Reviewed, UniProtKB/Swiss-Prot O94320 (AATM_SCHPO)

Names and origin

Protein names

Recommended name:
    Aspartate aminotransferase, mitochondrial
    EC=2.6.1.1
Alternative name(s):
    Transaminase A

Gene names

Name:	aat1
ORF Names:	SPBC725.01

Organism

Schizosaccharomyces pombe (Fission yeast) [Complete proteome]

Taxonomic identifier

4896 [NCBI]

Taxonomic lineage

Eukaryota › Fungi › Dikarya › Ascomycota › Taphrinomycotina › Schizosaccharomycetes › Schizosaccharomycetales › Schizosaccharomycetaceae › Schizosaccharomyces

Protein attributes

Sequence length	437 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at transcript level.

General annotation (Comments)

Catalytic activity	L-aspartate + 2-oxoglutarate = oxaloacetate + L-glutamate. UniProtKB Q01802
Cofactor	Pyridoxal phosphate By similarity. UniProtKB Q01802
Subunit structure	Homodimer By similarity. UniProtKB Q01802
Subcellular location	Mitochondrion matrix. Ref.2
Miscellaneous	In eukaryotes there are cytoplasmic, mitochondrial and chloroplastic isozymes.
Sequence similarities	Belongs to the class-I pyridoxal-phosphate-dependent aminotransferase family.

Ontologies

Keywords
Cellular component	Mitochondrion
Domain	Transit peptide
Ligand	Pyridoxal phosphate
Molecular function	Aminotransferase Transferase
Technical term	Complete proteome
Gene Ontology (GO)
Biological process	biosynthetic process Inferred from electronic annotation. Source: InterPro cellular amino acid metabolic process Inferred from electronic annotation. Source: InterPro
Cellular component	mitochondrial matrix Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	L-aspartate:2-oxoglutarate aminotransferase activity Inferred from electronic annotation. Source: EC 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 – ?		Mitochondrion Potential UniProtKB Q01802
	Chain	? – 437		Aspartate aminotransferase, mitochondrial UniProtKB Q01802		PRO_0000309452
Amino acid modifications
	Modified residue	284	1	N6-(pyridoxal phosphate)lysine By similarity

Sequences

	Sequence		Length	Mass (Da)
	O94320-1 [UniParc]. Last modified May 1, 1999. Version 1. Checksum: 991D245BB1047A63	FASTA	437	48,243
	10 20 30 40 50 60 MLARNLRCLH PNTFASLKTN VSYHGVKCLA SQSKRGFKVW ADVPMGPPDP IFGITEAYKK 70 80 90 100 110 120 DGDVKKMNLG AGTYRDDAGK PYVLPSVRQA ETELLSQKLD KEYAPITGIP SFRVQATKLA 130 140 150 160 170 180 YGDVYESIKD RLVSAQSISG TGALCIAANF LASFYPSKTI YVSDPTWGNH KNVFSRAGLT 190 200 210 220 230 240 VKSYKYYDPA TRGLDIKGML SDLTSAPDGS IILLHACAHN PTGVDPTKAQ WDDILKTMQK 250 260 270 280 290 300 KNHFALLDMA YQGFASGDFA RDAYATRLFA SSNVPMLLCQ SFAKNMGLYG ERAGCFSILA 310 320 330 340 350 360 NDAEEAARIE SQTKILIRAL YSNPPVNGAR IANHILSNPA LREQWAGEVV GMSERLKSMR 370 380 390 400 410 420 KALRNILEKD LKNKHSWKHI TDQIGMFCYT GLNPQQVDVL AKQYHIYLTK NGRISISGLN 430 TSNVRYFAEA INAVTSN

References

[1]

"The genome sequence of Schizosaccharomyces pombe." Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A., Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S., Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M. , Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S., Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S., Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D., Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P., Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K., O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M., Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N., Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A., Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R., Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M., Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A., Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A., Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H., Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S., Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C., Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A., Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M., del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S., Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R., Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G., Nurse P. Nature 415:871-880(2002) [PubMed: 11859360] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 38366 / 972.

[2]

"ORFeome cloning and global analysis of protein localization in the fission yeast Schizosaccharomyces pombe." Matsuyama A., Arai R., Yashiroda Y., Shirai A., Kamata A., Sekido S., Kobayashi Y., Hashimoto A., Hamamoto M., Hiraoka Y., Horinouchi S., Yoshida M. Nat. Biotechnol. 24:841-847(2006) [PubMed: 16823372] [Abstract] Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].

Cross-references

Sequence databases
EMBLGenBankDDBJ	CU329671 Genomic DNA. Translation: CAA22173.1.
PIR	T40653.
RefSeq	NP_595481.1.
3D structure databases
HSSP	HSSP built from PDB template 7AAT based on UniProtKB P00508.
ModBase	Search...
Protein-protein interaction databases
STRING	O94320.
Genome annotation databases
GeneID	2541186.
GenomeReviews	Gene locus aat1 in contig CU329671_GR.
KEGG	spo:SPBC725.01.
NMPDR	fig|4896.1.peg.1347.
Organism-specific databases
GeneDB_Spombe	SPBC725.01.
Phylogenomic databases
OMA	KEYSTIT.
Enzyme and pathway databases
BRENDA	2.6.1.1. 653.
Gene expression databases
ArrayExpress	O94320.
Family and domain databases
InterPro	IPR004839. Aminotransferase_I/II. IPR000796. Asp_trans. IPR004838. NHTrfase_class1_PyrdxlP-BS. IPR015421. PyrdxlP-dep_Trfase_major_sub1. [Graphical view]
Gene3D	G3DSA:3.40.640.10. PyrdxlP-dep_Trfase_major_sub1. 1 hit.
PANTHER	PTHR11879. Asp_trans. 1 hit.
Pfam	PF00155. Aminotran_1_2. 1 hit. [Graphical view]
PRINTS	PR00799. TRANSAMINASE.
PROSITE	PS00105. AA_TRANSFER_CLASS_1. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

AATM_SCHPO

Accession

Primary (citable) accession number: O94320

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 13, 2007
Last sequence update:	May 1, 1999
Last modified:	November 3, 2009
This is version 48 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

FPAP (Fungal Proteome Annotation Project)