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Protein

Alanine aminotransferase 1, mitochondrial

Gene

ALAAT1

Organism
Arabidopsis thaliana (Mouse-ear cress)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Major alanine aminotransferase in roots.1 Publication

Catalytic activityi

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

Cofactori

Pathwayi

GO - Molecular functioni

  1. ATP binding Source: TAIR
  2. L-alanine:2-oxoglutarate aminotransferase activity Source: TAIR
  3. pyridoxal phosphate binding Source: InterPro

GO - Biological processi

  1. biosynthetic process Source: InterPro
  2. L-alanine catabolic process, by transamination Source: TAIR
  3. response to cadmium ion Source: TAIR
  4. response to hypoxia Source: TAIR
Complete GO annotation...

Keywords - Molecular functioni

Aminotransferase, Transferase

Keywords - Ligandi

Pyridoxal phosphate

Enzyme and pathway databases

UniPathwayiUPA00322.
UPA00528; UER00586.

Names & Taxonomyi

Protein namesi
Recommended name:
Alanine aminotransferase 1, mitochondrial (EC:2.6.1.2)
Short name:
AtAlaAT1
Short name:
AtAlaATc
Alternative name(s):
Alanine-2-oxoglutarate aminotransferase 4 (EC:2.6.1.-)
Gene namesi
Name:ALAAT1
Synonyms:AOAT4
Ordered Locus Names:At1g17290
ORF Names:T13M22.3
OrganismiArabidopsis thaliana (Mouse-ear cress)
Taxonomic identifieri3702 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis
ProteomesiUP000006548 Componenti: Chromosome 1

Organism-specific databases

TAIRiAT1G17290.

Subcellular locationi

Mitochondrion 1 Publication

GO - Cellular componenti

  1. chloroplast Source: TAIR
  2. mitochondrion Source: TAIR
Complete GO annotation...

Keywords - Cellular componenti

Mitochondrion

Pathology & Biotechi

Disruption phenotypei

Strong overall decrease of alanine aminotransferase activity, especially in roots.1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transit peptidei1 – 4747MitochondrionSequence AnalysisAdd
BLAST
Chaini48 – 543496Alanine aminotransferase 1, mitochondrialPRO_0000416042Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei360 – 3601N6-(pyridoxal phosphate)lysineBy similarity

Post-translational modificationi

The N-terminus is blocked.By similarity

Proteomic databases

PRIDEiF4I7I0.
ProMEXiF4I7I0.

Expressioni

Tissue specificityi

Mostly expressed in roots and shoots, mostly in vascular tissues, and, to a lower extent, in flowers and leaves.2 Publications

Inductioni

Rapidly induced upon low-oxygen stress in roots and shoots. Induced by cadmium (at protein level).2 Publications

Gene expression databases

ExpressionAtlasiF4I7I0. baseline.

Interactioni

Subunit structurei

Homodimer.By similarity

Protein-protein interaction databases

IntActiF4I7I0. 1 interaction.
STRINGi3702.AT1G17290.1-P.

Structurei

3D structure databases

ProteinModelPortaliF4I7I0.
SMRiF4I7I0. Positions 66-542.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Keywords - Domaini

Transit peptide

Phylogenomic databases

HOGENOMiHOG000215020.
InParanoidiF4I7I0.
KOiK00814.
OMAiKAWGTDV.

Family and domain databases

Gene3Di3.40.640.10. 1 hit.
3.90.1150.10. 1 hit.
InterProiIPR004839. Aminotransferase_I/II.
IPR015424. PyrdxlP-dep_Trfase.
IPR015421. PyrdxlP-dep_Trfase_major_sub1.
IPR015422. PyrdxlP-dep_Trfase_major_sub2.
[Graphical view]
PfamiPF00155. Aminotran_1_2. 1 hit.
[Graphical view]
SUPFAMiSSF53383. SSF53383. 1 hit.

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

F4I7I0-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MRRFVIGQAK NLIDQSRRRQ LHHHKNLSFV SLIPPFSAPS DSSSRHLSSS
60 70 80 90 100
SSSDMSASDS SSSLPVTLDT INPKVIKCEY AVRGEIVNIA QKLQEDLKTN
110 120 130 140 150
KDAYPFDEII YCNIGNPQSL GQQPITFFRE VLALCSYTAL LDESATHGLF
160 170 180 190 200
SSDSIERAWK ILDQIPGRAT GAYSHSQGIK GLRDAIADGI EARDGFPADP
210 220 230 240 250
NDIFMTDGAS PGVHMMMQLL ITSEKDGILC PIPQYPLYSA SIALHGGTLV
260 270 280 290 300
PYYLDEASGW GLEISELKKQ LEDARSKGIT VRALAVINPG NPTGQVLSEE
310 320 330 340 350
NQRDVVKFCK QEGLVLLADE VYQENVYVPD KKFHSFKKVA RSMGYGEKDL
360 370 380 390 400
ALVSFQSVSK GYYGECGKRG GYMEVTGFTS DVREQIYKMA SVNLCSNISG
410 420 430 440 450
QILASLIMSP PKPGDDSYES YIAEKDGILS SLARRAKTLE EALNKLEGVT
460 470 480 490 500
CNRAEGAMYL FPCLHLPQKA IAAAEAEKTA PDNFYCKRLL KATGIVVVPG
510 520 530 540
SGFRQVPGTW HFRCTILPQE DKIPAIVDRL TAFHQSFMDE FRD
Length:543
Mass (Da):59,821
Last modified:June 27, 2011 - v1
Checksum:i4ED08F2CA3414E4B
GO

