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A4XJN8 (ARGB_CALS8) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 47. 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:
Acetylglutamate kinase

EC=2.7.2.8
Alternative name(s):
N-acetyl-L-glutamate 5-phosphotransferase
NAG kinase
Short name=AGK
Gene names
Name:argB
Ordered Locus Names:Csac_1530
OrganismCaldicellulosiruptor saccharolyticus (strain ATCC 43494 / DSM 8903) [Complete proteome] [HAMAP]
Taxonomic identifier351627 [NCBI]
Taxonomic lineageBacteriaFirmicutesClostridiaThermoanaerobacteralesThermoanaerobacterales Family III. Incertae SedisCaldicellulosiruptor

Protein attributes

Sequence length293 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Catalytic activity

ATP + N-acetyl-L-glutamate = ADP + N-acetyl-L-glutamate 5-phosphate. HAMAP-Rule MF_00082

Pathway

Amino-acid biosynthesis; L-arginine biosynthesis; N(2)-acetyl-L-ornithine from L-glutamate: step 2/4. HAMAP-Rule MF_00082

Subcellular location

Cytoplasm By similarity HAMAP-Rule MF_00082.

Sequence similarities

Belongs to the acetylglutamate kinase family.

Ontologies

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

Inferred from electronic annotation. Source: UniProtKB-HAMAP

proline biosynthetic process

Inferred from electronic annotation. Source: InterPro

   Cellular_componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionATP binding

Inferred from electronic annotation. Source: UniProtKB-HAMAP

acetylglutamate kinase activity

Inferred from electronic annotation. Source: UniProtKB-HAMAP

glutamate 5-kinase activity

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 293293Acetylglutamate kinase HAMAP-Rule MF_00082
PRO_0000335616

Regions

Region68 – 692Substrate binding By similarity

Sites

Binding site901Substrate By similarity
Binding site1891Substrate By similarity
Site331Transition state stabilizer By similarity
Site2511Transition state stabilizer By similarity

Sequences

Sequence LengthMass (Da)Tools
A4XJN8 [UniParc].

Last modified May 29, 2007. Version 1.
Checksum: F862454708B87149

FASTA29332,014
        10         20         30         40         50         60 
MYEEMDKLIE KASILIEALP YIQKLYGKTV VIKYGGNAMI NDKLKNWVME DITLLKYIGV 

        70         80         90        100        110        120 
NPIVVHGGGP EINSVLKKLN VESQFVNGLR VTDMQTMEVA QMVLVGKTNK ELVSMLNQKG 

       130        140        150        160        170        180 
GKAIGICGID GNLIQARKHY EIVNGEKVDL GYVGEVVSIN AKVLEMLAKD EYIPVVAPIG 

       190        200        210        220        230        240 
VGEDGTSYNI NADTVAAEIA KAIKAEKLMF MTDVEGLKYD KNSSEIISAI SADEVLKMID 

       250        260        270        280        290 
EGKIDGGMIP KVLGCIDALK HGVNRTHILD GRIPHCILLE IFTDKGIGTM IHL 

« Hide

References

[1]"Genome sequence of the thermophilic hydrogen-producing bacterium Caldicellulosiruptor saccharolyticus DSM 8903."
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., Kiss H., Brettin T., Bruce D., Han C., Schmutz J., Larimer F., Land M. expand/collapse author list , Hauser L., Kyrpides N., Lykidis A., van de Werken H.J.G., Verhaart M.R.A., VanFossen A.L., Lewis D.L., Nichols J.D., Goorissen H.P., van Niel E.W.J., Stams F.J.M., Willquist K.U., Ward D.E., van der Oost J., Kelly R.M., Kengen S.M.W., Richardson P.
Submitted (APR-2007) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 43494 / DSM 8903.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000679 Genomic DNA. Translation: ABP67123.1.
RefSeqYP_001180314.1. NC_009437.1.

3D structure databases

ProteinModelPortalA4XJN8.
SMRA4XJN8. Positions 9-292.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING351627.Csac_1530.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABP67123; ABP67123; Csac_1530.
GeneID5088112.
KEGGcsc:Csac_1530.
PATRIC21252756. VBICalSac56748_1688.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0548.
HOGENOMHOG000233259.
KOK00930.
OMAPGVLDKN.
OrthoDBEOG6T1WVF.

Enzyme and pathway databases

BioCycCSAC351627:GJ17-1567-MONOMER.
UniPathwayUPA00068; UER00107.

Family and domain databases

Gene3D3.40.1160.10. 1 hit.
HAMAPMF_00082_A. ArgB_A.
MF_00082_B. ArgB_B.
InterProIPR004662. AcgluKinase.
IPR001048. Asp/Glu/Uridylate_kinase.
IPR001057. Glu/AcGlu_kinase.
[Graphical view]
PfamPF00696. AA_kinase. 1 hit.
[Graphical view]
PIRSFPIRSF000728. NAGK. 1 hit.
PRINTSPR00474. GLU5KINASE.
SUPFAMSSF53633. SSF53633. 1 hit.
TIGRFAMsTIGR00761. argB. 1 hit.
ProtoNetSearch...

Entry information

Entry nameARGB_CALS8
AccessionPrimary (citable) accession number: A4XJN8
Entry history
Integrated into UniProtKB/Swiss-Prot: May 20, 2008
Last sequence update: May 29, 2007
Last modified: May 14, 2014
This is version 47 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