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Q8TX15 (ARGJ_METKA) Reviewed, UniProtKB/Swiss-Prot

Last modified December 14, 2011. Version 57. 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:
Arginine biosynthesis bifunctional protein ArgJ

Including the following 2 domains:

  1. Glutamate N-acetyltransferase
    EC=2.3.1.35
    Alternative name(s):
    Ornithine acetyltransferase
    Short name=OATase
    Ornithine transacetylase
  2. Amino-acid acetyltransferase
    EC=2.3.1.1
    Alternative name(s):
    N-acetylglutamate synthase
    Short name=AGS
Gene names
Name:argJ
Ordered Locus Names:MK0865
OrganismMethanopyrus kandleri (strain AV19 / DSM 6324 / JCM 9639 / NBRC 100938)
Taxonomic identifier190192 [NCBI]
Taxonomic lineageArchaeaEuryarchaeotaMethanopyriMethanopyralesMethanopyraceaeMethanopyrus

Protein attributes

Sequence length387 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceInferred from homology

General annotation (Comments)

Function

Catalyzes two activities which are involved in the cyclic version of arginine biosynthesis: the synthesis of acetylglutamate from glutamate and acetyl-CoA, and of ornithine by transacetylation between acetylornithine and glutamate By similarity. HAMAP MF_01106

Catalytic activity

N(2)-acetyl-L-ornithine + L-glutamate = L-ornithine + N-acetyl-L-glutamate. HAMAP MF_01106

Acetyl-CoA + L-glutamate = CoA + N-acetyl-L-glutamate. HAMAP MF_01106

Pathway

Amino-acid biosynthesis; L-arginine biosynthesis; L-ornithine and N-acetyl-L-glutamate from L-glutamate and N(2)-acetyl-L-ornithine (cyclic): step 1/1. HAMAP MF_01106

Amino-acid biosynthesis; L-arginine biosynthesis; N(2)-acetyl-L-ornithine from L-glutamate: step 1/4. HAMAP MF_01106

Subunit structure

Heterotetramer of two alpha and two beta chains By similarity.

Subcellular location

Cytoplasm Probable HAMAP MF_01106.

Miscellaneous

Some bacteria possess a monofunctional ArgJ, i.e., capable of catalyzing only the fifth step of the arginine biosynthetic pathway. HAMAP MF_01106

Sequence similarities

Belongs to the ArgJ family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 172172Arginine biosynthesis bifunctional protein ArgJ alpha chain By similarity
PRO_0000002275
Chain173 – 387215Arginine biosynthesis bifunctional protein ArgJ beta chain By similarity
PRO_0000002276

Sequences

Sequence LengthMass (Da)Tools
Q8TX15 [UniParc].

Last modified June 1, 2002. Version 1.
Checksum: ED311EC1F47D56DD

FASTA38741,840
        10         20         30         40         50         60 
MRAPEGFLLG GIKREGIGVG LIFSERRCAV AGTFTENTLR AAPVEHSEEV CDRGVARGVI 

        70         80         90        100        110        120 
VNSGHANAMT GEEGYQDVLR TAEAIAELMG APEDEIVVCS TGVIGERPPV DKIVRYAREV 

       130        140        150        160        170        180 
WEDIGPTERH VREFSRAIMT TDTEEKIALY EGDGWSLLGI AKGAGMIHPN MSTMLAFLLT 

       190        200        210        220        230        240 
DVGAKPKELQ MWLRDVVNDT FNMITVDGDE STNDSVVLLA NGSSNLKVGS DVTITEFQRA 

       250        260        270        280        290        300 
LEEVCTELAE KIVRDGEGAT KLMIVCVHGA SNEVEARRAA RAIASSNLVK AALFGENPNW 

       310        320        330        340        350        360 
GRIGAAVGAA RVDVDPDELR IAFRSSEGEI VTYEGGPVDF DEEKAKRVLS ASEVEIVVDL 

       370        380 
GVGDASARAW GCDLTYEYVR INAEYRT 

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References

[1]"The complete genome of hyperthermophile Methanopyrus kandleri AV19 and monophyly of archaeal methanogens."
Slesarev A.I., Mezhevaya K.V., Makarova K.S., Polushin N.N., Shcherbinina O.V., Shakhova V.V., Belova G.I., Aravind L., Natale D.A., Rogozin I.B., Tatusov R.L., Wolf Y.I., Stetter K.O., Malykh A.G., Koonin E.V., Kozyavkin S.A.
Proc. Natl. Acad. Sci. U.S.A. 99:4644-4649(2002) [PubMed: 11930014] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: AV19 / DSM 6324 / JCM 9639 / NBRC 100938.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AE009439 Genomic DNA. Translation: AAM02078.1.
RefSeqNP_614148.1. NC_003551.1.

3D structure databases

ProteinModelPortalQ8TX15.
ModBaseSearch...

Protein family/group databases

MEROPST05.001.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID1476966.
GenomeReviewsGene locus MK0865 in contig AE009439_GR.
KEGGmka:MK0865.
NMPDRfig|190192.1.peg.861.

Phylogenomic databases

HOGENOMHBG284202.
OMAGRDPNWG.
PhylomeDBQ8TX15.
ProtClustDBPRK05388.

Enzyme and pathway databases

BioCycMKAN190192:MK0865-MONOMER.

Family and domain databases

HAMAPMF_01106. ArgJ. Divergent sequence.
[Tree]
InterProIPR002813. Arg_biosynth_ArgJ.
IPR016117. Pept_S58_DmpA/Arg_biosyn_ArgJ.
[Graphical view]
KOK00620.
PANTHERPTHR23100. ArgJ. 1 hit.
PfamPF01960. ArgJ. 1 hit.
[Graphical view]
ProDomPD004193. Arg_biosynth_ArgJ. 1 hit.
[Graphical view] [Entries sharing at least one domain]
SUPFAMSSF56266. Pept_S58_DmpA/Arg_biosyn_ArgJ. 1 hit.
TIGRFAMsTIGR00120. ArgJ. 1 hit.
ProtoNetSearch...

Entry information

Entry nameARGJ_METKA
AccessionPrimary (citable) accession number: Q8TX15
Entry history
Integrated into UniProtKB/Swiss-Prot: April 23, 2003
Last sequence update: June 1, 2002
Last modified: December 14, 2011
This is version 57 of the entry and version 1 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