AGT2_BOVIN
ID AGT2_BOVIN Reviewed; 514 AA.
AC Q17QF0;
DT 15-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT 25-JUL-2006, sequence version 1.
DT 03-AUG-2022, entry version 92.
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 Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Hereford; TISSUE=Fetal liver;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (JUN-2006) 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; BC118402; AAI18403.1; -; mRNA.
DR RefSeq; NP_001069289.1; NM_001075821.2.
DR AlphaFoldDB; Q17QF0; -.
DR SMR; Q17QF0; -.
DR STRING; 9913.ENSBTAP00000010113; -.
DR PaxDb; Q17QF0; -.
DR GeneID; 521553; -.
DR KEGG; bta:521553; -.
DR CTD; 64902; -.
DR eggNOG; KOG1404; Eukaryota.
DR InParanoid; Q17QF0; -.
DR OrthoDB; 145181at2759; -.
DR Proteomes; UP000009136; Unplaced.
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 GO; GO:0009436; P:glyoxylate catabolic process; IBA:GO_Central.
DR GO; GO:0019481; P:L-alanine catabolic process, by transamination; IBA:GO_Central.
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_0000292950"
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 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 417
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q3UEG6"
FT MOD_RES 417
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q3UEG6"
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; 57226 MW; 0DBDF242C3D338C5 CRC64;
MTGAWGHLLR SLHLKTLSLW IPKTCFSLKA RAFWTSVTRC GLHTKPSMPP CDFTPERYQS
LAYSRVLEIH KQHLSPVHTA YFPEPLLLHQ GHVEWLFDHE GNRYLDFFSG IVTVSVGHCH
PKVNAAAQRQ LGRLWHTSSV FFHPLIHEYA EKLSALLPEP LKVVFLVNSG SEANDLAMLM
ARAHSNSTDI ISFRGAYHGC SPYTLGLTNV GIYKMDLPHG MGCQPTMCPD IFHGPWGGSH
CRDSPVQTIR KCSCAPDCCQ AKDQYIEQFK DTLSTSVAKS IAGFFAEPIQ GVNGVVQYPK
GFLKEAFELV RERGGVCIAD EVQTGFGRLG SHFWGFQTHD VLPDIVTMAK GIGNGFPMAA
VVTTPDIAKS LTKRMLHFNT FGGNPMACAV GSAVLEVIKE ENLQENSQEV GTYMLLKLAK
LRDEFEIVGD VRGKGLMIGI EMVKDKESRQ PLPREEVNQI HHDCKCMGLL IGRGGLFSQT
FRIAPSMCIT KPEVDFAVEV FRSALIQHME RRAK
