P53001 (AAT1_BACSU) 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:	aspB
Ordered Locus Names:	BSU22370

Organism

Bacillus subtilis

Taxonomic identifier

1423 [NCBI]

Taxonomic lineage

Bacteria › Firmicutes › Bacillales › Bacillaceae › Bacillus

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
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
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 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 – 393	393	Aspartate aminotransferase		PRO_0000123836
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)
	P53001 [UniParc]. Last modified October 1, 1996. Version 1. Checksum: 97CDA1F389B8E13B	FASTA	393	43,088
	10 20 30 40 50 60 MKLAKRVSAL TPSTTLAITA KAKELKAAGH DVIGLGAGEP DFNTPQHIID AAVRSMNEGH 70 80 90 100 110 120 TKYTPSGGLA ELKNSIAEKF KRDQNIEYKP SQIIVCTGAK HALYTLFQVI LDEEDEVIIP 130 140 150 160 170 180 TPYWVSYPEQ VKLAGGKPVY VEGLEENHFK ISPEQLKNAI TEKTKAIVIN SPSNPTGVMY 190 200 210 220 230 240 TEEELSALGE VCLEHDILIV SDEIYEKLTY GGKKHVSIAQ LSDRLKEQTV IINGVSKSHS 250 260 270 280 290 300 MTGWRIGYAA GSEDIIKAMT NLASHSTSNP TSIAQYGAIA AYNGPSEPLE EMREAFEHRL 310 320 330 340 350 360 NTIYAKLIEI PGFSCVKPEG AFYLFPNAKE AAQSCGFKDV DEFVKALLEE EKVAIVPGSG 370 380 390 FGSPENVRLS YATSLDLLEE AIERIKRFVE KHS

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Sequence analysis of the Bacillus subtilis chromosome region between the serA and kdg loci cloned in a yeast artificial chromosome." Sorokin A.V., Azevedo V., Zumstein E., Galleron N., Ehrlich S.D., Serror P. Microbiology 142:2005-2016(1996) [PubMed: 8760912] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: 168 / Marburg / ATCC 6051 / DSM 10 / JCM 1465 / NBRC 13719 / NCIMB 3610 / VKM B-501.
[2]	"The complete genome sequence of the Gram-positive bacterium Bacillus subtilis." Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V., Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R., Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S., Bruschi C.V. , Caldwell B., Capuano V., Carter N.M., Choi S.-K., Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., Denizot F., Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., Entian K.-D., Errington J., Fabret C., Ferrari E., Foulger D., Fritz C., Fujita M., Fujita Y., Fuma S., Galizzi A., Galleron N., Ghim S.-Y., Glaser P., Goffeau A., Golightly E.J., Grandi G., Guiseppi G., Guy B.J., Haga K., Haiech J., Harwood C.R., Henaut A., Hilbert H., Holsappel S., Hosono S., Hullo M.-F., Itaya M., Jones L.-M., Joris B., Karamata D., Kasahara Y., Klaerr-Blanchard M., Klein C., Kobayashi Y., Koetter P., Koningstein G., Krogh S., Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J., Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C., Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S., Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B., Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S., Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G., Rey M., Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., Rose M., Sadaie Y., Sato T., Scanlan E., Schleich S., Schroeter R., Scoffone F., Sekiguchi J., Sekowska A., Seror S.J., Serror P., Shin B.-S., Soldo B., Sorokin A., Tacconi E., Takagi T., Takahashi H., Takemaru K., Takeuchi M., Tamakoshi A., Tanaka T., Terpstra P., Tognoni A., Tosato V., Uchiyama S., Vandenbol M., Vannier F., Vassarotti A., Viari A., Wambutt R., Wedler E., Wedler H., Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K., Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E., Yoshikawa H., Danchin A. Nature 390:249-256(1997) [PubMed: 9384377] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: 168.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	L47709 Genomic DNA. Translation: AAB38454.1. AL009126 Genomic DNA. Translation: CAB14153.1.
PIR	C69591.
RefSeq	NP_390118.1. NC_000964.3.
3D structure databases
ProteinModelPortal	P53001.
SMR	P53001. Positions 1-392.
ModBase	Search...
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	EBBACT00000002367; EBBACP00000002367; EBBACG00000002362.
GeneID	939037.
GenomeReviews	Gene locus BSU22370 in contig AL009126_GR.
KEGG	bsu:BSU22370.
NMPDR	fig|224308.1.peg.2241.
PATRIC	18976283. VBIBacSub10457_2332.
Organism-specific databases
GenoList	BSU22370. [Micado]
Phylogenomic databases
GeneTree	EBGT00070000031834.
HOGENOM	HBG645860.
OMA	VANISQR.
PhylomeDB	P53001.
ProtClustDB	PRK05764.
Enzyme and pathway databases
BioCyc	BSUB:BSU22370-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. IPR015422. PyrdxlP-dep_Trfase_major_sub2. [Graphical view]
Gene3D	G3DSA:3.40.640.10. PyrdxlP-dep_Trfase_major_sub1. 1 hit. G3DSA:3.90.1150.10. PyrdxlP-dep_Trfase_major_sub2. 1 hit.
KO	K00812.
Pfam	PF00155. Aminotran_1_2. 1 hit. [Graphical view]
PRINTS	PR00753. ACCSYNTHASE.
SUPFAM	SSF53383. PyrdxlP-dep_Trfase_major. 1 hit.
PROSITE	PS00105. AA_TRANSFER_CLASS_1. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

AAT1_BACSU

Accession

Primary (citable) accession number: P53001

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 1, 1996
Last sequence update:	October 1, 1996
Last modified:	January 25, 2012
This is version 84 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program