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P00509

- AAT_ECOLI

UniProt

P00509 - AAT_ECOLI

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Protein

Aspartate aminotransferase

Gene
aspC, b0928, JW0911
Organism
Escherichia coli (strain K12)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

Catalytic activityi

L-aspartate + 2-oxoglutarate = oxaloacetate + L-glutamate.1 Publication

Cofactori

Pyridoxal phosphate.1 Publication

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei34 – 341Aspartate; via amide nitrogen
Binding sitei130 – 1301Aspartate
Binding sitei183 – 1831Aspartate
Binding sitei374 – 3741Aspartate

GO - Molecular functioni

  1. identical protein binding Source: IntAct
  2. L-aspartate:2-oxoglutarate aminotransferase activity Source: EcoliWiki
  3. L-phenylalanine:2-oxoglutarate aminotransferase activity Source: UniProtKB-EC
  4. L-tyrosine:2-oxoglutarate aminotransferase activity Source: EcoliWiki
  5. pyridoxal phosphate binding Source: EcoliWiki

GO - Biological processi

  1. L-phenylalanine biosynthetic process Source: EcoliWiki
  2. L-phenylalanine biosynthetic process from chorismate via phenylpyruvate Source: EcoCyc
Complete GO annotation...

Keywords - Molecular functioni

Aminotransferase, Transferase

Keywords - Ligandi

Pyridoxal phosphate

Enzyme and pathway databases

BioCyciEcoCyc:ASPAMINOTRANS-MONOMER.
ECOL316407:JW0911-MONOMER.
MetaCyc:ASPAMINOTRANS-MONOMER.
BRENDAi2.6.1.1. 2026.
SABIO-RKP00509.

Names & Taxonomyi

Protein namesi
Recommended name:
Aspartate aminotransferase (EC:2.6.1.1)
Short name:
AspAT
Alternative name(s):
Transaminase A
Gene namesi
Name:aspC
Ordered Locus Names:b0928, JW0911
OrganismiEscherichia coli (strain K12)
Taxonomic identifieri83333 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
ProteomesiUP000000318: Chromosome, UP000000625: Chromosome

Organism-specific databases

EcoGeneiEG10096. aspC.

Subcellular locationi

GO - Cellular componenti

  1. cytoplasm Source: EcoliWiki
  2. cytosol Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi65 – 651Y → F or S: Slight changes in activity. 1 Publication
Mutagenesisi133 – 1331H → A: Slight increase in maximum velocity of the overall transamination reaction between aspartate and 2-oxoglutarate. 1 Publication
Mutagenesisi133 – 1331H → N: Decreases to 60% in maximum rate of the overall reactions in both directions. 1 Publication
Mutagenesisi280 – 2801R → V: Reduces first-order rate constant over 25000-fold. 1 Publication
Mutagenesisi374 – 3741R → A: Reduces first-order rate constant about 10000-fold. 2 Publications
Mutagenesisi374 – 3741R → F or Y: Second-order rate constants are reduced by >5 orders of magnitude. 2 Publications

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 396396Aspartate aminotransferasePRO_0000123838Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei246 – 2461N6-(pyridoxal phosphate)lysine1 Publication

Proteomic databases

PaxDbiP00509.
PRIDEiP00509.

2D gel databases

SWISS-2DPAGEP00509.

Expressioni

Gene expression databases

GenevestigatoriP00509.

Interactioni

Subunit structurei

Homodimer.

Binary interactionsi

WithEntry#Exp.IntActNotes
itself4EBI-907474,EBI-907474

Protein-protein interaction databases

DIPiDIP-9181N.
IntActiP00509. 4 interactions.
STRINGi511145.b0928.

