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UniProtKB - Q56232 (AAPAT_THET8)
Protein
Aspartate/prephenate aminotransferase
Gene
aspC
Organism
Thermus thermophilus (strain ATCC 27634 / DSM 579 / HB8)
Status
Functioni
Catalyzes the reversible conversion of aspartate and 2-oxoglutarate to glutamate and oxaloacetate (PubMed:8907187, PubMed:25070637).
Can also transaminate prephenate in the presence of aspartate (PubMed:25070637, PubMed:30771275).
3 PublicationsCatalytic activityi
Cofactori
pyridoxal 5'-phosphate2 Publications
Kineticsi
kcat is 7.7 sec(-1) toward prephenate. kcat is 32.2 sec(-1) toward oxaloacetate.1 Publication
- KM=1.1 mM for L-aspartate (at 45 degrees Celsius)1 Publication
- KM=1.0 mM for 2-oxoglutarate (at 45 degrees Celsius)1 Publication
- KM=150 µM for prephenate1 Publication
- KM=25.3 µM for oxaloacetate1 Publication
Sites
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Sitei | 12 | Important for prephenate aminotransferase activity1 Publication | 1 | |
Binding sitei | 39 | Aspartate; via amide nitrogenBy similarity | 1 | |
Binding sitei | 125 | AspartateCombined sources | 1 | |
Binding sitei | 175 | AspartateCombined sources | 1 | |
Binding sitei | 361 | AspartateCombined sources | 1 |
GO - Molecular functioni
- aspartate-prephenate aminotransferase activity Source: UniProtKB-EC
- L-aspartate:2-oxoglutarate aminotransferase activity Source: UniProtKB-EC
- pyridoxal phosphate binding Source: InterPro
GO - Biological processi
- biosynthetic process Source: InterPro
Keywordsi
Molecular function | Aminotransferase, Transferase |
Ligand | Pyridoxal phosphate |
Enzyme and pathway databases
BRENDAi | 2.6.1.1, 2305 |
Names & Taxonomyi
Protein namesi | |
Gene namesi | Name:aspC Ordered Locus Names:TTHA0046 |
Organismi | Thermus thermophilus (strain ATCC 27634 / DSM 579 / HB8) |
Taxonomic identifieri | 300852 [NCBI] |
Taxonomic lineagei | Bacteria › Deinococcus-Thermus › Deinococci › Thermales › Thermaceae › Thermus › |
Proteomesi |
|
Subcellular locationi
Cytoplasm and Cytosol
- Cytoplasm Curated
Other locations
- cytoplasm Source: UniProtKB-SubCell
Keywords - Cellular componenti
CytoplasmPathology & Biotechi
Mutagenesis
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Mutagenesisi | 12 | K → G: 10-fold increase in Km for prephenate. Does not affect Km for oxaloacetate. 1 Publication | 1 |
Chemistry databases
DrugBanki | DB04299, Maleic Acid DB02142, Pyridoxamine-5'-Phosphate |
PTM / Processingi
Molecule processing
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
ChainiPRO_0000123856 | 1 – 385 | Aspartate/prephenate aminotransferaseAdd BLAST | 385 |
Amino acid modifications
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Modified residuei | 234 | N6-(pyridoxal phosphate)lysineCombined sources2 Publications | 1 |
Interactioni
Subunit structurei
Homodimer.
2 PublicationsProtein-protein interaction databases
STRINGi | 300852.55771428 |
Structurei
Secondary structure
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details3D structure databases
SMRi | Q56232 |
ModBasei | Search... |
PDBe-KBi | Search... |
Miscellaneous databases
EvolutionaryTracei | Q56232 |
Family & Domainsi
Sequence similaritiesi
Belongs to the class-I pyridoxal-phosphate-dependent aminotransferase family.Curated
Phylogenomic databases
eggNOGi | COG0436, Bacteria |
HOGENOMi | CLU_017584_4_3_0 |
OMAi | IHMEVGQ |
PhylomeDBi | Q56232 |
Family and domain databases
Gene3Di | 3.40.640.10, 1 hit 3.90.1150.10, 1 hit |
InterProi | View protein in InterPro IPR004839, Aminotransferase_I/II IPR004838, NHTrfase_class1_PyrdxlP-BS IPR015424, PyrdxlP-dep_Trfase IPR015421, PyrdxlP-dep_Trfase_major IPR015422, PyrdxlP-dep_Trfase_small |
Pfami | View protein in Pfam PF00155, Aminotran_1_2, 1 hit |
SUPFAMi | SSF53383, SSF53383, 1 hit |
PROSITEi | View protein in PROSITE PS00105, AA_TRANSFER_CLASS_1, 1 hit |
i Sequence
Sequence statusi: Complete.
