AGT1_FELCA
ID AGT1_FELCA Reviewed; 414 AA.
AC P41689;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1995, sequence version 1.
DT 03-AUG-2022, entry version 120.
DE RecName: Full=Alanine--glyoxylate aminotransferase {ECO:0000250|UniProtKB:P21549};
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:0000250|UniProtKB:P21549}; Synonyms=AGT1;
OS Felis catus (Cat) (Felis silvestris catus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Carnivora; Feliformia; Felidae; Felinae; Felis.
OX NCBI_TaxID=9685;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND SUBCELLULAR LOCATION.
RC TISSUE=Liver;
RX PubMed=8168541; DOI=10.1111/j.1432-1033.1994.tb18714.x;
RA Lumb M.J., Purdue P.E., Danpure C.J.;
RT "Molecular evolution of alanine/glyoxylate aminotransferase 1 intracellular
RT targeting. Analysis of the feline gene.";
RL Eur. J. Biochem. 221:53-62(1994).
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 contributes to gluconeogenesis from the L-
CC 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:0000305|PubMed:8168541}. Note=More than 90% are mitochondrial.
CC {ECO:0000305|PubMed:8168541}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative initiation; Named isoforms=2;
CC Name=Mitochondrial;
CC IsoId=P41689-1; Sequence=Displayed;
CC Name=Peroxisomal;
CC IsoId=P41689-2; Sequence=VSP_018643;
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; X75923; CAA53527.1; -; mRNA.
DR PIR; S43253; S43253.
DR RefSeq; NP_001036031.1; NM_001042566.1. [P41689-1]
DR AlphaFoldDB; P41689; -.
DR SMR; P41689; -.
DR STRING; 9685.ENSFCAP00000009698; -.
DR Ensembl; ENSFCAT00000043147; ENSFCAP00000036433; ENSFCAG00000010448. [P41689-1]
DR GeneID; 727692; -.
DR KEGG; fca:727692; -.
DR CTD; 189; -.
DR eggNOG; KOG2862; Eukaryota.
DR GeneTree; ENSGT00940000153241; -.
DR InParanoid; P41689; -.
DR OrthoDB; 984738at2759; -.
DR SABIO-RK; P41689; -.
DR Proteomes; UP000011712; Chromosome C1.
DR Bgee; ENSFCAG00000010448; Expressed in liver and 4 other tissues.
DR GO; GO:0005759; C:mitochondrial matrix; IEA:UniProtKB-SubCell.
DR GO; GO:0005739; C:mitochondrion; TAS:HGNC-UCL.
DR GO; GO:0005782; C:peroxisomal matrix; IEA:Ensembl.
DR GO; GO:0005777; C:peroxisome; ISS:UniProtKB.
DR GO; GO:0008453; F:alanine-glyoxylate transaminase activity; ISS:UniProtKB.
DR GO; GO:0016597; F:amino acid binding; IEA:Ensembl.
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; IEA:Ensembl.
DR GO; GO:0004760; F:serine-pyruvate transaminase activity; IBA:GO_Central.
DR GO; GO:0019265; P:glycine biosynthetic process, by transamination of glyoxylate; IBA:GO_Central.
DR GO; GO:0009436; P:glyoxylate catabolic process; IEA:Ensembl.
DR GO; GO:0046487; P:glyoxylate metabolic process; ISS:UniProtKB.
DR GO; GO:0042853; P:L-alanine catabolic process; IEA:Ensembl.
DR GO; GO:0019448; P:L-cysteine catabolic process; IEA:Ensembl.
DR GO; GO:0006563; P:L-serine metabolic process; IEA:Ensembl.
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 2: Evidence at transcript level;
KW Acetylation; Alternative initiation; Aminotransferase; Mitochondrion;
KW Peroxisome; Pyridoxal phosphate; Reference proteome; Transferase;
KW Transit peptide.
FT TRANSIT 1..23
FT /note="Mitochondrion"
FT /evidence="ECO:0000250"
FT CHAIN 24..414
FT /note="Alanine--glyoxylate aminotransferase"
FT /id="PRO_0000001286"
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_018643"
SQ SEQUENCE 414 AA; 45508 MW; 0D1B01E0E9A199B3 CRC64;
MFRALARASA TLGPQVAGWA RTMATCQLLV APPEALLRPL SIPNRLLLGP GPSNLAPRVL
VAGGKQMIGH MHKEMFQIMD DIKQGIQYVF QTKNPLTLAI SGSGHCALEA ALFNILEPGD
PFLVGVNGIW GQRAADIGER IGARVHPMIK DPGNHYTLQE LEEALAQHKP VLLFLTQGES
SSGVLQPLDG YGELCHRYNC LLLVDSVASL CGTPIYMDQQ GIDVLYSGSQ KVLNSPPGTS
LISFSDKAKN KIYTRKTKPV SFYLDMKWLA NIWGCDGKPR IYHHTTPVVS LYSLRESLAL
IAEQGLENSW RQHREVTAYL HGRLQGLGLQ LFVKDPALRL PTVTTVAVPA GYDWRDIVNY
VMDHFDIEIT GGLGPSMGKV LRIGLLGCNA TRENVDRVIQ ALQEALQRCS RNKL
