Reviewed, UniProtKB/Swiss-Prot Q6HCP7 (ASSY_BACHK)

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:	BT9727_4364

Organism

Bacillus thuringiensis subsp. konkukian [Complete proteome] [HAMAP]

Taxonomic identifier

180856 [NCBI]

Taxonomic lineage

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

Protein attributes

Sequence length	401 AA.
Sequence status	Complete.
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. HAMAP MF_00005
Subcellular location	Cytoplasm Probable HAMAP MF_00005.
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_0000148569
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)
	Q6HCP7-1 [UniParc]. Last modified July 19, 2004. Version 1. Checksum: 0424B9208B00D845	FASTA	401	44,709
	10 20 30 40 50 60 MDKKKVVLAY 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 QALHAFLQET QKNVTGMVRV KLFKGHAIVE GRKSEYSLYD 370 380 390 400 EKLATYTAQD EFNHDAAVGF ISLFGLPTKV YSQVNQKKVE A

References

[1]

"Pathogenomic sequence analysis of Bacillus cereus and Bacillus thuringiensis isolates closely related to Bacillus anthracis." Han C.S., Xie G., Challacombe J.F., Altherr M.R., Bhotika S.S., 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., Hill K.K., Hitchcock P. , Jackson P.J., Keim P., Kewalramani A.R., Longmire J., Lucas S., Malfatti S., 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., Rubin E., Saunders E., Tapia R., Tesmer J.G., Thayer N., Thompson L.S., Tice H., Ticknor L.O., Wills P.L., Brettin T.S., Gilna P. J. Bacteriol. 188:3382-3390(2006) [PubMed: 16621833] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: 97-27.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AE017355 Genomic DNA. Translation: AAT63567.1.
RefSeq	YP_038679.1.
3D structure databases
SMR	Q6HCP7. Positions 5-396.
ModBase	Search...
Genome annotation databases
GeneID	2857662.
GenomeReviews	Gene locus BT9727_4364 in contig AE017355_GR.
KEGG	btk:BT9727_4364.
NMPDR	fig|281309.1.peg.4319.
Organism-specific databases
CMR	Search...
Phylogenomic databases
HOGENOM	HBG335267.
OMA	IAPVREW.
Enzyme and pathway databases
BioCyc	BTHU281309:BT9727_4364-MONOMER.
Family and domain databases
HAMAP	MF_00005. Arg_succ_synth_type1. [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_BACHK

Accession

Primary (citable) accession number: Q6HCP7

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 1, 2005
Last sequence update:	July 19, 2004
Last modified:	February 9, 2010
This is version 41 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)