Structurei

Secondary structure

1
396
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Turni2 – 43
Helixi12 – 2211
Beta strandi29 – 324
Beta strandi33 – 353
Turni39 – 413
Helixi47 – 5913
Helixi72 – 8312
Helixi88 – 914
Beta strandi95 – 1017
Helixi102 – 11716
Beta strandi122 – 1287
Helixi132 – 1398
Beta strandi143 – 1486
Turni152 – 1554
Helixi159 – 1668
Beta strandi174 – 1785
Beta strandi179 – 1813
Turni183 – 1853
Helixi191 – 20414
Beta strandi207 – 2137
Beta strandi217 – 2193
Helixi221 – 2244
Helixi226 – 2349
Beta strandi238 – 2436
Turni245 – 2495
Helixi251 – 2533
Beta strandi256 – 2616
Helixi265 – 28016
Turni281 – 2833
Helixi288 – 29811
Helixi301 – 33131
Helixi340 – 3434
Beta strandi346 – 3505
Helixi355 – 36511
Beta strandi367 – 3693
Turni371 – 3733
Beta strandi374 – 3763
Helixi377 – 3793
Turni382 – 3843
Helixi385 – 39511

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1AAMX-ray2.80A1-396[»]
1AAWX-ray2.40A1-396[»]
1AHEX-ray2.30A/B1-396[»]
1AHFX-ray2.30A/B1-396[»]
1AHGX-ray2.50A/B1-396[»]
1AHXX-ray2.00A/B1-396[»]
1AHYX-ray2.30A/B1-396[»]
1AIAX-ray2.20A/B1-396[»]
1AIBX-ray2.80A/B1-396[»]
1AICX-ray2.40A/B1-396[»]
1AMQX-ray2.20A1-396[»]
1AMRX-ray2.10A1-396[»]
1AMSX-ray2.70A1-396[»]
1ARGX-ray2.20A/B1-396[»]
1ARHX-ray2.30A/B1-396[»]
1ARIX-ray2.30A/B1-396[»]
1ARSX-ray1.80A1-396[»]
1ARTX-ray1.80A1-396[»]
1ASAX-ray2.40A1-396[»]
1ASBX-ray2.60A1-396[»]
1ASCX-ray2.40A1-396[»]
1ASDX-ray2.20A1-396[»]
1ASEX-ray2.50A1-396[»]
1ASFX-ray2.80A1-396[»]
1ASGX-ray2.80A1-396[»]
1ASLX-ray2.60A/B1-396[»]
1ASMX-ray2.35A/B1-396[»]
1ASNX-ray2.50A/B1-396[»]
1B4XX-ray2.45A1-396[»]
1BQAX-ray2.10A/B1-396[»]
1BQDX-ray2.10A/B1-396[»]
1C9CX-ray2.40A1-396[»]
1CQ6X-ray2.70A1-396[»]
1CQ7X-ray2.40A1-396[»]
1CQ8X-ray2.40A1-396[»]
1CZCX-ray2.50A1-396[»]
1CZEX-ray2.40A1-396[»]
1G4VX-ray2.00A1-396[»]
1G4XX-ray2.20A1-396[»]
1G7WX-ray2.20A1-396[»]
1G7XX-ray2.20A1-396[»]
1IX6X-ray2.20A1-396[»]
1IX7X-ray2.20A1-396[»]
1IX8X-ray2.20A1-396[»]
1QIRX-ray2.20A1-396[»]
1QISX-ray1.90A1-396[»]
1QITX-ray1.90A1-396[»]
1SPAX-ray2.00A1-396[»]
1TOEX-ray2.00A1-388[»]
1TOGX-ray2.31A/B1-388[»]
1TOIX-ray1.90A1-388[»]
1TOJX-ray1.90A1-388[»]
1TOKX-ray1.85A/B1-388[»]
1X28X-ray2.40A/B1-396[»]
1X29X-ray2.20A/B1-396[»]
1X2AX-ray2.20A/B1-396[»]
1YOOX-ray2.40A1-396[»]
2AATX-ray2.80A1-396[»]
2D5YX-ray1.98A1-396[»]
2D61X-ray2.01A1-396[»]
2D63X-ray2.05A1-396[»]
2D64X-ray2.05A1-396[»]
2D65X-ray2.30A1-396[»]
2D66X-ray2.18A1-396[»]
2D7YX-ray2.66A1-396[»]
2D7ZX-ray2.65A1-396[»]
2Q7WX-ray1.40A1-396[»]
2QA3X-ray1.75A1-396[»]
2QB2X-ray1.70A1-396[»]
2QB3X-ray1.45A1-396[»]
2QBTX-ray1.75A1-396[»]
3AATX-ray2.80A1-396[»]
3QN6X-ray1.79A1-396[»]
3QPGX-ray1.79A1-396[»]
3ZZJX-ray2.50A1-396[»]
3ZZKX-ray1.78A1-396[»]
4A00X-ray2.34A1-396[»]
4DBCX-ray1.50A1-396[»]
4F5FX-ray2.25A/B2-396[»]
4F5GX-ray1.67A/B2-396[»]
4F5HX-ray1.60A/B2-396[»]
4F5IX-ray2.20A/B2-396[»]
4F5JX-ray1.95A/B2-396[»]
4F5KX-ray2.20A/B2-396[»]
4F5LX-ray1.40A/B2-396[»]
4F5MX-ray1.65A/B2-396[»]
5EAAX-ray2.40A1-396[»]
ProteinModelPortaliP00509.
SMRiP00509. Positions 1-396.

