Reviewed, UniProtKB/Swiss-Prot Q7VTJ9 (ASSY_BORPE)

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:	BP3537

Organism

Bordetella pertussis [Complete proteome] [HAMAP]

Taxonomic identifier

520 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Betaproteobacteria › Burkholderiales › Alcaligenaceae › Bordetella

Protein attributes

Sequence length	445 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_00581
Pathway	Amino-acid biosynthesis; L-arginine biosynthesis; L-arginine from L-ornithine and carbamoyl phosphate: step 2/3. HAMAP MF_00581
Subunit structure	Homotetramer By similarity.
Subcellular location	Cytoplasm Probable.
Sequence similarities	Belongs to the argininosuccinate synthase family. Type 2 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 – 445	445	Argininosuccinate synthase HAMAP MF_00581		PRO_0000148692
Regions
	Nucleotide binding	17 – 25	9	ATP By similarity
Sites
	Binding site	43	1	ATP; via amide nitrogen and carbonyl oxygen By similarity
	Binding site	99	1	Citrulline By similarity
	Binding site	129	1	ATP; via amide nitrogen By similarity
	Binding site	131	1	Aspartate By similarity
	Binding site	131	1	ATP By similarity
	Binding site	135	1	Aspartate By similarity
	Binding site	135	1	Citrulline By similarity
	Binding site	136	1	Aspartate By similarity
	Binding site	136	1	ATP By similarity
	Binding site	139	1	Citrulline By similarity
	Binding site	192	1	Citrulline By similarity
	Binding site	194	1	ATP By similarity
	Binding site	201	1	Citrulline By similarity
	Binding site	203	1	Citrulline By similarity
	Binding site	280	1	Citrulline By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q7VTJ9-1 [UniParc]. Last modified October 1, 2003. Version 1. Checksum: 81278F1EBC07CE61	FASTA	445	49,323
	10 20 30 40 50 60 MTTILPNLPT GQKVGIAFSG GLDTSAALLW MRQKGAVPYA YTANLGQPDE PDYDEIPRRA 70 80 90 100 110 120 MQYGAEAARL VDCRAQLVAE GIAALQAGAF HISTAGLTYF NTTPIGRAVT GTMLVAAMKE 130 140 150 160 170 180 DGVNIWGDGS TFKGNDIERF YRYGLLTNPD LKIYKPWLDQ TFIDELGGRA EMSEYMRQAG 190 200 210 220 230 240 FDYKMSAEKA YSTDSNMLGA THEAKDLELL SAGIRIVQPI MGVAFWQDSV QIKAEEVTVR 250 260 270 280 290 300 FEEGQPVALN GVEYADPVEL LLEANRIGGR HGLGMSDQIE NRIIEAKSRG IYEAPGLALL 310 320 330 340 350 360 FIAYERLVTG IHNEDTIEQY RENGRKLGRL LYQGRWFDPQ AIMLRETAQR WVARAITGEV 370 380 390 400 410 420 TLELRRGNDY SLLNTESANL TYAPERLSME KVENAPFTPA DRIGQLTMRN LDIVDTREKL 430 440 FTYVKTGLLA PSAGSALPQI KDGKK

References

[1]

"Comparative analysis of the genome sequences of Bordetella pertussis, Bordetella parapertussis and Bordetella bronchiseptica." Parkhill J., Sebaihia M., Preston A., Murphy L.D., Thomson N.R., Harris D.E., Holden M.T.G., Churcher C.M., Bentley S.D., Mungall K.L., Cerdeno-Tarraga A.-M., Temple L., James K.D., Harris B., Quail M.A., Achtman M., Atkin R., Baker S. , Basham D., Bason N., Cherevach I., Chillingworth T., Collins M., Cronin A., Davis P., Doggett J., Feltwell T., Goble A., Hamlin N., Hauser H., Holroyd S., Jagels K., Leather S., Moule S., Norberczak H., O'Neil S., Ormond D., Price C., Rabbinowitsch E., Rutter S., Sanders M., Saunders D., Seeger K., Sharp S., Simmonds M., Skelton J., Squares R., Squares S., Stevens K., Unwin L., Whitehead S., Barrell B.G., Maskell D.J. Nat. Genet. 35:32-40(2003) [PubMed: 12910271] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: Tohama I / ATCC BAA-589 / NCTC 13251.

Cross-references

Sequence databases
EMBLGenBankDDBJ	BX640421 Genomic DNA. Translation: CAE43796.1.
RefSeq	NP_882052.1.
3D structure databases
SMR	Q7VTJ9. Positions 2-442.
ModBase	Search...
Genome annotation databases
GeneID	2664934.
GenomeReviews	Gene locus BP3537 in contig BX470248_GR.
KEGG	bpe:BP3537.
NMPDR	fig|257313.1.peg.3122.
Organism-specific databases
CMR	Search...
Phylogenomic databases
HOGENOM	Q7VTJ9.
OMA	GGRKEMS.
Enzyme and pathway databases
BioCyc	BPER257313:BP3537-MON.
BRENDA	6.3.4.5. 21511.
Family and domain databases
HAMAP	MF_00581. [Tree]
InterPro	IPR001518. Arginosuc_synth. IPR018223. Arginosuc_synth_CS. [Graphical view]
PANTHER	PTHR11587. Arginosuc_synth. 1 hit.
Pfam	PF00764. Arginosuc_synth. 2 hits. [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_BORPE

Accession

Primary (citable) accession number: Q7VTJ9

Entry history

Integrated into UniProtKB/Swiss-Prot:	May 24, 2004
Last sequence update:	October 1, 2003
Last modified:	November 3, 2009
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)