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O42652 (AATC_SCHPO) Reviewed, UniProtKB/Swiss-Prot

Last modified December 14, 2011. Version 67. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
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to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Aspartate aminotransferase, cytoplasmic
EC=2.6.1.1
Alternative name(s):
Transaminase A
Gene names
Name:aat2
ORF Names:SPAC10F6.13c
OrganismSchizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Taxonomic identifier284812 [NCBI]
Taxonomic lineageEukaryota › Fungi › Dikarya › Ascomycota › Taphrinomycotina › Schizosaccharomycetes › Schizosaccharomycetales › Schizosaccharomycetaceae › Schizosaccharomyces

Protein attributes

Sequence length409 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence 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.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed By similarity UniProtKB P23542
Chain2 – 409408Aspartate aminotransferase, cytoplasmic UniProtKB P23542
PRO_0000309451

Sites

Binding site381Aspartate; via amide nitrogen By similarity
Binding site1381Aspartate By similarity
Binding site1911Aspartate By similarity
Binding site3831Aspartate By similarity

Amino acid modifications

Modified residue21N-acetylserine By similarity UniProtKB P23542
Modified residue2551N6-(pyridoxal phosphate)lysine By similarity
Modified residue3851Phosphoserine By similarity UniProtKB P23542

Sequences

Sequence LengthMass (Da)Tools
O42652 [UniParc].

Last modified June 1, 1998. Version 1.
Checksum: 6CE10FFCC18D3E4A

FASTA40946,140
        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

« Hide

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. expand/collapse author list , 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: 972 / ATCC 24843.
[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].
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		CU329670 Genomic DNA. Translation: CAA15726.1.
PIRT37507.
RefSeqNP_593264.1. NM_001018661.1.

3D structure databases

HSSPHSSP built from PDB template 1YAA based on UniProtKB P23542.
ProteinModelPortalO42652.
SMRO42652. Positions 6-408.
ModBaseSearch...

Protein-protein interaction databases

STRINGO42652.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiSPAC10F6.13c.1; SPAC10F6.13c.1:pep; SPAC10F6.13c.
GeneID2543020.
GenomeReviewsGene locus aat2 in contig CU329670_GR.
KEGGspo:SPAC10F6.13c.
NMPDRfig|4896.1.peg.3234.

Organism-specific databases

GeneDB_SpombeSPAC10F6.13c.

Phylogenomic databases

eggNOGfuNOG05116.
GeneTreeEFGT00050000000248.
HOGENOMHBG446828.
OMAAFFDCAY.
OrthoDBEOG4BP4M8.

Gene expression databases

ArrayExpressO42652.

Family and domain databases

InterProIPR004839. Aminotransferase_I/II.
IPR000796. Asp_trans.
IPR015424. PyrdxlP-dep_Trfase_major_dom.
IPR015421. PyrdxlP-dep_Trfase_major_sub1.
[Graphical view]
Gene3DG3DSA:3.40.640.10. PyrdxlP-dep_Trfase_major_sub1. 1 hit.
KOK14454.
PANTHERPTHR11879. Asp_trans. 1 hit.
PfamPF00155. Aminotran_1_2. 1 hit.
[Graphical view]
PRINTSPR00799. TRANSAMINASE.
SUPFAMSSF53383. PyrdxlP-dep_Trfase_major. 1 hit.
PROSITEPS00105. AA_TRANSFER_CLASS_1. False negative.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameAATC_SCHPO
AccessionPrimary (citable) accession number: O42652
Entry history
Integrated into UniProtKB/Swiss-Prot: November 13, 2007
Last sequence update: June 1, 1998
Last modified: December 14, 2011
This is version 67 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Relevant documents

Schizosaccharomyces pombe

Schizosaccharomyces pombe: entries and gene names

SIMILARITY comments

Index of protein domains and families

to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents