Reviewed, UniProtKB/Swiss-Prot Q1IIZ2 (ASSY_ACIBL)

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:	Acid345_4158

Organism

Acidobacteria bacterium (strain Ellin345) [Complete proteome] [HAMAP]

Taxonomic identifier

204669 [NCBI]

Taxonomic lineage

Bacteria › Acidobacteria › Candidatus Koribacter

Protein attributes

Sequence length	405 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 – 405	405	Argininosuccinate synthase HAMAP MF_00005		PRO_0000263903
Regions
	Nucleotide binding	8 – 16	9	ATP By similarity
Sites
	Binding site	86	1	Citrulline By similarity
	Binding site	91	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	175	1	Citrulline By similarity
	Binding site	184	1	Citrulline By similarity
	Binding site	260	1	Citrulline By similarity
	Binding site	272	1	Citrulline By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q1IIZ2-1 [UniParc]. Last modified June 13, 2006. Version 1. Checksum: 603714E0DE921FEE	FASTA	405	44,366
	10 20 30 40 50 60 MREKIVLAYS GGLDTSIIIP WLKENYSCDV IAMVGDVGQG DDIDAVVAKA HKTGASKVIV 70 80 90 100 110 120 KDLREEFLTQ YVYPAISTGA VYEHKYLLGT SLARPPIAKA QVEVALAEGA TAVSHGCTGK 130 140 150 160 170 180 GNDQVRFEHA FQALAPELKI IAPWREWTLK SREDCLDYAE AHGISVAQSR EKIHSRDRNL 190 200 210 220 230 240 LHVSHEGGEL EDPNNAPLDT TWTWTKSPQE APDRVEEVTI GFEGGVPVSI NGMKLEPLAL 250 260 270 280 290 300 IELLNEIGAR NAIGRIDLVE NRFVGIKSRG CYETPGGSLL LAAHRELEAL CLDRDTLHYK 310 320 330 340 350 360 QEVALKWAEL VYFGLWFTPL RESLDAFVAS TQKNIAGAVK LALYKGNIAV AGRTSPKSLY 370 380 390 400 RPDIASFTMG AGYDQKDAEG FIRILGLPAR SRALIENAGK EKVSK

References

[1]

"Three genomes from the phylum Acidobacteria provide insight into the lifestyles of these microorganisms in soils." Ward N.L., Challacombe J.F., Janssen P.H., Henrissat B., Coutinho P.M., Wu M., Xie G., Haft D.H., Sait M., Badger J., Barabote R.D., Bradley B., Brettin T.S., Brinkac L.M., Bruce D., Creasy T., Daugherty S.C., Davidsen T.M. , DeBoy R.T., Detter J.C., Dodson R.J., Durkin A.S., Ganapathy A., Gwinn-Giglio M., Han C.S., Khouri H., Kiss H., Kothari S.P., Madupu R., Nelson K.E., Nelson W.C., Paulsen I., Penn K., Ren Q., Rosovitz M.J., Selengut J.D., Shrivastava S., Sullivan S.A., Tapia R., Thompson L.S., Watkins K.L., Yang Q., Yu C., Zafar N., Zhou L., Kuske C.R. Appl. Environ. Microbiol. 75:2046-2056(2009) [PubMed: 19201974] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases
EMBLGenBankDDBJ	CP000360 Genomic DNA. Translation: ABF43158.1.
RefSeq	YP_593232.1.
3D structure databases
ModBase	Search...
Protein-protein interaction databases
STRING	Q1IIZ2.
Genome annotation databases
GeneID	4072117.
GenomeReviews	Gene locus Acid345_4158 in contig CP000360_GR.
KEGG	aba:Acid345_4158.
NMPDR	fig|204669.6.peg.4139.
Organism-specific databases
CMR	Search...
Phylogenomic databases
HOGENOM	Q1IIZ2.
OMA	IAPVREW.
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_ACIBL

Accession

Primary (citable) accession number: Q1IIZ2

Entry history

Integrated into UniProtKB/Swiss-Prot:	December 12, 2006
Last sequence update:	June 13, 2006
Last modified:	November 3, 2009
This is version 20 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)