AGT1_CALJA
ID AGT1_CALJA Reviewed; 414 AA.
AC P31029;
DT 01-JUL-1993, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-1993, sequence version 1.
DT 03-AUG-2022, entry version 127.
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 Callithrix jacchus (White-tufted-ear marmoset).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Platyrrhini; Cebidae;
OC Callitrichinae; Callithrix; Callithrix.
OX NCBI_TaxID=9483;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND SUBCELLULAR LOCATION.
RX PubMed=1339350; DOI=10.1111/j.1432-1033.1992.tb17106.x;
RA Purdue P.E., Lumb M.J., Danpure C.J.;
RT "Molecular evolution of alanine/glyoxylate aminotransferase 1 intracellular
RT targeting. Analysis of the marmoset and rabbit genes.";
RL Eur. J. Biochem. 207:757-766(1992).
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:0000305|PubMed:1339350}.
CC -!- SUBCELLULAR LOCATION: [Isoform Mitochondrial]: Mitochondrion matrix
CC {ECO:0000305|PubMed:1339350}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative initiation; Named isoforms=2;
CC Name=Mitochondrial {ECO:0000303|PubMed:1339350};
CC IsoId=P31029-1; Sequence=Displayed;
CC Name=Peroxisomal {ECO:0000303|PubMed:1339350};
CC IsoId=P31029-2; Sequence=VSP_018642;
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; M84414; AAA35397.1; -; mRNA.
DR PIR; S24154; S24154.
DR RefSeq; XP_002750020.2; XM_002749974.3. [P31029-1]
DR AlphaFoldDB; P31029; -.
DR SMR; P31029; -.
DR STRING; 9483.ENSCJAP00000011833; -.
DR GeneID; 100390388; -.
DR KEGG; cjc:100390388; -.
DR CTD; 189; -.
DR eggNOG; KOG2862; Eukaryota.
DR HOGENOM; CLU_027686_0_0_1; -.
DR InParanoid; P31029; -.
DR OMA; KNWLPIM; -.
DR OrthoDB; 984738at2759; -.
DR TreeFam; TF313234; -.
DR Proteomes; UP000008225; Chromosome 6.
DR Bgee; ENSCJAG00000006403; Expressed in liver and 4 other tissues.
DR GO; GO:0005759; C:mitochondrial matrix; IEA:UniProtKB-SubCell.
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; IEA:UniProtKB-EC.
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: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 CHAIN 24..414
FT /note="Alanine--glyoxylate aminotransferase"
FT /id="PRO_0000001284"
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 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_018642"
SQ SEQUENCE 414 AA; 45054 MW; 604866DA42EEDDE1 CRC64;
MFQALAKASA ALGPRAAGWV RTMASHQLLV APPKALLKPL SIPTRLLLGP GPSNLPPRTM
AAGGLQMLGH MHKETYQIMD EIKEGIQYVF QTRNPLTLVI SGSGHCALEA ALINVLEPGD
SFLVGVNGIW GQRAADIGER LGARVHPMTK DPGGHYTLQE VEEGLAQHKP VLLFLTHGES
SSGVLQPLDG FGELCHRYKC LLLVDSVASL GGAPLYMDQQ GIDILYSGSQ KVLNAPPGTS
LLSFSDTAKN KIYSRKTKPS SFYLDVKYLA NLWGCDGQPR MYHHTTPVVS LYSLREGLAL
LSEQGLENSW RKHREAAAYL HGRLQALGLR LFVKDPALRL PTVTTVAVPT GYDWRDIVSY
LIERFGIEIT GGLGPSTGKV LRIGLMGCNA TRENVDLVTE ALREALQHCP KKKL
