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Q56YA5 (SGAT_ARATH) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 66. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
Serine--glyoxylate aminotransferase

EC=2.6.1.45
Alternative name(s):
Alanine--glyoxylate aminotransferase
Short name=AGT
EC=2.6.1.44
Serine--pyruvate aminotransferase
EC=2.6.1.51
Gene names
Name:AGT1
Ordered Locus Names:At2g13360
ORF Names:F14O4.7
OrganismArabidopsis thaliana (Mouse-ear cress) [Reference proteome]
Taxonomic identifier3702 [NCBI]
Taxonomic lineageEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonscore eudicotyledonsrosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis

Protein attributes

Sequence length401 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Photorespiratory enzyme that catalyzes transamination reactions with multiple substrates.

Catalytic activity

L-serine + glyoxylate = 3-hydroxypyruvate + glycine.

L-alanine + glyoxylate = pyruvate + glycine.

L-serine + pyruvate = 3-hydroxypyruvate + L-alanine.

Cofactor

Pyridoxal phosphate.

Subunit structure

Homodimer.

Subcellular location

Peroxisome Ref.7.

Tissue specificity

Ubiquitous. Preferentially expressed in green, leafy tissues. Ref.7

Miscellaneous

Preferentially acts as a serine--glyoxylate aminotransferase in vitro.

Sequence similarities

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

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 401401Serine--glyoxylate aminotransferase
PRO_0000150234

Regions

Motif399 – 4013Microbody targeting signal Potential

Amino acid modifications

Modified residue2011N6-(pyridoxal phosphate)lysine By similarity
Modified residue3301Phosphotyrosine Ref.8

Experimental info

Mutagenesis2511P → L: Abolishes aminotransferase activity. Ref.7

Sequences

Sequence LengthMass (Da)Tools
Q56YA5 [UniParc].

Last modified September 13, 2005. Version 2.
Checksum: 608E7EFD840C84D3

FASTA40144,208
        10         20         30         40         50         60 
MDYMYGPGRH HLFVPGPVNI PEPVIRAMNR NNEDYRSPAI PALTKTLLED VKKIFKTTSG 

        70         80         90        100        110        120 
TPFLFPTTGT GAWESALTNT LSPGDRIVSF LIGQFSLLWI DQQKRLNFNV DVVESDWGQG 

       130        140        150        160        170        180 
ANLQVLASKL SQDENHTIKA ICIVHNETAT GVTNDISAVR TLLDHYKHPA LLLVDGVSSI 

       190        200        210        220        230        240 
CALDFRMDEW GVDVALTGSQ KALSLPTGLG IVCASPKALE ATKTSKSLKV FFDWNDYLKF 

       250        260        270        280        290        300 
YKLGTYWPYT PSIQLLYGLR AALDLIFEEG LENIIARHAR LGKATRLAVE AWGLKNCTQK 

       310        320        330        340        350        360 
EEWISNTVTA VMVPPHIDGS EIVRRAWQRY NLSLGLGLNK VAGKVFRIGH LGNVNELQLL 

