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Q9LDV4 (ALAT2_ARATH) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 89. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Alanine aminotransferase 2, mitochondrial

Short name=AtAlaAT2
Short name=AtAlaATm
EC=2.6.1.2
Alternative name(s):
Alanine-2-oxoglutarate aminotransferase 3
EC=2.6.1.-
Gene names
Name:ALAAT2
Synonyms:AOAT3
Ordered Locus Names:At1g72330
ORF Names:T10D10.20, T9N14.10
OrganismArabidopsis thaliana (Mouse-ear cress) [Reference proteome]
Taxonomic identifier3702 [NCBI]
Taxonomic lineageEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis

Protein attributes

Sequence length540 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at transcript level

General annotation (Comments)

Catalytic activity

L-alanine + 2-oxoglutarate = pyruvate + L-glutamate.

Cofactor

Pyridoxal phosphate By similarity.

Pathway

Photosynthesis; C4 acid pathway.

Amino-acid degradation; L-alanine degradation via transaminase pathway; pyruvate from L-alanine: step 1/1.

Subunit structure

Homodimer By similarity.

Subcellular location

Mitochondrion Potential.

Tissue specificity

Expressed in shoots, essentially in leaves and flowers, mostly in vascular tissues. Also detected in stems and roots. Ref.5 Ref.6

Induction

Rapidly induced upon low-oxygen stress in roots and shoots. Ref.6

Post-translational modification

The N-terminus is blocked By similarity.

Sequence similarities

Belongs to the class-I pyridoxal-phosphate-dependent aminotransferase family. Alanine aminotransferase subfamily.

Sequence caution

The sequence AAG51787.1 differs from that shown. Reason: Erroneous gene model prediction.

The sequence AEE35307.1 differs from that shown. Reason: Erroneous gene model prediction.

Ontologies

Keywords
   Cellular componentMitochondrion
   Coding sequence diversityAlternative splicing
   DomainTransit peptide
   LigandPyridoxal phosphate
   Molecular functionAminotransferase
Transferase
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processL-alanine catabolic process

Inferred from electronic annotation. Source: UniProtKB-UniPathway

biosynthetic process

Inferred from electronic annotation. Source: InterPro

response to hypoxia

Inferred from expression pattern Ref.6. Source: UniProtKB

   Cellular_componentmitochondrion

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionL-alanine:2-oxoglutarate aminotransferase activity

Inferred from electronic annotation. Source: UniProtKB-EC

pyridoxal phosphate binding

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q9LDV4-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
Isoform 2 (identifier: Q9LDV4-2)

The sequence of this isoform differs from the canonical sequence as follows:
     410-540: PGDDSYDSYM...HKSFMDEFRN → KEMEFSHPWLNVQRLWKTLSTV
Note: Derived from EST data. No experimental confirmation available.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Transit peptide1 – 4646Mitochondrion Potential
Chain47 – 540494Alanine aminotransferase 2, mitochondrial
PRO_0000416043

Amino acid modifications

Modified residue3571N6-(pyridoxal phosphate)lysine By similarity

Natural variations

Alternative sequence410 – 540131PGDDS…DEFRN → KEMEFSHPWLNVQRLWKTLS TV in isoform 2.
VSP_042467

Experimental info

Sequence conflict2651K → E in AAK59591. Ref.4

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified October 1, 2000. Version 1.
Checksum: 4D1D4D4102CBD661

FASTA54059,511
        10         20         30         40         50         60 
MRRFLINQAK GLVDHSRRQH HHKSPSFLSP QPRPLASSPP ALSRFFSSTS EMSASDSTSS 

        70         80         90        100        110        120 
LPVTLDSINP KVLKCEYAVR GEIVNIAQKL QEDLKTNKDA YPFDEIIYCN IGNPQSLGQL 

       130        140        150        160        170        180 
PIKFFREVLA LCDHASLLDE SETHGLFSTD SIDRAWRILD HIPGRATGAY SHSQGIKGLR 

       190        200        210        220        230        240 
DVIAAGIEAR DGFPADPNDI FLTDGASPAV HMMMQLLLSS EKDGILSPIP QYPLYSASIA 

       250        260        270        280        290        300 
LHGGSLVPYY LDEATGWGLE ISDLKKQLEE ARSKGISVRA LVVINPGNPT GQVLAEENQR 

       310        320        330        340        350        360 
DIVNFCKQEG LVLLADEVYQ ENVYVPDKKF HSFKKVARSL GYGEKDISLV SFQSVSKGYY 

       370        380        390        400        410        420 
GECGKRGGYM EVTGFTSDVR EQIYKMASVN LCSNISGQIL ASLVMSPPKP GDDSYDSYMA 

       430        440        450        460        470        480 
ERDGILSSMA KRAKTLEDAL NSLEGVTCNR AEGAMYLFPR INLPQKAIEA AEAEKTAPDA 

       490        500        510        520        530        540 
FYCKRLLNAT GVVVVPGSGF GQVPGTWHFR CTILPQEDKI PAIVNRLTEF HKSFMDEFRN 

« Hide

Isoform 2 [UniParc].

