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B2U204

- ASSY_SHIB3

UniProt

B2U204 - ASSY_SHIB3

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Protein

Argininosuccinate synthase

Gene

argG

Organism
Shigella boydii serotype 18 (strain CDC 3083-94 / BS512)
Status
Reviewed - 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

Pathwayi

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

  1. argininosuccinate synthase activity Source: UniProtKB-HAMAP
  2. ATP binding Source: UniProtKB-HAMAP

GO - Biological processi

  1. arginine biosynthetic process Source: UniProtKB-HAMAP
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

BioCyciSBOY344609:GI0O-3599-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:SbBS512_E3599
OrganismiShigella boydii serotype 18 (strain CDC 3083-94 / BS512)
Taxonomic identifieri344609 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeShigella
ProteomesiUP000001030: Chromosome

Subcellular locationi

Cytoplasm UniRule annotation

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB-HAMAP
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 447447Argininosuccinate synthasePRO_1000129769Add
BLAST

Interactioni

Subunit structurei

Homotetramer.UniRule annotation

Protein-protein interaction databases

STRINGi344609.SbBS512_E3599.

Structurei

3D structure databases

ProteinModelPortaliB2U204.
SMRiB2U204. 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.
OMAiRQEMSEF.
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.

B2U204-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MTTILKHLPV GQRIGIAFSG GLDTSAALLW MRQKGAVPYA YTANLGQPDE
60 70 80 90 100
EDYDAIPRRA MEYGAENARL IDCRKQLVAE GIAAIQCGAF HNTTGGLTYF
110 120 130 140 150
NTTPLGRAVT GTMLVAAMKE DGVNIWGDGS TYKGNDIERF YRYGLLTNAE
160 170 180 190 200
LQIYKPWLDT DFIDELGGRH EMSEFMIACG FDYKMSVEKA YSTDSNMLGA
210 220 230 240 250
THEAKDLEYL NSSVKIVNPI MGVKFWDESV KIPAEEVTVR FEQGHPVALN
260 270 280 290 300
GKTFSNDVEM MLEANRIGGR HGLGMSDQIE NRIIEAKSRG IYEAPGMALL
310 320 330 340 350
HIAYERLLTG IHNEDTIEQY HAHGRQLGRL LYQGRWFDSQ ALMLRDSLQR
360 370 380 390 400
WVASQITGEV TLELRRGNDY SILNTVSENL TYKPERLTME KGDSVFSPDD
410 420 430 440
RIGQLTMRNL DITDTREKLF GYAKTGLLSS SATSGVPQVE NMENKGQ
Length:447
Mass (Da):49,945
Last modified:July 1, 2008 - v1
Checksum:i5901AFBF9C8FB6F6
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP001063 Genomic DNA. Translation: ACD09925.1.
RefSeqiYP_001881912.1. NC_010658.1.

Genome annotation databases

EnsemblBacteriaiACD09925; ACD09925; SbBS512_E3599.
GeneIDi6270007.
KEGGisbc:SbBS512_E3599.
PATRICi18674463. VBIShiBoy129590_3959.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP001063 Genomic DNA. Translation: ACD09925.1 .
RefSeqi YP_001881912.1. NC_010658.1.

3D structure databases

ProteinModelPortali B2U204.
SMRi B2U204. Positions 2-445.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 344609.SbBS512_E3599.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai ACD09925 ; ACD09925 ; SbBS512_E3599 .
GeneIDi 6270007.
KEGGi sbc:SbBS512_E3599.
PATRICi 18674463. VBIShiBoy129590_3959.

Phylogenomic databases

eggNOGi COG0137.
HOGENOMi HOG000230094.
KOi K01940.
OMAi RQEMSEF.
OrthoDBi EOG6K9QCV.

Enzyme and pathway databases

UniPathwayi UPA00068 ; UER00113 .
BioCyci SBOY344609:GI0O-3599-MONOMER.

Family and domain databases

Gene3Di 1.10.287.400. 1 hit.
3.40.50.620. 1 hit.
3.90.1260.10. 1 hit.
HAMAPi MF_00581. Arg_succ_synth_type2.
InterProi IPR023437. 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 ]
Pfami PF00764. Arginosuc_synth. 1 hit.
[Graphical view ]
TIGRFAMsi TIGR00032. argG. 1 hit.
PROSITEi PS00564. ARGININOSUCCIN_SYN_1. 1 hit.
PS00565. ARGININOSUCCIN_SYN_2. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

  1. "Complete sequence of Shigella boydii serotype 18 strain BS512."
    Rasko D.A., Rosovitz M., Maurelli A.T., Myers G., Seshadri R., Cer R., Jiang L., Ravel J., Sebastian Y.
    Submitted (MAY-2008) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: CDC 3083-94 / BS512.

Entry informationi

Entry nameiASSY_SHIB3
AccessioniPrimary (citable) accession number: B2U204
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 14, 2009
Last sequence update: July 1, 2008
Last modified: October 29, 2014
This is version 46 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