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Protein

Argininosuccinate synthase

Gene

argG

Organism
Magnetospirillum magneticum (strain AMB-1 / ATCC 700264)
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. Ornithine carbamoyltransferase (argF)
  2. Argininosuccinate synthase (argG)
  3. 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 sitei38 – 381ATP; via amide nitrogen and carbonyl oxygenUniRule annotation
Binding sitei91 – 911CitrullineUniRule annotation
Binding sitei96 – 961CitrullineUniRule annotation
Binding sitei121 – 1211ATP; via amide nitrogenUniRule annotation
Binding sitei123 – 1231AspartateUniRule annotation
Binding sitei127 – 1271AspartateUniRule annotation
Binding sitei127 – 1271CitrullineUniRule annotation
Binding sitei128 – 1281AspartateUniRule annotation
Binding sitei131 – 1311CitrullineUniRule annotation
Binding sitei182 – 1821CitrullineUniRule annotation
Binding sitei191 – 1911CitrullineUniRule annotation
Binding sitei267 – 2671CitrullineUniRule annotation
Binding sitei279 – 2791CitrullineUniRule annotation

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi11 – 199ATPUniRule 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

BioCyciMMAG342108:GJNU-1140-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:amb1125
OrganismiMagnetospirillum magneticum (strain AMB-1 / ATCC 700264)
Taxonomic identifieri342108 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaAlphaproteobacteriaRhodospirillalesRhodospirillaceaeMagnetospirillum
ProteomesiUP000007058 Componenti: Chromosome

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 – 404404Argininosuccinate synthasePRO_0000263936Add
BLAST

Interactioni

Subunit structurei

Homotetramer.UniRule annotation

Protein-protein interaction databases

STRINGi342108.amb1125.

Structurei

3D structure databases

ProteinModelPortaliQ2W896.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the argininosuccinate synthase family. Type 1 subfamily.UniRule annotation

Phylogenomic databases

eggNOGiCOG0137.
HOGENOMiHOG000230093.
KOiK01940.
OMAiIYNGYWW.
OrthoDBiEOG6K9QCV.

Family and domain databases

Gene3Di3.40.50.620. 1 hit.
3.90.1260.10. 1 hit.
HAMAPiMF_00005. Arg_succ_synth_type1.
InterProiIPR001518. 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]
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.

Q2W896-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MKGEVKKVVL AYSGGLDTSI ILRWLQDQYQ CEVVTFTADL GQGEELEPAR
60 70 80 90 100
AKARLMGIKE ENIFIDDLRE EFVRDFVFPM FRANALYEGV YLLGTSIARP
110 120 130 140 150
LISKRQIEIA NMVGADAVSH GATGKGNDQV RFEMGYYALK PDIKVIAPWR
160 170 180 190 200
LWDLTSRTKL LDFAEKHQIP IAKDKRGEAP YSTDANLLHI SYEGKALEDP
210 220 230 240 250
WVEPFEDMYT RSVAPENAPD KPTYIEIEFE KGDAVAIDGV RLSPAALLTK
260 270 280 290 300
LNELGGANGI GRLDLVENRF VGMKSRGVYE TPGGSVLIVA HRAMESLTLD
310 320 330 340 350
RGESHLKDEL MPRYAELIYN GFWFAPERIA IQTMIDKVSE NVSGTVRLKL
360 370 380 390 400
FKGVASVVGR KSPKSLYRMD YVTFEEDSVY DQRDAQGFIK LNALRMRLAK

MARG
Length:404
Mass (Da):45,417
Last modified:January 10, 2006 - v1
Checksum:i96B9B801F752D365
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AP007255 Genomic DNA. Translation: BAE49929.1.
RefSeqiWP_011383538.1. NC_007626.1.

Genome annotation databases

EnsemblBacteriaiBAE49929; BAE49929; amb1125.
KEGGimag:amb1125.
PATRICi22436525. VBIMagMag129836_1119.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AP007255 Genomic DNA. Translation: BAE49929.1.
RefSeqiWP_011383538.1. NC_007626.1.

3D structure databases

ProteinModelPortaliQ2W896.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi342108.amb1125.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiBAE49929; BAE49929; amb1125.
KEGGimag:amb1125.
PATRICi22436525. VBIMagMag129836_1119.

Phylogenomic databases

eggNOGiCOG0137.
HOGENOMiHOG000230093.
KOiK01940.
OMAiIYNGYWW.
OrthoDBiEOG6K9QCV.

Enzyme and pathway databases

UniPathwayiUPA00068; UER00113.
BioCyciMMAG342108:GJNU-1140-MONOMER.

Family and domain databases

Gene3Di3.40.50.620. 1 hit.
3.90.1260.10. 1 hit.
HAMAPiMF_00005. Arg_succ_synth_type1.
InterProiIPR001518. 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]
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 genome sequence of the facultative anaerobic magnetotactic bacterium Magnetospirillum sp. strain AMB-1."
    Matsunaga T., Okamura Y., Fukuda Y., Wahyudi A.T., Murase Y., Takeyama H.
    DNA Res. 12:157-166(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: AMB-1 / ATCC 700264.

Entry informationi

Entry nameiASSY_MAGSA
AccessioniPrimary (citable) accession number: Q2W896
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 12, 2006
Last sequence update: January 10, 2006
Last modified: July 22, 2015
This is version 67 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, Reference 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.