Miscellaneous databases

EvolutionaryTraceiP00509.

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

eggNOGiCOG1448.
HOGENOMiHOG000185899.
KOiK00813.
OMAiRVGACTI.
OrthoDBiEOG6C2WBK.
PhylomeDBiP00509.

Family and domain databases

Gene3Di3.40.640.10. 1 hit.
InterProiIPR004839. Aminotransferase_I/II.
IPR000796. Asp_trans.
IPR004838. NHTrfase_class1_PyrdxlP-BS.
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.
PROSITEiPS00105. AA_TRANSFER_CLASS_1. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P00509-1 [UniParc]FASTAAdd to Basket

« Hide

MFENITAAPA DPILGLADLF RADERPGKIN LGIGVYKDET GKTPVLTSVK    50
KAEQYLLENE TTKNYLGIDG IPEFGRCTQE LLFGKGSALI NDKRARTAQT 100
PGGTGALRVA ADFLAKNTSV KRVWVSNPSW PNHKSVFNSA GLEVREYAYY 150
DAENHTLDFD ALINSLNEAQ AGDVVLFHGC CHNPTGIDPT LEQWQTLAQL 200
SVEKGWLPLF DFAYQGFARG LEEDAEGLRA FAAMHKELIV ASSYSKNFGL 250
YNERVGACTL VAADSETVDR AFSQMKAAIR ANYSNPPAHG ASVVATILSN 300
DALRAIWEQE LTDMRQRIQR MRQLFVNTLQ EKGANRDFSF IIKQNGMFSF 350
SGLTKEQVLR LREEFGVYAV ASGRVNVAGM TPDNMAPLCE AIVAVL 396
Length:396
Mass (Da):43,573
Last modified:July 21, 1986 - v1
Checksum:i9F0437E76DD4FC0F
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
X03629 Genomic DNA. Translation: CAA27279.1.
X05904 Genomic DNA. Translation: CAA29333.1.
U00096 Genomic DNA. Translation: AAC74014.1.
AP009048 Genomic DNA. Translation: BAA35674.1.
PIRiA00598. XNECD.
RefSeqiNP_415448.1. NC_000913.3.
YP_489200.1. NC_007779.1.

Genome annotation databases

EnsemblBacteriaiAAC74014; AAC74014; b0928.
BAA35674; BAA35674; BAA35674.
GeneIDi12931027.
945553.
KEGGiecj:Y75_p0900.
eco:b0928.
PATRICi32117069. VBIEscCol129921_0959.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
X03629 Genomic DNA. Translation: CAA27279.1 .
X05904 Genomic DNA. Translation: CAA29333.1 .
U00096 Genomic DNA. Translation: AAC74014.1 .
AP009048 Genomic DNA. Translation: BAA35674.1 .
PIRi A00598. XNECD.
RefSeqi NP_415448.1. NC_000913.3.
YP_489200.1. NC_007779.1.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1AAM X-ray 2.80 A 1-396 [» ]
1AAW X-ray 2.40 A 1-396 [» ]
1AHE X-ray 2.30 A/B 1-396 [» ]
1AHF X-ray 2.30 A/B 1-396 [» ]
1AHG X-ray 2.50 A/B 1-396 [» ]
1AHX X-ray 2.00 A/B 1-396 [» ]
1AHY X-ray 2.30 A/B 1-396 [» ]
1AIA X-ray 2.20 A/B 1-396 [» ]
1AIB X-ray 2.80 A/B 1-396 [» ]
1AIC X-ray 2.40 A/B 1-396 [» ]
1AMQ X-ray 2.20 A 1-396 [» ]
1AMR X-ray 2.10 A 1-396 [» ]
1AMS X-ray 2.70 A 1-396 [» ]
1ARG X-ray 2.20 A/B 1-396 [» ]
1ARH X-ray 2.30 A/B 1-396 [» ]
1ARI X-ray 2.30 A/B 1-396 [» ]
1ARS X-ray 1.80 A 1-396 [» ]
1ART X-ray 1.80 A 1-396 [» ]
1ASA X-ray 2.40 A 1-396 [» ]
1ASB X-ray 2.60 A 1-396 [» ]
1ASC X-ray 2.40 A 1-396 [» ]
1ASD X-ray 2.20 A 1-396 [» ]
1ASE X-ray 2.50 A 1-396 [» ]
1ASF X-ray 2.80 A 1-396 [» ]
1ASG X-ray 2.80 A 1-396 [» ]
1ASL X-ray 2.60 A/B 1-396 [» ]
1ASM X-ray 2.35 A/B 1-396 [» ]
1ASN X-ray 2.50 A/B 1-396 [» ]
1B4X X-ray 2.45 A 1-396 [» ]
1BQA X-ray 2.10 A/B 1-396 [» ]
1BQD X-ray 2.10 A/B 1-396 [» ]
1C9C X-ray 2.40 A 1-396 [» ]
1CQ6 X-ray 2.70 A 1-396 [» ]
1CQ7 X-ray 2.40 A 1-396 [» ]
1CQ8 X-ray 2.40 A 1-396 [» ]
1CZC X-ray 2.50 A 1-396 [» ]
1CZE X-ray 2.40 A 1-396 [» ]
1G4V X-ray 2.00 A 1-396 [» ]
1G4X X-ray 2.20 A 1-396 [» ]
1G7W X-ray 2.20 A 1-396 [» ]
1G7X X-ray 2.20 A 1-396 [» ]
1IX6 X-ray 2.20 A 1-396 [» ]
1IX7 X-ray 2.20 A 1-396 [» ]
1IX8 X-ray 2.20 A 1-396 [» ]
1QIR X-ray 2.20 A 1-396 [» ]
1QIS X-ray 1.90 A 1-396 [» ]
1QIT X-ray 1.90 A 1-396 [» ]
1SPA X-ray 2.00 A 1-396 [» ]
1TOE X-ray 2.00 A 1-388 [» ]
1TOG X-ray 2.31 A/B 1-388 [» ]
1TOI X-ray 1.90 A 1-388 [» ]
1TOJ X-ray 1.90 A 1-388 [» ]
1TOK X-ray 1.85 A/B 1-388 [» ]
1X28 X-ray 2.40 A/B 1-396 [» ]
1X29 X-ray 2.20 A/B 1-396 [» ]
1X2A X-ray 2.20 A/B 1-396 [» ]
1YOO X-ray 2.40 A 1-396 [» ]
2AAT X-ray 2.80 A 1-396 [» ]
2D5Y X-ray 1.98 A 1-396 [» ]
2D61 X-ray 2.01 A 1-396 [» ]
2D63 X-ray 2.05 A 1-396 [» ]
2D64 X-ray 2.05 A 1-396 [» ]
2D65 X-ray 2.30 A 1-396 [» ]
2D66 X-ray 2.18 A 1-396 [» ]
2D7Y X-ray 2.66 A 1-396 [» ]
2D7Z X-ray 2.65 A 1-396 [» ]
2Q7W X-ray 1.40 A 1-396 [» ]
2QA3 X-ray 1.75 A 1-396 [» ]
2QB2 X-ray 1.70 A 1-396 [» ]
2QB3 X-ray 1.45 A 1-396 [» ]
2QBT X-ray 1.75 A 1-396 [» ]
3AAT X-ray 2.80 A 1-396 [» ]
3QN6 X-ray 1.79 A 1-396 [» ]
3QPG X-ray 1.79 A 1-396 [» ]
3ZZJ X-ray 2.50 A 1-396 [» ]
3ZZK X-ray 1.78 A 1-396 [» ]
4A00 X-ray 2.34 A 1-396 [» ]
4DBC X-ray 1.50 A 1-396 [» ]
4F5F X-ray 2.25 A/B 2-396 [» ]
4F5G X-ray 1.67 A/B 2-396 [» ]
4F5H X-ray 1.60 A/B 2-396 [» ]
4F5I X-ray 2.20 A/B 2-396 [» ]
4F5J X-ray 1.95 A/B 2-396 [» ]
4F5K X-ray 2.20 A/B 2-396 [» ]
4F5L X-ray 1.40 A/B 2-396 [» ]
4F5M X-ray 1.65 A/B 2-396 [» ]
5EAA X-ray 2.40 A 1-396 [» ]
ProteinModelPortali P00509.
SMRi P00509. Positions 1-396.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

DIPi DIP-9181N.
IntActi P00509. 4 interactions.
STRINGi 511145.b0928.

2D gel databases

SWISS-2DPAGE P00509.

Proteomic databases

PaxDbi P00509.
PRIDEi P00509.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai AAC74014 ; AAC74014 ; b0928 .
BAA35674 ; BAA35674 ; BAA35674 .
GeneIDi 12931027.
945553.
KEGGi ecj:Y75_p0900.
eco:b0928.
PATRICi 32117069. VBIEscCol129921_0959.

Organism-specific databases

EchoBASEi EB0094.
EcoGenei EG10096. aspC.

Phylogenomic databases

eggNOGi COG1448.
HOGENOMi HOG000185899.
KOi K00813.
OMAi RVGACTI.
OrthoDBi EOG6C2WBK.
PhylomeDBi P00509.

Enzyme and pathway databases

BioCyci EcoCyc:ASPAMINOTRANS-MONOMER.
ECOL316407:JW0911-MONOMER.
MetaCyc:ASPAMINOTRANS-MONOMER.
BRENDAi 2.6.1.1. 2026.
SABIO-RK P00509.

Miscellaneous databases

EvolutionaryTracei P00509.
PROi P00509.

Gene expression databases

Genevestigatori P00509.

Family and domain databases

Gene3Di 3.40.640.10. 1 hit.
InterProi IPR004839. Aminotransferase_I/II.
IPR000796. Asp_trans.
IPR004838. NHTrfase_class1_PyrdxlP-BS.
IPR015424. PyrdxlP-dep_Trfase.
IPR015421. PyrdxlP-dep_Trfase_major_sub1.
[Graphical view ]
PANTHERi PTHR11879. PTHR11879. 1 hit.
Pfami PF00155. Aminotran_1_2. 1 hit.
[Graphical view ]
PRINTSi PR00799. TRANSAMINASE.
SUPFAMi SSF53383. SSF53383. 1 hit.
PROSITEi PS00105. AA_TRANSFER_CLASS_1. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "The complete amino acid sequence of aspartate aminotransferase from Escherichia coli: sequence comparison with pig isoenzymes."
    Kondo K., Wakabayashi S., Yagi T., Kagamiyama H.
    Biochem. Biophys. Res. Commun. 122:62-67(1984) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE.
  2. "Aspartate aminotransferase of Escherichia coli: nucleotide sequence of the aspC gene."
    Kuramitsu S., Okuno S., Ogawa T., Ogawa H., Kagamiyama H.
    J. Biochem. 97:1259-1262(1985) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  3. "The cloning and sequence analysis of the aspC and tyrB genes from Escherichia coli K12. Comparison of the primary structures of the aspartate aminotransferase and aromatic aminotransferase of E. coli with those of the pig aspartate aminotransferase isoenzymes."
    Fotheringham I.G., Dacey S.A., Taylor P.P., Smith T.J., Hunter M.G., Finlay M.E., Primrose S.B., Parker D.M., Edwards R.M.
    Biochem. J. 234:593-604(1986) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  4. "Structural studies on aspartate aminotransferase from Escherichia coli. Covalent structure."
    Kondo K., Wakabayashi S., Kagamiyama H.
    J. Biol. Chem. 262:8648-8657(1987) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE.
  5. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
  6. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / MG1655 / ATCC 47076.
  7. "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110."
    Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.
    Mol. Syst. Biol. 2:E1-E5(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
  8. "Comparing the predicted and observed properties of proteins encoded in the genome of Escherichia coli K-12."
    Link A.J., Robison K., Church G.M.
    Electrophoresis 18:1259-1313(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 1-12.
    Strain: K12 / EMG2.
  9. "Site-directed mutagenesis of Escherichia coli aspartate aminotransferase: role of Tyr70 in the catalytic processes."
