Reviewed, UniProtKB/Swiss-Prot P00509 (AAT_ECOLI)

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) [Complete proteome] [HAMAP]

Taxonomic identifier

83333 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia

Protein attributes

Sequence length	396 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at protein level.

General annotation (Comments)

Catalytic activity	L-aspartate + 2-oxoglutarate = oxaloacetate + L-glutamate.
Cofactor	Pyridoxal phosphate.
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
Gene Ontology (GO)
Biological process	amino acid metabolic process Inferred from electronic annotation. Source: InterPro biosynthetic process Inferred from electronic annotation. Source: InterPro
Cellular component	cytosol Inferred from direct assay. Source: UniProtKB
Molecular function	aspartate transaminase activity Inferred from electronic annotation. Source: EC protein binding Inferred from physical interaction. Source: IntAct pyridoxal phosphate binding Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
nadE	P18843	1	EBI-907474,EBI-548960

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

246

1

Pyridoxal phosphate (covalent)

Binding site

374

1

Substrate

Experimental info

Mutagenesis

65

1

Y → F or S: Slight changes in activity

Mutagenesis

133

1

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

Mutagenesis

133

1

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

Mutagenesis

374

1

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

Secondary structure

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396

Helix Strand Turn

Details...

Beta strand

29 – 32

4

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

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

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

374 – 376

3

Helix

377 – 379

3

Turn

382 – 384

3

Helix

385 – 395

11

Sequences

	Sequence		Length	Mass (Da)
	P00509-1 [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: 6378205] [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: 3897210] [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: 3521591] [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: 3298240] [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: 8905232] [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: 9278503] [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: 16738553] [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: 9298646] [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: 1868057] [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: 2007566] [Abstract] Cited for: MUTAGENESIS OF HIS-133.
[11]	"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: 2513875] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF MUTANT ALA-246.
[12]	"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: 1993208] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS), MUTAGENESIS OF ARG-374.
[13]	"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: 9891001] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) OF MUTANT.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBLGenBankDDBJ

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

AP_001558.1.
NP_415448.1.

3D structure databases

PDBMSD

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	1-396	[»]
1TOG	X-ray	2.31	A/B	1-396	[»]
1TOI	X-ray	1.90	A	1-396	[»]