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Protein

Argininosuccinate synthase

Gene

argG

Organism
Burkholderia ambifaria (strain ATCC BAA-244 / AMMD) (Burkholderia cepacia (strain AMMD))
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Protein inferred from homologyi

Functioni

Catalytic activityi

ATP + L-citrulline + L-aspartate = AMP + diphosphate + N(omega)-(L-arginino)succinate.UniRule annotation

Pathway:iL-arginine biosynthesis

This protein is involved in step 2 of the subpathway that synthesizes L-arginine from L-ornithine and carbamoyl phosphate.UniRule annotation
Proteins known to be involved in the 3 steps of the subpathway in this organism are:
  1. no protein annotated in this organism
  2. Argininosuccinate synthase (argG)
  3. Argininosuccinate lyase (Bamb_6457), Argininosuccinate lyase (argH)
This subpathway is part of the pathway L-arginine biosynthesis, which is itself part of Amino-acid biosynthesis.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes L-arginine from L-ornithine and carbamoyl phosphate, the pathway L-arginine biosynthesis and in Amino-acid biosynthesis.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei43 – 431ATPUniRule annotation
Binding sitei99 – 991CitrullineUniRule annotation
Binding sitei129 – 1291ATP; via amide nitrogenUniRule annotation
Binding sitei131 – 1311AspartateUniRule annotation
Binding sitei131 – 1311ATPUniRule annotation
Binding sitei135 – 1351AspartateUniRule annotation
Binding sitei135 – 1351CitrullineUniRule annotation
Binding sitei136 – 1361AspartateUniRule annotation
Binding sitei136 – 1361ATPUniRule annotation
Binding sitei139 – 1391CitrullineUniRule annotation
Binding sitei192 – 1921CitrullineUniRule annotation
Binding sitei194 – 1941ATPUniRule annotation
Binding sitei201 – 2011CitrullineUniRule annotation
Binding sitei203 – 2031CitrullineUniRule annotation
Binding sitei280 – 2801CitrullineUniRule annotation

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi17 – 259ATPUniRule annotation

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Ligase

Keywords - Biological processi

Amino-acid biosynthesis, Arginine biosynthesis

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Enzyme and pathway databases

BioCyciBAMB339670:GH48-5530-MONOMER.
UniPathwayiUPA00068; UER00113.

Names & Taxonomyi

Protein namesi
Recommended name:
Argininosuccinate synthaseUniRule annotation (EC:6.3.4.5UniRule annotation)
Alternative name(s):
Citrulline--aspartate ligaseUniRule annotation
Gene namesi
Name:argGUniRule annotation
Ordered Locus Names:Bamb_5452
OrganismiBurkholderia ambifaria (strain ATCC BAA-244 / AMMD) (Burkholderia cepacia (strain AMMD))
Taxonomic identifieri339670 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaBetaproteobacteriaBurkholderialesBurkholderiaceaeBurkholderiaBurkholderia cepacia complex
ProteomesiUP000000662 Componenti: Chromosome 2

Subcellular locationi

  • Cytoplasm UniRule annotation

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 445445Argininosuccinate synthasePRO_1000129741Add
BLAST

Interactioni

Subunit structurei

Homotetramer.UniRule annotation

Protein-protein interaction databases

STRINGi339670.Bamb_5452.

Structurei

3D structure databases

ProteinModelPortaliQ0B4C4.
SMRiQ0B4C4. Positions 2-445.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the argininosuccinate synthase family. Type 2 subfamily.UniRule annotation

Phylogenomic databases

eggNOGiCOG0137.
HOGENOMiHOG000230094.
KOiK01940.
OMAiMRNLDIA.
OrthoDBiEOG6K9QCV.

Family and domain databases

Gene3Di1.10.287.400. 1 hit.
3.40.50.620. 1 hit.
3.90.1260.10. 1 hit.
HAMAPiMF_00581. Arg_succ_synth_type2.
InterProiIPR023437. 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]
PfamiPF00764. Arginosuc_synth. 1 hit.
[Graphical view]
TIGRFAMsiTIGR00032. argG. 1 hit.
PROSITEiPS00564. ARGININOSUCCIN_SYN_1. 1 hit.
PS00565. ARGININOSUCCIN_SYN_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q0B4C4-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSTILESLPT GQKVGIAFSG GLDTSAALHW MKLKGAVPYA YTANLGQPDE
60 70 80 90 100
DDYDAIPKRA IEYGAAGARL IDCRAQLVAE GIAALQSGAF HITTAGVTYF
110 120 130 140 150
NTTPIGRAVT GTMLVAAMKE DGVNIWGDGS TYKGNDIERF YRYGLLVNPD
160 170 180 190 200
LKIYKPWLDQ TFIDELGGRA EMSEFMNQAG FAYKMSAEKA YSTDSNLLGA
210 220 230 240 250
THEAKDLESL ESGIKIVNPI MGVAFWRDDV KIAAEEVTVR FEAGQPVALN
260 270 280 290 300
GVEYKDPVEL LLEANRIGGR HGLGMSDQIE NRIIEAKSRG IYEAPGLALL
310 320 330 340 350
YIAYERLVTG IHNEDTIEQY RENGRRLGRL LYQGRWFDPQ AIMLRETAQR
360 370 380 390 400
WVARAITGEV KIELRRGNDY SILSTKSPNL TYQPERLSME KVASTFSPRD
410 420 430 440
RIGQLTMRNL DITDTRDKLR VYSQVGLLTP GESSALPQIK GDSDK
Length:445
Mass (Da):49,238
Last modified:October 17, 2006 - v1
Checksum:i421324120E81576F
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000441 Genomic DNA. Translation: ABI90999.1.
RefSeqiWP_011660368.1. NZ_CP009799.1.

Genome annotation databases

EnsemblBacteriaiABI90999; ABI90999; Bamb_5452.
KEGGibam:Bamb_5452.
PATRICi19026895. VBIBurAmb61564_5697.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000441 Genomic DNA. Translation: ABI90999.1.
RefSeqiWP_011660368.1. NZ_CP009799.1.

3D structure databases

ProteinModelPortaliQ0B4C4.
SMRiQ0B4C4. Positions 2-445.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi339670.Bamb_5452.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiABI90999; ABI90999; Bamb_5452.
KEGGibam:Bamb_5452.
PATRICi19026895. VBIBurAmb61564_5697.

Phylogenomic databases

eggNOGiCOG0137.
HOGENOMiHOG000230094.
KOiK01940.
OMAiMRNLDIA.
OrthoDBiEOG6K9QCV.

Enzyme and pathway databases

UniPathwayiUPA00068; UER00113.
BioCyciBAMB339670:GH48-5530-MONOMER.

Family and domain databases

Gene3Di1.10.287.400. 1 hit.
3.40.50.620. 1 hit.
3.90.1260.10. 1 hit.
HAMAPiMF_00581. Arg_succ_synth_type2.
InterProiIPR023437. 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]
PfamiPF00764. Arginosuc_synth. 1 hit.
[Graphical view]
TIGRFAMsiTIGR00032. argG. 1 hit.
PROSITEiPS00564. ARGININOSUCCIN_SYN_1. 1 hit.
PS00565. ARGININOSUCCIN_SYN_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  1. "Complete sequence of chromosome 2 of Burkholderia cepacia AMMD."
    Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina del Rio T., Hammon N., Israni S., Pitluck S., Bruce D., Chain P., Malfatti S., Shin M., Vergez L., Schmutz J., Larimer F., Land M., Hauser L.
    , Kyrpides N., Kim E., Parke J., Coenye T., Konstantinidis K., Ramette A., Tiedje J., Richardson P.
    Submitted (AUG-2006) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC BAA-244 / AMMD.

Entry informationi

Entry nameiASSY_BURCM
AccessioniPrimary (citable) accession number: Q0B4C4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 14, 2009
Last sequence update: October 17, 2006
Last modified: July 22, 2015
This is version 64 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.