AGT1_RABIT
ID AGT1_RABIT Reviewed; 392 AA.
AC P31030;
DT 01-JUL-1993, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-1993, sequence version 1.
DT 03-AUG-2022, entry version 107.
DE RecName: Full=Alanine--glyoxylate aminotransferase;
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 {ECO:0000269|PubMed:10347152};
GN Name=AGXT {ECO:0000250|UniProtKB:P21549}; Synonyms=AGT1;
OS Oryctolagus cuniculus (Rabbit).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Lagomorpha; Leporidae; Oryctolagus.
OX NCBI_TaxID=9986;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Liver;
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).
RN [2]
RP MICROBODY TARGETING SIGNAL.
RX PubMed=7559790; DOI=10.1083/jcb.131.1.95;
RA Motley A., Lumb M.J., Oatey P.B., Jennings P.R., de Zoysa P.A.,
RA Wanders R.J.A., Tabak H.F., Danpure C.J.;
RT "Mammalian alanine/glyoxylate aminotransferase 1 is imported into
RT peroxisomes via the PTS1 translocation pathway. Increased degeneracy and
RT context specificity of the mammalian PTS1 motif and implications for the
RT peroxisome-to-mitochondrion mistargeting of AGT in primary hyperoxaluria
RT type 1.";
RL J. Cell Biol. 131:95-109(1995).
RN [3]
RP FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=10347152; DOI=10.1074/jbc.274.23.16028;
RA Xue H.H., Sakaguchi T., Fujie M., Ogawa H., Ichiyama A.;
RT "Flux of the L-serine metabolism in rabbit, human, and dog livers.
RT Substantial contributions of both mitochondrial and peroxisomal
RT serine:pyruvate/alanine:glyoxylate aminotransferase.";
RL J. Biol. Chem. 274:16028-16033(1999).
CC -!- FUNCTION: Peroxisomal aminotransferase that catalyzes the
CC transamination of glyoxylate to glycine and contributes to the
CC glyoxylate detoxification (By similarity). Also catalyzes the
CC transamination between L-serine and pyruvate and contributes to
CC gluconeogenesis from the L-serine metabolism (PubMed:10347152).
CC {ECO:0000250|UniProtKB:P21549, ECO:0000269|PubMed:10347152}.
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:0000269|PubMed:10347152};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:22853;
CC Evidence={ECO:0000269|PubMed:10347152};
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; M84647; AAA31158.1; -; mRNA.
DR PIR; S24155; S24155.
DR RefSeq; NP_001075778.1; NM_001082309.1.
DR AlphaFoldDB; P31030; -.
DR SMR; P31030; -.
DR STRING; 9986.ENSOCUP00000022506; -.
DR PRIDE; P31030; -.
DR GeneID; 100009147; -.
DR KEGG; ocu:100009147; -.
DR CTD; 189; -.
DR eggNOG; KOG2862; Eukaryota.
DR InParanoid; P31030; -.
DR OrthoDB; 984738at2759; -.
DR Proteomes; UP000001811; 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; IDA:UniProtKB.
DR GO; GO:0046487; P:glyoxylate metabolic process; ISS:UniProtKB.
DR GO; GO:0006563; P:L-serine metabolic process; IDA: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 1: Evidence at protein level;
KW Acetylation; Aminotransferase; Peroxisome; Pyridoxal phosphate;
KW Reference proteome; Transferase.
FT CHAIN 1..392
FT /note="Alanine--glyoxylate aminotransferase"
FT /id="PRO_0000150238"
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; 43148 MW; 5261DD14564582D3 CRC64;
MASRQLLVAP PEALRKPLCT PHRLLLGPGP SNLPPRVLAA GGLQMIGHMH EEMYQVMDEI
KQGIQYAFQT RNALTLAVSG SGHCALETAL FNLLEPGDAF LVGANGIWGQ RAAEVGERIG
ARVHPMIKDP GSHYTLQEVE ECLAQHKPVL LFLTHGESST GVLQPLDGFG ELCHRYKCLL
LVDSVASLGG APIYMDQQGI DVLYSGSQKA LNAPPGTSLI SFSDKAKSKI YARKTKPFSF
YMDVQLLANI WGCDGKPRMY HHTTPVIGIF ALRESLALLV EQGLEKSWQR HREVAQHLYR
RLQELGLQLF VKDPALRLPT VTTVIVPASY RWRDIVSYVM HHFGIEITGG LGPSADKVLR
IGLLGCNATR ENVDRLATAL REALQHCAQS QL