Checksum: 62385DCABF0834D1
Show »

FASTA43147,710

References

« Hide 'large scale' references
[1]"Cloning and characterization of Arabidopsis alanine aminotransferase genes."
Ismond K.P., Dennis E.S., Dolferus R.
Submitted (JUN-2000) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
Strain: cv. C24.
[2]"Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana."
Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O., Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E., Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K. expand/collapse author list , Conn L., Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P., Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D., Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J., Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L., Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A., Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A., Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M., Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M., Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P., Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D., Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D., Yu G., Fraser C.M., Venter J.C., Davis R.W.
Nature 408:816-820(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: cv. Columbia.
[3]The Arabidopsis Information Resource (TAIR)
Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases
Cited for: GENOME REANNOTATION.
Strain: cv. Columbia.
[4]"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] OF 9-540 (ISOFORM 1).
Strain: cv. Columbia.
[5]"Identification of photorespiratory glutamate:glyoxylate aminotransferase (GGAT) gene in Arabidopsis."
Igarashi D., Miwa T., Seki M., Kobayashi M., Kato T., Tabata S., Shinozaki K., Ohsumi C.
Plant J. 33:975-987(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: TISSUE SPECIFICITY, GENE FAMILY, NOMENCLATURE.
[6]"Alanine aminotransferase catalyses the breakdown of alanine after hypoxia in Arabidopsis thaliana."
Miyashita Y., Dolferus R., Ismond K.P., Good A.G.
Plant J. 49:1108-1121(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: TISSUE SPECIFICITY, INDUCTION BY HYPOXIC STRESS.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF275371 mRNA. Translation: AAF82781.1.
AC016529 Genomic DNA. Translation: AAG52580.1.
AC067754 Genomic DNA. Translation: AAG51787.1. Sequence problems.
CP002684 Genomic DNA. Translation: AEE35305.1.
CP002684 Genomic DNA. Translation: AEE35306.1.
CP002684 Genomic DNA. Translation: AEE35307.1. Sequence problems.
AY035086 mRNA. Translation: AAK59591.2.
PIRB96747.
RefSeqNP_001077811.1. NM_001084342.1. [Q9LDV4-2]
NP_001185380.1. NM_001198451.1.
NP_565040.2. NM_105892.4. [Q9LDV4-1]
UniGeneAt.15579.

3D structure databases

ProteinModelPortalQ9LDV4.
SMRQ9LDV4. Positions 63-539.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING3702.AT1G72330.1-P.

Proteomic databases

PRIDEQ9LDV4.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblPlantsAT1G72330.1; AT1G72330.1; AT1G72330. [Q9LDV4-1]
GeneID843565.
KEGGath:AT1G72330.

Organism-specific databases

TAIRAT1G72330.

Phylogenomic databases

HOGENOMHOG000215020.
InParanoidQ9LDV4.
KOK00814.
PhylomeDBQ9LDV4.

Enzyme and pathway databases

BioCycARA:GQT-1694-MONOMER.
ARA:GQT-1695-MONOMER.
UniPathwayUPA00322.
UPA00528; UER00586.

Gene expression databases

GenevestigatorQ9LDV4.

Family and domain databases

Gene3D3.40.640.10. 1 hit.
3.90.1150.10. 1 hit.
InterProIPR004839. Aminotransferase_I/II.
IPR015424. PyrdxlP-dep_Trfase.
IPR015421. PyrdxlP-dep_Trfase_major_sub1.
IPR015422. PyrdxlP-dep_Trfase_major_sub2.
[Graphical view]
PfamPF00155. Aminotran_1_2. 1 hit.
[Graphical view]
SUPFAMSSF53383. SSF53383. 2 hits.
ProtoNetSearch...

Entry information

Entry nameALAT2_ARATH
AccessionPrimary (citable) accession number: Q9LDV4
Secondary accession number(s): F4IDA2 expand/collapse secondary AC list , F4IDA4, Q94C83, Q9C7S4
Entry history
Integrated into UniProtKB/Swiss-Prot: March 21, 2012
Last sequence update: October 1, 2000
Last modified: May 14, 2014
This is version 89 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways

Arabidopsis thaliana

Arabidopsis thaliana: entries and gene names