UniProtKB - Q635F1 (ARGJ_BACCZ)
Protein
Arginine biosynthesis bifunctional protein ArgJ
Gene
argJ
Organism
Bacillus cereus (strain ZK / E33L)
Status
Functioni
Catalyzes two activities which are involved in the cyclic version of arginine biosynthesis: the synthesis of N-acetylglutamate from glutamate and acetyl-CoA as the acetyl donor, and of ornithine by transacetylation between N2-acetylornithine and glutamate.UniRule annotation
Miscellaneous
Some bacteria possess a monofunctional ArgJ, i.e. capable of catalyzing only the fifth step of the arginine biosynthetic pathway.
Catalytic activityi
: L-arginine biosynthesis Pathwayi
This protein is involved in step 1 of the subpathway that synthesizes L-ornithine and N-acetyl-L-glutamate from L-glutamate and N(2)-acetyl-L-ornithine (cyclic).UniRule annotationProteins known to be involved in this subpathway in this organism are:
- Arginine biosynthesis bifunctional protein ArgJ (argJ)
View all proteins of this organism that are known to be involved in the subpathway that synthesizes L-ornithine and N-acetyl-L-glutamate from L-glutamate and N(2)-acetyl-L-ornithine (cyclic), the pathway L-arginine biosynthesis and in Amino-acid biosynthesis.
Pathwayi: L-arginine biosynthesis
This protein is involved in step 1 of the subpathway that synthesizes N(2)-acetyl-L-ornithine from L-glutamate.UniRule annotationProteins known to be involved in the 4 steps of the subpathway in this organism are:
- Arginine biosynthesis bifunctional protein ArgJ (argJ)
- Acetylglutamate kinase (argB)
- N-acetyl-gamma-glutamyl-phosphate reductase (argC)
- Acetylornithine aminotransferase (argD)
View all proteins of this organism that are known to be involved in the subpathway that synthesizes N(2)-acetyl-L-ornithine from L-glutamate, the pathway L-arginine biosynthesis and in Amino-acid biosynthesis.
Sites
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Sitei | 121 | Involved in the stabilization of negative charge on the oxyanion by the formation of the oxyanion holeUniRule annotation | 1 | |
Sitei | 122 | Involved in the stabilization of negative charge on the oxyanion by the formation of the oxyanion holeUniRule annotation | 1 | |
Binding sitei | 158 | SubstrateUniRule annotation | 1 | |
Binding sitei | 184 | SubstrateUniRule annotation | 1 | |
Active sitei | 195 | NucleophileUniRule annotation | 1 | |
Binding sitei | 195 | SubstrateUniRule annotation | 1 | |
Binding sitei | 281 | SubstrateUniRule annotation | 1 | |
Binding sitei | 403 | SubstrateUniRule annotation | 1 | |
Binding sitei | 408 | SubstrateUniRule annotation | 1 |
GO - Molecular functioni
- acetyl-CoA:L-glutamate N-acetyltransferase activity Source: UniProtKB-UniRule
- glutamate N-acetyltransferase activity Source: UniProtKB-UniRule
- methione N-acyltransferase activity Source: UniProtKB-EC
GO - Biological processi
- arginine biosynthetic process Source: UniProtKB-UniRule
Keywordsi
Molecular function | Acyltransferase, Multifunctional enzyme, Transferase |
Biological process | Amino-acid biosynthesis, Arginine biosynthesis |
Enzyme and pathway databases
UniPathwayi | UPA00068;UER00106 UPA00068;UER00111 |
Names & Taxonomyi
Protein namesi | Recommended name: Arginine biosynthesis bifunctional protein ArgJUniRule annotationCleaved into the following 2 chains: Arginine biosynthesis bifunctional protein ArgJ alpha chainUniRule annotation Arginine biosynthesis bifunctional protein ArgJ beta chainUniRule annotation Including the following 2 domains: Alternative name(s): Ornithine acetyltransferaseUniRule annotation Short name: OATaseUniRule annotation Ornithine transacetylaseUniRule annotation Alternative name(s): N-acetylglutamate synthaseUniRule annotation Short name: AGSaseUniRule annotation |
Gene namesi | Name:argJUniRule annotation Ordered Locus Names:BCE33L3886 |
Organismi | Bacillus cereus (strain ZK / E33L) |
Taxonomic identifieri | 288681 [NCBI] |
Taxonomic lineagei | Bacteria › Firmicutes › Bacilli › Bacillales › Bacillaceae › Bacillus › Bacillus cereus group › |
Proteomesi |
|
Subcellular locationi
- Cytoplasm UniRule annotation
GO - Cellular componenti
- cytoplasm Source: UniProtKB-SubCell
Keywords - Cellular componenti
CytoplasmPTM / Processingi
Molecule processing
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
ChainiPRO_0000002111 | 1 – 194 | Arginine biosynthesis bifunctional protein ArgJ alpha chainUniRule annotationAdd BLAST | 194 | |
ChainiPRO_0000002112 | 195 – 408 | Arginine biosynthesis bifunctional protein ArgJ beta chainUniRule annotationAdd BLAST | 214 |
Sites
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Sitei | 194 – 195 | Cleavage; by autolysisUniRule annotation | 2 |
Keywords - PTMi
Autocatalytic cleavageInteractioni
Subunit structurei
Heterotetramer of two alpha and two beta chains.
