P54264 (ASNA_LACDA) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Aspartate--ammonia ligase
EC=6.3.1.1

Alternative name(s):
Asparagine synthetase A

Gene names

Name:	asnA
Ordered Locus Names:	Ldb1194

Organism

Lactobacillus delbrueckii subsp. bulgaricus (strain ATCC 11842 / DSM 20081) [Complete proteome] [HAMAP]

Taxonomic identifier

390333 [NCBI]

Taxonomic lineage

Bacteria › Firmicutes › Lactobacillales › Lactobacillaceae › Lactobacillus

Protein attributes

Sequence length	338 AA.
Sequence status	Complete.
Protein existence	Inferred from homology

General annotation (Comments)

Catalytic activity	ATP + L-aspartate + NH3 = AMP + diphosphate + L-asparagine. HAMAP MF_00555
Pathway	Amino-acid biosynthesis; L-asparagine biosynthesis; L-asparagine from L-aspartate (ammonia route): step 1/1. HAMAP MF_00555
Subcellular location	Cytoplasm HAMAP MF_00555.
Sequence similarities	Belongs to the class-II aminoacyl-tRNA synthetase family. AsnA subfamily.

Ontologies

Keywords
Biological process	Amino-acid biosynthesis Asparagine biosynthesis
Cellular component	Cytoplasm
Ligand	ATP-binding Nucleotide-binding
Molecular function	Ligase
Technical term	Complete proteome
Gene Ontology (GO)
Biological process	asparagine biosynthetic process Inferred from electronic annotation. Source: UniProtKB-KW tRNA aminoacylation for protein translation Inferred from electronic annotation. Source: InterPro
Cellular component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW aminoacyl-tRNA ligase activity Inferred from electronic annotation. Source: InterPro aspartate-ammonia ligase activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 338	338	Aspartate--ammonia ligase HAMAP MF_00555		PRO_0000195879
Experimental info
	Sequence conflict	17 – 32	16	RETEK…ETFQT → AKRKRQSATSGKPSS in CAA61602. Ref.1
	Sequence conflict	310 – 314	5	GKAHI → QGPH in CAA61602. Ref.1

Sequences

	Sequence		Length	Mass (Da)
	P54264 [UniParc]. Last modified October 17, 2006. Version 2. Checksum: 6718FB1A6A6C6123	FASTA	338	38,786
	10 20 30 40 50 60 MAKLVIPSDY DPKMTIRETE KAIRYIRETF QTEFGTAMNL ERISAPMFVK KSSGLNDNLS 70 80 90 100 110 120 GWEKPVSFTL HDGNEGELQI VHSLAKWKRW ALKHYGFSHG EGLFTNMNAI RKDEEVLDNL 130 140 150 160 170 180 HSVYVDQWDW EKVIDKSERT EATLRQTVQR IFETIKGMEY HVRALYPQAA YHLPEEISFV 190 200 210 220 230 240 TSEELEARWP SLTPSEREDK ICQEKGAVFL EHIGGALPLS KKPHDLRAPD YDDWTLNGDL 250 260 270 280 290 300 LFWYEPLQRA FEVSSMSIRV DEDRLQEQLK LAGAEDRLDL PFHQALLKGD LPYSIGGGIG 310 320 330 QSRLCMLLLG KAHIGEVQAS IWPDEIVEKC QAAKIQLL

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Lactobacillus bulgaricus asparagine synthetase and asparaginyl-tRNA synthetase: coregulation by transcription antitermination?" Kim S.I., Germond J.-E., Pridmore D., Soell D. J. Bacteriol. 178:2459-2461(1996) [PubMed: 8636057] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]	"The complete genome sequence of Lactobacillus bulgaricus reveals extensive and ongoing reductive evolution." van de Guchte M., Penaud S., Grimaldi C., Barbe V., Bryson K., Nicolas P., Robert C., Oztas S., Mangenot S., Couloux A., Loux V., Dervyn R., Bossy R., Bolotin A., Batto J.-M., Walunas T., Gibrat J.-F., Bessieres P. , Weissenbach J., Ehrlich S.D., Maguin E. Proc. Natl. Acad. Sci. U.S.A. 103:9274-9279(2006) [PubMed: 16754859] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 11842 / DSM 20081.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	X89438 Genomic DNA. Translation: CAA61602.1. CR954253 Genomic DNA. Translation: CAI97996.1.
PIR	S71073.
RefSeq	YP_619094.1. NC_008054.1.
3D structure databases
ProteinModelPortal	P54264.
ModBase	Search...
Protein-protein interaction databases
STRING	P54264.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	4084369.
GenomeReviews	Gene locus Ldb1194 in contig CR954253_GR.
KEGG	ldb:Ldb1194.
PATRIC	22217889. VBILacDel123523_1064.
Organism-specific databases
CMR	Search...
Phylogenomic databases
eggNOG	COG2502.
HOGENOM	HBG288146.
OMA	LNDNLNG.
PhylomeDB	P54264.
ProtClustDB	PRK05425.
Enzyme and pathway databases
BioCyc	LDEL390333:LDB1194-MONOMER.
Family and domain databases
HAMAP	MF_00555. AsnA. [Tree]
InterPro	IPR006195. aa-tRNA-synth_II. IPR004618. AsnA. [Graphical view]
KO	K01914.
Pfam	PF03590. AsnA. 1 hit. [Graphical view]
PIRSF	PIRSF001555. Asp_ammon_ligase. 1 hit.
TIGRFAMs	TIGR00669. AsnA. 1 hit.
PROSITE	PS50862. AA_TRNA_LIGASE_II. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

ASNA_LACDA

Accession

Primary (citable) accession number: P54264
Secondary accession number(s): Q1G9Z6

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 1, 1996
Last sequence update:	October 17, 2006
Last modified:	January 25, 2012
This is version 72 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program