Q56232-1 [UniParc]FASTAAdd to basket
10 20 30 40 50
MRGLSRRVQA MKPSATVAVN AKALELRRQG VDLVALTAGE PDFDTPEHVK
60 70 80 90 100
EAARRALAQG KTKYAPPAGI PELREALAEK FRRENGLSVT PEETIVTVGG
110 120 130 140 150
KQALFNLFQA ILDPGDEVIV LSPYWVSYPE MVRFAGGVVV EVETLPEEGF
160 170 180 190 200
VPDPERVRRA ITPRTKALVV NSPNNPTGAV YPKEVLEALA RLAVEHDFYL
210 220 230 240 250
VSDEIYEHLL YEGEHFSPGR VAPEHTLTVN GAAKAFAMTG WRIGYACGPK
260 270 280 290 300
EVIKAMASVS SQSTTSPDTI AQWATLEALT NQEASRAFVE MAREAYRRRR
310 320 330 340 350
DLLLEGLTAL GLKAVRPSGA FYVLMDTSPI APDEVRAAER LLEAGVAVVP
360 370 380
GTDFAAFGHV RLSYATSEEN LRKALERFAR VLGRA
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | D38459 Genomic DNA Translation: BAA07487.1 AP008226 Genomic DNA Translation: BAD69869.1 |
RefSeqi | WP_011227669.1, NC_006461.1 YP_143312.1, NC_006461.1 |
Genome annotation databases
EnsemblBacteriai | BAD69869; BAD69869; BAD69869 |
GeneIDi | 3168657 |
KEGGi | ttj:TTHA0046 |
PATRICi | fig|300852.9.peg.44 |
Similar proteinsi
Cross-referencesi
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | D38459 Genomic DNA Translation: BAA07487.1 AP008226 Genomic DNA Translation: BAD69869.1 |
RefSeqi | WP_011227669.1, NC_006461.1 YP_143312.1, NC_006461.1 |
3D structure databases
Select the link destinations: PDBei RCSB PDBi PDBji Links Updated | PDB entry | Method | Resolution (Å) | Chain | Positions | PDBsum |
1B5O | X-ray | 2.20 | A/B | 1-385 | [»] | |
1B5P | X-ray | 1.80 | A/B | 1-385 | [»] | |
1BJW | X-ray | 1.80 | A/B | 1-382 | [»] | |
1BKG | X-ray | 2.60 | A/B/C/D | 1-385 | [»] | |
1GC3 | X-ray | 3.30 | A/B/C/D/E/F/G/H | 1-385 | [»] | |
1GC4 | X-ray | 3.30 | A/B/C/D | 1-385 | [»] | |
1GCK | X-ray | 2.50 | A/B | 1-385 | [»] | |
5BJ3 | X-ray | 2.20 | A/B/C/D | 1-385 | [»] | |
5BJ4 | X-ray | 2.00 | A/B | 1-385 | [»] | |
SMRi | Q56232 | |||||
ModBasei | Search... | |||||
PDBe-KBi | Search... |
Protein-protein interaction databases
STRINGi | 300852.55771428 |
Chemistry databases
DrugBanki | DB04299, Maleic Acid DB02142, Pyridoxamine-5'-Phosphate |
Genome annotation databases
EnsemblBacteriai | BAD69869; BAD69869; BAD69869 |
GeneIDi | 3168657 |
KEGGi | ttj:TTHA0046 |
PATRICi | fig|300852.9.peg.44 |
Phylogenomic databases
eggNOGi | COG0436, Bacteria |
HOGENOMi | CLU_017584_4_3_0 |
OMAi | IHMEVGQ |
PhylomeDBi | Q56232 |
Enzyme and pathway databases
BRENDAi | 2.6.1.1, 2305 |
Miscellaneous databases
EvolutionaryTracei | Q56232 |
Family and domain databases
Gene3Di | 3.40.640.10, 1 hit 3.90.1150.10, 1 hit |
InterProi | View protein in InterPro IPR004839, Aminotransferase_I/II IPR004838, NHTrfase_class1_PyrdxlP-BS IPR015424, PyrdxlP-dep_Trfase IPR015421, PyrdxlP-dep_Trfase_major IPR015422, PyrdxlP-dep_Trfase_small |
Pfami | View protein in Pfam PF00155, Aminotran_1_2, 1 hit |
SUPFAMi | SSF53383, SSF53383, 1 hit |
PROSITEi | View protein in PROSITE PS00105, AA_TRANSFER_CLASS_1, 1 hit |
MobiDBi | Search... |
Entry informationi
Entry namei | AAPAT_THET8 | |
Accessioni | Q56232Primary (citable) accession number: Q56232 Secondary accession number(s): Q5SM97 | |
Entry historyi | Integrated into UniProtKB/Swiss-Prot: | May 30, 2000 |
Last sequence update: | November 1, 1996 | |
Last modified: | September 29, 2021 | |
This is version 137 of the entry and version 1 of the sequence. See complete history. | ||
Entry statusi | Reviewed (UniProtKB/Swiss-Prot) | |
Annotation program | Prokaryotic Protein Annotation Program |
Miscellaneousi
Keywords - Technical termi
3D-structure, Reference proteomeDocuments
- PDB cross-references
Index of Protein Data Bank (PDB) cross-references - SIMILARITY comments
Index of protein domains and families