Sequence cautioni

The sequence BAD94892.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti307 – 3071K → N in AAF82782 (Ref. 1) Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF275372 mRNA. Translation: AAF82782.1.
AC026479 Genomic DNA. Translation: AAF79891.1.
CP002684 Genomic DNA. Translation: AEE29570.1.
AY039970 mRNA. Translation: AAK64147.2.
AK221072 mRNA. Translation: BAD94892.1. Different initiation.
PIRiD86309.
RefSeqiNP_173173.3. NM_101591.5.
UniGeneiAt.23768.

Genome annotation databases

EnsemblPlantsiAT1G17290.1; AT1G17290.1; AT1G17290.
GeneIDi838301.
KEGGiath:AT1G17290.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF275372 mRNA. Translation: AAF82782.1.
AC026479 Genomic DNA. Translation: AAF79891.1.
CP002684 Genomic DNA. Translation: AEE29570.1.
AY039970 mRNA. Translation: AAK64147.2.
AK221072 mRNA. Translation: BAD94892.1. Different initiation.
PIRiD86309.
RefSeqiNP_173173.3. NM_101591.5.
UniGeneiAt.23768.

3D structure databases

ProteinModelPortaliF4I7I0.
SMRiF4I7I0. Positions 66-542.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiF4I7I0. 1 interaction.
STRINGi3702.AT1G17290.1-P.

Proteomic databases

PRIDEiF4I7I0.
ProMEXiF4I7I0.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblPlantsiAT1G17290.1; AT1G17290.1; AT1G17290.
GeneIDi838301.
KEGGiath:AT1G17290.

Organism-specific databases

GeneFarmi4386.
TAIRiAT1G17290.

Phylogenomic databases

HOGENOMiHOG000215020.
InParanoidiF4I7I0.
KOiK00814.
OMAiKAWGTDV.

Enzyme and pathway databases

UniPathwayiUPA00322.
UPA00528; UER00586.

Gene expression databases

ExpressionAtlasiF4I7I0. baseline.

Family and domain databases

Gene3Di3.40.640.10. 1 hit.
3.90.1150.10. 1 hit.
InterProiIPR004839. Aminotransferase_I/II.
IPR015424. PyrdxlP-dep_Trfase.
IPR015421. PyrdxlP-dep_Trfase_major_sub1.
IPR015422. PyrdxlP-dep_Trfase_major_sub2.
[Graphical view]
PfamiPF00155. Aminotran_1_2. 1 hit.
[Graphical view]
SUPFAMiSSF53383. SSF53383. 1 hit.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Cloning and characterization of Arabidopsis alanine aminotransferase genes."
    Ismond K.P., Dennis E.S., Dolferus R.
    Submitted (MAY-2000) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    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.
    , 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(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] OF 75-543.
    Strain: cv. Columbia.
  3. The Arabidopsis Information Resource (TAIR)
    Submitted (MAR-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.
    , 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(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 3-543.
    Strain: cv. Columbia.
  5. "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.
    , Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J., Hayashizaki Y., Shinozaki K.
    Submitted (FEB-2005) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 448-543.
    Strain: cv. Columbia.
  6. "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(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: TISSUE SPECIFICITY, GENE FAMILY, NOMENCLATURE.
  7. "Experimental analysis of the Arabidopsis mitochondrial proteome highlights signaling and regulatory components, provides assessment of targeting prediction programs, and indicates plant-specific mitochondrial proteins."
    Heazlewood J.L., Tonti-Filippini J.S., Gout A.M., Day D.A., Whelan J., Millar A.H.
    Plant Cell 16:241-256(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
    Strain: cv. Landsberg erecta.
  8. "The early responses of Arabidopsis thaliana cells to cadmium exposure explored by protein and metabolite profiling analyses."
    Sarry J.-E., Kuhn L., Ducruix C., Lafaye A., Junot C., Hugouvieux V., Jourdain A., Bastien O., Fievet J.B., Vailhen D., Amekraz B., Moulin C., Ezan E., Garin J., Bourguignon J.
    Proteomics 6:2180-2198(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: INDUCTION BY CADMIUM [LARGE SCALE ANALYSIS].
    Strain: cv. Columbia.
  9. "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(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, TISSUE SPECIFICITY, INDUCTION BY HYPOXIC STRESS, DISRUPTION PHENOTYPE.

Entry informationi

Entry nameiALAT1_ARATH
AccessioniPrimary (citable) accession number: F4I7I0
Secondary accession number(s): Q56Z96
, Q94BP8, Q9LKJ4, Q9LN15
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 20, 2012
Last sequence update: June 27, 2011
Last modified: March 31, 2015
This is version 31 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Arabidopsis thaliana
    Arabidopsis thaliana: entries and gene names
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.