AGT2_RAT
ID AGT2_RAT Reviewed; 512 AA.
AC Q64565; O08616; Q642F1;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 13-SEP-2005, sequence version 2.
DT 03-AUG-2022, entry version 148.
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; Synonyms=Agt2;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND PARTIAL PROTEIN SEQUENCE.
RC STRAIN=Wistar; TISSUE=Kidney;
RX PubMed=7592550; DOI=10.1093/oxfordjournals.jbchem.a124787;
RA Matsui-Lee I.S., Muragaki Y., Ideguchi T., Hase T., Tsuji M., Ooshima A.,
RA Okuno E., Kido R.;
RT "Molecular cloning and sequencing of a cDNA encoding alanine-glyoxylate
RT aminotransferase 2 from rat kidney.";
RL J. Biochem. 117:856-862(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], AND PROTEIN SEQUENCE OF 40-57.
RC STRAIN=Sprague-Dawley; TISSUE=Liver;
RX PubMed=10989446; DOI=10.1016/s0076-6879(00)24247-x;
RA Tamaki N., Sakata S.F., Matsuda K.;
RT "Purification, properties, and sequencing of aminoisobutyrate
RT aminotransferases from rat liver.";
RL Methods Enzymol. 324:376-389(2000).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Kidney;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
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 -!- SUBUNIT: Homotetramer.
CC -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000250|UniProtKB:Q9BYV1}.
CC -!- SIMILARITY: Belongs to the class-III pyridoxal-phosphate-dependent
CC aminotransferase family. {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; D38100; BAA07281.1; -; mRNA.
DR EMBL; AB002584; BAA19549.1; -; mRNA.
DR EMBL; BC081765; AAH81765.1; -; mRNA.
DR RefSeq; NP_114023.1; NM_031835.2.
DR AlphaFoldDB; Q64565; -.
DR SMR; Q64565; -.
DR STRING; 10116.ENSRNOP00000024035; -.
DR iPTMnet; Q64565; -.
DR PhosphoSitePlus; Q64565; -.
DR PaxDb; Q64565; -.
DR PRIDE; Q64565; -.
DR Ensembl; ENSRNOT00000024035; ENSRNOP00000024035; ENSRNOG00000017821.
DR GeneID; 83784; -.
DR KEGG; rno:83784; -.
DR CTD; 64902; -.
DR RGD; 621767; Agxt2.
DR eggNOG; KOG1404; Eukaryota.
DR GeneTree; ENSGT00940000156125; -.
DR HOGENOM; CLU_016922_8_0_1; -.
DR InParanoid; Q64565; -.
DR OMA; PFMVPTY; -.
DR OrthoDB; 145181at2759; -.
DR BRENDA; 2.6.1.40; 5301.
DR BRENDA; 2.6.1.44; 5301.
DR Reactome; R-RNO-389661; Glyoxylate metabolism and glycine degradation.
DR SABIO-RK; Q64565; -.
DR PRO; PR:Q64565; -.
DR Proteomes; UP000002494; Chromosome 2.
DR Bgee; ENSRNOG00000017821; Expressed in adult mammalian kidney and 11 other tissues.
DR Genevisible; Q64565; RN.
DR GO; GO:0005759; C:mitochondrial matrix; TAS:Reactome.
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:0016223; F:beta-alanine-pyruvate transaminase activity; ISO:RGD.
DR GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR GO; GO:0019265; P:glycine biosynthetic process, by transamination of glyoxylate; ISO:RGD.
DR GO; GO:0009436; P:glyoxylate catabolic process; ISO:RGD.
DR GO; GO:0019481; P:L-alanine catabolic process, by transamination; ISO:RGD.
DR GO; GO:0045429; P:positive regulation of nitric oxide biosynthetic process; ISO:RGD.
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 1: Evidence at protein level;
KW Acetylation; Aminotransferase; Direct protein sequencing; Mitochondrion;
KW Pyridoxal phosphate; Reference proteome; Transferase; Transit peptide.
FT TRANSIT 1..39
FT /note="Mitochondrion"
FT /evidence="ECO:0000269|PubMed:10989446"
FT CHAIN 40..512
FT /note="Alanine--glyoxylate aminotransferase 2,
FT mitochondrial"
FT /id="PRO_0000001270"
FT MOD_RES 55
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q3UEG6"
FT MOD_RES 69
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q3UEG6"
FT MOD_RES 69
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q3UEG6"
FT MOD_RES 82
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q3UEG6"
FT MOD_RES 260
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q3UEG6"
FT MOD_RES 260
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q3UEG6"
FT MOD_RES 302
FT /note="N6-succinyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q3UEG6"
FT MOD_RES 348
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000250"
FT MOD_RES 415
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q3UEG6"
FT MOD_RES 415
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q3UEG6"
FT MOD_RES 418
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q3UEG6"
FT MOD_RES 418
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q3UEG6"
FT MOD_RES 452
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q3UEG6"
FT CONFLICT 305
FT /note="F -> L (in Ref. 1; BAA07281)"
FT /evidence="ECO:0000305"
FT CONFLICT 332
FT /note="W -> Y (in Ref. 1; BAA07281)"
FT /evidence="ECO:0000305"
FT CONFLICT 337..338
FT /note="HD -> QA (in Ref. 1; BAA07281)"
FT /evidence="ECO:0000305"
FT CONFLICT 435..436
FT /note="MV -> WW (in Ref. 1; BAA07281)"
FT /evidence="ECO:0000305"
FT CONFLICT 494..496
FT /note="FAF -> LAL (in Ref. 1; BAA07281)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 512 AA; 57201 MW; C35E389789516B5C CRC64;
MSLAWRTLQK AFYLETSLRI LQMRPSLSCA SRIYVPKLTL HTKHNMPPCD FSPEKYQSLA
YNHVLEIHKQ HLSPVNTAYF QKPLLLHQGH MEWLFDSEGN RYLDFFSGIV TVGVGHCHPK
VTAVAKKQMD RLWHTSSVFF HSPMHEYAER LSALLPEPLK VIFLVNSGSE ANDLAMVMAR
AYSNHTDIIS FRGAYHGCSP YTLGLTNVGI YKMKVPSTIA CQSTMCPDVF RGPWGGSHCR
DSPVQTVRKC SCAPDGCQAK ERYIEQFKDT LNTSVATSIA GFFAEPIQGV NGVVQYPKEF
LKEAFALVRE RGGVCIADEV QTGFGRLGSH FWGFQTHDTM PDIVTMAKGI GNGFPMAAVV
TTPEIASSLA KHLHHFSTFG GSPLACAIGS AVLEVIEEEN LQRNSQEVGT YMLLKFAKLR
DEFDIVGDVR GKGLMVGIEM VQDKISRQPL PKTEVNQIHE DCKDMGLLVG RGGNFSQTFR
IAPPMRVTKL EVDFAFEVFR SALTQHMERR AK
