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Q9BYV1 (AGT2_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 109. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (5) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Alanine--glyoxylate aminotransferase 2, mitochondrial

Short name=AGT 2
EC=2.6.1.44
Alternative name(s):
(R)-3-amino-2-methylpropionate--pyruvate transaminase
EC=2.6.1.40
Beta-ALAAT II
Beta-alanine-pyruvate aminotransferase
D-AIBAT
Gene names
Name:AGXT2
Synonyms:AGT2
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length514 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Can metabolize asymmetric dimethylarginine (ADMA) via transamination to alpha-keto-delta-(NN-dimethylguanidino) valeric acid (DMGV). ADMA is a potent inhibitor of nitric-oxide (NO) synthase, and this activity provides mechanism through which the kidney regulates blood pressure. Ref.4 Ref.5

Catalytic activity

L-alanine + glyoxylate = pyruvate + glycine.

(R)-3-amino-2-methylpropanoate + pyruvate = 2-methyl-3-oxopropanoate + L-alanine.

Cofactor

Pyridoxal phosphate.

Subunit structure

Homotetramer By similarity.

Subcellular location

Mitochondrion Ref.4.

Sequence similarities

Belongs to the class-III pyridoxal-phosphate-dependent aminotransferase family.

Ontologies

Keywords
   Cellular componentMitochondrion
   Coding sequence diversityPolymorphism
   DomainTransit peptide
   LigandPyridoxal phosphate
   Molecular functionAminotransferase
Transferase
   PTMAcetylation
   Technical termComplete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processL-alanine catabolic process, by transamination

Inferred from direct assay Ref.4. Source: BHF-UCL

cellular nitrogen compound metabolic process

Traceable author statement. Source: Reactome

glycine biosynthetic process, by transamination of glyoxylate

Inferred from direct assay Ref.4. Source: BHF-UCL

glyoxylate catabolic process

Inferred from direct assay Ref.4. Source: BHF-UCL

glyoxylate metabolic process

Traceable author statement. Source: Reactome

nucleobase-containing small molecule metabolic process

Traceable author statement. Source: Reactome

positive regulation of nitric oxide biosynthetic process

Inferred from direct assay Ref.4. Source: BHF-UCL

pyrimidine nucleobase metabolic process

Traceable author statement. Source: Reactome

pyrimidine nucleoside catabolic process

Traceable author statement. Source: Reactome

small molecule metabolic process

Traceable author statement. Source: Reactome

   Cellular_componentmitochondrial matrix

Traceable author statement. Source: Reactome

mitochondrion

Inferred from direct assay Ref.4. Source: BHF-UCL

   Molecular_function(R)-3-amino-2-methylpropionate-pyruvate transaminase activity

Inferred from electronic annotation. Source: UniProtKB-EC

alanine-glyoxylate transaminase activity

Inferred from direct assay Ref.4. Source: BHF-UCL

beta-alanine-pyruvate transaminase activity

Inferred from electronic annotation. Source: Ensembl

pyridoxal phosphate binding

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Transit peptide1 – 4141Mitochondrion Ref.4
Chain42 – 514473Alanine--glyoxylate aminotransferase 2, mitochondrial
PRO_0000001269

Amino acid modifications

Modified residue711N6-acetyllysine; alternate By similarity
Modified residue711N6-succinyllysine; alternate By similarity
Modified residue841N6-acetyllysine By similarity
Modified residue2621N6-acetyllysine; alternate By similarity
Modified residue2621N6-succinyllysine; alternate By similarity
Modified residue3041N6-succinyllysine By similarity
Modified residue3501N6-(pyridoxal phosphate)lysine By similarity
Modified residue4171N6-acetyllysine; alternate By similarity
Modified residue4171N6-succinyllysine; alternate By similarity
Modified residue4201N6-acetyllysine; alternate By similarity
Modified residue4201N6-succinyllysine; alternate By similarity

