Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

A6TL10 (ASSY_ALKMQ) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 44. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Argininosuccinate synthase

EC=6.3.4.5
Alternative name(s):
Citrulline--aspartate ligase
Gene names
Name:argG
Ordered Locus Names:Amet_0653
OrganismAlkaliphilus metalliredigens (strain QYMF) [Complete proteome] [HAMAP]
Taxonomic identifier293826 [NCBI]
Taxonomic lineageBacteriaFirmicutesClostridiaClostridialesClostridiaceaeAlkaliphilus

Protein attributes

Sequence length414 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

Pathway

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

Subunit structure

Homotetramer By similarity. HAMAP-Rule MF_00005

Subcellular location

Cytoplasm By similarity HAMAP-Rule MF_00005.

Sequence similarities

Belongs to the argininosuccinate synthase family. Type 1 subfamily.

Ontologies

Keywords
   Biological processAmino-acid biosynthesis
Arginine biosynthesis
   Cellular componentCytoplasm
   LigandATP-binding
Nucleotide-binding
   Molecular functionLigase
   Technical termComplete proteome
Gene Ontology (GO)
   Biological_processarginine biosynthetic process

Inferred from electronic annotation. Source: UniProtKB-HAMAP

   Cellular_componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionATP binding

Inferred from electronic annotation. Source: UniProtKB-HAMAP

argininosuccinate synthase activity

Inferred from electronic annotation. Source: UniProtKB-HAMAP

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 414414Argininosuccinate synthase HAMAP-Rule MF_00005
PRO_0000321299

Regions

Nucleotide binding12 – 209ATP By similarity

Sites

Binding site901Citrulline By similarity
Binding site951Citrulline By similarity
Binding site1201ATP; via amide nitrogen By similarity
Binding site1221Aspartate By similarity
Binding site1261Aspartate By similarity
Binding site1261Citrulline By similarity
Binding site1271Aspartate By similarity
Binding site1301Citrulline By similarity
Binding site1791Citrulline By similarity
Binding site1881Citrulline By similarity
Binding site2641Citrulline By similarity
Binding site2761Citrulline By similarity

Sequences

Sequence LengthMass (Da)Tools
A6TL10 [UniParc].

Last modified August 21, 2007. Version 1.
Checksum: 47FCF9714C88AAA9

FASTA41445,983
        10         20         30         40         50         60 
METKNKKKVV LAYSGGLDTS VILKWLEETY GYEVIAACVN VGQTEDFAAI KKKALATGAS 

        70         80         90        100        110        120 
KAYIVDVTEE FITDYIFPTL KAGAVYEDDY LLGTSFARPL ISKKLVEIAE KEGAVAIAHG 

       130        140        150        160        170        180 
ATGKGNDQVR FEATIKALNP NLKIIAPWRT WDLKSREDCI DYAVQHGIPI PVTKKDIYSR 

       190        200        210        220        230        240 
DENIWHISHE GGNLENPWNE HDDTIYKLSV SPEKSPDTPT YVELEFYKGI PVAVDGVKYE 

       250        260        270        280        290        300 
PIDMLTTLNK LGGAHGVGII DIVENRLVGM KSRGVYETPG GTLLFAAHKA LEKLTLDRDT 

       310        320        330        340        350        360 
TSFKKGISVK YAQLVYDGLW HTPLKDALDQ FVNSTQEFVT GQVKLKLYKG NCTAVASASP 

       370        380        390        400        410 
FSLYNEDFVT FGEDHVYNQQ DAEGFINLFA LPLTIRALML EEKLQGEAKE KKII 

« Hide

References

[1]"Complete sequence of Alkaliphilus metalliredigens QYMF."
Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S., Chertkov O., Brettin T., Bruce D., Han C., Schmutz J., Larimer F., Land M. expand/collapse author list , Hauser L., Kyrpides N., Mikhailova N., Ye Q., Zhou J., Fields M., Richardson P.
Submitted (JUN-2007) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: QYMF.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000724 Genomic DNA. Translation: ABR46878.1.
RefSeqYP_001318537.1. NC_009633.1.

3D structure databases

ProteinModelPortalA6TL10.
SMRA6TL10. Positions 8-399.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING293826.Amet_0653.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABR46878; ABR46878; Amet_0653.
GeneID5310696.
KEGGamt:Amet_0653.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0137.
HOGENOMHOG000230093.
KOK01940.
OMAAPPEEAY.
OrthoDBEOG6K9QCV.

Enzyme and pathway databases

BioCycAMET293826:GI5P-670-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 nameASSY_ALKMQ
AccessionPrimary (citable) accession number: A6TL10
Entry history
Integrated into UniProtKB/Swiss-Prot: February 26, 2008
Last sequence update: August 21, 2007
Last modified: May 14, 2014
This is version 44 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways