AGT1_PONAB
ID AGT1_PONAB Reviewed; 392 AA.
AC Q5RDP0;
DT 28-NOV-2006, integrated into UniProtKB/Swiss-Prot.
DT 21-DEC-2004, sequence version 1.
DT 03-AUG-2022, entry version 81.
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 {ECO:0000250|UniProtKB:P21549};
DE Short=SPT;
DE EC=2.6.1.51;
GN Name=AGXT {ECO:0000250|UniProtKB:P21549};
OS Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Pongo.
OX NCBI_TaxID=9601;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Liver;
RG The German cDNA consortium;
RL Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Peroxisomal aminotransferase that catalyzes the
CC transamination of glyoxylate to glycine and contributes to the
CC glyoxylate detoxification. Also catalyzes the transamination between L-
CC serine and pyruvate and contributes to gluconeogenesis from the L-
CC serine metabolism. {ECO:0000250|UniProtKB:P21549}.
CC -!- CATALYTIC ACTIVITY:
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:P21549};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:22853;
CC Evidence={ECO:0000250|UniProtKB:P21549};
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: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: Peroxisome {ECO:0000250|UniProtKB:P21549}.
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; CR857864; CAH90117.1; -; mRNA.
DR RefSeq; NP_001125018.1; NM_001131546.1.
DR AlphaFoldDB; Q5RDP0; -.
DR SMR; Q5RDP0; -.
DR GeneID; 100171897; -.
DR KEGG; pon:100171897; -.
DR CTD; 189; -.
DR eggNOG; KOG2862; Eukaryota.
DR InParanoid; Q5RDP0; -.
DR OrthoDB; 984738at2759; -.
DR Proteomes; UP000001595; Unplaced.
DR GO; GO:0005777; C:peroxisome; ISS:UniProtKB.
DR GO; GO:0008453; F:alanine-glyoxylate transaminase activity; ISS:UniProtKB.
DR GO; GO:0042803; F:protein homodimerization activity; ISS:UniProtKB.
DR GO; GO:0043621; F:protein self-association; ISS:UniProtKB.
DR GO; GO:0004760; F:serine-pyruvate transaminase activity; IEA:UniProtKB-EC.
DR GO; GO:0046487; P:glyoxylate metabolic process; ISS:UniProtKB.
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; Aminotransferase; Peroxisome; Pyridoxal phosphate;
KW Reference proteome; Transferase.
FT CHAIN 1..392
FT /note="Alanine--glyoxylate aminotransferase"
FT /id="PRO_0000260250"
FT MOTIF 390..392
FT /note="Microbody targeting signal"
FT BINDING 360
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT MOD_RES 209
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000250"
FT MOD_RES 225
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:O35423"
FT MOD_RES 225
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:O35423"
FT MOD_RES 234
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:O35423"
FT MOD_RES 312
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:O35423"
SQ SEQUENCE 392 AA; 43155 MW; DF2E465AE6968493 CRC64;
MASHKLLVHP PKALLKPLSI PNRLLLGPGP SNLAPRIMAA GGLQIIGPMS KDMYQIMDEI
KEGIRYVFQT RNPLTLVISG SAHCALEAAL VNVLEPGDSF LVGANGIWGQ RAVDIGERMG
ARVHPMTKDP GGHYTLQEVE EGLAQHKPVL LFLTHGESST GVLQPLDGFG ELCHRYKCLL
LVDSVVSVGG TPVYMDQQGI DILYSGSQKA LNAPPGTSLI SFSDKAKKKM YSRKTKPFSF
YLDIKWLANF WGCDDQPRMY HHTIPIISLY SLRESLALIA EQGLENSWRK HREAAAYLHG
RLQALGLQLF VKDPALRLPT VTTVAVPAGY DWRDIVSYVM DHFDIEIMGG LGPPTGKVLR
IGLLGYNATH ENVDRVTEAL RAALQHCPKK KL
