Q81M96 (ARGJ_BACAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Arginine biosynthesis bifunctional protein ArgJ

Cleaved into the following 2 chains:

1. Arginine biosynthesis bifunctional protein ArgJ alpha chain
2. Arginine biosynthesis bifunctional protein ArgJ beta chain

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

Organism

Bacillus anthracis

Taxonomic identifier

1392 [NCBI]

Taxonomic lineage

Bacteria › Firmicutes › Bacillales › Bacillaceae › Bacillus › Bacillus cereus group

Protein attributes

Sequence length	407 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Inferred 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.

Ontologies

Keywords
Biological process	Amino-acid biosynthesis Arginine biosynthesis
Cellular component	Cytoplasm
Molecular function	Acyltransferase Transferase
PTM	Autocatalytic cleavage
Technical term	Complete proteome Multifunctional enzyme Reference proteome
Gene Ontology (GO)
Biological process	arginine biosynthetic process Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	acetyl-CoA:L-glutamate N-acetyltransferase activity Inferred from electronic annotation. Source: EC glutamate N-acetyltransferase activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 193	193	Arginine biosynthesis bifunctional protein ArgJ alpha chain By similarity		PRO_0000002103
	Chain	194 – 407	214	Arginine biosynthesis bifunctional protein ArgJ beta chain By similarity		PRO_0000002104
Sites
	Site	193 – 194	2	Cleavage; by autolysis By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q81M96 [UniParc]. Last modified June 1, 2003. Version 1. Checksum: BC3C984B1A18530B	FASTA	407	43,740
	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

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. , 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.
RefSeq	NP_846586.1. NC_003997.3. YP_020999.1. NC_007530.2. YP_030289.1. NC_005945.1.
3D structure databases
ProteinModelPortal	Q81M96.
SMR	Q81M96. Positions 3-405.
ModBase	Search...
Protein-protein interaction databases
IntAct	Q81M96. 1 interaction.
Protein family/group databases
MEROPS	T05.001.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	EBBACT00000012995; EBBACP00000012751; EBBACG00000012987. EBBACT00000014502; EBBACP00000014123; EBBACG00000014494. EBBACT00000023067; EBBACP00000022552; EBBACG00000023058.
GeneID	1087579. 2815492. 2850280.
GenomeReviews	Gene locus BA_4354 in contig AE016879_GR. Gene locus BAS4039 in contig AE017225_GR. Gene locus GBAA_4354 in contig AE017334_GR.
KEGG	ban:BA_4354. bar:GBAA_4354. bat:BAS4039.
TIGR	BA_4354. GBAA_4354.
Phylogenomic databases
GeneTree	EBGT00050000002382.
HOGENOM	HBG284202.
OMA	GRDPNWG.
ProtClustDB	PRK05388.
Enzyme and pathway databases
BioCyc	BANT260799:BAS4039-MONOMER. BANT261594:GBAA4354-MONOMER.
Family and domain databases
HAMAP	MF_01106. ArgJ. [Tree]
InterPro	IPR002813. Arg_biosynth_ArgJ. IPR016117. Pept_S58_DmpA/Arg_biosyn_ArgJ. [Graphical view]
KO	K00620.
PANTHER	PTHR23100. ArgJ. 1 hit.
Pfam	PF01960. ArgJ. 1 hit. [Graphical view]
ProDom	PD004193. Arg_biosynth_ArgJ. 1 hit. [Graphical view] [Entries sharing at least one domain]
SUPFAM	SSF56266. Pept_S58_DmpA/Arg_biosyn_ArgJ. 1 hit.
TIGRFAMs	TIGR00120. ArgJ. 1 hit.
ProtoNet	Search...

Entry information

Entry name

ARGJ_BACAN

Accession

Primary (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 status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program