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B4RQS8 (ASSY_NEIG2) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 40. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Argininosuccinate synthase

EC=6.3.4.5
Alternative name(s):
Citrulline--aspartate ligase
Gene names
Name:argG
Ordered Locus Names:NGK_2284
OrganismNeisseria gonorrhoeae (strain NCCP11945) [Complete proteome] [HAMAP]
Taxonomic identifier521006 [NCBI]
Taxonomic lineageBacteriaProteobacteriaBetaproteobacteriaNeisserialesNeisseriaceaeNeisseria

Protein attributes

Sequence length447 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Catalytic activity

ATP + L-citrulline + L-aspartate = AMP + diphosphate + N(omega)-(L-arginino)succinate. HAMAP-Rule MF_00581

Pathway

Amino-acid biosynthesis; L-arginine biosynthesis; L-arginine from L-ornithine and carbamoyl phosphate: step 2/3. HAMAP-Rule MF_00581

Subunit structure

Homotetramer By similarity. HAMAP-Rule MF_00581

Subcellular location

Cytoplasm By similarity HAMAP-Rule MF_00581.

Sequence similarities

Belongs to the argininosuccinate synthase family. Type 2 subfamily.

Ontologies

Keywords
   Biological processAmino-acid biosynthesis
Arginine biosynthesis
   Cellular componentCytoplasm
   LigandATP-binding
Nucleotide-binding
   Molecular functionLigase
   Technical termComplete proteome
Gene Ontology (GO)
   Biological_processarginine biosynthetic process

Inferred from electronic annotation. Source: UniProtKB-HAMAP

   Cellular_componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionATP binding

Inferred from electronic annotation. Source: UniProtKB-HAMAP

argininosuccinate synthase activity

Inferred from electronic annotation. Source: UniProtKB-HAMAP

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 447447Argininosuccinate synthase HAMAP-Rule MF_00581
PRO_1000129757

Regions

Nucleotide binding20 – 289ATP By similarity

Sites

Binding site461ATP By similarity
Binding site1021Citrulline By similarity
Binding site1321ATP; via amide nitrogen By similarity
Binding site1341Aspartate By similarity
Binding site1341ATP By similarity
Binding site1381Aspartate By similarity
Binding site1381Citrulline By similarity
Binding site1391Aspartate By similarity
Binding site1391ATP By similarity
Binding site1421Citrulline By similarity
Binding site1951Citrulline By similarity
Binding site1971ATP By similarity
Binding site2041Citrulline By similarity
Binding site2061Citrulline By similarity
Binding site2831Citrulline By similarity

Sequences

Sequence LengthMass (Da)Tools
B4RQS8 [UniParc].

Last modified September 23, 2008. Version 1.
Checksum: 5599BEE27EB3BA46

FASTA44749,688
        10         20         30         40         50         60 
MNQNHTILQN LPVGQKVGIA FSGGLDTSAA LLWMKLKGAL PYAYTANLGQ PDEDDYNAIP 

        70         80         90        100        110        120 
KKAMEYGAEN ARLIDCRAQL AHEGIAAIQC GAFHVSTGGI AYFNTTPLGR AVTGTMLVSA 

       130        140        150        160        170        180 
MKEDDVNIWG DGSTYKGNDI ERFYRYGLLT NPALKIYKPW LDQQFIDELG GRHEMSEFLI 

       190        200        210        220        230        240 
ANGFNYKMSV EKAYSTDSNM LGATHEAKDL EFLNSGIKIV KPIMGVAFWD ENVEIEPEEV 

       250        260        270        280        290        300 
SVRFEEGVPV ALNGKEYADP VELFLEANRI GGRHGLGMSD QIENRIIEAK SRGIYEAPGM 

       310        320        330        340        350        360 
ALFHIAYERL VTGIHNEDTI EQYRINGLRL GRLLYQGRWF DSQALMLRET AQRWVAKAVT 

       370        380        390        400        410        420 
GEVTLELRRG NDYSILNTES PNLTYQPERL SMEKVEGAAF TPLDRIGQLT MRNLDITDTR 

       430        440 
AKLGIYSQSG LLSLGEGSVL PQLGNKQ 

« Hide

References

[1]"Complete genome sequence of Neisseria gonorrhoeae NCCP11945."
Chung G.T., Yoo J.S., Oh H.B., Lee Y.S., Cha S.H., Kim S.J., Yoo C.K.
J. Bacteriol. 190:6035-6036(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: NCCP11945.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP001050 Genomic DNA. Translation: ACF30888.1.
RefSeqYP_002002909.1. NC_011035.1.

3D structure databases

ProteinModelPortalB4RQS8.
SMRB4RQS8. Positions 6-445.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING521006.NGK_2284.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaACF30888; ACF30888; NGK_2284.
GeneID6447033.
KEGGngk:NGK_2284.
PATRIC20343235. VBINeiGon87511_2461.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0137.
HOGENOMHOG000230094.
KOK01940.
OMAMRNLDIA.
OrthoDBEOG6K9QCV.
ProtClustDBPRK05370.

Enzyme and pathway databases

BioCycNGON521006:GJ73-2336-MONOMER.
UniPathwayUPA00068; UER00113.

Family and domain databases

Gene3D1.10.287.400. 1 hit.
3.40.50.620. 1 hit.
3.90.1260.10. 1 hit.
HAMAPMF_00581. Arg_succ_synth_type2.
InterProIPR023437. Arg_succ_synth_type2_subfam.
IPR001518. Arginosuc_synth.
IPR018223. Arginosuc_synth_CS.
IPR024074. AS_cat/multimer_dom_body.
IPR024073. AS_multimer_C_tail.
IPR014729. Rossmann-like_a/b/a_fold.
[Graphical view]
PfamPF00764. Arginosuc_synth. 1 hit.
[Graphical view]
TIGRFAMsTIGR00032. argG. 1 hit.
PROSITEPS00564. ARGININOSUCCIN_SYN_1. 1 hit.
PS00565. ARGININOSUCCIN_SYN_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameASSY_NEIG2
AccessionPrimary (citable) accession number: B4RQS8
Entry history
Integrated into UniProtKB/Swiss-Prot: April 14, 2009
Last sequence update: September 23, 2008
Last modified: February 19, 2014
This is version 40 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways