F4I7I0 (ALAT1_ARATH) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Alanine aminotransferase 1, mitochondrial
Short name=AtAlaAT1
Short name=AtAlaATc
EC=2.6.1.2

Alternative name(s):
Alanine-2-oxoglutarate aminotransferase 4
EC=2.6.1.-

Gene names

Name:	ALAAT1
Synonyms:	AOAT4
Ordered Locus Names:	At1g17290
ORF Names:	T13M22.3

Organism

Arabidopsis thaliana (Mouse-ear cress) [Reference proteome]

Taxonomic identifier

3702 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Viridiplantae › Streptophyta › Streptophytina › Embryophyta › Tracheophyta › Euphyllophyta › Spermatophyta › Magnoliophyta › eudicotyledons › core eudicotyledons › rosids › malvids › Brassicales › Brassicaceae › Camelineae › Arabidopsis

Protein attributes

Sequence length	543 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Major alanine aminotransferase in roots. Ref.9
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.
Tissue specificity	Mostly expressed in roots and shoots, mostly in vascular tissues, and, to a lower extent, in flowers and leaves. Ref.6 Ref.9
Induction	Rapidly induced upon low-oxygen stress in roots and shoots. Induced by cadmium (at protein level). Ref.9
Post-translational modification	The N-terminus is blocked By similarity.
Disruption phenotype	Strong overall decrease of alanine aminotransferase activity, especially in roots. Ref.9
Sequence similarities	Belongs to the class-I pyridoxal-phosphate-dependent aminotransferase family. Alanine aminotransferase subfamily.
Sequence caution	The sequence BAD94892.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.

Ontologies

Keywords
Cellular component	Mitochondrion
Domain	Transit peptide
Ligand	Pyridoxal phosphate
Molecular function	Aminotransferase Transferase
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	L-alanine catabolic process, by transamination Inferred from mutant phenotype Ref.9. Source: TAIR biosynthetic process Inferred from electronic annotation. Source: InterPro response to cadmium ion Inferred from expression pattern Ref.8PubMed 17075075. Source: TAIR response to hypoxia Inferred from expression pattern Ref.9. Source: TAIR
Cellular_component	chloroplast Inferred from direct assay PubMed 15028209. Source: TAIR mitochondrion Inferred from direct assay PubMed 11743115Ref.7PubMed 17137349PubMed 18385124. Source: TAIR
Molecular_function	ATP binding Inferred from direct assay PubMed 17137349. Source: TAIR L-alanine:2-oxoglutarate aminotransferase activity Inferred from direct assay Ref.9. Source: TAIR pyridoxal phosphate binding Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Transit peptide	1 – 47	47	Mitochondrion Potential
	Chain	48 – 543	496	Alanine aminotransferase 1, mitochondrial		PRO_0000416042
Amino acid modifications
	Modified residue	360	1	N6-(pyridoxal phosphate)lysine By similarity
Experimental info
	Sequence conflict	307	1	K → N in AAF82782. Ref.1

Sequences

	Sequence		Length	Mass (Da)
	F4I7I0 [UniParc]. Last modified June 28, 2011. Version 1. Checksum: 4ED08F2CA3414E4B	FASTA	543	59,821
	10 20 30 40 50 60 MRRFVIGQAK NLIDQSRRRQ LHHHKNLSFV SLIPPFSAPS DSSSRHLSSS SSSDMSASDS 70 80 90 100 110 120 SSSLPVTLDT INPKVIKCEY AVRGEIVNIA QKLQEDLKTN KDAYPFDEII YCNIGNPQSL 130 140 150 160 170 180 GQQPITFFRE VLALCSYTAL LDESATHGLF SSDSIERAWK ILDQIPGRAT GAYSHSQGIK 190 200 210 220 230 240 GLRDAIADGI EARDGFPADP NDIFMTDGAS PGVHMMMQLL ITSEKDGILC PIPQYPLYSA 250 260 270 280 290 300 SIALHGGTLV PYYLDEASGW GLEISELKKQ LEDARSKGIT VRALAVINPG NPTGQVLSEE 310 320 330 340 350 360 NQRDVVKFCK QEGLVLLADE VYQENVYVPD KKFHSFKKVA RSMGYGEKDL ALVSFQSVSK 370 380 390 400 410 420 GYYGECGKRG GYMEVTGFTS DVREQIYKMA SVNLCSNISG QILASLIMSP PKPGDDSYES 430 440 450 460 470 480 YIAEKDGILS SLARRAKTLE EALNKLEGVT CNRAEGAMYL FPCLHLPQKA IAAAEAEKTA 490 500 510 520 530 540 PDNFYCKRLL KATGIVVVPG SGFRQVPGTW HFRCTILPQE DKIPAIVDRL TAFHQSFMDE FRD

References

	« Hide 'large scale' referencesShow '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]. 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(2000) [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 (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. , 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 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 (MAR-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(2003) [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(2004) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], 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(2006) [PubMed] [Europe PMC] [Abstract] Cited for: INDUCTION BY CADMIUM [LARGE SCALE ANALYSIS], IDENTIFICATION BY MASS SPECTROMETRY [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(2007) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, TISSUE SPECIFICITY, INDUCTION BY HYPOXIC STRESS, DISRUPTION PHENOTYPE.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	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.
IPI	IPI00545847.
PIR	D86309.
RefSeq	NP_173173.3. NM_101591.5.
UniGene	At.23768.
3D structure databases
ProteinModelPortal	F4I7I0.
SMR	F4I7I0. Positions 66-542.
ModBase	Search...
Protein-protein interaction databases
IntAct	F4I7I0. 1 interaction.
STRING	3702.AT1G17290.1-P.
Proteomic databases
PRIDE	F4I7I0.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblPlants	AT1G17290.1; AT1G17290.1; AT1G17290.
GeneID	838301.
KEGG	ath:AT1G17290.
Organism-specific databases
GeneFarm	4386.
TAIR	At1g17290.
Phylogenomic databases
HOGENOM	HOG000215020.
KO	K00814.
OMA	LKLMSVR.
Enzyme and pathway databases
UniPathway	UPA00322. UPA00528; UER00586.
Family and domain databases
Gene3D	3.40.640.10. 1 hit. 3.90.1150.10. 1 hit.
InterPro	IPR004839. Aminotransferase_I/II. IPR015424. PyrdxlP-dep_Trfase. IPR015421. PyrdxlP-dep_Trfase_major_sub1. IPR015422. PyrdxlP-dep_Trfase_major_sub2. [Graphical view]
Pfam	PF00155. Aminotran_1_2. 1 hit. [Graphical view]
SUPFAM	SSF53383. PyrdxlP-dep_Trfase_major. 1 hit.
ProtoNet	Search...

Entry information

Entry name

ALAT1_ARATH

Accession

Primary (citable) accession number: F4I7I0
Secondary accession number(s): Q56Z96 , Q94BP8, Q9LKJ4, Q9LN15

Entry history

Integrated into UniProtKB/Swiss-Prot:	March 21, 2012
Last sequence update:	June 28, 2011
Last modified:	April 3, 2013
This is version 20 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Plant Protein Annotation Program