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Protein

Aspartate aminotransferase, cytoplasmic

Gene

aat2

Organism
Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Protein inferred from homologyi

Functioni

Plays a key role in amino acid metabolism.By similarity

Catalytic activityi

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

Cofactori

pyridoxal 5'-phosphateBy similarity

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei38 – 381Aspartate; via amide nitrogenBy similarity
Binding sitei138 – 1381AspartateBy similarity
Binding sitei191 – 1911AspartateBy similarity
Binding sitei383 – 3831AspartateBy similarity

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Aminotransferase, Transferase

Keywords - Ligandi

Pyridoxal phosphate

Enzyme and pathway databases

ReactomeiR-SPO-70263. Gluconeogenesis.
R-SPO-70614. Amino acid synthesis and interconversion (transamination).

Names & Taxonomyi

Protein namesi
Recommended name:
Aspartate aminotransferase, cytoplasmic (EC:2.6.1.1)
Alternative name(s):
Transaminase A
Gene namesi
Name:aat2By similarity
ORF Names:SPAC10F6.13c
OrganismiSchizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Taxonomic identifieri284812 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaTaphrinomycotinaSchizosaccharomycetesSchizosaccharomycetalesSchizosaccharomycetaceaeSchizosaccharomyces
Proteomesi
  • UP000002485 Componenti: Chromosome I

Organism-specific databases

EuPathDBiFungiDB:SPAC10F6.13c.
PomBaseiSPAC10F6.13c.

Subcellular locationi

GO - Cellular componenti

  • cytoplasm Source: PomBase
  • cytosol Source: PomBase
  • nucleus Source: PomBase
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methionineiRemovedBy similarity
Chaini2 – 409408Aspartate aminotransferase, cytoplasmicBy similarityPRO_0000309451Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylserineBy similarity
Modified residuei255 – 2551N6-(pyridoxal phosphate)lysineBy similarity
Modified residuei385 – 3851PhosphoserineBy similarity

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

MaxQBiO42652.
PRIDEiO42652.

Interactioni

Subunit structurei

Homodimer.By similarity

Protein-protein interaction databases

BioGridi279456. 57 interactions.
MINTiMINT-4673185.

Structurei

3D structure databases

ProteinModelPortaliO42652.
SMRiO42652. Positions 6-408.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

HOGENOMiHOG000185898.
InParanoidiO42652.
KOiK14454.
OMAiHFAFFDC.
OrthoDBiEOG793BHW.
PhylomeDBiO42652.

Family and domain databases

Gene3Di3.40.640.10. 1 hit.
InterProiIPR004839. Aminotransferase_I/II.
IPR000796. Asp_trans.
IPR015424. PyrdxlP-dep_Trfase.
IPR015421. PyrdxlP-dep_Trfase_major_sub1.
[Graphical view]
PANTHERiPTHR11879. PTHR11879. 1 hit.
PfamiPF00155. Aminotran_1_2. 1 hit.
[Graphical view]
PRINTSiPR00799. TRANSAMINASE.
SUPFAMiSSF53383. SSF53383. 1 hit.

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

O42652-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSDYGFANIE EAKADAIFKL NAQYHQDEDP KKVNMSVGAY RDDTGKPWIL
60 70 80 90 100
PAVKKASKIV EEQASFNHEY LPIAGLPRFT KAAAEVLFRP NPHLLSEDRV
110 120 130 140 150
ASMQSVSGTG ANFLAASFIE TFYVKHTGAH VYISNPTWPV HRTLWEKLGV
160 170 180 190 200
TVDTYPYWDA KNRSFDYEGM LSTIKSAPEG SIFLLHACAH NPTGIDPTRE
210 220 230 240 250
QWLSIFESLL SRKHLVVFDI AYQGFASGDL NRDSWALNEF VKYNKDFFVC
260 270 280 290 300
QSFAKNMGLY GERTGCMHYV AKDASTKNKV LSQLCIVQRN TISNPPAYGA
310 320 330 340 350
RIAAEILNSP QLFAEWEQDL KTMSSRIIEM RKRLRDSLVA LKTPGSWDHI
360 370 380 390 400
TQQIGMFSFT GLTPAQVQFC QERYHLYFSA NGRISMAGLN NSNVEHVAQA

FNHAVRELP
Length:409
Mass (Da):46,140
Last modified:June 1, 1998 - v1
Checksum:i6CE10FFCC18D3E4A
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CU329670 Genomic DNA. Translation: CAA15726.1.
PIRiT37507.
RefSeqiNP_593264.1. NM_001018661.2.

Genome annotation databases

EnsemblFungiiSPAC10F6.13c.1; SPAC10F6.13c.1:pep; SPAC10F6.13c.
GeneIDi2543020.
KEGGispo:SPAC10F6.13c.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CU329670 Genomic DNA. Translation: CAA15726.1.
PIRiT37507.
RefSeqiNP_593264.1. NM_001018661.2.

3D structure databases

ProteinModelPortaliO42652.
SMRiO42652. Positions 6-408.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi279456. 57 interactions.
MINTiMINT-4673185.

Proteomic databases

MaxQBiO42652.
PRIDEiO42652.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiSPAC10F6.13c.1; SPAC10F6.13c.1:pep; SPAC10F6.13c.
GeneIDi2543020.
KEGGispo:SPAC10F6.13c.

Organism-specific databases

EuPathDBiFungiDB:SPAC10F6.13c.
PomBaseiSPAC10F6.13c.

Phylogenomic databases

HOGENOMiHOG000185898.
InParanoidiO42652.
KOiK14454.
OMAiHFAFFDC.
OrthoDBiEOG793BHW.
PhylomeDBiO42652.

Enzyme and pathway databases

ReactomeiR-SPO-70263. Gluconeogenesis.
R-SPO-70614. Amino acid synthesis and interconversion (transamination).

Miscellaneous databases

PROiO42652.

Family and domain databases

Gene3Di3.40.640.10. 1 hit.
InterProiIPR004839. Aminotransferase_I/II.
IPR000796. Asp_trans.
IPR015424. PyrdxlP-dep_Trfase.
IPR015421. PyrdxlP-dep_Trfase_major_sub1.
[Graphical view]
PANTHERiPTHR11879. PTHR11879. 1 hit.
PfamiPF00155. Aminotran_1_2. 1 hit.
[Graphical view]
PRINTSiPR00799. TRANSAMINASE.
SUPFAMiSSF53383. SSF53383. 1 hit.
ProtoNetiSearch...

Publicationsi

  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] [Europe PMC] [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] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiAATC_SCHPO
AccessioniPrimary (citable) accession number: O42652
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 13, 2007
Last sequence update: June 1, 1998
Last modified: June 8, 2016
This is version 99 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Miscellaneous

In eukaryotes there are cytoplasmic, mitochondrial and chloroplastic isozymes.Curated

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Schizosaccharomyces pombe
    Schizosaccharomyces pombe: entries and gene names
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.