P00509 (AAT_ECOLI) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Aspartate aminotransferase
Short name=AspAT
EC=2.6.1.1

Alternative name(s):
Transaminase A

Gene names

Name:	aspC
Ordered Locus Names:	b0928, JW0911

Organism

Escherichia coli (strain K12) [Reference proteome] [HAMAP]

Taxonomic identifier

83333 [NCBI]

Taxonomic lineage

cellular organisms › Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia › Escherichia coli

Protein attributes

Sequence length	396 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Catalytic activity	L-aspartate + 2-oxoglutarate = oxaloacetate + L-glutamate. Ref.12
Cofactor	Pyridoxal phosphate. Ref.16
Subunit structure	Homodimer.
Subcellular location	Cytoplasm.
Sequence similarities	Belongs to the class-I pyridoxal-phosphate-dependent aminotransferase family.

Ontologies

Keywords
Cellular component	Cytoplasm
Ligand	Pyridoxal phosphate
Molecular function	Aminotransferase Transferase
Technical term	3D-structure Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	L-phenylalanine biosynthetic process from chorismate via phenylpyruvate Inferred from mutant phenotype PubMed 15983. Source: EcoCyc
Cellular_component	cytosol Inferred from direct assay PubMed 16858726. Source: UniProtKB
Molecular_function	L-aspartate:2-oxoglutarate aminotransferase activity Inferred from mutant phenotype PubMed 15983. Source: EcoliWiki L-phenylalanine:2-oxoglutarate aminotransferase activity Inferred from electronic annotation. Source: EC L-tyrosine:2-oxoglutarate aminotransferase activity Inferred from mutant phenotype PubMed 15983. Source: EcoliWiki pyridoxal phosphate binding Inferred from direct assay PubMed 352693. Source: EcoliWiki
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 396

396

Aspartate aminotransferase

PRO_0000123838

Sites

Binding site

34

1

Aspartate; via amide nitrogen

Binding site

130

1

Aspartate

Binding site

183

1

Aspartate

Binding site

374

1

Aspartate

Amino acid modifications

Modified residue

246

1

N6-(pyridoxal phosphate)lysine Ref.4

Experimental info

Mutagenesis

65

1

Y → F or S: Slight changes in activity. Ref.9

Mutagenesis

133

1

H → A: Slight increase in maximum velocity of the overall transamination reaction between aspartate and 2-oxoglutarate. Ref.10

Mutagenesis

133

1

H → N: Decreases to 60% in maximum rate of the overall reactions in both directions. Ref.10

Mutagenesis

280

1

R → V: Reduces first-order rate constant over 25000-fold. Ref.12

Mutagenesis

374

1

R → A: Reduces first-order rate constant about 10000-fold. Ref.12 Ref.14

Mutagenesis

374

1

R → F or Y: Second-order rate constants are reduced by >5 orders of magnitude. Ref.12 Ref.14

Secondary structure

1

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396

Helix Strand Turn

Details...

