A0PP79 (ASSY_MYCUA) Reviewed, UniProtKB/Swiss-Prot

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:	MUL_1650

Organism

Mycobacterium ulcerans (strain Agy99) [Complete proteome] [HAMAP]

Taxonomic identifier

362242 [NCBI]

Taxonomic lineage

cellular organisms › Bacteria › Actinobacteria › Actinobacteria › Actinobacteridae › Actinomycetales › Corynebacterineae › Mycobacteriaceae › Mycobacterium › Mycobacterium ulcerans

Protein attributes

Sequence length	398 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-Rule MF_00005
Pathway	Amino-acid biosynthesis; L-arginine biosynthesis; L-arginine from L-ornithine and carbamoyl phosphate: step 2/3. HAMAP-Rule MF_00005
Subunit structure	Homotetramer By similarity. HAMAP-Rule MF_00005
Subcellular location	Cytoplasm By similarity HAMAP-Rule 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 – 398	398	Argininosuccinate synthase HAMAP-Rule MF_00005		PRO_1000000412
Regions
	Nucleotide binding	8 – 16	9	ATP By similarity
Sites
	Binding site	87	1	Citrulline By similarity
	Binding site	117	1	ATP; via amide nitrogen By similarity
	Binding site	119	1	Aspartate By similarity
	Binding site	123	1	Aspartate By similarity
	Binding site	123	1	Citrulline By similarity
	Binding site	124	1	Aspartate By similarity
	Binding site	127	1	Citrulline By similarity
	Binding site	175	1	Citrulline By similarity
	Binding site	260	1	Citrulline By similarity
	Binding site	272	1	Citrulline By similarity

Sequences

	Sequence		Length	Mass (Da)
	A0PP79 [UniParc]. Last modified January 9, 2007. Version 1. Checksum: EAFDDC543AFD53F2	FASTA	398	43,831
	10 20 30 40 50 60 MSERVILAYS GGLDTSVAIS WIGEETGREV VAVAIDLGQG GEDMEVVCQR ALDCGAVEAV 70 80 90 100 110 120 VVDARDEFAE GYCLPTILNN ALYMDRYPLV SAISRPLIVK HLVEAAREHG GGIVAHGCTG 130 140 150 160 170 180 KGNDQVRFEV GFASLAPDLE VLAPVRDYAW TREKAIAFAE ENAIPINVTK RSPFSIDQNV 190 200 210 220 230 240 WGRAVETGFL EHLWNAPTKD VYSYTEDPTV NWNTPDEVIV GFERGMPVSI DGNAVTMLQA 250 260 270 280 290 300 IEELNRRAGA QGVGRLDVVE DRLVGIKSRE IYEAPGAMVL ITAHAELEHV TLERELARFK 310 320 330 340 350 360 RHTDQRWAEL VYDGLWYSPL KTALESFVAK TQEHVSGEIR LVLHGGHIAV NGRRSAESLY 370 380 390 DFNLATYDEG DTFDQSAAKG FVYVHGLSSK LSARRDLQ

References

[1]

"Reductive evolution and niche adaptation inferred from the genome of Mycobacterium ulcerans, the causative agent of Buruli ulcer." Stinear T.P., Seemann T., Pidot S., Frigui W., Reysset G., Garnier T., Meurice G., Simon D., Bouchier C., Ma L., Tichit M., Porter J.L., Ryan J., Johnson P.D.R., Davies J.K., Jenkin G.A., Small P.L.C., Jones L.M. , Tekaia F., Laval F., Daffe M., Parkhill J., Cole S.T. Genome Res. 17:192-200(2007) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: Agy99.

Cross-references

Sequence databases
EMBL GenBank DDBJ	CP000325 Genomic DNA. Translation: ABL04148.1.
RefSeq	YP_905619.1. NC_008611.1.
3D structure databases
ProteinModelPortal	A0PP79.
ModBase	Search...
Protein-protein interaction databases
STRING	362242.MUL_1650.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	ABL04148; ABL04148; MUL_1650.
GeneID	4552063.
KEGG	mul:MUL_1650.
PATRIC	18170252. VBIMycUlc37413_1979.
Organism-specific databases
GenoList	MUL_1650.
CMR	Search...
Phylogenomic databases
eggNOG	COG0137.
HOGENOM	HOG000230093.
KO	K01940.
OMA	NDQFRFE.
ProtClustDB	PRK00509.
Enzyme and pathway databases
UniPathway	UPA00068; UER00113.
Family and domain databases
Gene3D	3.40.50.620. 1 hit. 3.90.1260.10. 1 hit.
HAMAP	MF_00005. Arg_succ_synth_type1.
InterPro	IPR001518. Arginosuc_synth. IPR018223. Arginosuc_synth_CS. IPR023434. Arginosuc_synth_type_1_subfam. IPR024074. AS_cat/multimer_dom_body. IPR014729. Rossmann-like_a/b/a_fold. [Graphical view]
PANTHER	PTHR11587. PTHR11587. 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_MYCUA

Accession

Primary (citable) accession number: A0PP79

Entry history

Integrated into UniProtKB/Swiss-Prot:	January 15, 2008
Last sequence update:	January 9, 2007
Last modified:	May 1, 2013
This is version 45 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program