661; Glyoxylate metabolism and glycine degradation.
DR Reactome; R-RNO-9033241; Peroxisomal protein import.
DR SABIO-RK; P09139; -.
DR PRO; PR:P09139; -.
DR Proteomes; UP000002494; Chromosome 9.
DR Bgee; ENSRNOG00000023856; Expressed in liver and 1 other tissue.
DR ExpressionAtlas; P09139; baseline and differential.
DR Genevisible; P09139; RN.
DR GO; GO:0005759; C:mitochondrial matrix; IDA:HGNC-UCL.
DR GO; GO:0005739; C:mitochondrion; IDA:RGD.
DR GO; GO:0005782; C:peroxisomal matrix; ISO:RGD.
DR GO; GO:0005777; C:peroxisome; IDA:HGNC-UCL.
DR GO; GO:0008453; F:alanine-glyoxylate transaminase activity; IDA:RGD.
DR GO; GO:0016597; F:amino acid binding; IDA:RGD.
DR GO; GO:0042802; F:identical protein binding; ISO:RGD.
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:RGD.
DR GO; GO:0004760; F:serine-pyruvate transaminase activity; IDA:RGD.
DR GO; GO:0008483; F:transaminase activity; ISO:RGD.
DR GO; GO:0019265; P:glycine biosynthetic process, by transamination of glyoxylate; IDA:RGD.
DR GO; GO:0009436; P:glyoxylate catabolic process; ISO:RGD.
DR GO; GO:0046487; P:glyoxylate metabolic process; ISS:UniProtKB.
DR GO; GO:0042853; P:L-alanine catabolic process; ISO:RGD.
DR GO; GO:0019448; P:L-cysteine catabolic process; ISO:RGD.
DR GO; GO:0006563; P:L-serine metabolic process; ISO:RGD.
DR GO; GO:0007219; P:Notch signaling pathway; ISO:RGD.
DR GO; GO:0046724; P:oxalic acid secretion; ISO:RGD.
DR GO; GO:0042866; P:pyruvate biosynthetic process; IDA:RGD.
DR GO; GO:0051591; P:response to cAMP; IDA:RGD.
DR GO; GO:0051384; P:response to glucocorticoid; IDA:RGD.
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 Acetylation; Alternative initiation; Aminotransferase;
KW Direct protein sequencing; Mitochondrion; Peroxisome; Pyridoxal phosphate;
KW Reference proteome; Transferase; Transit peptide.
FT TRANSIT 1..23
FT /note="Mitochondrion"
FT CHAIN 24..414
FT /note="Alanine--glyoxylate aminotransferase"
FT /id="PRO_0000001290"
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:0000250|UniProtKB:O35423"
FT MOD_RES 247
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:O35423"
FT MOD_RES 256
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:O35423"
FT MOD_RES 334
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:O35423"
FT VAR_SEQ 1..22
FT /note="Missing (in isoform Peroxisomal)"
FT /evidence="ECO:0000305"
FT /id="VSP_018645"
SQ SEQUENCE 414 AA; 45834 MW; 3FBD66ED36C3D9EF CRC64;
MFRMLAKASV TLGSRAASWV RNMGSHQLLV PPPEALSKPL SIPKRLLLGP GPSNLAPRVL
AAGSLRMIGH MQKEMFQIMD EIKQGIQYVF QTRNPLTLVV SGSGHCAMET ALFNLLEPGD
SFLVGTNGIW GIRAAEIAER IGARVHQMIK KPGEHYTLQE VEEGLAQHKP VLLFLTHGES
STGVLQPLDG FGELCHRYQC LLLVDSVASL GGVPIYMDQQ GIDILYSGSQ KVLNAPPGIS
LISFNDKAKS KVYSRKTKPV SFYTDITYLS KLWGCEGKTR VIHHTLPVIS LYCLRESLAL
ISEQGLENSW RRHREATAHL HKCLRELGLK FFVKDPEIRL PTITTVTVPA GYNWRDIVSY
VLDHFNIEIS GGLGPSEDKV LRIGLLGYNA TTENADRVAE ALREALQHCP KNKL
