Q56232 (AAT_THET8) 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:	TTHA0046

Organism

Thermus thermophilus (strain HB8 / ATCC 27634 / DSM 579) [Reference proteome] [HAMAP]

Taxonomic identifier

300852 [NCBI]

Taxonomic lineage

cellular organisms › Bacteria › Deinococcus-Thermus › Deinococci › Thermales › Thermaceae › Thermus › Thermus thermophilus

Protein attributes

Sequence length	385 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Catalytic activity	L-aspartate + 2-oxoglutarate = oxaloacetate + L-glutamate.
Cofactor	Pyridoxal phosphate. Ref.4
Subunit structure	Homodimer. Ref.3 Ref.4
Subcellular location	Cytoplasm By similarity.
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 Reference proteome
Gene Ontology (GO)
Biological_process	biosynthetic process Inferred from electronic annotation. Source: InterPro
Cellular_component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular_function	L-aspartate:2-oxoglutarate aminotransferase activity Inferred from electronic annotation. Source: EC L-phenylalanine:2-oxoglutarate aminotransferase activity Inferred from electronic annotation. Source: EC pyridoxal phosphate binding Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 385

385

Aspartate aminotransferase

PRO_0000123856

Sites

Binding site

39

1

Aspartate; via amide nitrogen By similarity

Binding site

125

1

Aspartate

Binding site

175

1

Aspartate

Binding site

361

1

Aspartate

Amino acid modifications

Modified residue

234

1

N6-(pyridoxal phosphate)lysine

Secondary structure

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385

Helix Strand Turn

Details...

Helix

6 – 10

5

Helix

15 – 28

14

Helix

47 – 58

12

Helix

71 – 83

13

Helix

91 – 93

3

Beta strand

94 – 98

5

Helix

99 – 111

13

Beta strand

117 – 123

7

Helix

127 – 134

8

Beta strand

138 – 143

6

Helix

146 – 148

3

Helix

154 – 158

5

Beta strand

165 – 173

9

Turn

175 – 177

3

Helix

183 – 195

13

Beta strand

199 – 203

5

Turn

205 – 208

4

Beta strand

210 – 213

4

Helix

218 – 220

3

Turn

223 – 225

3

Beta strand

226 – 232

7

Turn

233 – 237

5

Helix

239 – 241

3

Beta strand

244 – 247

4

Helix

250 – 261

12

Turn

262 – 264

3

Beta strand

265 – 267

3

Helix

269 – 280

12

Helix

282 – 310

29

Beta strand

318 – 326

9

Turn

328 – 330

3

Helix

334 – 343

10

Beta strand

349 – 351

3

Helix

352 – 354

3

Beta strand

359 – 363

5

Helix

368 – 377

10

Helix

378 – 381

4

Sequences

	Sequence		Length	Mass (Da)
	Q56232 [UniParc]. Last modified November 1, 1996. Version 1. Checksum: EADF7B7EA127F39B	FASTA	385	42,051
	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

References

	« Hide 'large scale' referencesShow '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] [Europe PMC] [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]. Strain: HB8 / ATCC 27634 / DSM 579.
[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] [Europe PMC] [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] [Europe PMC] [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.

RefSeq

YP_143312.1. NC_006461.1.

3D structure databases

PDBe
RCSB PDB
PDBj

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	[»]

ProteinModelPortal

Q56232.

SMR

Q56232. Positions 1-382.

ModBase

Search...

Protein-protein interaction databases

STRING

300852.TTHA0046.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

EnsemblBacteria

BAD69869; BAD69869; BAD69869.

GeneID

3168657.

KEGG

ttj:TTHA0046.

PATRIC

23955021. VBITheThe93045_0044.

Phylogenomic databases

eggNOG

COG0436.

HOGENOM

HOG000223062.

KO

K00812.

OMA

FVEMARE.

ProtClustDB

CLSK444633.

Family and domain databases

Gene3D

3.40.640.10. 1 hit.
3.90.1150.10. 1 hit.

InterPro

IPR004839. Aminotransferase_I/II.
IPR004838. NHTrfase_class1_PyrdxlP-BS.
IPR015424. PyrdxlP-dep_Trfase.
IPR015421. PyrdxlP-dep_Trfase_major_sub1.
IPR015422. PyrdxlP-dep_Trfase_major_sub2.
[Graphical view]

Pfam

PF00155. Aminotran_1_2. 1 hit.
[Graphical view]

SUPFAM

SSF53383. PyrdxlP-dep_Trfase_major. 1 hit.

PROSITE

PS00105. AA_TRANSFER_CLASS_1. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

EvolutionaryTrace

Q56232.

Entry information

Entry name

AAT_THET8

Accession

Primary (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:	May 1, 2013
This is version 94 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program