       370        380        390        400 
GCLAGVEMIL KDVGYPVVMG SGVAAASTYL QHHIPLIPSR I 

« Hide

References

« Hide 'large scale' references
[1]"Sequence analysis of a cDNA encoding alanine:glyoxylate aminotransferase from Arabidopsis thaliana."
Liepman A.H., Olsen L.J.
Plant Gene Register PGR98-113
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Strain: cv. Columbia.
[2]"Molecular characterization of serine:glyoxylate aminotransferase localized in plant leaf peroxisomes."
Yamaguchi K., Takeuchi Y., Nishimura M.
Submitted (SEP-2000) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Strain: cv. Columbia.
[3]"Sequence and analysis of chromosome 2 of the plant Arabidopsis thaliana."
Lin X., Kaul S., Rounsley S.D., Shea T.P., Benito M.-I., Town C.D., Fujii C.Y., Mason T.M., Bowman C.L., Barnstead M.E., Feldblyum T.V., Buell C.R., Ketchum K.A., Lee J.J., Ronning C.M., Koo H.L., Moffat K.S., Cronin L.A. expand/collapse author list , Shen M., Pai G., Van Aken S., Umayam L., Tallon L.J., Gill J.E., Adams M.D., Carrera A.J., Creasy T.H., Goodman H.M., Somerville C.R., Copenhaver G.P., Preuss D., Nierman W.C., White O., Eisen J.A., Salzberg S.L., Fraser C.M., Venter J.C.
Nature 402:761-768(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: cv. Columbia.
[4]The Arabidopsis Information Resource (TAIR)
Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases
Cited for: GENOME REANNOTATION.
Strain: cv. Columbia.
[5]"Empirical analysis of transcriptional activity in the Arabidopsis genome."
Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M., Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G., Liu S.X., Lam B., Sakano H., Wu T., Yu G. expand/collapse author list , Miranda M., Quach H.L., Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C., Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J., Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A., Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C., Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X., Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M., Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K., Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A., Ecker J.R.
Science 302:842-846(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: cv. Columbia.
[6]"Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs."
Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A., Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y., Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K. expand/collapse author list , Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J., Hayashizaki Y., Shinozaki K.
Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 278-401.
Strain: cv. Columbia.
[7]"Peroxisomal alanine:glyoxylate aminotransferase (AGT1) is a photorespiratory enzyme with multiple substrates in Arabidopsis thaliana."
Liepman A.H., Olsen L.J.
Plant J. 25:487-498(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: CHARACTERIZATION, TISSUE SPECIFICITY, SUBCELLULAR LOCATION, MUTAGENESIS OF PRO-251.
[8]"Large-scale analysis of in vivo phosphorylated membrane proteins by immobilized metal ion affinity chromatography and mass spectrometry."
Nuehse T.S., Stensballe A., Jensen O.N., Peck S.C.
Mol. Cell. Proteomics 2:1234-1243(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-330, MASS SPECTROMETRY.
Strain: cv. La-0.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF063901 mRNA. Translation: AAC26854.1.
AB048945 mRNA. Translation: BAB20811.1.
AC007209 Genomic DNA. Translation: AAD28669.1.
CP002685 Genomic DNA. Translation: AEC06227.1.
CP002685 Genomic DNA. Translation: AEC06228.1.
AY096498 mRNA. Translation: AAM20136.1.
AY114010 mRNA. Translation: AAM45058.1.
AK221418 mRNA. Translation: BAD94403.1.
IPIIPI00540396.
PIRT52250.
RefSeqNP_178969.1. NM_126925.4.
NP_849951.1. NM_179620.2.
UniGeneAt.24853.

3D structure databases

ProteinModelPortalQ56YA5.
SMRQ56YA5. Positions 12-352.
ModBaseSearch...

Protein-protein interaction databases

IntActQ56YA5. 3 interactions.

Proteomic databases

PaxDbQ56YA5.
PRIDEQ56YA5.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblPlantsAT2G13360.1; AT2G13360.1; AT2G13360.
AT2G13360.2; AT2G13360.2; AT2G13360.
GeneID815822.
KEGGath:AT2G13360.

Organism-specific databases

GeneFarm5080.
TAIRAt2g13360.

Phylogenomic databases

eggNOGCOG0075.
HOGENOMHOG000171814.
InParanoidQ56YA5.
KOK00830.
OMARINHMGI.
PhylomeDBQ56YA5.
ProtClustDBPLN02409.

Enzyme and pathway databases

BioCycMetaCyc:AT2G13360-MONOMER.
BRENDA2.6.1.44. 399.
SABIO-RKQ56YA5.

Gene expression databases

GenevestigatorQ56YA5.
GermOnlineAT2G13360. Arabidopsis thaliana.

Family and domain databases

Gene3D3.40.640.10. 1 hit.
3.90.1150.10. 1 hit.
InterProIPR000192. Aminotrans_V/Cys_dSase.
IPR020578. Aminotrans_V_PyrdxlP_BS.
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. PyrdxlP-dep_Trfase_major. 1 hit.
PROSITEPS00595. AA_TRANSFER_CLASS_5. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameSGAT_ARATH
AccessionPrimary (citable) accession number: Q56YA5
Secondary accession number(s): O81248
Entry history
Integrated into UniProtKB/Swiss-Prot: September 13, 2005
Last sequence update: September 13, 2005
Last modified: May 1, 2013
This is version 66 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Relevant documents

Arabidopsis thaliana

Arabidopsis thaliana: entries and gene names

SIMILARITY comments

Index of protein domains and families