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Q9PEM7 (ARGB_XYLFA) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 72. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
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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:XF_1001
OrganismXylella fastidiosa [Complete proteome] [HAMAP]
Taxonomic identifier2371 [NCBI]
Taxonomic lineageBacteria › Proteobacteria › Gammaproteobacteria › Xanthomonadales › Xanthomonadaceae › Xylella

Protein attributes

Sequence length421 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 MF_00082_B

Pathway

Amino-acid biosynthesis; L-arginine biosynthesis; N(2)-acetyl-L-ornithine from L-glutamate: step 2/4. HAMAP MF_00082_B

Subcellular location

Cytoplasm By similarity HAMAP MF_00082_B.

Sequence similarities

In the N-terminal section; belongs to the acetylglutamate kinase family.

Contains 1 N-acetyltransferase domain.

Sequence caution

The sequence AAF83811.1 differs from that shown. Reason: Erroneous initiation.

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-KW

   Cellular componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular functionATP binding

Inferred from electronic annotation. Source: UniProtKB-KW

N-acetyltransferase activity

Inferred from electronic annotation. Source: InterPro

acetylglutamate kinase activity

Inferred from electronic annotation. Source: EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 421421Acetylglutamate kinase HAMAP MF_00082_B
PRO_0000112687

Regions

Domain275 – 406132N-acetyltransferase
Region1 – 252252Acetylglutamate kinase HAMAP MF_00082_B
Region59 – 602Substrate binding By similarity

Sites

Binding site811Substrate By similarity
Binding site1701Substrate By similarity
Site261Transition state stabilizer By similarity
Site2311Transition state stabilizer By similarity

Sequences

Sequence LengthMass (Da)Tools
Q9PEM7 [UniParc].

Last modified February 12, 2003. Version 2.
Checksum: 6D4AF549E6392A77

FASTA42146,963
        10         20         30         40         50         60 
MASTKEISQY LKRFSQLDAK RFAVVKVGGA VLRDDVDALT SSLSFLQEVG LTPIVLHGAG 

        70         80         90        100        110        120 
PQLDEELTAA GIQKKTVNGF RVTLPETMAI VRKVFHTSNL QLIEALQRNG ARATSITGGV 

       130        140        150        160        170        180 
FEAHYLDQET YGLVGEISAV NLAPIEASLR AASIPVIASL GETPSGQILN INADVAANEL 

       190        200        210        220        230        240 
VHVLQPYKII FLTGTGGLLD ADGKIINSIN LSTEYEQLIQ QPWVYGGMKL KIEQIKHLLD 

       250        260        270        280        290        300 
RLPLESSVSI TRPADLAKEL FTHKGSGTLV RRGERVIRAT TWKDLDLPRL QHLIQSSFRR 

       310        320        330        340        350        360 
TLIPHYFETT PLLRAYVSEN YRAAVILTKL GNVPYLDKFA VLDDAQGEGL GRAVWSIMRE 

       370        380        390        400        410        420 
ETPQLFWRSR HNNQANAFYY AESDGYYKQD HWKIFWNGLH HFQQIQQCVA HCAQHPPTLI 


