Reviewed, UniProtKB/Swiss-Prot Q56232 (AAT_THET8)

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) [Complete proteome] [HAMAP]

Taxonomic identifier

300852 [NCBI]

Taxonomic lineage

Bacteria › Deinococcus-Thermus › Deinococci › Thermales › Thermaceae › Thermus

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.
Subunit structure	Homodimer.
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
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	1-aminocyclopropane-1-carboxylate synthase activity Inferred from electronic annotation. Source: InterPro L-aspartate: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 – 9

4

Helix

15 – 28

14

Helix

47 – 58

12

Helix

71 – 85

15

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

Helix

269 – 280

12

Helix

282 – 310

29

Beta strand

319 – 326

8

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)
	Q56232-1 [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: 8907187] [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].
[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: 10029535] [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: 11432784] [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.

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	[»]

ModBase

Search...

Protein-protein interaction databases

STRING

Q56232.

Genome annotation databases

GeneID

3168657.

GenomeReviews

Gene locus TTHA0046 in contig AP008226_GR.

KEGG

ttj:TTHA0046.

NMPDR

fig|300852.3.peg.77.

Organism-specific databases

CMR

Search...

Phylogenomic databases

eggNOG

COG0436.

HOGENOM

HBG645860.

OMA

FVEMARE.

Enzyme and pathway databases

BioCyc

TTHE300852:TTHA0046-MONOMER.

Family and domain databases

InterPro

IPR001176. ACC_synthase.
IPR004839. Aminotransferase_I/II.
IPR004838. NHTrfase_class1_PyrdxlP-BS.
IPR015424. PyrdxlP-dep_Trfase_major_dom.
IPR015421. PyrdxlP-dep_Trfase_major_sub1.
[Graphical view]

Gene3D

G3DSA:3.40.640.10. PyrdxlP-dep_Trfase_major_sub1. 1 hit.

Pfam

PF00155. Aminotran_1_2. 1 hit.
[Graphical view]

PRINTS

PR00753. ACCSYNTHASE.

PROSITE

PS00105. AA_TRANSFER_CLASS_1. 1 hit.
[Graphical view]

ProtoNet

Search...

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:	February 9, 2010
This is version 73 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)