    Inoue K., Kuramitsu S., Okamoto A., Hirotsu K., Higuchi T., Kagamiyama H.
    Biochemistry 30:7796-7801(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: MUTAGENESIS OF TYR-65.
  10. "The role of His143 in the catalytic mechanism of Escherichia coli aspartate aminotransferase."
    Yano T., Kuramitsu S., Tanase S., Morino Y., Hiromi K., Kagamiyama H.
    J. Biol. Chem. 266:6079-6085(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: MUTAGENESIS OF HIS-133.
  11. "Escherichia coli proteome analysis using the gene-protein database."
    VanBogelen R.A., Abshire K.Z., Moldover B., Olson E.R., Neidhardt F.C.
    Electrophoresis 18:1243-1251(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY 2D-GEL.
  12. "The aspartate aminotransferase-catalysed exchange of the alpha-protons of aspartate and glutamate: the effects of the R386A and R292V mutations on this exchange reaction."
    Mahon M.M., Graber R., Christen P., Malthouse J.P.
    Biochim. Biophys. Acta 1434:191-201(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: CATALYTIC ACTIVITY, MUTAGENESIS OF ARG-280 AND ARG-374.
  13. "2.8-A-resolution crystal structure of an active-site mutant of aspartate aminotransferase from Escherichia coli."
    Smith D.L., Almo S.C., Toney M.D., Ringe D.
    Biochemistry 28:8161-8167(1989) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF MUTANT ALA-246.
  14. "Activity and structure of the active-site mutants R386Y and R386F of Escherichia coli aspartate aminotransferase."
    Danishefsky A.T., Onnufer J.J., Petsko G.A., Ringe D.
    Biochemistry 30:1980-1985(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS), MUTAGENESIS OF ARG-374.
  15. "Redesigning the substrate specificity of an enzyme by cumulative effects of the mutations of non-active site residues."
    Oue S., Okamoto A., Yano T., Kagamiyama H.
    J. Biol. Chem. 274:2344-2349(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) OF MUTANT.
  16. "Strain is more important than electrostatic interaction in controlling the pKa of the catalytic group in aspartate aminotransferase."
    Mizuguchi H., Hayashi H., Okada K., Miyahara I., Hirotsu K., Kagamiyama H.
    Biochemistry 40:353-360(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF MUTANTS ALA-183/PHE-214; ALA-183/LEU-280; ALA-183/LEU-374 AND ALA-183/LEU-280/LEU-374 IN COMPLEXES WITH PYRIDOXAL PHOSPHATE, COFACTOR, PYRIDOXAL PHOSPHATE AT LYS-246.
  17. "Inactivation of Escherichia coli L-aspartate aminotransferase by (S)-4-amino-4,5-dihydro-2-thiophenecarboxylic acid reveals 'a tale of two mechanisms'."
    Liu D., Pozharski E., Lepore B.W., Fu M., Silverman R.B., Petsko G.A., Ringe D.
    Biochemistry 46:10517-10527(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.4 ANGSTROMS) IN COMPLEX WITH PYRIDOXAL PHOSPHATE AND SADTA, PYRIDOXAL PHOSPHATE AT LYS-246.

Entry informationi

Entry nameiAAT_ECOLI
AccessioniPrimary (citable) accession number: P00509
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: July 21, 1986
Last modified: May 14, 2014
This is version 154 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Escherichia coli
    Escherichia coli (strain K12): entries and cross-references to EcoGene
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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