D

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References

[1]"The genome sequence of the plant pathogen Xylella fastidiosa."
Simpson A.J.G., Reinach F.C., Arruda P., Abreu F.A., Acencio M., Alvarenga R., Alves L.M.C., Araya J.E., Baia G.S., Baptista C.S., Barros M.H., Bonaccorsi E.D., Bordin S., Bove J.M., Briones M.R.S., Bueno M.R.P., Camargo A.A., Camargo L.E.A. expand/collapse author list , Carraro D.M., Carrer H., Colauto N.B., Colombo C., Costa F.F., Costa M.C.R., Costa-Neto C.M., Coutinho L.L., Cristofani M., Dias-Neto E., Docena C., El-Dorry H., Facincani A.P., Ferreira A.J.S., Ferreira V.C.A., Ferro J.A., Fraga J.S., Franca S.C., Franco M.C., Frohme M., Furlan L.R., Garnier M., Goldman G.H., Goldman M.H.S., Gomes S.L., Gruber A., Ho P.L., Hoheisel J.D., Junqueira M.L., Kemper E.L., Kitajima J.P., Krieger J.E., Kuramae E.E., Laigret F., Lambais M.R., Leite L.C.C., Lemos E.G.M., Lemos M.V.F., Lopes S.A., Lopes C.R., Machado J.A., Machado M.A., Madeira A.M.B.N., Madeira H.M.F., Marino C.L., Marques M.V., Martins E.A.L., Martins E.M.F., Matsukuma A.Y., Menck C.F.M., Miracca E.C., Miyaki C.Y., Monteiro-Vitorello C.B., Moon D.H., Nagai M.A., Nascimento A.L.T.O., Netto L.E.S., Nhani A. Jr., Nobrega F.G., Nunes L.R., Oliveira M.A., de Oliveira M.C., de Oliveira R.C., Palmieri D.A., Paris A., Peixoto B.R., Pereira G.A.G., Pereira H.A. Jr., Pesquero J.B., Quaggio R.B., Roberto P.G., Rodrigues V., de Rosa A.J.M., de Rosa V.E. Jr., de Sa R.G., Santelli R.V., Sawasaki H.E., da Silva A.C.R., da Silva A.M., da Silva F.R., Silva W.A. Jr., da Silveira J.F., Silvestri M.L.Z., Siqueira W.J., de Souza A.A., de Souza A.P., Terenzi M.F., Truffi D., Tsai S.M., Tsuhako M.H., Vallada H., Van Sluys M.A., Verjovski-Almeida S., Vettore A.L., Zago M.A., Zatz M., Meidanis J., Setubal J.C.
Nature 406:151-159(2000) [PubMed: 10910347] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: 9a5c.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		AE003849 Genomic DNA. Translation: AAF83811.1. Different initiation.
PIRH82734.
RefSeqNP_298291.1. NC_002488.3.

3D structure databases

ProteinModelPortalQ9PEM7.
ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID1126538.
GenomeReviewsGene locus XF_1001 in contig AE003849_GR.
KEGGxfa:XF1001.
NMPDRfig|160492.1.peg.998.
PATRIC24132066. VBIXylFas578_1071.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMHBG331277.
OMADSFCKPA.
ProtClustDBPRK04531.

Enzyme and pathway databases

BioCycXFAS160492:XF1001-MONOMER.

Family and domain databases

HAMAPMF_00082_B. ArgB_B. Fused.
[Tree]
InterProIPR011242. AcGlu_kinase_DUF619-contain.
IPR004662. AcgluKinase.
IPR000182. AcTrfase_GCN5-related_dom.
IPR016181. Acyl_CoA_acyltransferase.
IPR001048. Asp/Glu/Uridylate_kinase.
IPR006855. DUF619.
[Graphical view]
Gene3DG3DSA:3.40.1160.10. Aa_kinase. 1 hit.
G3DSA:3.40.630.30. Acyl_CoA_acyltransferase. 1 hit.
KOK00930.
PfamPF00696. AA_kinase. 1 hit.
PF04768. DUF619. 1 hit.
[Graphical view]
PIRSFPIRSF036441. NAGK_DUF619. 1 hit.
SUPFAMSSF53633. Aa_kinase. 1 hit.
SSF55729. Acyl_CoA_acyltransferase. 1 hit.
TIGRFAMsTIGR00761. ArgB. 1 hit.
PROSITEPS51186. GNAT. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameARGB_XYLFA
AccessionPrimary (citable) accession number: Q9PEM7
Entry history
Integrated into UniProtKB/Swiss-Prot: February 12, 2003
Last sequence update: February 12, 2003
Last modified: January 25, 2012
This is version 72 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

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