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Protein

Argininosuccinate synthase

Gene

argG

Organism
Prosthecochloris aestuarii (strain DSM 271 / SK 413)
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 (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 sitei87 – 871CitrullineUniRule annotation
Binding sitei117 – 1171ATP; via amide nitrogenUniRule annotation
Binding sitei119 – 1191AspartateUniRule annotation
Binding sitei123 – 1231AspartateUniRule annotation
Binding sitei123 – 1231CitrullineUniRule annotation
Binding sitei124 – 1241AspartateUniRule annotation
Binding sitei127 – 1271CitrullineUniRule annotation
Binding sitei176 – 1761CitrullineUniRule annotation
Binding sitei185 – 1851CitrullineUniRule annotation
Binding sitei261 – 2611CitrullineUniRule annotation
Binding sitei273 – 2731CitrullineUniRule annotation

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi9 – 179ATPUniRule 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

BioCyciPAES290512:GHUT-1108-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:Paes_1071
OrganismiProsthecochloris aestuarii (strain DSM 271 / SK 413)
Taxonomic identifieri290512 [NCBI]
Taxonomic lineageiBacteriaChlorobiChlorobiaChlorobialesChlorobiaceaeProsthecochloris
ProteomesiUP000002725 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 – 401401Argininosuccinate synthasePRO_1000089049Add
BLAST

Interactioni

Subunit structurei

Homotetramer.UniRule annotation

Protein-protein interaction databases

STRINGi290512.Paes_1071.

Structurei

3D structure databases

ProteinModelPortaliB4S7R9.
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.

B4S7R9-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSKEKIALAY SGGLDTSVMI KWLKDKYDAE IVAVTGNLGQ EKEVENLEEK
60 70 80 90 100
AIATGASSFA FLDLRKEFVE SCIWPALKAG ALYEDVYPLA TALGRPLIAK
110 120 130 140 150
ALVDIALENN CTMLAHGCTG KGNDQVRFEV TFASLAPQLA VLAPLREWEF
160 170 180 190 200
TSREAEIAYA MEHNIPVSAT KKSPYSIDEN IWGISIECGV LEDPMTPAPE
210 220 230 240 250
DAYQITTSPE KAPDKAAVID IEFEQGVPVA LDGKAMEGLD LIVELNKVGA
260 270 280 290 300
AHGVGRLDMV ENRVVGIKSR EIYEAPAATI LHFAHRELER LTLEKSVFQY
310 320 330 340 350
KKNVSQDYAN LIYNGTWFSP MREALDGFIE ATQKTVTGLV RVKLFKGSVT
360 370 380 390 400
LLGRTSPWSL YNEDLATYTE ADTFNHKAAE GFIHLYGLGL KTWSEVKANN

S
Length:401
Mass (Da):44,134
Last modified:September 23, 2008 - v1
Checksum:iB30FAA413DCC290B
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP001108 Genomic DNA. Translation: ACF46106.1.
RefSeqiWP_012505643.1. NC_011059.1.

Genome annotation databases

EnsemblBacteriaiACF46106; ACF46106; Paes_1071.
KEGGipaa:Paes_1071.
PATRICi23041906. VBIProAes37017_1129.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP001108 Genomic DNA. Translation: ACF46106.1.
RefSeqiWP_012505643.1. NC_011059.1.

3D structure databases

ProteinModelPortaliB4S7R9.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi290512.Paes_1071.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiACF46106; ACF46106; Paes_1071.
KEGGipaa:Paes_1071.
PATRICi23041906. VBIProAes37017_1129.

Phylogenomic databases

eggNOGiCOG0137.
HOGENOMiHOG000230093.
KOiK01940.
OMAiIYNGYWW.
OrthoDBiEOG6K9QCV.

Enzyme and pathway databases

UniPathwayiUPA00068; UER00113.
BioCyciPAES290512:GHUT-1108-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 sequence of chromosome of Prosthecochloris aestuarii DSM 271."
    US DOE Joint Genome Institute
    Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H., Bruce D., Goodwin L., Pitluck S., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N., Anderson I., Liu Z., Li T., Zhao F.
    , Overmann J., Bryant D.A., Richardson P.
    Submitted (JUN-2008) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: DSM 271 / SK 413.

Entry informationi

Entry nameiASSY_PROA2
AccessioniPrimary (citable) accession number: B4S7R9
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 24, 2009
Last sequence update: September 23, 2008
Last modified: July 22, 2015
This is version 50 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.