Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

P43567 (AGX1_YEAST) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 119. 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 1

EC=2.6.1.44
Gene names
Name:AGX1
Ordered Locus Names:YFL030W
OrganismSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) [Reference proteome]
Taxonomic identifier559292 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces

Protein attributes

Sequence length385 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Has alanine:glyoxylate aminotransferase activity. Ref.3 Ref.6

Catalytic activity

L-alanine + glyoxylate = pyruvate + glycine.

Cofactor

Pyridoxal phosphate. Ref.6

Pathway

Amino-acid biosynthesis; glycine biosynthesis; glycine from glyoxylate: step 1/1.

Subunit structure

Homodimer. Ref.6

Disruption phenotype

Alanine:glyoxylate aminotransferase activity is reduced by 98% relative to wild-type. Ref.6

Miscellaneous

Present with 339 molecules/cell in log phase SD medium. Expression levels higher in stationary phase than in exponential growth phase when grown in complex medium with glucose.

Sequence similarities

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

Biophysicochemical properties

Kinetic parameters:

KM=2.26 mM for L-alanine Ref.6

KM=0.18 mM for glyoxylate

Vmax=180 µmol/min/mg enzyme

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 385385Alanine--glyoxylate aminotransferase 1
PRO_0000150239

Sites

Binding site3541Substrate

Amino acid modifications

Modified residue2011N6-(pyridoxal phosphate)lysine

Secondary structure

............................................................... 385
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P43567 [UniParc].

Last modified November 1, 1995. Version 1.
Checksum: 460D5DCCA8FDF79F

FASTA38541,907
        10         20         30         40         50         60 
MTKSVDTLLI PGPIILSGAV QKALDVPSLG HTSPEFVSIF QRVLKNTRAV FKSAAASKSQ 

        70         80         90        100        110        120 
PFVLAGSGTL GWDIFASNFI LSKAPNKNVL VVSTGTFSDR FADCLRSYGA QVDVVRPLKI 

       130        140        150        160        170        180 
GESVPLELIT EKLSQNSYGA VTVTHVDTST AVLSDLKAIS QAIKQTSPET FFVVDAVCSI 

       190        200        210        220        230        240 
GCEEFEFDEW GVDFALTASQ KAIGAPAGLS ISLCSSRFMD YALNDSKNGH VHGYFSSLRR 

       250        260        270        280        290        300 
WTPIMENYEA GKGAYFATPP VQLINSLDVA LKEILEEGLH KRWDLHREMS DWFKDSLVNG 

       310        320        330        340        350        360 
LQLTSVSRYP SNMSAHGLTA VYVADPPDVI AFLKSHGVVI AGGIHKDIGP KYIRIGHMGV 

       370        380 
TACNKNLPYM KNCFDLIKLA LQRKK 

« Hide

References

« Hide 'large scale' references
[1]"Analysis of the nucleotide sequence of chromosome VI from Saccharomyces cerevisiae."
Murakami Y., Naitou M., Hagiwara H., Shibata T., Ozawa M., Sasanuma S., Sasanuma M., Tsuchiya Y., Soeda E., Yokoyama K., Yamazaki M., Tashiro H., Eki T.
Nat. Genet. 10:261-268(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 204508 / S288c.
[2]"The reference genome sequence of Saccharomyces cerevisiae: Then and now."
Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R., Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S., Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.
G3 (Bethesda) 4:389-398(2014) [PubMed] [Europe PMC] [Abstract]
Cited for: GENOME REANNOTATION.
Strain: ATCC 204508 / S288c.
[3]"Characteristics of alanine:glyoxylate aminotransferase from Saccharomyces cerevisiae, a regulatory enzyme in the glyoxylate pathway of glycine and serine biosynthesis from tricarboxylic acid-cycle intermediates."
Takada Y., Noguchi T.
Biochem. J. 231:157-163(1985) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[4]"Global analysis of protein expression in yeast."
Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N., O'Shea E.K., Weissman J.S.
Nature 425:737-741(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
[5]"Alanine:glyoxylate aminotransferase of Saccharomyces cerevisiae-encoding gene AGX1 and metabolic significance."
Schlosser T., Gatgens C., Weber U., Stahmann K.-P.
Yeast 21:63-73(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: CHARACTERIZATION.
[6]"Crystal structure and confirmation of the alanine:glyoxylate aminotransferase activity of the YFL030w yeast protein."
Meyer P., Liger D., Leulliot N., Quevillon-Cheruel S., Zhou C.-Z., Borel F., Ferrer J.-L., Poupon A., Janin J., van Tilbeurgh H.
Biochimie 87:1041-1047(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.57 ANGSTROMS) IN COMPLEX WITH PYRODOXAL PHOSPHATE AND GLYOXYLATE, BIOPHYSICOCHEMICAL PROPERTIES, COFACTOR, DISRUPTION PHENOTYPE, FUNCTION, SUBUNIT.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
D50617 Genomic DNA. Translation: BAA09208.1.
BK006940 Genomic DNA. Translation: DAA12410.1.
PIRS56224.
RefSeqNP_116623.1. NM_001179936.1.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2BKWX-ray2.57A1-385[»]
ProteinModelPortalP43567.
SMRP43567. Positions 3-383.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid31116. 17 interactions.
DIPDIP-5433N.
MINTMINT-513813.
STRING4932.YFL030W.

Proteomic databases

MaxQBP43567.
PaxDbP43567.
PeptideAtlasP43567.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiYFL030W; YFL030W; YFL030W.
GeneID850514.
KEGGsce:YFL030W.

Organism-specific databases

CYGDYFL030w.
SGDS000001864. AGX1.

Phylogenomic databases

eggNOGCOG0075.
GeneTreeENSGT00390000006648.
HOGENOMHOG000171814.
KOK00830.
OMAAMARPTI.
OrthoDBEOG7BZW2X.

Enzyme and pathway databases

BioCycMetaCyc:MONOMER-13656.
YEAST:MONOMER3O-372.
BRENDA2.6.1.44. 984.
SABIO-RKP43567.
UniPathwayUPA00288; UER00428.

Gene expression databases

GenevestigatorP43567.

Family and domain databases

Gene3D3.40.640.10. 1 hit.
3.90.1150.10. 1 hit.
InterProIPR000192. Aminotrans_V/Cys_dSase.
IPR015424. PyrdxlP-dep_Trfase.
IPR015421. PyrdxlP-dep_Trfase_major_sub1.
IPR015422. PyrdxlP-dep_Trfase_major_sub2.
IPR024169. SP_NH2Trfase/AEP_transaminase.
[Graphical view]
PfamPF00266. Aminotran_5. 1 hit.
[Graphical view]
PIRSFPIRSF000524. SPT. 1 hit.
SUPFAMSSF53383. SSF53383. 1 hit.
PROSITEPS00595. AA_TRANSFER_CLASS_5. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP43567.
NextBio966233.
PROP43567.

Entry information

Entry nameAGX1_YEAST
AccessionPrimary (citable) accession number: P43567
Secondary accession number(s): D6VTK0
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1995
Last sequence update: November 1, 1995
Last modified: May 14, 2014
This is version 119 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Relevant documents

Yeast chromosome VI

Yeast (Saccharomyces cerevisiae) chromosome VI: entries and gene names

Yeast

Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

PATHWAY comments

Index of metabolic and biosynthesis pathways