Natural variations

Natural variant1021S → I.
Corresponds to variant rs37370 [ dbSNP | Ensembl ].
VAR_061006
Natural variant1021S → N. Ref.2 Ref.3
Corresponds to variant rs37370 [ dbSNP | Ensembl ].
VAR_023483
Natural variant1021S → T.
Corresponds to variant rs37370 [ dbSNP | Ensembl ].
VAR_061007
Natural variant1321G → R.
Corresponds to variant rs16870794 [ dbSNP | Ensembl ].
VAR_048231
Natural variant1401V → I. Ref.2 Ref.3
Corresponds to variant rs37369 [ dbSNP | Ensembl ].
VAR_022140
Natural variant2121T → I. Ref.2 Ref.3
Corresponds to variant rs180749 [ dbSNP | Ensembl ].
VAR_022141
Natural variant4921P → R.
Corresponds to variant rs17245714 [ dbSNP | Ensembl ].
VAR_048232
Natural variant4981V → L. Ref.3
Corresponds to variant rs16899974 [ dbSNP | Ensembl ].
VAR_029513

Sequences

Sequence LengthMass (Da)Tools
Q9BYV1 [UniParc].

Last modified June 1, 2001. Version 1.
Checksum: CA562F84FF39B5AC

FASTA51457,156
        10         20         30         40         50         60 
MTLIWRHLLR PLCLVTSAPR ILEMHPFLSL GTSRTSVTKL SLHTKPRMPP CDFMPERYQS 

        70         80         90        100        110        120 
LGYNRVLEIH KEHLSPVVTA YFQKPLLLHQ GHMEWLFDAE GSRYLDFFSG IVTVSVGHCH 

       130        140        150        160        170        180 
PKVNAVAQKQ LGRLWHTSTV FFHPPMHEYA EKLAALLPEP LKVIFLVNSG SEANELAMLM 

       190        200        210        220        230        240 
ARAHSNNIDI ISFRGAYHGC SPYTLGLTNV GTYKMELPGG TGCQPTMCPD VFRGPWGGSH 

       250        260        270        280        290        300 
CRDSPVQTIR KCSCAPDCCQ AKDQYIEQFK DTLSTSVAKS IAGFFAEPIQ GVNGVVQYPK 

       310        320        330        340        350        360 
GFLKEAFELV RARGGVCIAD EVQTGFGRLG SHFWGFQTHD VLPDIVTMAK GIGNGFPMAA 

       370        380        390        400        410        420 
VITTPEIAKS LAKCLQHFNT FGGNPMACAI GSAVLEVIKE ENLQENSQEV GTYMLLKFAK 

       430        440        450        460        470        480 
LRDEFEIVGD VRGKGLMIGI EMVQDKISCR PLPREEVNQI HEDCKHMGLL VGRGSIFSQT 

       490        500        510 
FRIAPSMCIT KPEVDFAVEV FRSALTQHME RRAK 

« Hide

References

« Hide 'large scale' references
[1]"The human ortholog for rat alanine-glyoxylate aminotransferase 2."
Jenne D.E.
Submitted (JAN-2001) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]"Human beta-alanine-pyruvate aminotransferase cDNA."
Matsuda K., Horikawa Y., Kaneko M., Sakata S., Tamaki N.
Submitted (OCT-2004) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA], VARIANTS ASN-102; ILE-140 AND ILE-212.
[3]Suzuki Y., Sugano S., Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S.
Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], VARIANTS ASN-102; ILE-140; ILE-212 AND LEU-498.
Tissue: Kidney.
[4]"Human alanine-glyoxylate aminotransferase 2 lowers asymmetric dimethylarginine and protects from inhibition of nitric oxide production."
Rodionov R.N., Murry D.J., Vaulman S.F., Stevens J.W., Lentz S.R.
J. Biol. Chem. 285:5385-5391(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF N-TERMINUS, FUNCTION, TRANSIT PEPTIDE CLEAVAGE SITE, SUBCELLULAR LOCATION.
[5]"Alanine-Glyoxylate aminotransferase-2 metabolizes endogenous methylarginines, regulates NO, and controls blood pressure."
Caplin B., Wang Z., Slaviero A., Tomlinson J., Dowsett L., Delahaye M., Salama A., Wheeler D.C., Leiper J.
Arterioscler. Thromb. Vasc. Biol. 32:2892-2900(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AJ292204 mRNA. Translation: CAC24841.1.
AB193309 mRNA. Translation: BAD66662.1.
AK223128 mRNA. Translation: BAD96848.1.
AK223144 mRNA. No translation available.
AK223375 mRNA. Translation: BAD97095.1.
RefSeqNP_114106.1. NM_031900.3.
UniGeneHs.34494.

