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Reviewed, UniProtKB/Swiss-Prot A1UUF5 (ASSY_BARBK)

Last modified November 3, 2009. Version 18. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

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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: BARBAKC583_1361
OrganismBartonella bacilliformis (strain ATCC 35685 / KC583) [Complete proteome] [HAMAP]
Taxonomic identifier360095 [NCBI]
Taxonomic lineageBacteria › Proteobacteria › Alphaproteobacteria › Rhizobiales › Bartonellaceae › Bartonella

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Protein attributes

Sequence length407 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
Protein existenceInferred from homology.

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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.

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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...

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Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 407407Argininosuccinate synthase HAMAP MF_00005
PRO_1000000383

Regions

Nucleotide binding13 – 219ATP By similarity

Sites

Binding site401ATP; via amide nitrogen and carbonyl oxygen By similarity
Binding site911Citrulline By similarity
Binding site961Citrulline By similarity
Binding site1211ATP; via amide nitrogen By similarity
Binding site1231Aspartate By similarity
Binding site1271Aspartate By similarity
Binding site1271Citrulline By similarity
Binding site1281Aspartate By similarity
Binding site1311Citrulline By similarity
Binding site1821Citrulline By similarity
Binding site1911Citrulline By similarity
Binding site2671Citrulline By similarity
Binding site2791Citrulline By similarity

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Sequences

Sequence LengthMass (Da)Tools
A1UUF5-1 [UniParc].

Last modified February 6, 2007. Version 1.
Checksum: 1B1F433D647340C0

FASTA40745,389
        10         20         30         40         50         60 
MNKWTDVKKV VLAYSGGLDT SIILKWLQSE LGAEVVTFTA DLGQGEELES ARRKAEIMGI 

        70         80         90        100        110        120 
KEIYIEDLRE EFVRDFVFPM FRANAVYEGV YLLGTSIARP LISKRLIEIA KETGADAIAH 

       130        140        150        160        170        180 
GATGKGNDQV RFELSAYALD PDIKIIAPWR DWTFKSRTDL IEFARVHQIP VEKDKEGEAP 

       190        200        210        220        230        240 
FSVDANLLHS SSEGKILENP AIPAPEYVHM RTLSPETAPD KATIITIGFK KGDAVSINGE 

       250        260        270        280        290        300 
MLSPATLLAQ LNNYGRDNGI GRLDLVENRF VGMKSRGIYE TPGGTILLTA HRAIESLTLD 

       310        320        330        340        350        360 
RGAAHLKDEL MPRYAELIYY GFWFSPERKM LQAAIDLSQE HVEGEVTLKL YKGNVIVEGR 

       370        380        390        400 
QSKKSLYFDK LVTFEDDQGA YDQKDAAGFI KLNALRLRTL AARSSVL

« Hide

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References

[1]Hendrix L., Mohamoud Y., Radune D., Shvartsbeyn A., Daugherty S., Dodson R., Durkin A.S., Harkins D., Huot H., Kothari S.P., Madupu R., Li J., Nelson W.C., Shrivastava S., Giglio M.G., Haft D., Selengut J., Fraser-Ligget C., Seshadri R.
Submitted (DEC-2006) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

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Cross-references

Sequence databases

CP000524 Genomic DNA. Translation: ABM45481.1.
RefSeqYP_989608.1.

3D structure databases

ModBaseSearch...

Protein-protein interaction databases

STRINGA1UUF5.

Genome annotation databases

GeneID4684191.
GenomeReviewsGene locus BARBAKC583_1361 in contig CP000524_GR.
KEGGbbk:BARBAKC583_1361.
NMPDRfig|360095.3.peg.1162.
TIGRBARBAKC583_1361.

Phylogenomic databases

OMAYVFPMFR.

Family and domain databases

HAMAPMF_00005.
[Tree]
InterProIPR001518. Arginosuc_synth.
IPR018223. Arginosuc_synth_CS.
IPR014729. Rossmann-like_a/b/a_fold.
[Graphical view]
Gene3DG3DSA:3.40.50.620. Rossmann-like_a/b/a_fold. 1 hit.
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...

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Entry information

Entry nameASSY_BARBK
AccessionPrimary (citable) accession number: A1UUF5
Entry history
Integrated into UniProtKB/Swiss-Prot: January 15, 2008
Last sequence update: February 6, 2007
Last modified: November 3, 2009
This is version 18 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)

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Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents