Reviewed, UniProtKB/Swiss-Prot Q9PM71 (HIS2_CAMJE)

Names and origin

Protein names

Recommended name:
    Histidine biosynthesis bifunctional protein hisIE
Including the following 2 domains:
    1- Recommended name:
            Phosphoribosyl-AMP cyclohydrolase
                Short name=PRA-CH
              EC=3.5.4.19
    2- Recommended name:
            Phosphoribosyl-ATP pyrophosphatase
                Short name=PRA-PH
              EC=3.6.1.31

Gene names

Name:	hisI
Synonyms:	hisIE
Ordered Locus Names:	Cj1604

Organism

Campylobacter jejuni [Complete proteome] [HAMAP]

Taxonomic identifier

197 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Epsilonproteobacteria › Campylobacterales › Campylobacteraceae › Campylobacter

Protein attributes

Sequence length	207 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Inferred from homology.

General annotation (Comments)

Catalytic activity	1-(5-phosphoribosyl)-ATP + H2O = 1-(5-phosphoribosyl)-AMP + diphosphate. HAMAP MF_01019 1-(5-phosphoribosyl)-AMP + H2O = 1-(5-phosphoribosyl)-5-((5-phosphoribosylamino)methylideneamino)imidazole-4-carboxamide. HAMAP MF_01019
Pathway	Amino-acid biosynthesis; L-histidine biosynthesis; L-histidine from 5-phospho-alpha-D-ribose 1-diphosphate: step 2/9. HAMAP MF_01019 Amino-acid biosynthesis; L-histidine biosynthesis; L-histidine from 5-phospho-alpha-D-ribose 1-diphosphate: step 3/9.
Subcellular location	Cytoplasm By similarity.
Sequence similarities	In the N-terminal section; belongs to the PRA-CH family. In the C-terminal section; belongs to the PRA-PH family.

Ontologies

Keywords
Biological process	Amino-acid biosynthesis Histidine biosynthesis
Cellular component	Cytoplasm
Ligand	ATP-binding Nucleotide-binding
Molecular function	Hydrolase
Technical term	Complete proteome Multifunctional enzyme
Gene Ontology (GO)
Biological process	histidine biosynthetic process Inferred from electronic annotation. Source: HAMAP
Cellular component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW phosphoribosyl-AMP cyclohydrolase activity Inferred from electronic annotation. Source: HAMAP phosphoribosyl-ATP diphosphatase activity Inferred from electronic annotation. Source: HAMAP
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 207	207	Histidine biosynthesis bifunctional protein hisIE HAMAP MF_01019		PRO_0000136408
Regions
	Region	1 – 117	117	Phosphoribosyl-AMP cyclohydrolase HAMAP MF_01019
	Region	118 – 207	90	Phosphoribosyl-ATP pyrophosphohydrolase HAMAP MF_01019

Sequences

	Sequence		Length	Mass (Da)
	Q9PM71-1 [UniParc]. Last modified October 1, 2000. Version 1. Checksum: F5E4E6374D6E99C1	FASTA	207	23,176
	10 20 30 40 50 60 MQNFKELNEK IAWQKVDNLL PVIIQDAKTC EVLMLGFMNN EALEKSLESG KVVFFSRTKQ 70 80 90 100 110 120 RLWMKGEESG NFLNIIDLSL DCDNDTLLIL ANPVGPTCHT GDISCFEKIS KNADFVFLAR 130 140 150 160 170 180 LEKLINARKN ADENTSYTAK LFKSGTKRIA QKVGEEGVET ALAATVKDKE ELICEAADLM 190 200 YHLSVLLADA NLSFSDVISK LKERHKA

References

[1]

"The genome sequence of the food-borne pathogen Campylobacter jejuni reveals hypervariable sequences." Parkhill J., Wren B.W., Mungall K.L., Ketley J.M., Churcher C.M., Basham D., Chillingworth T., Davies R.M., Feltwell T., Holroyd S., Jagels K., Karlyshev A.V., Moule S., Pallen M.J., Penn C.W., Quail M.A., Rajandream M.A., Rutherford K.M. , van Vliet A.H.M., Whitehead S., Barrell B.G. Nature 403:665-668(2000) [PubMed: 10688204] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: NCTC 11168 / Serotype O:2.

Cross-references

Sequence databases
EMBLGenBankDDBJ	AL111168 Genomic DNA. Translation: CAL35701.1.
PIR	B81256.
RefSeq	YP_002344973.1.
3D structure databases
ModBase	Search...
Protein-protein interaction databases
IntAct	Q9PM71. 8 interactions.
Genome annotation databases
GeneID	905159.
GenomeReviews	Gene locus Cj1604 in contig AL111168_GR.
KEGG	cje:Cj1604.
Organism-specific databases
CMR	Search...
Phylogenomic databases
OMA	Q9PM71. VHYWSRS.
Enzyme and pathway databases
BioCyc	CJEJ192222:CJ1604-MON.
BRENDA	3.5.4.19. 255835. 3.6.1.31. 255835.
Family and domain databases
HAMAP	MF_01019. [Tree]
InterPro	IPR002496. PRA_CycHdrlase. IPR008179. PRib-ATP_pyrophosphohydrolase. [Graphical view]
Pfam	PF01502. PRA-CH. 1 hit. PF01503. PRA-PH. 1 hit. [Graphical view]
ProDom	PD002610. PRA_cyclohydro. 1 hit. PD002611. Pra_PH/CH. 1 hit. [Graphical view] [Entries sharing at least one domain]
TIGRFAMs	TIGR03188. histidine_hisI. 1 hit.
ProtoNet	Search...

Entry information

Entry name

HIS2_CAMJE

Accession

Primary (citable) accession number: Q9PM71
Secondary accession number(s): Q0P824

Entry history

Integrated into UniProtKB/Swiss-Prot:	June 6, 2002
Last sequence update:	October 1, 2000
Last modified:	June 16, 2009
This is version 52 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)