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B1LFS3

- ASSY_ECOSM

UniProt

B1LFS3 - ASSY_ECOSM

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Protein

Argininosuccinate synthase

Gene

argG

Organism
Escherichia coli (strain SMS-3-5 / SECEC)
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

BioCyciECOL439855:GHHB-3465-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:EcSMS35_3468
OrganismiEscherichia coli (strain SMS-3-5 / SECEC)
Taxonomic identifieri439855 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
ProteomesiUP000007011: 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_1000129752Add
BLAST

Proteomic databases

PRIDEiB1LFS3.

Interactioni

Subunit structurei

Homotetramer.UniRule annotation

Protein-protein interaction databases

STRINGi439855.EcSMS35_3468.

Structurei

3D structure databases

ProteinModelPortaliB1LFS3.
SMRiB1LFS3. 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.

B1LFS3-1 [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
GKTFSDDVEM 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 SAASGVPQVE NLENKGQ
Length:447
Mass (Da):49,898
Last modified:April 29, 2008 - v1
Checksum:iD5E7E51BD06E1813
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000970 Genomic DNA. Translation: ACB17267.1.
RefSeqiYP_001745445.1. NC_010498.1.

Genome annotation databases

EnsemblBacteriaiACB17267; ACB17267; EcSMS35_3468.
GeneIDi6143631.
KEGGiecm:EcSMS35_3468.
PATRICi18435861. VBIEscCol6161_3622.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000970 Genomic DNA. Translation: ACB17267.1 .
RefSeqi YP_001745445.1. NC_010498.1.

3D structure databases

ProteinModelPortali B1LFS3.
SMRi B1LFS3. Positions 2-445.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 439855.EcSMS35_3468.

Proteomic databases

PRIDEi B1LFS3.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai ACB17267 ; ACB17267 ; EcSMS35_3468 .
GeneIDi 6143631.
KEGGi ecm:EcSMS35_3468.
PATRICi 18435861. VBIEscCol6161_3622.

Phylogenomic databases

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

Enzyme and pathway databases

UniPathwayi UPA00068 ; UER00113 .
BioCyci ECOL439855:GHHB-3465-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. "Insights into the environmental resistance gene pool from the genome sequence of the multidrug-resistant environmental isolate Escherichia coli SMS-3-5."
    Fricke W.F., Wright M.S., Lindell A.H., Harkins D.M., Baker-Austin C., Ravel J., Stepanauskas R.
    J. Bacteriol. 190:6779-6794(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: SMS-3-5 / SECEC.

Entry informationi

Entry nameiASSY_ECOSM
AccessioniPrimary (citable) accession number: B1LFS3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 14, 2009
Last sequence update: April 29, 2008
Last modified: October 29, 2014
This is version 48 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