3D structure databases

ProteinModelPortalQ9BYV1.
SMRQ9BYV1. Positions 62-510.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid122342. 2 interactions.
IntActQ9BYV1. 2 interactions.
STRING9606.ENSP00000231420.

Chemistry

DrugBankDB00145. Glycine.
DB00160. L-Alanine.
DB00114. Pyridoxal Phosphate.
DB00119. Pyruvic acid.

PTM databases

PhosphoSiteQ9BYV1.

Polymorphism databases

DMDM17432913.

Proteomic databases

PaxDbQ9BYV1.
PRIDEQ9BYV1.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000231420; ENSP00000231420; ENSG00000113492.
GeneID64902.
KEGGhsa:64902.
UCSCuc003jjf.3. human.

Organism-specific databases

CTD64902.
GeneCardsGC05M035033.
HGNCHGNC:14412. AGXT2.
HPAHPA037382.
MIM612471. gene.
neXtProtNX_Q9BYV1.
PharmGKBPA24634.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG0160.
HOGENOMHOG000020206.
HOVERGENHBG004196.
InParanoidQ9BYV1.
KOK00827.
OMAGHCHPHL.
OrthoDBEOG79KPF2.
PhylomeDBQ9BYV1.
TreeFamTF105945.

Enzyme and pathway databases

BioCycMetaCyc:HS03685-MONOMER.
ReactomeREACT_111217. Metabolism.

Gene expression databases

ArrayExpressQ9BYV1.
BgeeQ9BYV1.
CleanExHS_AGXT2.
GenevestigatorQ9BYV1.

Family and domain databases

Gene3D3.40.640.10. 1 hit.
3.90.1150.10. 1 hit.
InterProIPR005814. Aminotrans_3.
IPR015424. PyrdxlP-dep_Trfase.
IPR015421. PyrdxlP-dep_Trfase_major_sub1.
IPR015422. PyrdxlP-dep_Trfase_major_sub2.
[Graphical view]
PANTHERPTHR11986. PTHR11986. 1 hit.
PfamPF00202. Aminotran_3. 1 hit.
[Graphical view]
PIRSFPIRSF000521. Transaminase_4ab_Lys_Orn. 1 hit.
SUPFAMSSF53383. SSF53383. 1 hit.
PROSITEPS00600. AA_TRANSFER_CLASS_3. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSAGXT2. human.
GenomeRNAi64902.
NextBio67053.
PROQ9BYV1.
SOURCESearch...

Entry information

Entry nameAGT2_HUMAN
AccessionPrimary (citable) accession number: Q9BYV1
Secondary accession number(s): Q53FB4 expand/collapse secondary AC list , Q53FY7, Q53G03, Q5W7Q1
Entry history
Integrated into UniProtKB/Swiss-Prot: December 5, 2001
Last sequence update: June 1, 2001
Last modified: April 16, 2014
This is version 109 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Relevant documents

SIMILARITY comments

Index of protein domains and families

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 5

Human chromosome 5: entries, gene names and cross-references to MIM