ID   AGT2_PONAB              Reviewed;         514 AA.
AC   Q5RFA3;
DT   13-SEP-2005, integrated into UniProtKB/Swiss-Prot.
DT   21-DEC-2004, sequence version 1.
DT   03-AUG-2022, entry version 87.
DE   RecName: Full=Alanine--glyoxylate aminotransferase 2, mitochondrial;
DE            Short=AGT 2;
DE            EC=2.6.1.44;
DE   AltName: Full=(R)-3-amino-2-methylpropionate--pyruvate transaminase;
DE            EC=2.6.1.40;
DE   AltName: Full=Beta-ALAAT II;
DE   AltName: Full=Beta-alanine-pyruvate aminotransferase;
DE   AltName: Full=D-AIBAT;
DE   Flags: Precursor;
GN   Name=AGXT2;
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=Kidney;
RG   The German cDNA consortium;
RL   Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Can metabolize asymmetric dimethylarginine (ADMA) via
CC       transamination to alpha-keto-delta-(NN-dimethylguanidino) valeric acid
CC       (DMGV). ADMA is a potent inhibitor of nitric-oxide (NO) synthase, and
CC       this activity provides mechanism through which the kidney regulates
CC       blood pressure (By similarity). {ECO:0000250|UniProtKB:Q9BYV1}.
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   -!- CATALYTIC ACTIVITY:
CC       Reaction=(R)-3-amino-2-methylpropanoate + pyruvate = 2-methyl-3-
CC         oxopropanoate + L-alanine; Xref=Rhea:RHEA:18393, ChEBI:CHEBI:15361,
CC         ChEBI:CHEBI:57700, ChEBI:CHEBI:57731, ChEBI:CHEBI:57972; EC=2.6.1.40;
CC   -!- COFACTOR:
CC       Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC         Evidence={ECO:0000250};
CC   -!- SUBUNIT: Homotetramer. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000250|UniProtKB:Q9BYV1}.
CC   -!- SIMILARITY: Belongs to the class-III pyridoxal-phosphate-dependent
CC       aminotransferase family. {ECO:0000305}.
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DR   EMBL; CR857258; CAH89554.1; -; mRNA.
DR   RefSeq; NP_001124677.1; NM_001131205.2.
DR   AlphaFoldDB; Q5RFA3; -.
DR   SMR; Q5RFA3; -.
DR   STRING; 9601.ENSPPYP00000017192; -.
DR   GeneID; 100171524; -.
DR   KEGG; pon:100171524; -.
DR   CTD; 64902; -.
DR   eggNOG; KOG1404; Eukaryota.
DR   InParanoid; Q5RFA3; -.
DR   OrthoDB; 145181at2759; -.
DR   Proteomes; UP000001595; Unplaced.
DR   GO; GO:0005759; C:mitochondrial matrix; IEA:UniProt.
DR   GO; GO:0005739; C:mitochondrion; ISS:UniProtKB.
DR   GO; GO:0047305; F:(R)-3-amino-2-methylpropionate-pyruvate transaminase activity; IEA:UniProtKB-EC.
DR   GO; GO:0008453; F:alanine-glyoxylate transaminase activity; ISS:UniProtKB.
DR   GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR   CDD; cd00610; OAT_like; 1.
DR   Gene3D; 3.40.640.10; -; 1.
DR   Gene3D; 3.90.1150.10; -; 1.
DR   InterPro; IPR005814; Aminotrans_3.
DR   InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR   InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR   InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
DR   Pfam; PF00202; Aminotran_3; 1.
DR   PIRSF; PIRSF000521; Transaminase_4ab_Lys_Orn; 1.
DR   SUPFAM; SSF53383; SSF53383; 1.
DR   PROSITE; PS00600; AA_TRANSFER_CLASS_3; 1.
PE   2: Evidence at transcript level;
KW   Acetylation; Aminotransferase; Mitochondrion; Pyridoxal phosphate;
KW   Reference proteome; Transferase; Transit peptide.
FT   TRANSIT         1..41
FT                   /note="Mitochondrion"
FT                   /evidence="ECO:0000250"
FT   CHAIN           42..514
FT                   /note="Alanine--glyoxylate aminotransferase 2,
FT                   mitochondrial"
FT                   /id="PRO_0000041878"
FT   MOD_RES         71
FT                   /note="N6-acetyllysine; alternate"
FT                   /evidence="ECO:0000250|UniProtKB:Q3UEG6"
FT   MOD_RES         71
FT                   /note="N6-succinyllysine; alternate"
FT                   /evidence="ECO:0000250|UniProtKB:Q3UEG6"
FT   MOD_RES         84
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:Q3UEG6"
FT   MOD_RES         262
FT                   /note="N6-acetyllysine; alternate"
FT                   /evidence="ECO:0000250|UniProtKB:Q3UEG6"
FT   MOD_RES         262
FT                   /note="N6-succinyllysine; alternate"
FT                   /evidence="ECO:0000250|UniProtKB:Q3UEG6"
FT   MOD_RES         304
FT                   /note="N6-succinyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:Q3UEG6"
FT   MOD_RES         350
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         420
FT                   /note="N6-acetyllysine; alternate"
FT                   /evidence="ECO:0000250|UniProtKB:Q3UEG6"
FT   MOD_RES         420
FT                   /note="N6-succinyllysine; alternate"
FT                   /evidence="ECO:0000250|UniProtKB:Q3UEG6"
SQ   SEQUENCE   514 AA;  57344 MW;  02EBDB1A37569F58 CRC64;
     MTLIWRHLLR PLCLVTPAPR ILEMRPFLNL GASWTSVTKL SLHTKPRMPP CDFMPERYQS
     LGYNRVLEIH KEHLSPVVTA YFQKPLLLHQ GHMEWLFDAE GNRYLDFFSG IVTVSVGHCH
     PKVNAVAQKQ LGRLWHTSTV FFHPPMHEYA EKLAALLPEP LKVIFLVNSG SEANELAMLM
     ARAHSNNIDI ISFRGAYHGC SPYTLGLTNI GTYKMELPGG TGCQPTMCPD VFRGPWGGSH
     CRDSPVQTIR KCSCAPDCCQ AKDQYIEQFK DTLSTSVAKS IAGFFAEPIQ GVNGVVQYPK
     GFLKEAFELV RARGGVCIAD EVQTGFGRLG SHFRGFQTHD VLPDIVTMAK GIGNGFPMAA
     VVTTPEIAKS LVKRLQHFNT FGGNPMACAI GSAVLEVIKE ENLQENSQEV GTYMLLQFAK
     LRDEFEIVGD VRGKGLMIGI EMVQDKISRR PLPREEVNQI HEDCKHMGLL VGRGSIFSQT
     FRIAPSMCIT KPEVDFAVEV FRSALTQHME RRAK