Q5HBE9 (Q5HBE9_EHRRW) Unreviewed, UniProtKB/TrEMBL

Names and origin

Protein names

Recommended name:
Arginine biosynthesis bifunctional protein ArgJ HAMAP MF_01106

Gene names

Name:	argJ HAMAP MF_01106 EMBL CAH58102.1
Ordered Locus Names:	Erum3800, ERWE_CDS_03920

Organism

Ehrlichia ruminantium (strain Welgevonden) [Complete proteome] [HAMAP]

Taxonomic identifier

254945 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Alphaproteobacteria › Rickettsiales › Anaplasmataceae › Ehrlichia

Protein attributes

Sequence length	419 AA.
Sequence status	Complete.
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	Acetyl-CoA + L-glutamate = CoA + N-acetyl-L-glutamate. HAMAP MF_01106 N(2)-acetyl-L-ornithine + L-glutamate = L-ornithine + 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. HAMAP MF_01106
Subcellular location	Cytoplasm By similarity HAMAP MF_01106.
Miscellaneous	Some bacteria possess a monofunctional ArgJ, i.e., capable of catalyzing only the fifth step of the arginine biosynthetic pathway By similarity. HAMAP MF_01106
Sequence similarities	Belongs to the ArgJ family. HAMAP MF_01106

Ontologies

Keywords
Biological process	Amino-acid biosynthesis Arginine biosynthesis HAMAP MF_01106
Cellular component	Cytoplasm HAMAP MF_01106
Molecular function	Acyltransferase HAMAP MF_01106 EMBL CAH58102.1 Transferase
PTM	Autocatalytic cleavage HAMAP MF_01106
Technical term	Complete proteome Multifunctional enzyme HAMAP MF_01106
Gene Ontology (GO)
Biological process	arginine biosynthetic process Inferred from electronic annotation. Source: HAMAP
Cellular component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	acetyl-CoA:L-glutamate N-acetyltransferase activity Inferred from electronic annotation. Source: HAMAP glutamate N-acetyltransferase activity Inferred from electronic annotation. Source: HAMAP
Complete GO annotation...

Sequences

	Sequence		Length	Mass (Da)
	Q5HBE9 [UniParc]. Last modified February 15, 2005. Version 1. Checksum: 8BD4624BB6C6EBC2	FASTA	419	45,338
	10 20 30 40 50 60 MSKNSSYTSS GFSISPLAPT KFPVMPKING VNLYSFSSGV KSSGKLDLLV VEMQDQSSVA 70 80 90 100 110 120 GVFTNSYTAS SNVEHCRNII SYGKAKVLIV NSGNANVAVG ANGYKVVEEI TTLCAEKFSC 130 140 150 160 170 180 STNEVYFCST GIIGVPLPID KIKSVLINGI WSVSENSWRD AALSIITTDT FPKMVTKEVF 190 200 210 220 230 240 IGGEKVTING ICKGSGMIAP NMATMLAYVF TDANITSDVL QRLLKKYVDI SFNSITVDGD 250 260 270 280 290 300 MSTSDSVLIF ATNLANHKQI CSVDDQLIDD FKIALKDVLV EMAHLIVKDG EGATKFVTIN 310 320 330 340 350 360 VNKVVSLESA RKLAFSIANS PLVKTAIAGE DANWGRIVMA IGKAGEPLDK NRISIKIGDN 370 380 390 400 410 VIVMNGEISS VYDKSYVDSY MKGNNILIDV CINTGNFNTT VWTCDLTRRF IDINAHYFT

References

[1]

"The genome of the heartwater agent Ehrlichia ruminantium contains multiple tandem repeats of actively variable copy number." Collins N.E., Liebenberg J., de Villiers E.P., Brayton K.A., Louw E., Pretorius A., Faber F.E., van Heerden H., Josemans A., van Kleef M., Steyn H.C., van Strijp M.F., Zweygarth E., Jongejan F., Maillard J.C., Berthier D., Botha M., Joubert F. , Corton C.H., Thomson N.R., Allsopp M.T., Allsopp B.A. Proc. Natl. Acad. Sci. U.S.A. 102:838-843(2005) [PubMed: 15637156] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: Welgevonden [ARC-OVI].

[2]

"Comparative genomic analysis of three strains of Ehrlichia ruminantium reveals an active process of genome size plasticity." Frutos R., Viari A., Ferraz C., Morgat A., Eychenie S., Kandassamy Y., Chantal I., Bensaid A., Coissac E., Vachiery N., Demaille J., Martinez D. J. Bacteriol. 188:2533-2542(2006) [PubMed: 16547041] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: Welgevonden [CIRAD].

Cross-references

Sequence databases
EMBL GenBank DDBJ	CR767821 Genomic DNA. Translation: CAH58102.1. CR925678 Genomic DNA. Translation: CAI26886.1.
RefSeq	YP_180245.1. NC_005295.2. YP_197268.1. NC_006832.1.
3D structure databases
ProteinModelPortal	Q5HBE9.
ModBase	Search...
Protein-protein interaction databases
STRING	Q5HBE9.
Protein family/group databases
MEROPS	T05.001.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	3233277. 3260972.
GenomeReviews	Gene locus Erum3800 in contig CR767821_GR. Gene locus ERWE_CDS_03920 in contig CR925678_GR.
KEGG	eru:Erum3800. erw:ERWE_CDS_03920.
PATRIC	20580599. VBIEhrRum92411_0417.
Organism-specific databases
CMR	Search...
Phylogenomic databases
eggNOG	COG1364.
HOGENOM	HBG284202.
OMA	FPKLATR.
PhylomeDB	Q5HBE9.
ProtClustDB	PRK05388.
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

Q5HBE9_EHRRW

Accession

Primary (citable) accession number: Q5HBE9
Secondary accession number(s): Q5FDU3

Entry history

Integrated into UniProtKB/TrEMBL:	February 15, 2005
Last sequence update:	February 15, 2005
Last modified:	January 25, 2012
This is version 62 of the entry and version 1 of the sequence. [Complete history]

Entry status

Unreviewed (UniProtKB/TrEMBL)