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Q5P0Z7 (ASSY_AROAE) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 62. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
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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:AZOSEA28920
ORF Names:ebA5097
OrganismAromatoleum aromaticum (strain EbN1) (Azoarcus sp. (strain EbN1)) [Complete proteome] [HAMAP]
Taxonomic identifier76114 [NCBI]
Taxonomic lineageBacteria › Proteobacteria › Betaproteobacteria › Rhodocyclales › Rhodocyclaceae › Aromatoleum ›

Protein attributes

Sequence length409 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_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 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: HAMAP

   Cellular_componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionATP binding

Inferred from electronic annotation. Source: HAMAP

argininosuccinate synthase activity

Inferred from electronic annotation. Source: HAMAP

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 409409Argininosuccinate synthase HAMAP-Rule MF_00005
PRO_0000148563

Regions

Nucleotide binding10 – 189ATP By similarity

Sites

Binding site371ATP; via amide nitrogen and carbonyl oxygen By similarity
Binding site901Citrulline By similarity
Binding site951Citrulline By similarity
Binding site1201ATP; via amide nitrogen By similarity
Binding site1221Aspartate By similarity
Binding site1261Aspartate By similarity
Binding site1261Citrulline By similarity
Binding site1271Aspartate By similarity
Binding site1301Citrulline By similarity
Binding site1821Citrulline By similarity
Binding site1911Citrulline By similarity
Binding site2671Citrulline By similarity
Binding site2791Citrulline By similarity

Sequences

Sequence LengthMass (Da)Tools
Q5P0Z7 [UniParc].

Last modified January 4, 2005. Version 1.
Checksum: 46DE77550B89E80F

FASTA40946,012
        10         20         30         40         50         60 
MSDVKKAVLA YSGGLDTSVI LKWLQDTYQC EVVTFTADLG QGEELEPARQ KALKFGIKPD 

        70         80         90        100        110        120 
NIFIDDLREE FVRDFVFPMF RCNTVYEGEY LLGTSIARPL IAKRQIEIAR ATGADAVSHG 

       130        140        150        160        170        180 
ATGKGNDQVR FELGYYALMP GVKVIAPWRE WDLLSREKLL AYAEKHGIPI EMKHKQGGSP 

       190        200        210        220        230        240 
YSMDANLLHI SFEGRHLENP AAEAEESMWR WTVSPEAAPD AAEYLDLEFE RGDLVAINGT 

       250        260        270        280        290        300 
RMKAHELLAK LNELGGKHGI GRLDLVENRY VGMKSRGCYE TPGGTILLRA HRAIESVTLD 

       310        320        330        340        350        360 
REVAHLKDDL MPRYASLIYN GYWWSPERRA LQALIDNTQE SVNGWVRVKL YKGNVIVTGR 

       370        380        390        400 
DSKTDSLFDP TIATFEDDQG AYNQKDAHGF IRLNALRMRI AANAQTKRG

« Hide

References

[1]"The genome sequence of an anaerobic aromatic-degrading denitrifying bacterium, strain EbN1."
Rabus R., Kube M., Heider J., Beck A., Heitmann K., Widdel F., Reinhardt R.
Arch. Microbiol. 183:27-36(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: EbN1.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		CR555306 Genomic DNA. Translation: CAI09017.1.
RefSeqYP_159918.1. NC_006513.1.

3D structure databases

ProteinModelPortalQ5P0Z7.
SMRQ5P0Z7. Positions 6-402.
ModBaseSearch...

Protein-protein interaction databases

STRING76114.ebA5097.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaCAI09017; CAI09017; ebA5097.
GeneID3181098.
KEGGeba:ebA5097.
PATRIC20971988. VBIAroAro98752_2922.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0137.
HOGENOMHOG000230093.
KOK01940.
OMAIYNGYWW.
ProtClustDBPRK00509.

Enzyme and pathway databases

BioCycAARO76114:GJTA-2933-MONOMER.
UniPathwayUPA00068; UER00113.

Family and domain databases

Gene3D3.40.50.620. 1 hit.
3.90.1260.10. 1 hit.
HAMAPMF_00005. Arg_succ_synth_type1.
InterProIPR001518. 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]
PANTHERPTHR11587. PTHR11587. 1 hit.
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_AROAE
AccessionPrimary (citable) accession number: Q5P0Z7
Entry history
Integrated into UniProtKB/Swiss-Prot: March 15, 2005
Last sequence update: January 4, 2005
Last modified: May 1, 2013
This is version 62 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

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