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C4L2P2 (C4L2P2_EXISA) Unreviewed, UniProtKB/TrEMBL

Last modified June 11, 2014. Version 37. Feed History...

Clusters with 100%, 90%, 50% identity | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry infoCustomize order

Names and origin

Protein namesRecommended name:
Argininosuccinate synthase HAMAP-Rule MF_00005

EC=6.3.4.5 HAMAP-Rule MF_00005
Alternative name(s):
Citrulline--aspartate ligase HAMAP-Rule MF_00005
Gene names
Name:argG HAMAP-Rule MF_00005
Ordered Locus Names:EAT1b_0368 EMBL ACQ69300.1
OrganismExiguobacterium sp. (strain ATCC BAA-1283 / AT1b) [Complete proteome] [HAMAP] EMBL ACQ69300.1
Taxonomic identifier360911 [NCBI]
Taxonomic lineageBacteriaFirmicutesBacilliBacillalesBacillales Family XII. Incertae SedisExiguobacterium

Protein attributes

Sequence length403 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Catalytic activity

ATP + L-citrulline + L-aspartate = AMP + diphosphate + N(omega)-(L-arginino)succinate. HAMAP-Rule MF_00005 SAAS SAAS001518

Pathway

Amino-acid biosynthesis; L-arginine biosynthesis; L-arginine from L-ornithine and carbamoyl phosphate: step 2/3. HAMAP-Rule MF_00005 SAAS SAAS001518

Subunit structure

Homotetramer By similarity. HAMAP-Rule MF_00005 SAAS SAAS001518

Subcellular location

Cytoplasm By similarity HAMAP-Rule MF_00005 SAAS SAAS001518.

Sequence similarities

Belongs to the argininosuccinate synthase family. Type 1 subfamily. HAMAP-Rule MF_00005

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Regions

Nucleotide binding8 – 169ATP By similarity HAMAP-Rule MF_00005

Sites

Binding site851Citrulline By similarity HAMAP-Rule MF_00005
Binding site1151ATP; via amide nitrogen By similarity HAMAP-Rule MF_00005
Binding site1171Aspartate By similarity HAMAP-Rule MF_00005
Binding site1211Aspartate By similarity HAMAP-Rule MF_00005
Binding site1211Citrulline By similarity HAMAP-Rule MF_00005
Binding site1221Aspartate By similarity HAMAP-Rule MF_00005
Binding site1251Citrulline By similarity HAMAP-Rule MF_00005
Binding site1731Citrulline By similarity HAMAP-Rule MF_00005
Binding site2581Citrulline By similarity HAMAP-Rule MF_00005
Binding site2701Citrulline By similarity HAMAP-Rule MF_00005

Sequences

Sequence LengthMass (Da)Tools
C4L2P2 [UniParc].

Last modified July 7, 2009. Version 1.
Checksum: 81DE9FF1AD22E53B

FASTA40344,369
        10         20         30         40         50         60 
MKQKLVLAYS GGLDTSVAIK WLDEQGYDVI AVCLNVGEGK DLEKIQQKAM KVGAKKSIVI 

        70         80         90        100        110        120 
DAVDEFVNEF ARYSMQAHTL YEGIYPLVSA LSRPLISKKL VEVAQAEGAV AVAHGCTGKG 

       130        140        150        160        170        180 
NDQVRFEVSI HALDPSLEIV APVREWKWSR EEEIAYAAKH QIPIPIVQEE PFSIDQNIWG 

       190        200        210        220        230        240 
RAIECGILED PWAAPPASAY ELTAALEDTP HEPTYLEIEF KSGVPVAIDG KSQSFTDILK 

       250        260        270        280        290        300 
ELNIVAGAHG VGKIDHIENR VVGIKSREVY EAPGAMTLIT AHKALEALTL VREVAHFKPI 

       310        320        330        340        350        360 
VEQKLTETIY NGLWYSQLTK ALLAFIDETQ ATVTGTVRMK LYKGQAIVDG RKSPISLYDE 

       370        380        390        400 
ELATYTSADT FDQQAAVGFI KLWGLPTKVQ SEVLMEKGAF VNE 

« Hide

References

[1]"Complete sequence of Exiguobacterium sp. AT1b."
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., Saunders E., Brettin T., Detter J.C., Han C., Larimer F., Land M., Hauser L., Kyrpides N., Ovchinnikova G. expand/collapse author list , Ramaley R.F., Rodrigues D.F., Vishnivetskaya T.A., Kathariou S., Tiedje J.M., Richardson P.
Submitted (MAY-2009) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC BAA-1283 / AT1b.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP001615 Genomic DNA. Translation: ACQ69300.1.
RefSeqYP_002884745.1. NC_012673.1.

3D structure databases

ProteinModelPortalC4L2P2.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING360911.EAT1b_0368.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaACQ69300; ACQ69300; EAT1b_0368.
GeneID7868483.
KEGGeat:EAT1b_0368.
PATRIC21875830. VBIExiSp39724_0354.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0137.
HOGENOMHOG000230093.
KOK01940.
OMAAPPEEAY.
OrthoDBEOG6K9QCV.

Enzyme and pathway databases

BioCycESP360911:GI4R-370-MONOMER.
UniPathwayUPA00068; UER00113.

Family and domain databases

Gene3D3.40.50.620. 1 hit.
3.90.1260.10. 1 hit.
HAMAPMF_00005. Arg_succ_synth_type1.
InterProIPR001518. 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]
PfamPF00764. Arginosuc_synth. 1 hit.
[Graphical view]
TIGRFAMsTIGR00032. argG. 1 hit.
PROSITEPS00564. ARGININOSUCCIN_SYN_1. 1 hit.
PS00565. ARGININOSUCCIN_SYN_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameC4L2P2_EXISA
AccessionPrimary (citable) accession number: C4L2P2
Entry history
Integrated into UniProtKB/TrEMBL: July 7, 2009
Last sequence update: July 7, 2009
Last modified: June 11, 2014
This is version 37 of the entry and version 1 of the sequence. [Complete history]
Entry statusUnreviewed (UniProtKB/TrEMBL)