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Reviewed, UniProtKB/Swiss-Prot Q2T1W2 (ASSY_BURTA)

Last modified June 16, 2009. Version 22. 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: BTH_I0279
OrganismBurkholderia thailandensis (strain E264 / ATCC 700388 / DSM 13276 / CIP 106301) [Complete proteome] [HAMAP]
Taxonomic identifier271848 [NCBI]
Taxonomic lineageBacteria › Proteobacteria › Betaproteobacteria › Burkholderiales › Burkholderiaceae › Burkholderia › pseudomallei group

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Protein attributes

Sequence length446 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_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.

Subcellular location

Cytoplasm Probable.

Sequence similarities

Belongs to the argininosuccinate synthase family. Type 2 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 – 446446Argininosuccinate synthase HAMAP MF_00581
PRO_1000025418

Regions

Nucleotide binding17 – 259ATP By similarity

Sites

Binding site431ATP 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

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Sequences

Sequence LengthMass (Da)Tools
Q2T1W2-1 [UniParc].

Last modified January 24, 2006. Version 1.
Checksum: DB3CB1F6F54C217D

FASTA44649,724
        10         20         30         40         50         60 
MTTILENLPA GQKVGIAFSG GLDTSAALHW MRIKGAVPYA YTANLGQPDE DDYDAIPKRA 

        70         80         90        100        110        120 
IQYGAEGARL IDCRAQLVAE GIAALQCGAF HISTAGVTYF NTTPIGRAVT GTMLVAAMKE 

       130        140        150        160        170        180 
DGVNIWGDGS TYKGNDIERF YRYGLLVNPD LKIYKPWLDQ QFIDELGGRA EMSEFMRQAG 

       190        200        210        220        230        240 
FEYKMSAEKA YSTDSNLLGA THEAKDLESL ESGIKIVNPI MGVAFWRDDV KIDKEAVTVR 

       250        260        270        280        290        300 
FEEGRPVALN GVEYKDAVEL LLEANRIGGR HGLGMSDQIE NRIIEAKSRG IYEAPGLALL 

       310        320        330        340        350        360 
YIAYERLVTG IHNEDTIEQY RENGRRLGRL LYQGRWFDPQ AIMLRETAQR WVARAVTGEV 

       370        380        390        400        410        420 
TVELRRGNDY SILATRSPNL TYQPERLSME KVQSTFSPRD RIGQLTMRNL DITDTRDKLR 

       430        440 
IYSEVGLLTP GESSALPKLK EDESGN

« Hide

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Cross-references

Sequence databases

CP000086 Genomic DNA. Translation: ABC37394.1.
RefSeqYP_440837.1.

3D structure databases

SMRQ2T1W2. Positions 2-444.
ModBaseSearch...

Genome annotation databases

GeneID3848636.
GenomeReviewsGene locus BTH_I0279 in contig CP000086_GR.
KEGGbte:BTH_I0279.
TIGRBTH_I0279.

Phylogenomic databases

HOGENOMQ2T1W2.
OMAQ2T1W2. GGRKEMS.

Enzyme and pathway databases

BioCycBTHA271848:BTH_I0279-MON.

Family and domain databases

HAMAPMF_00581.
[Tree]
InterProIPR001518. Arginosuc_synth.
IPR018223. Arginosuc_synth_CS.
[Graphical view]
PANTHERPTHR11587. Arginosuc_synth. 1 hit.
PfamPF00764. Arginosuc_synth. 2 hits.
[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_BURTA
AccessionPrimary (citable) accession number: Q2T1W2
Entry history
Integrated into UniProtKB/Swiss-Prot: January 15, 2008
Last sequence update: January 24, 2006
Last modified: June 16, 2009
This is version 22 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