Reviewed, UniProtKB/Swiss-Prot A0RJM4 (ASSY_BACAH)

Names and origin

Protein names

Recommended name:
    Argininosuccinate synthase
    EC=6.3.4.5
Alternative name(s):
    Citrulline--aspartate ligase

Gene names

Name:	argG
Ordered Locus Names:	BALH_4210

Organism

Bacillus thuringiensis (strain Al Hakam) [Complete proteome] [HAMAP]

Taxonomic identifier

412694 [NCBI]

Taxonomic lineage

Bacteria › Firmicutes › Bacillales › Bacillaceae › Bacillus › Bacillus cereus group

Protein attributes

Sequence length	401 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Inferred from homology.

General annotation (Comments)

Catalytic activity	ATP + L-citrulline + L-aspartate = AMP + diphosphate + N(omega)-(L-arginino)succinate. HAMAP MF_00005
Pathway	Amino-acid biosynthesis; L-arginine biosynthesis; L-arginine from L-ornithine and carbamoyl phosphate: step 2/3. HAMAP MF_00005
Subunit structure	Homotetramer By similarity.
Subcellular location	Cytoplasm Probable.
Sequence similarities	Belongs to the argininosuccinate synthase family. Type 1 subfamily.

Ontologies

Keywords
Biological process	Amino-acid biosynthesis Arginine biosynthesis
Cellular component	Cytoplasm
Ligand	ATP-binding Nucleotide-binding
Molecular function	Ligase
Technical term	Complete proteome
Gene Ontology (GO)
Biological process	arginine biosynthetic process Inferred from electronic annotation. Source: HAMAP
Cellular component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	ATP binding Inferred from electronic annotation. Source: HAMAP argininosuccinate synthase activity Inferred from electronic annotation. Source: HAMAP
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 401	401	Argininosuccinate synthase HAMAP MF_00005		PRO_0000321302
Regions
	Nucleotide binding	9 – 17	9	ATP By similarity
Sites
	Binding site	86	1	Citrulline By similarity
	Binding site	116	1	ATP; via amide nitrogen By similarity
	Binding site	118	1	Aspartate By similarity
	Binding site	122	1	Aspartate By similarity
	Binding site	122	1	Citrulline By similarity
	Binding site	123	1	Aspartate By similarity
	Binding site	126	1	Citrulline By similarity
	Binding site	174	1	Citrulline By similarity
	Binding site	183	1	Citrulline By similarity
	Binding site	259	1	Citrulline By similarity
	Binding site	271	1	Citrulline By similarity

Sequences

	Sequence		Length	Mass (Da)
	A0RJM4-1 [UniParc]. Last modified February 26, 2008. Version 2. Checksum: D3E21C76DC5D4AD0	FASTA	401	44,670
	10 20 30 40 50 60 MEKKKVVLAY SGGLDTSVAI KWLQEKNYDI IALCLDLGEG KDLAFVKEKA LSVGAIKSYM 70 80 90 100 110 120 IDVQEEFANE YALMAMQAHT LYEGKYPLVS ALSRPLIAKK LVEIAEQEGA TAVAHGCTGK 130 140 150 160 170 180 GNDQVRFEVS IQALNPYLEV IAPVREWKWS REEEIAYAKE NNVPIPINLD SPFSIDQNLW 190 200 210 220 230 240 GRSNECGILE DPWAAPPEDA YEMTLALEDT PNKPEFVEIG FEAGVPTTLN GTAYPLSELI 250 260 270 280 290 300 KTLNALAGKH GVGRIDHVEN RLVGIKSREV YECPAAMTLI TAHKELEDLT LVKEVAHFKP 310 320 330 340 350 360 MIEQKITELI YNGLWFSPLK QALNAFLQET QKNVTGTVRV KLFKGHAIVE GRKSEYSLYD 370 380 390 400 EKLATYTAQD EFNHDAAVGF ISLFGLPTKV YSQVNQKKVE A

References

[1]

"The complete genome sequence of Bacillus thuringiensis Al Hakam." Challacombe J.F., Altherr M.R., Xie G., Bhotika S.S., Brown N., Bruce D., Campbell C.S., Campbell M.L., Chen J., Chertkov O., Cleland C., Dimitrijevic M., Doggett N.A., Fawcett J.J., Glavina T., Goodwin L.A., Green L.D., Han C.S. , Hill K.K., Hitchcock P., Jackson P.J., Keim P., Kewalramani A.R., Longmire J., Lucas S., Malfatti S., Martinez D., McMurry K., Meincke L.J., Misra M., Moseman B.L., Mundt M., Munk A.C., Okinaka R.T., Parson-Quintana B., Reilly L.P., Richardson P., Robinson D.L., Saunders E., Tapia R., Tesmer J.G., Thayer N., Thompson L.S., Tice H., Ticknor L.O., Wills P.L., Gilna P., Brettin T.S. J. Bacteriol. 189:3680-3681(2007) [PubMed: 17337577] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases
EMBLGenBankDDBJ	CP000485 Genomic DNA. Translation: ABK87417.1. Different initiation.
RefSeq	YP_896924.1.
3D structure databases
ModBase	Search...
Protein-protein interaction databases
STRING	A0RJM4.
Genome annotation databases
GeneID	4544007.
GenomeReviews	Gene locus BALH_4210 in contig CP000485_GR.
KEGG	btl:BALH_4210.
Organism-specific databases
CMR	Search...
Family and domain databases
HAMAP	MF_00005. [Tree]
InterPro	IPR001518. Arginosuc_synth. IPR018223. Arginosuc_synth_CS. IPR014729. Rossmann-like_a/b/a_fold. [Graphical view]
Gene3D	G3DSA:3.40.50.620. Rossmann-like_a/b/a_fold. 1 hit.
PANTHER	PTHR11587. Arginosuc_synth. 1 hit.
Pfam	PF00764. Arginosuc_synth. 1 hit. [Graphical view]
TIGRFAMs	TIGR00032. argG. 1 hit.
PROSITE	PS00564. ARGININOSUCCIN_SYN_1. 1 hit. PS00565. ARGININOSUCCIN_SYN_2. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

ASSY_BACAH

Accession

Primary (citable) accession number: A0RJM4

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 26, 2008
Last sequence update:	February 26, 2008
Last modified:	September 1, 2009
This is version 19 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

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