Turn

2 – 4

3

Turn

12 – 14

3

Helix

15 – 22

8

Beta strand

29 – 32

4

Beta strand

33 – 35

3

Turn

39 – 41

3

Helix

47 – 59

13

Helix

72 – 83

12

Helix

88 – 91

4

Beta strand

95 – 101

7

Helix

102 – 117

16

Beta strand

122 – 128

7

Helix

132 – 139

8

Beta strand

143 – 148

6

Turn

152 – 155

4

Helix

159 – 166

8

Beta strand

174 – 178

5

Beta strand

179 – 181

3

Turn

183 – 185

3

Helix

191 – 204

14

Beta strand

207 – 213

7

Beta strand

217 – 219

3

Helix

221 – 224

4

Helix

226 – 234

9

Beta strand

238 – 243

6

Turn

245 – 249

5

Helix

251 – 253

3

Beta strand

256 – 261

6

Helix

265 – 280

16

Turn

281 – 283

3

Helix

288 – 298

11

Helix

301 – 331

31

Helix

340 – 343

4

Beta strand

346 – 350

5

Helix

355 – 365

11

Beta strand

367 – 369

3

Turn

371 – 373

3

Beta strand

374 – 376

3

Helix

377 – 379

3

Turn

382 – 384

3

Helix

385 – 395

11

Sequences

	Sequence		Length	Mass (Da)
	P00509 [UniParc]. Last modified July 21, 1986. Version 1. Checksum: 9F0437E76DD4FC0F	FASTA	396	43,573
	10 20 30 40 50 60 MFENITAAPA DPILGLADLF RADERPGKIN LGIGVYKDET GKTPVLTSVK KAEQYLLENE 70 80 90 100 110 120 TTKNYLGIDG IPEFGRCTQE LLFGKGSALI NDKRARTAQT PGGTGALRVA ADFLAKNTSV 130 140 150 160 170 180 KRVWVSNPSW PNHKSVFNSA GLEVREYAYY DAENHTLDFD ALINSLNEAQ AGDVVLFHGC 190 200 210 220 230 240 CHNPTGIDPT LEQWQTLAQL SVEKGWLPLF DFAYQGFARG LEEDAEGLRA FAAMHKELIV 250 260 270 280 290 300 ASSYSKNFGL YNERVGACTL VAADSETVDR AFSQMKAAIR ANYSNPPAHG ASVVATILSN 310 320 330 340 350 360 DALRAIWEQE LTDMRQRIQR MRQLFVNTLQ EKGANRDFSF IIKQNGMFSF SGLTKEQVLR 370 380 390 LREEFGVYAV ASGRVNVAGM TPDNMAPLCE AIVAVL

References

	« Hide 'large scale' referencesShow 'large scale' references »
[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]	"A 718-kb DNA sequence of the Escherichia coli K-12 genome corresponding to the 12.7-28.0 min region on the linkage map." Oshima T., Aiba H., Baba T., Fujita K., Hayashi K., Honjo A., Ikemoto K., Inada T., Itoh T., Kajihara M., Kanai K., Kashimoto K., Kimura S., Kitagawa M., Makino K., Masuda S., Miki T., Mizobuchi K. , Mori H., Motomura K., Nakamura Y., Nashimoto H., Nishio Y., Saito N., Sampei G., Seki Y., Tagami H., Takemoto K., Wada C., Yamamoto Y., Yano M., Horiuchi T. DNA Res. 3:137-155(1996) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[6]	"The complete genome sequence of Escherichia coli K-12." Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V., Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F., Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B., Shao Y. Science 277:1453-1474(1997) [PubMed] [Europe PMC] [Abstract] 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.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

X03629 Genomic DNA. Translation: CAA27279.1.
X05904 Genomic DNA. Translation: CAA29333.1.
U00096 Genomic DNA. Translation: AAC74014.1.
AP009048 Genomic DNA. Translation: BAA35674.1.

PIR

XNECD. A00598.

RefSeq

NP_415448.1. NC_000913.2.
YP_489200.1. NC_007779.1.

3D structure databases

PDBe
RCSB PDB
PDBj

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	[»]
4F5M	X-ray	1.65	A/B	2-396	[»]
5EAA	X-ray	2.40	A	1-396	[»]

ProteinModelPortal

P00509.

SMR

P00509. Positions 1-396.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-9181N.

IntAct

P00509. 4 interactions.

STRING

511145.b0928.

2D gel databases

SWISS-2DPAGE

P00509.

Proteomic databases

PaxDb

P00509.

PRIDE

P00509.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

EnsemblBacteria

AAC74014; AAC74014; b0928.
BAA35674; BAA35674; BAA35674.

GeneID

12931027.
945553.

KEGG

ecj:Y75_p0900.
eco:b0928.

PATRIC

32117069. VBIEscCol129921_0959.

Organism-specific databases

EchoBASE

EB0094.

EcoGene

EG10096. aspC.

Phylogenomic databases

eggNOG

COG1448.

HOGENOM

HOG000185899.

KO

K00813.

OMA

EFAIYIV.

ProtClustDB

PRK09257.

Enzyme and pathway databases

BioCyc

EcoCyc:ASPAMINOTRANS-MONOMER.
ECOL316407:JW0911-MONOMER.
MetaCyc:ASPAMINOTRANS-MONOMER.

BRENDA

2.6.1.1. 2026.

SABIO-RK

P00509.

Gene expression databases

Genevestigator

P00509.

Family and domain databases

Gene3D

3.40.640.10. 1 hit.

InterPro

IPR004839. Aminotransferase_I/II.
IPR000796. Asp_trans.
IPR004838. NHTrfase_class1_PyrdxlP-BS.
IPR015424. PyrdxlP-dep_Trfase.
IPR015421. PyrdxlP-dep_Trfase_major_sub1.
[Graphical view]

PANTHER

PTHR11879. PTHR11879. 1 hit.

Pfam

PF00155. Aminotran_1_2. 1 hit.
[Graphical view]

PRINTS

PR00799. TRANSAMINASE.

SUPFAM

SSF53383. PyrdxlP-dep_Trfase_major. 1 hit.

PROSITE

PS00105. AA_TRANSFER_CLASS_1. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

EvolutionaryTrace

P00509.

Entry information

Entry name

AAT_ECOLI

Accession

Primary (citable) accession number: P00509

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 21, 1986
Last sequence update:	July 21, 1986
Last modified:	May 1, 2013
This is version 146 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program