Reviewed, UniProtKB/Swiss-Prot P77973 (ASSY_SYNY3)

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:	slr0585

Organism

Synechocystis sp. (strain PCC 6803) [Complete proteome] [HAMAP]

Taxonomic identifier

1148 [NCBI]

Taxonomic lineage

Bacteria › Cyanobacteria › Chroococcales › Synechocystis

Protein attributes

Sequence length	400 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at protein level.

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 protein binding Inferred from physical interaction. Source: IntAct
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
trxA	P52231	1	EBI-862317,EBI-862916

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 400	400	Argininosuccinate synthase HAMAP MF_00005		PRO_0000148655
Regions
	Nucleotide binding	10 – 18	9	ATP By similarity
Sites
	Binding site	38	1	ATP; via amide nitrogen and carbonyl oxygen By similarity
	Binding site	89	1	Citrulline By similarity
	Binding site	119	1	ATP; via amide nitrogen By similarity
	Binding site	121	1	Aspartate By similarity
	Binding site	125	1	Aspartate By similarity
	Binding site	125	1	Citrulline By similarity
	Binding site	126	1	Aspartate By similarity
	Binding site	129	1	Citrulline By similarity
	Binding site	177	1	Citrulline By similarity
	Binding site	186	1	Citrulline By similarity
	Binding site	262	1	Citrulline By similarity
	Binding site	274	1	Citrulline By similarity

Sequences

	Sequence		Length	Mass (Da)
	P77973-1 [UniParc]. Last modified February 1, 1997. Version 1. Checksum: 37BDB758CBB82C05	FASTA	400	44,485
	10 20 30 40 50 60 MGRAKKVVLA YSGGVDTSVC IPYLMHEWGV EEVITLAADL GQGDELGPIQ EKALRCGAVE 70 80 90 100 110 120 SLVIDGKEEF VKEYAFRSIQ ANALYENRYP LSTALARPLI AKMLVEAAEK YGADAVAHGC 130 140 150 160 170 180 TGKGNDQVRF DISIMALNPN LKVLAPAREW KMSREETIAY GERYGVESPV KKSSPYSIDR 190 200 210 220 230 240 NILGRSIEAG PLEDPMTEPT EEIYLMTKAI ADTPDEPEYV DIGFEKGIPV SLNGVMLDPV 250 260 270 280 290 300 TLVERLNEIA GNHGVGRLDM VENRVVGIKS REIYEAPALL VLIDAHRDLE SLTQTADVTH 310 320 330 340 350 360 YKNTVEEIYS QLIYRGLWYS PLKEALDAFI VKTQERVTGM VRVKFFKGNA NVAGRKSDYS 370 380 390 400 IYDAELATYG MEDQFDHKAA EGFIYIWGLP TKVWAQKMRG

References

[1]

"Sequence analysis of the genome of the unicellular cyanobacterium Synechocystis sp. strain PCC6803. II. Sequence determination of the entire genome and assignment of potential protein-coding regions." Kaneko T., Sato S., Kotani H., Tanaka A., Asamizu E., Nakamura Y., Miyajima N., Hirosawa M., Sugiura M., Sasamoto S., Kimura T., Hosouchi T., Matsuno A., Muraki A., Nakazaki N., Naruo K., Okumura S., Shimpo S. , Takeuchi C., Wada T., Watanabe A., Yamada M., Yasuda M., Tabata S. DNA Res. 3:109-136(1996) [PubMed: 8905231] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases
EMBLGenBankDDBJ	BA000022 Genomic DNA. Translation: BAA18841.1.
PIR	S76929.
RefSeq	NP_443029.1.
3D structure databases
HSSP	HSSP built from PDB template 1KP2 based on UniProtKB P22767.
ModBase	Search...
Protein-protein interaction databases
IntAct	P77973. 7 interactions.
Genome annotation databases
GeneID	951914.
GenomeReviews	Gene locus slr0585 in contig BA000022_GR.
KEGG	syn:slr0585.
NMPDR	fig|1148.1.peg.3130.
Organism-specific databases
CMR	Search...
Phylogenomic databases
HOGENOM	P77973.
OMA	P77973. ISHYSIN.
Enzyme and pathway databases
BioCyc	SSP1148:SLR0585-MON.
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_SYNY3

Accession

Primary (citable) accession number: P77973

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 1997
Last sequence update:	February 1, 1997
Last modified:	June 16, 2009
This is version 64 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)