Reviewed, UniProtKB/Swiss-Prot Q59228 (AAT_BACST)

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

Organism

Bacillus stearothermophilus (Geobacillus stearothermophilus)

Taxonomic identifier

1422 [NCBI]

Taxonomic lineage

Bacteria › Firmicutes › Bacillales › Bacillaceae › Geobacillus

Protein attributes

Sequence length	393 AA.
Sequence status	Complete.
Protein existence	Inferred from homology.

General annotation (Comments)

Catalytic activity	L-aspartate + 2-oxoglutarate = oxaloacetate + L-glutamate.
Cofactor	Pyridoxal phosphate.
Subunit structure	Homodimer By similarity.
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
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 – 393	393	Aspartate aminotransferase		PRO_0000123835
Sites
	Binding site	38	1	Aspartate; via amide nitrogen By similarity
	Binding site	124	1	Aspartate By similarity
	Binding site	174	1	Aspartate By similarity
Amino acid modifications
	Modified residue	237	1	N6-(pyridoxal phosphate)lysine By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q59228-1 [UniParc]. Last modified November 1, 1996. Version 1. Checksum: 4628CCD998A065A7	FASTA	393	42,402
	10 20 30 40 50 60 MKLAKRVASL TPSATLAITE KAKELKAAGH DVIGLGAGEP DFNTPQHILD AAIKAMNEGH 70 80 90 100 110 120 TKYTPSGGLP ALKEEIIKKF ARDQGLDYEP AEVIVCVGAK HALYTLFQVL LDEGDEVIIP 130 140 150 160 170 180 TPYWVSYPEQ VKLAGGVPVY VEGLEQNHFK ITPEQLKQAI TPRTKAVIIN SPSNPTGMIY 190 200 210 220 230 240 TAEELKALGE VCLAHGVLIV SDEIYEKLTY GGAKHVSIAE LSPELKAQTV IINGVSKSHS 250 260 270 280 290 300 MTGWRIGYAA GPKDIIKAMT DLASHSTSNP TSIAQYAAIA AYSGPQEPVE QMRQAFEQRL 310 320 330 340 350 360 NIIYDKLVQI PGFTCVKPQG AFYLFPNARE AAAMAGCRTV DEFVAALLEE AKVALVPGSG 370 380 390 FGAPDNVRLS YATSLDALET AVERIHRFME ARA

References

[1]

"Stereospecific production of the herbicide phosphinothricin (glufosinate): purification of aspartate transaminase from Bacillus stearothermophilus, cloning of the corresponding gene, aspC, and application in a coupled transaminase process." Bartsch K., Schneider R., Schulz A. Appl. Environ. Microbiol. 62:3794-3799(1996) [PubMed: 8837436] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: ATCC 12980 / DSM 22 / IFO 12550 / NCIB 8923 / NCTC 10339.

Cross-references

Sequence databases
EMBL GenBank DDBJ	X93600 Genomic DNA. Translation: CAA63799.1.
3D structure databases
SMR	Q59228. Positions 1-391.
ModBase	Search...
Enzyme and pathway databases
BRENDA	2.6.1.1. 266715.
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_BACST

Accession

Primary (citable) accession number: Q59228

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 1997
Last sequence update:	November 1, 1996
Last modified:	February 9, 2010
This is version 56 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)