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Q3MBE6 (ASSY_ANAVT) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 43. 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:Ava_2068
OrganismAnabaena variabilis (strain ATCC 29413 / PCC 7937) [Complete proteome] [HAMAP]
Taxonomic identifier240292 [NCBI]
Taxonomic lineageBacteria › Cyanobacteria › Nostocales › Nostocaceae › Anabaena

Protein attributes

Sequence length400 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 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. HAMAP MF_00005

Subcellular location

Cytoplasm By similarity HAMAP 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: UniProtKB-KW

   Cellular componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular functionATP binding

Inferred from electronic annotation. Source: UniProtKB-KW

argininosuccinate synthase activity

Inferred from electronic annotation. Source: EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 400400Argininosuccinate synthase HAMAP MF_00005
PRO_0000263906

Regions

Nucleotide binding10 – 189ATP By similarity

Sites

Binding site381ATP; via amide nitrogen and carbonyl oxygen By similarity
Binding site891Citrulline By similarity
Binding site1191ATP; via amide nitrogen By similarity
Binding site1211Aspartate By similarity
Binding site1251Aspartate By similarity
Binding site1251Citrulline By similarity
Binding site1261Aspartate By similarity
Binding site1291Citrulline By similarity
Binding site1771Citrulline By similarity
Binding site1861Citrulline By similarity
Binding site2621Citrulline By similarity
Binding site2741Citrulline By similarity

Sequences

Sequence LengthMass (Da)Tools
Q3MBE6 [UniParc].

Last modified October 25, 2005. Version 1.
Checksum: 720C4C6C608EF417

FASTA40043,959
        10         20         30         40         50         60 
MGRAKKVVLA YSGGVDTSVC IPYLKQEWGV EEVITLAADL GQGDELEPIR EKALKSGASE 

        70         80         90        100        110        120 
SLVADVKESF IKDYAFPAIQ ANALYENRYP LGTALARPLI AKILVEAAEK YGADAIAHGC 

       130        140        150        160        170        180 
TGKGNDQVRF DVSCTALNPK LKILAPAREW GMSREATIAY GEKFGIPSPV KKSSPYSIDK 

       190        200        210        220        230        240 
NLLGRSIEAG ALEDPKFEPP EEIYEMTKAI ADTPNEPEYI EIGFTQGLPT TINGTPKDPV 

       250        260        270        280        290        300 
ALIQELNQLV GSHGVGRIDM IENRLVGIKS REIYESPAML VLIQAHRDLE SLTLTADVSH 

       310        320        330        340        350        360 
YKRGIEETYS QIVYNGLWYS PLKAALDAFI QKTQERVSGI VRVKLFKGNA TIVGRWSDSS 

       370        380        390        400 
LYTPDLATYG AEDQFDHKAA EGFIYVWGLP TRIWAQQDRG

« Hide

References

[1]"Complete sequence of Anabaena variabilis ATCC 29413."
Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T., Hammon N., Israni S., Pitluck S., Saunders E.H., Schmutz J., Larimer F., Land M., Kyrpides N., Mavrommatis K., Richardson P.
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 29413 / PCC 7937.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		CP000117 Genomic DNA. Translation: ABA21690.1.
RefSeqYP_322585.1. NC_007413.1.

3D structure databases

HSSPHSSP built from PDB template 1VL2 based on UniProtKB Q9X2A1.
ProteinModelPortalQ3MBE6.
ModBaseSearch...

Protein-protein interaction databases

STRINGQ3MBE6.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID3680541.
GenomeReviewsGene locus Ava_2068 in contig CP000117_GR.
KEGGava:Ava_2068.
NMPDRfig|240292.3.peg.1347.
PATRIC35424873. VBIAnaVar43351_2991.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0137.
HOGENOMHBG335267.
OMALATYDTG.
PhylomeDBQ3MBE6.
ProtClustDBPRK00509.

Enzyme and pathway databases

BioCycAVAR240292:AVA_2068-MONOMER.

Family and domain databases

HAMAPMF_00005. Arg_succ_synth_type1.
[Tree]
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]
Gene3DG3DSA:3.90.1260.10. G3DSA:3.90.1260.10. 1 hit.
G3DSA:3.40.50.620. Rossmann-like_a/b/a_fold. 1 hit.
KOK01940.
PANTHERPTHR11587. Arginosuc_synth. 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_ANAVT
AccessionPrimary (citable) accession number: Q3MBE6
Entry history
Integrated into UniProtKB/Swiss-Prot: December 12, 2006
Last sequence update: October 25, 2005
Last modified: January 25, 2012
This is version 43 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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