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Reviewed, UniProtKB/Swiss-Prot O94320 (AATM_SCHPO)

Last modified November 25, 2008. Version 41. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    Aspartate aminotransferase, mitochondrial
    EC=2.6.1.1
Alternative name(s):
    Transaminase A
Gene names
Name: aat1
ORF Names: SPBC725.01
OrganismSchizosaccharomyces pombe (Fission yeast) [Complete proteome]
Taxonomic identifier4896 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaTaphrinomycotinaSchizosaccharomycetesSchizosaccharomycetalesSchizosaccharomycetaceaeSchizosaccharomyces

Protein attributes

Sequence length437 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at transcript level.

General annotation (Comments)

Catalytic activity

L-aspartate + 2-oxoglutarate = oxaloacetate + L-glutamate.

Cofactor

Pyridoxal phosphate By similarity.

Subunit structure

Homodimer By similarity.

Subcellular location

Mitochondrion matrix.

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 componentMitochondrion
   DomainTransit peptide
   LigandPyridoxal phosphate
   Molecular functionAminotransferase
Transferase
   Technical termComplete proteome

Gene Ontology (GO)

   Biological processamino acid metabolic process

Inferred from electronic annotation. Source: InterPro

biosynthetic process

Inferred from electronic annotation. Source: InterPro

   Cellular componentmitochondrial matrix

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular functionaspartate transaminase activity

Inferred from electronic annotation. Source: EC

pyridoxal phosphate binding

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Transit peptide1 – ?Mitochondrion Potential
Chain? – 437Aspartate aminotransferase, mitochondrialPRO_0000309452

Sites

Binding site2841Pyridoxal phosphate (covalent) By similarity

Sequences

Sequence LengthMass (Da)Tools
O94320-1 [UniParc].

Last modified May 1, 1999. Version 1.
Checksum: 991D245BB1047A63

FASTA43748,243
        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 

« 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: 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

CU329671 Genomic DNA. Translation: CAA22173.1.
PIRT40653.
RefSeqNP_595481.1.

3D structure databases

HSSPHSSP built from PDB template 7AAT based on UniProtKB P00508.
ModBaseSearch...

Genome annotation databases

GeneID2541186.
KEGGspo:SPBC725.01.
NMPDRfig|4896.1.peg.1347.

Organism-specific databases

GeneDB_SpombeSPBC725.01.

Gene expression databases

ArrayExpressO94320.

Family and domain databases

InterProIPR004839. Aminotrans_I/II.
IPR000796. Asp_trans.
IPR004838. NHTrfase_class1_PyrdxlP-BS.
IPR015421. PyrdxlP-dep_Trfase_major_sub1.
[Graphical view]
Gene3DG3DSA:3.40.640.10. PyrdxlP-dep_Trfase_major_sub1. 1 hit.
PANTHERPTHR11879. Asp_trans. 1 hit.
PfamPF00155. Aminotran_1_2. 1 hit.
[Graphical view]
PRINTSPR00799. TRANSAMINASE.
PROSITEPS00105. AA_TRANSFER_CLASS_1. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameAATM_SCHPO
AccessionPrimary (citable) accession number: O94320
Entry history
Integrated into UniProtKB/Swiss-Prot: November 13, 2007
Last sequence update: May 1, 1999
Last modified: November 25, 2008
This is version 41 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectFPAP (Fungal Proteome Annotation Project)

Relevant documents

Schizosaccharomyces pombe

Schizosaccharomyces pombe: entries and gene names

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents