Reviewed, UniProtKB/Swiss-Prot Q940M2 (AGT21_ARATH)

Names and origin

Protein names

Recommended name:
    Alanine--glyoxylate aminotransferase 2 homolog 1, mitochondrial
    EC=2.6.1.44
Alternative name(s):
    Beta-alanine-pyruvate aminotransferase 1

Gene names

Name:	AGT2
Ordered Locus Names:	At4g39660
ORF Names:	T19P19.50

Organism

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

Taxonomic identifier

3702 [NCBI]

Taxonomic lineage

Eukaryota › Viridiplantae › Streptophyta › Embryophyta › Tracheophyta › Spermatophyta › Magnoliophyta › eudicotyledons › core eudicotyledons › rosids › malvids › Brassicales › Brassicaceae › Arabidopsis

Protein attributes

Sequence length	476 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)

Catalytic activity	L-alanine + glyoxylate = pyruvate + glycine.
Cofactor	Pyridoxal phosphate.
Subunit structure	Homotetramer By similarity.
Subcellular location	Mitochondrion Ref.4.
Sequence similarities	Belongs to the class-III pyridoxal-phosphate-dependent aminotransferase family.
Sequence caution	The sequence CAA18752.1 differs from that shown. Reason: Erroneous gene model prediction. The sequence CAB80629.1 differs from that shown. Reason: Erroneous gene model prediction.

Ontologies

Keywords
Biological process	Photorespiration
Cellular component	Mitochondrion
Domain	Transit peptide
Ligand	Pyridoxal phosphate
Molecular function	Aminotransferase Transferase
Technical term	Complete proteome
Gene Ontology (GO)
Biological process	arginine catabolic process to glutamate Ref.1 Inferred from direct assay. Source: UniProtKB photorespiration Inferred from electronic annotation. Source: UniProtKB-KW response to cadmium ion Inferred from expression pattern. Source: TAIR
Cellular component	mitochondrion Ref.1 Ref.4 Inferred from direct assay. Source: UniProtKB plasma membrane Inferred from direct assay. Source: TAIR
Molecular function	alanine-glyoxylate transaminase activity Ref.1 Inferred from direct assay. Source: UniProtKB 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 – 12	12	Mitochondrion Potential
	Chain	13 – 476	464	Alanine--glyoxylate aminotransferase 2 homolog 1, mitochondrial		PRO_0000041945
Amino acid modifications
	Modified residue	320	1	N6-(pyridoxal phosphate)lysine By similarity
Experimental info
	Sequence conflict	240	1	H → Q in AAD48837. Ref.1

Sequences

	Sequence		Length	Mass (Da)
	Q940M2-1 [UniParc]. Last modified December 1, 2001. Version 1. Checksum: 9E5ABC10C3C2EC83	FASTA	476	51,953
	10 20 30 40 50 60 MALQRQLLKR ATSDIYHRRA ISLLRTDFST SPSIADAPPH IPPFVHQPRP YKGPSADEVL 70 80 90 100 110 120 QKRKKFLGPS LFHYYQKPLN IVEGKMQYLY DESGRRYLDA FAGIVTVSCG HCHPDILNAI 130 140 150 160 170 180 TEQSKLLQHA TTIYLHHAIG DFAEALAAKM PGNLKVVYFV NSGSEANELA MMMARLYTGS 190 200 210 220 230 240 LEMISLRNAY HGGSSNTIGL TALNTWKYPL PQGEIHHVVN PDPYRGVFGS DGSLYAKDVH 250 260 270 280 290 300 DHIEYGTSGK VAGFIAETIQ GVGGAVELAP GYLKSVYEIV RNAGGVCIAD EVQTGFGRTG 310 320 330 340 350 360 SHYWGFQTQD VVPDIVTMAK GIGNGLPLGA VVTTPEIASV LASKILFNTF GGNPVCSAGG 370 380 390 400 410 420 LAVLNVIDKE KRQEHCAEVG SHLIQRLKDV QKRHDIIGDV RGRGLMVGIE LVSDRKDKTP 430 440 450 460 470 AKAETSVLFE QLRELGILVG KGGLHGNVFR IKPPMCFTKD DADFLVDALD YSISRL

References

[1]	"Alanine aminotransferase homologs catalyze the glutamate:glyoxylate aminotransferase reaction in peroxisomes of Arabidopsis." Liepman A.H., Olsen L.J. Plant Physiol. 131:215-227(2003) [PubMed: 12529529] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Strain: cv. Columbia.
[2]	"Sequence and analysis of chromosome 4 of the plant Arabidopsis thaliana." Mayer K.F.X., Schueller C., Wambutt R., Murphy G., Volckaert G., Pohl T., Duesterhoeft A., Stiekema W., Entian K.-D., Terryn N., Harris B., Ansorge W., Brandt P., Grivell L.A., Rieger M., Weichselgartner M., de Simone V., Obermaier B. , Mache R., Mueller M., Kreis M., Delseny M., Puigdomenech P., Watson M., Schmidtheini T., Reichert B., Portetelle D., Perez-Alonso M., Boutry M., Bancroft I., Vos P., Hoheisel J., Zimmermann W., Wedler H., Ridley P., Langham S.-A., McCullagh B., Bilham L., Robben J., van der Schueren J., Grymonprez B., Chuang Y.-J., Vandenbussche F., Braeken M., Weltjens I., Voet M., Bastiaens I., Aert R., Defoor E., Weitzenegger T., Bothe G., Ramsperger U., Hilbert H., Braun M., Holzer E., Brandt A., Peters S., van Staveren M., Dirkse W., Mooijman P., Klein Lankhorst R., Rose M., Hauf J., Koetter P., Berneiser S., Hempel S., Feldpausch M., Lamberth S., Van den Daele H., De Keyser A., Buysshaert C., Gielen J., Villarroel R., De Clercq R., van Montagu M., Rogers J., Cronin A., Quail M.A., Bray-Allen S., Clark L., Doggett J., Hall S., Kay M., Lennard N., McLay K., Mayes R., Pettett A., Rajandream M.A., Lyne M., Benes V., Rechmann S., Borkova D., Bloecker H., Scharfe M., Grimm M., Loehnert T.-H., Dose S., de Haan M., Maarse A.C., Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Fartmann B., Granderath K., Dauner D., Herzl A., Neumann S., Argiriou A., Vitale D., Liguori R., Piravandi E., Massenet O., Quigley F., Clabauld G., Muendlein A., Felber R., Schnabl S., Hiller R., Schmidt W., Lecharny A., Aubourg S., Chefdor F., Cooke R., Berger C., Monfort A., Casacuberta E., Gibbons T., Weber N., Vandenbol M., Bargues M., Terol J., Torres A., Perez-Perez A., Purnelle B., Bent E., Johnson S., Tacon D., Jesse T., Heijnen L., Schwarz S., Scholler P., Heber S., Francs P., Bielke C., Frishman D., Haase D., Lemcke K., Mewes H.-W., Stocker S., Zaccaria P., Bevan M., Wilson R.K., de la Bastide M., Habermann K., Parnell L., Dedhia N., Gnoj L., Schutz K., Huang E., Spiegel L., Sekhon M., Murray J., Sheet P., Cordes M., Abu-Threideh J., Stoneking T., Kalicki J., Graves T., Harmon G., Edwards J., Latreille P., Courtney L., Cloud J., Abbott A., Scott K., Johnson D., Minx P., Bentley D., Fulton B., Miller N., Greco T., Kemp K., Kramer J., Fulton L., Mardis E., Dante M., Pepin K., Hillier L.W., Nelson J., Spieth J., Ryan E., Andrews S., Geisel C., Layman D., Du H., Ali J., Berghoff A., Jones K., Drone K., Cotton M., Joshu C., Antonoiu B., Zidanic M., Strong C., Sun H., Lamar B., Yordan C., Ma P., Zhong J., Preston R., Vil D., Shekher M., Matero A., Shah R., Swaby I.K., O'Shaughnessy A., Rodriguez M., Hoffman J., Till S., Granat S., Shohdy N., Hasegawa A., Hameed A., Lodhi M., Johnson A., Chen E., Marra M.A., Martienssen R., McCombie W.R. Nature 402:769-777(1999) [PubMed: 10617198] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: cv. Columbia.
[3]	"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: 14593172] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Strain: cv. Columbia.
[4]	"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: 14671022] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AF166351 mRNA. Translation: AAD48837.1. AL022605 Genomic DNA. Translation: CAA18752.1. Sequence problems. AL161595 Genomic DNA. Translation: CAB80629.1. Sequence problems. AY054264 mRNA. Translation: AAL06923.1. BT002306 mRNA. Translation: AAN73303.1.
IPI	IPI00519673.
PIR	T05003.
RefSeq	NP_568064.1.
UniGene	At.22488 Rra.1685 Rsa.8726
3D structure databases
SMR	Q940M2. Positions 58-475.
ModBase	Search...
Protein-protein interaction databases
STRING	Q940M2.
Proteomic databases
PRIDE	Q940M2.
Genome annotation databases
GeneID	830120.
GenomeReviews	Gene locus AT4G39660 in contig CT486007_GR.
KEGG	ath:AT4G39660.
NMPDR	fig|3702.1.peg.22105.
Organism-specific databases
GeneFarm	5077. 483.
TAIR	At4g39660.
Phylogenomic databases
HOGENOM	HBG725944.
InParanoid	Q940M2.
OMA	GIVTVSC.
PhylomeDB	Q940M2.
Enzyme and pathway databases
BRENDA	2.6.1.44. 302.
Gene expression databases
Genevestigator	Q940M2.
GermOnline	AT4G39660. Arabidopsis thaliana.
Family and domain databases
InterPro	IPR005814. Aminotrans_3. IPR015424. PyrdxlP-dep_Trfase_major_dom. IPR015421. PyrdxlP-dep_Trfase_major_sub1. [Graphical view]
Gene3D	G3DSA:3.40.640.10. PyrdxlP-dep_Trfase_major_sub1. 1 hit.
PANTHER	PTHR11986. Aminotrans_3. 1 hit.
Pfam	PF00202. Aminotran_3. 1 hit. [Graphical view]
PROSITE	PS00600. AA_TRANSFER_CLASS_3. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

AGT21_ARATH

Accession

Primary (citable) accession number: Q940M2
Secondary accession number(s): Q9SU41, Q9SWE2

Entry history

Integrated into UniProtKB/Swiss-Prot:	September 13, 2005
Last sequence update:	December 1, 2001
Last modified:	February 9, 2010
This is version 59 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

PPAP (Plant Proteome Annotation Project)