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P59607 (ASSY_BRAJA) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 64. 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:bll0522
OrganismBradyrhizobium japonicum
Taxonomic identifier375 [NCBI]
Taxonomic lineageBacteria › Proteobacteria › Alphaproteobacteria › Rhizobiales › Bradyrhizobiaceae › Bradyrhizobium

Protein attributes

Sequence length445 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_00581

Pathway

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

Subunit structure

Homotetramer By similarity. HAMAP MF_00581

Subcellular location

Cytoplasm Probable HAMAP 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
Reference 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

protein homodimerization activity

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 445445Argininosuccinate synthase HAMAP MF_00581
PRO_0000148693

Regions

Nucleotide binding17 – 259ATP By similarity

Sites

Binding site431ATP; via amide nitrogen and carbonyl oxygen By similarity
Binding site991Citrulline By similarity
Binding site1291ATP; via amide nitrogen By similarity
Binding site1311Aspartate By similarity
Binding site1311ATP By similarity
Binding site1351Aspartate By similarity
Binding site1351Citrulline By similarity
Binding site1361Aspartate By similarity
Binding site1361ATP By similarity
Binding site1391Citrulline By similarity
Binding site1921Citrulline By similarity
Binding site1941ATP By similarity
Binding site2011Citrulline By similarity
Binding site2031Citrulline By similarity
Binding site2801Citrulline By similarity

Sequences

Sequence LengthMass (Da)Tools
P59607 [UniParc].

Last modified April 23, 2003. Version 1.
Checksum: 7A5112563C7A8529

FASTA44549,231
        10         20         30         40         50         60 
MTTILKSLPK GEKVGIAFSG GLDTSAALLW MKQKGARCYA YTANLGQPDE ADYNEIPRKA 

        70         80         90        100        110        120 
QEFGAEKAVL VDCRTQLVHE GIAAIQSGAF HISTGGITYF NTTPLGRAVT GTMLVAAMKE 

       130        140        150        160        170        180 
DGVNIWGDGS TFKGNDIERF YRYGLLTNPS LRIYKPWLDQ QFIDELGGRA EMSAFMTAQG 

       190        200        210        220        230        240 
FAYKMSAEKA YSTDSNLLGA THEAKDLESL DSGIKIVNPI MGVPFWREDC NVKAEKVVVR 

       250        260        270        280        290        300 
FEEGQPTALN GQTFTDPVAL FLEANAIGGR HGLGMSDQIE NRIIEAKSRG IYEAPGMALL 

       310        320        330        340        350        360 
HIAYERLVTG IHNEDTIEQY RISGMRLGRL LYQGRWFDSQ ALMLRETAQR WVARAVTGEV 

       370        380        390        400        410        420 
TLELRRGNDY SILNTESPNL TYAPERLSME KVEDAAFTPA DRIGQLTMRN LDIADTRTKL 

       430        440 
KLYTDTGLLS GSEGSQIFRL ENDKG

« Hide

References

[1]"Complete genomic sequence of nitrogen-fixing symbiotic bacterium Bradyrhizobium japonicum USDA110."
Kaneko T., Nakamura Y., Sato S., Minamisawa K., Uchiumi T., Sasamoto S., Watanabe A., Idesawa K., Iriguchi M., Kawashima K., Kohara M., Matsumoto M., Shimpo S., Tsuruoka H., Wada T., Yamada M., Tabata S.
DNA Res. 9:189-197(2002) [PubMed: 12597275] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: USDA 110.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		BA000040 Genomic DNA. Translation: BAC45787.1.
RefSeqNP_767162.1. NC_004463.1.

3D structure databases

ProteinModelPortalP59607.
SMRP59607. Positions 2-442.
ModBaseSearch...

Proteomic databases

PRIDEP59607.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID1049678.
GenomeReviewsGene locus bll0522 in contig BA000040_GR.
KEGGbja:bll0522.
NMPDRfig|224911.1.peg.522.
PATRIC21184521. VBIBraJap65052_0538.

Phylogenomic databases

HOGENOMHBG289560.
OMAGGRKEMS.
PhylomeDBP59607.
ProtClustDBPRK05370.

Enzyme and pathway databases

BioCycBJAP224911:BLL0522-MONOMER.

Family and domain databases

HAMAPMF_00581. Arg_succ_synth_type2.
[Tree]
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]
Gene3DG3DSA:1.10.287.400. G3DSA:1.10.287.400. 1 hit.
G3DSA: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_BRAJA
AccessionPrimary (citable) accession number: P59607
Entry history
Integrated into UniProtKB/Swiss-Prot: April 23, 2003
Last sequence update: April 23, 2003
Last modified: January 25, 2012
This is version 64 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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