Reviewed, UniProtKB/Swiss-Prot O42652 (AATC_SCHPO)

Names and origin

Protein names

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

Gene names

Name:	aat2
ORF Names:	SPAC10F6.13c

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	409 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)

Function	Plays a key role in amino acid metabolism By similarity.
Catalytic activity	L-aspartate + 2-oxoglutarate = oxaloacetate + L-glutamate. UniProtKB P23542
Cofactor	Pyridoxal phosphate By similarity. UniProtKB P23542
Subunit structure	Homodimer By similarity. UniProtKB P23542
Subcellular location	Cytoplasm 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	Cytoplasm
Ligand	Pyridoxal phosphate
Molecular function	Aminotransferase Transferase
PTM	Acetylation Phosphoprotein
Technical term	Complete proteome
Gene Ontology (GO)
Biological process	2-oxoglutarate metabolic process Inferred from sequence or structural similarity. Source: UniProtKB aspartate metabolic process Inferred from sequence or structural similarity. Source: UniProtKB biosynthetic process Inferred from electronic annotation. Source: InterPro glutamate metabolic process Inferred from sequence or structural similarity. Source: UniProtKB
Cellular component	cytosol Ref.2 Inferred from direct assay. Source: GeneDB_SPombe nucleus Ref.2 Inferred from direct assay. Source: GeneDB_SPombe
Molecular function	L-aspartate:2-oxoglutarate aminotransferase activity Inferred from sequence or structural similarity. 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
	Initiator methionine	1	1	Removed By similarity UniProtKB P23542
	Chain	2 – 409	408	Aspartate aminotransferase, cytoplasmic UniProtKB P23542		PRO_0000309451
Sites
	Binding site	38	1	Aspartate; via amide nitrogen By similarity
	Binding site	138	1	Aspartate By similarity
	Binding site	191	1	Aspartate By similarity
	Binding site	383	1	Aspartate By similarity
Amino acid modifications
	Modified residue	2	1	N-acetylserine By similarity UniProtKB P23542
	Modified residue	255	1	N6-(pyridoxal phosphate)lysine By similarity
	Modified residue	385	1	Phosphoserine By similarity UniProtKB P23542

Sequences

	Sequence		Length	Mass (Da)
	O42652-1 [UniParc]. Last modified June 1, 1998. Version 1. Checksum: 6CE10FFCC18D3E4A	FASTA	409	46,140
	10 20 30 40 50 60 MSDYGFANIE EAKADAIFKL NAQYHQDEDP KKVNMSVGAY RDDTGKPWIL PAVKKASKIV 70 80 90 100 110 120 EEQASFNHEY LPIAGLPRFT KAAAEVLFRP NPHLLSEDRV ASMQSVSGTG ANFLAASFIE 130 140 150 160 170 180 TFYVKHTGAH VYISNPTWPV HRTLWEKLGV TVDTYPYWDA KNRSFDYEGM LSTIKSAPEG 190 200 210 220 230 240 SIFLLHACAH NPTGIDPTRE QWLSIFESLL SRKHLVVFDI AYQGFASGDL NRDSWALNEF 250 260 270 280 290 300 VKYNKDFFVC QSFAKNMGLY GERTGCMHYV AKDASTKNKV LSQLCIVQRN TISNPPAYGA 310 320 330 340 350 360 RIAAEILNSP QLFAEWEQDL KTMSSRIIEM RKRLRDSLVA LKTPGSWDHI TQQIGMFSFT 370 380 390 400 GLTPAQVQFC QERYHLYFSA NGRISMAGLN NSNVEHVAQA FNHAVRELP

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
EMBL GenBank DDBJ	CU329670 Genomic DNA. Translation: CAA15726.1.
PIR	T37507.
RefSeq	NP_593264.1.
3D structure databases
HSSP	HSSP built from PDB template 1YAA based on UniProtKB P23542.
SMR	O42652. Positions 6-408.
ModBase	Search...
Protein-protein interaction databases
STRING	O42652.
Genome annotation databases
GeneID	2543020.
GenomeReviews	Gene locus aat2 in contig CU329670_GR.
KEGG	spo:SPAC10F6.13c.
NMPDR	fig|4896.1.peg.3234.
Organism-specific databases
GeneDB_Spombe	SPAC10F6.13c.
Phylogenomic databases
eggNOG	fuNOG05116.
HOGENOM	HBG446828.
OMA	EFRTCAS.
OrthoDB	EOG9JDJQ6.
PhylomeDB	O42652.
Enzyme and pathway databases
BRENDA	2.6.1.1. 653.
Gene expression databases
ArrayExpress	O42652.
Family and domain databases
InterPro	IPR004839. Aminotransferase_I/II. IPR000796. Asp_trans. 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	PTHR11879. Asp_trans. 1 hit.
Pfam	PF00155. Aminotran_1_2. 1 hit. [Graphical view]
PRINTS	PR00799. TRANSAMINASE.
PROSITE	PS00105. AA_TRANSFER_CLASS_1. False negative. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

AATC_SCHPO

Accession

Primary (citable) accession number: O42652

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 13, 2007
Last sequence update:	June 1, 1998
Last modified:	February 9, 2010
This is version 52 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

FPAP (Fungal Proteome Annotation Project)