UniRule annotationFamily & Domainsi
Sequence similaritiesi
Belongs to the ArgJ family.UniRule annotation
Phylogenomic databases
OMAi | GMIAPNM |
Family and domain databases
CDDi | cd02152, OAT, 1 hit |
Gene3Di | 3.10.20.340, 1 hit |
HAMAPi | MF_01106, ArgJ, 1 hit |
InterProi | View protein in InterPro IPR002813, Arg_biosynth_ArgJ IPR016117, ArgJ-like_dom_sf IPR042195, ArgJ_beta_C |
PANTHERi | PTHR23100, PTHR23100, 1 hit |
Pfami | View protein in Pfam PF01960, ArgJ, 1 hit |
SUPFAMi | SSF56266, SSF56266, 1 hit |
TIGRFAMsi | TIGR00120, ArgJ, 1 hit |
i Sequence
Sequence statusi: Complete.
: The displayed sequence is further processed into a mature form. Sequence processingi
Q635F1-1 [UniParc]FASTAAdd to basket
10 20 30 40 50
MMVKVASITK LEDGSIVTPK GFSAIGTAIG LKKGKKDLGA IVCDTPASCA
60 70 80 90 100
AVYTTNQIQA APLQVTKDSI ATEGKLQAII VNSGNANACT GMKGLQDAYE
110 120 130 140 150
MRALGAEHFG VKENYVAVAS TGVIGVPLPM EIIRKGIVTL IPAKEENEAH
160 170 180 190 200
SFSEAILTTD LITKETCYEM IIDGKKVTIA GVAKGSGMIH PNMATMLSFI
210 220 230 240 250
TTDAHIEHDV LQTALSQITN HTFNQITVDG DTSTNDMVIA MASGLSETKP
260 270 280 290 300
IDMEHADWET FVFALQKVCE DLAKKIAQDG EGATKLIEVN VLGAQTNEEA
310 320 330 340 350
KKIAKQIVGS SLVKTAIHGE DPNWGRIISS IGQSEVAINP NTIDITLQSI
360 370 380 390 400
VVLKNSEPQM FSEEEMKMRL QEHEIMIDVY LHLGEETGSA WGCDLSYEYV
KINACYRT
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | CP000001 Genomic DNA Translation: AAU16382.1 |
Genome annotation databases
EnsemblBacteriai | AAU16382; AAU16382; BCE33L3886 |
KEGGi | bcz:BCE33L3886 |
Similar proteinsi
Cross-referencesi
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | CP000001 Genomic DNA Translation: AAU16382.1 |
3D structure databases
SMRi | Q635F1 |
ModBasei | Search... |
Genome annotation databases
EnsemblBacteriai | AAU16382; AAU16382; BCE33L3886 |
KEGGi | bcz:BCE33L3886 |
Phylogenomic databases
OMAi | GMIAPNM |
Enzyme and pathway databases
UniPathwayi | UPA00068;UER00106 UPA00068;UER00111 |
Family and domain databases
CDDi | cd02152, OAT, 1 hit |
Gene3Di | 3.10.20.340, 1 hit |
HAMAPi | MF_01106, ArgJ, 1 hit |
InterProi | View protein in InterPro IPR002813, Arg_biosynth_ArgJ IPR016117, ArgJ-like_dom_sf IPR042195, ArgJ_beta_C |
PANTHERi | PTHR23100, PTHR23100, 1 hit |
Pfami | View protein in Pfam PF01960, ArgJ, 1 hit |
SUPFAMi | SSF56266, SSF56266, 1 hit |
TIGRFAMsi | TIGR00120, ArgJ, 1 hit |
ProtoNeti | Search... |
MobiDBi | Search... |
Entry informationi
Entry namei | ARGJ_BACCZ | |
Accessioni | Q635F1Primary (citable) accession number: Q635F1 | |
Entry historyi | Integrated into UniProtKB/Swiss-Prot: | March 1, 2005 |
Last sequence update: | October 25, 2004 | |
Last modified: | December 2, 2020 | |
This is version 106 of the entry and version 1 of the sequence. See complete history. | ||
Entry statusi | Reviewed (UniProtKB/Swiss-Prot) | |
Annotation program | Prokaryotic Protein Annotation Program |
Miscellaneousi
Documents
- PATHWAY comments
Index of metabolic and biosynthesis pathways - SIMILARITY comments
Index of protein domains and families