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Q81M96 (ARGJ_BACAN) Reviewed, UniProtKB/Swiss-Prot

Last modified November 16, 2011. Version 62. 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:BA_4354, GBAA_4354, BAS4039
OrganismBacillus anthracis
Taxonomic identifier1392 [NCBI]
Taxonomic lineageBacteriaFirmicutesBacillalesBacillaceaeBacillusBacillus cereus group

Protein attributes

Sequence length407 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 caution

The sequence AAT56340.1 differs from that shown. Reason: Erroneous initiation.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 193193Arginine biosynthesis bifunctional protein ArgJ alpha chain By similarity
PRO_0000002103
Chain194 – 407214Arginine biosynthesis bifunctional protein ArgJ beta chain By similarity
PRO_0000002104

Sites

Site193 – 1942Cleavage; by autolysis By similarity

Sequences

Sequence LengthMass (Da)Tools
Q81M96 [UniParc].

Last modified June 1, 2003. Version 1.
Checksum: BC3C984B1A18530B

FASTA40743,740
        10         20         30         40         50         60 
MIKVASITKV EDGSIVTPKG FSAIGTAIGL KKGKKDLGAI VCDVPASCAA VYTTNQIQAA 

        70         80         90        100        110        120 
PLQVTKDSIT TEGKLQAIIV NSGNANACTG MKGLQDAYEM RALGAEHFGL KEKYVAVAST 

       130        140        150        160        170        180 
GVIGVPLPMD IIRKGIVTLI PAKEENGAHS FSEAILTTDL ITKETCYEMI IDGKKVMIAG 

       190        200        210        220        230        240 
VAKGSGMIHP NMATMLSFIT TDARIEHDVL QTALSQITNH TFNQITVDGD TSTNDMVIAM 

       250        260        270        280        290        300 
ASGLSETKPI DMEHADWETF VFALQKVCED LAKKIAQDGE GATKLIEVNV LGVQTNEEAK 

       310        320        330        340        350        360 
KIAKQIVGSS LVKTAIHGED PNWGRIISSI GQSEVAINPN TIDITLQSIS VLKNSEPQTF 

       370        380        390        400 
SEEEMKERLQ EDEIVINVYL HLGKETGSAW GCDLSYEYVK INACYRT 

« Hide

References

[1]"The genome sequence of Bacillus anthracis Ames and comparison to closely related bacteria."
Read T.D., Peterson S.N., Tourasse N.J., Baillie L.W., Paulsen I.T., Nelson K.E., Tettelin H., Fouts D.E., Eisen J.A., Gill S.R., Holtzapple E.K., Okstad O.A., Helgason E., Rilstone J., Wu M., Kolonay J.F., Beanan M.J., Dodson R.J. expand/collapse author list , Brinkac L.M., Gwinn M.L., DeBoy R.T., Madpu R., Daugherty S.C., Durkin A.S., Haft D.H., Nelson W.C., Peterson J.D., Pop M., Khouri H.M., Radune D., Benton J.L., Mahamoud Y., Jiang L., Hance I.R., Weidman J.F., Berry K.J., Plaut R.D., Wolf A.M., Watkins K.L., Nierman W.C., Hazen A., Cline R.T., Redmond C., Thwaite J.E., White O., Salzberg S.L., Thomason B., Friedlander A.M., Koehler T.M., Hanna P.C., Kolstoe A.-B., Fraser C.M.
Nature 423:81-86(2003) [PubMed: 12721629] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: Ames / isolate Porton.
[2]"Bacillus anthracis comparative genomics."
Ravel J., Rasko D.A., Shumway M.F., Jiang L., Cer R.Z., Federova N.B., Wilson M., Stanley S., Decker S., Read T.D., Salzberg S.L., Fraser C.M.
Submitted (MAY-2004) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: Ames ancestor.
[3]"Complete genome sequence of Bacillus anthracis Sterne."
Brettin T.S., Bruce D., Challacombe J.F., Gilna P., Han C., Hill K., Hitchcock P., Jackson P., Keim P., Longmire J., Lucas S., Okinaka R., Richardson P., Rubin E., Tice H.
Submitted (JAN-2004) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: Sterne.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AE016879 Genomic DNA. Translation: AAP28072.1.
AE017334 Genomic DNA. Translation: AAT33474.1.
AE017225 Genomic DNA. Translation: AAT56340.1. Different initiation.
RefSeqNP_846586.1. NC_003997.3.
YP_020999.1. NC_007530.2.
YP_030289.1. NC_005945.1.

3D structure databases

ProteinModelPortalQ81M96.
SMRQ81M96. Positions 3-405.
ModBaseSearch...

Protein-protein interaction databases

IntActQ81M96. 1 interaction.

Protein family/group databases

MEROPST05.001.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaEBBACT00000012995; EBBACP00000012751; EBBACG00000012987.
EBBACT00000014502; EBBACP00000014123; EBBACG00000014494.
EBBACT00000023067; EBBACP00000022552; EBBACG00000023058.
GeneID1087579.
2815492.
2850280.
GenomeReviewsGene locus BA_4354 in contig AE016879_GR.
Gene locus BAS4039 in contig AE017225_GR.
Gene locus GBAA_4354 in contig AE017334_GR.
KEGGban:BA_4354.
bar:GBAA_4354.
bat:BAS4039.
TIGRBA_4354.
GBAA_4354.

Phylogenomic databases

GeneTreeEBGT00050000002382.
HOGENOMHBG284202.
OMAGRDPNWG.
ProtClustDBPRK05388.

Enzyme and pathway databases

BioCycBANT260799:BAS4039-MONOMER.
BANT261594:GBAA4354-MONOMER.

Family and domain databases

HAMAPMF_01106. ArgJ.
[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_BACAN
AccessionPrimary (citable) accession number: Q81M96
Secondary accession number(s): Q6HTP9, Q6KMY8
Entry history
Integrated into UniProtKB/Swiss-Prot: June 21, 2004
Last sequence update: June 1, 2003
Last modified: November 16, 2011
This is version 62 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