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Reviewed, UniProtKB/Swiss-Prot Q56232 (AAT_THET8)

Last modified February 9, 2010. Version 73. 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
      Short name=AspAT
    EC=2.6.1.1
Alternative name(s):
    Transaminase A
Gene names
Name: aspC
Ordered Locus Names: TTHA0046
OrganismThermus thermophilus (strain HB8 / ATCC 27634 / DSM 579) [Complete proteome] [HAMAP]
Taxonomic identifier300852 [NCBI]
Taxonomic lineageBacteriaDeinococcus-ThermusDeinococciThermalesThermaceaeThermus

Protein attributes

Sequence length385 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level.

General annotation (Comments)

Catalytic activity

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

Cofactor

Pyridoxal phosphate.

Subunit structure

Homodimer.

Subcellular location

Cytoplasm By similarity.

Sequence similarities

Belongs to the class-I pyridoxal-phosphate-dependent aminotransferase family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 385385Aspartate aminotransferase
PRO_0000123856

Sites

Binding site391Aspartate; via amide nitrogen By similarity
Binding site1251Aspartate
Binding site1751Aspartate
Binding site3611Aspartate

Amino acid modifications

Modified residue2341N6-(pyridoxal phosphate)lysine

Secondary structure

.................................................................. 385
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Q56232-1 [UniParc].

Last modified November 1, 1996. Version 1.
Checksum: EADF7B7EA127F39B

FASTA38542,051
        10         20         30         40         50         60 
MRGLSRRVQA MKPSATVAVN AKALELRRQG VDLVALTAGE PDFDTPEHVK EAARRALAQG 

        70         80         90        100        110        120 
KTKYAPPAGI PELREALAEK FRRENGLSVT PEETIVTVGG KQALFNLFQA ILDPGDEVIV 

       130        140        150        160        170        180 
LSPYWVSYPE MVRFAGGVVV EVETLPEEGF VPDPERVRRA ITPRTKALVV NSPNNPTGAV 

       190        200        210        220        230        240 
YPKEVLEALA RLAVEHDFYL VSDEIYEHLL YEGEHFSPGR VAPEHTLTVN GAAKAFAMTG 

       250        260        270        280        290        300 
WRIGYACGPK EVIKAMASVS SQSTTSPDTI AQWATLEALT NQEASRAFVE MAREAYRRRR 

       310        320        330        340        350        360 
DLLLEGLTAL GLKAVRPSGA FYVLMDTSPI APDEVRAAER LLEAGVAVVP GTDFAAFGHV 

       370        380 
RLSYATSEEN LRKALERFAR VLGRA 

« Hide

References

« Hide 'large scale' references
[1]"An aspartate aminotransferase from an extremely thermophilic bacterium, Thermus thermophilus HB8."
Okamoto A., Kato R., Masui R., Yamagishi A., Oshima T., Kuramitsu S.
J. Biochem. 119:135-144(1996) [PubMed: 8907187] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]"Complete genome sequence of Thermus thermophilus HB8."
Masui R., Kurokawa K., Nakagawa N., Tokunaga F., Koyama Y., Shibata T., Oshima T., Yokoyama S., Yasunaga T., Kuramitsu S.
Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[3]"Structure of Thermus thermophilus HB8 aspartate aminotransferase and its complex with maleate."
Nakai T., Okada K., Akutsu S., Miyahara I., Kawaguchi S., Kato R., Kuramitsu S., Hirotsu K.
Biochemistry 38:2413-2424(1999) [PubMed: 10029535] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) IN COMPLEX WITH MALEIC ACID AND PYRIDOXAL PHOSPHATE, SUBUNIT.
[4]"Substrate recognition mechanism of thermophilic dual-substrate enzyme."
Ura H., Nakai T., Kawaguchi S., Miyahara I., Hirotsu K., Kuramitsu S.
J. Biochem. 130:89-98(2001) [PubMed: 11432784] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) IN COMPLEXES WITH PYRIDOXAL PHOSPHATE AND ASPARTATE, COFACTOR, SUBUNIT.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
D38459 Genomic DNA. Translation: BAA07487.1.
AP008226 Genomic DNA. Translation: BAD69869.1.
RefSeqYP_143312.1.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1B5OX-ray2.20A/B1-385[»]
1B5PX-ray1.80A/B1-385[»]
1BJWX-ray1.80A/B1-382[»]
1BKGX-ray2.60A/B/C/D1-385[»]
1GC3X-ray3.30A/B/C/D/E/F/G/H1-385[»]
1GC4X-ray3.30A/B/C/D1-385[»]
1GCKX-ray2.50A/B1-385[»]
5BJ3X-ray2.20A/B/C/D1-385[»]
5BJ4X-ray2.00A/B1-385[»]
ModBaseSearch...

Protein-protein interaction databases

STRINGQ56232.

Genome annotation databases

GeneID3168657.
GenomeReviewsGene locus TTHA0046 in contig AP008226_GR.
KEGGttj:TTHA0046.
NMPDRfig|300852.3.peg.77.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0436.
HOGENOMHBG645860.
OMAFVEMARE.

Enzyme and pathway databases

BioCycTTHE300852:TTHA0046-MONOMER.

Family and domain databases

InterProIPR001176. ACC_synthase.
IPR004839. Aminotransferase_I/II.
IPR004838. NHTrfase_class1_PyrdxlP-BS.
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.
PfamPF00155. Aminotran_1_2. 1 hit.
[Graphical view]
PRINTSPR00753. ACCSYNTHASE.
PROSITEPS00105. AA_TRANSFER_CLASS_1. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameAAT_THET8
AccessionPrimary (citable) accession number: Q56232
Secondary accession number(s): Q5SM97
Entry history
Integrated into UniProtKB/Swiss-Prot: May 30, 2000
Last sequence update: November 1, 1996
Last modified: February 9, 2010
This is version 73 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)

Relevant documents

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

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