Q7VJ02 (HIS2_HELHP) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Histidine biosynthesis bifunctional protein HisIE

Including the following 2 domains:

1. Phosphoribosyl-AMP cyclohydrolase
   Short name=PRA-CH
   EC=3.5.4.19
2. Phosphoribosyl-ATP pyrophosphatase
   Short name=PRA-PH
   EC=3.6.1.31

Gene names

Name:	hisI
Synonyms:	hisIE
Ordered Locus Names:	HH_0449

Organism

Helicobacter hepaticus (strain ATCC 51449 / 3B1) [Complete proteome] [HAMAP]

Taxonomic identifier

235279 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Epsilonproteobacteria › Campylobacterales › Helicobacteraceae › Helicobacter

Protein attributes

Sequence length	231 AA.
Sequence status	Complete.
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 HAMAP MF_01019.
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: UniProtKB-KW
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: EC phosphoribosyl-ATP diphosphatase 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 – 231	231	Histidine biosynthesis bifunctional protein HisIE HAMAP MF_01019		PRO_0000136416
Regions
	Region	1 – 130	130	Phosphoribosyl-AMP cyclohydrolase HAMAP MF_01019
	Region	131 – 231	101	Phosphoribosyl-ATP pyrophosphohydrolase HAMAP MF_01019

Sequences

	Sequence		Length	Mass (Da)
	Q7VJ02 [UniParc]. Last modified October 1, 2003. Version 1. Checksum: AB35A5FEE6E68307	FASTA	231	26,830
	10 20 30 40 50 60 MQDVFRQIDW ERYELIPTIV QEKQSQQILM LAYSSKQSLE LSLQTHLAHY FSRSKQRIWQ 70 80 90 100 110 120 KGEQSGHIQH IKEVKLDCDN DSLIFIVEQV GVACHTGEKS CFFRIFSLDK NCQNPPVSMP 130 140 150 160 170 180 QKYPIGVYHI LDDLYHIIEQ RRCENIEHSY TASLLAKGVN GIGKKIIEEA GELCFALKDK 190 200 210 220 230 DEKAIIYECA DLFYHILVGL ALEHITPERV LQELRRRMGQ SGIEEKASRK H

References

[1]

"The complete genome sequence of the carcinogenic bacterium Helicobacter hepaticus." Suerbaum S., Josenhans C., Sterzenbach T., Drescher B., Brandt P., Bell M., Droege M., Fartmann B., Fischer H.-P., Ge Z., Hoerster A., Holland R., Klein K., Koenig J., Macko L., Mendz G.L., Nyakatura G., Schauer D.B. , Shen Z., Weber J., Frosch M., Fox J.G. Proc. Natl. Acad. Sci. U.S.A. 100:7901-7906(2003) [PubMed: 12810954] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 51449 / 3B1.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AE017125 Genomic DNA. Translation: AAP77046.1.
RefSeq	NP_859980.1. NC_004917.1.
3D structure databases
ProteinModelPortal	Q7VJ02.
ModBase	Search...
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	1493503.
GenomeReviews	Gene locus HH_0449 in contig AE017125_GR.
KEGG	hhe:HH0449.
NMPDR	fig|235279.1.peg.449.
PATRIC	20588350. VBIHelHep90276_0454.
Organism-specific databases
CMR	Search...
Phylogenomic databases
HOGENOM	HBG294308.
OMA	VMACKDD.
Enzyme and pathway databases
BioCyc	HHEP235279:HH_0449-MONOMER.
Family and domain databases
HAMAP	MF_01019. HisIE. [Tree]
InterPro	IPR023019. His_synth_HisIE. IPR008179. PRib-ATP_PPHydrolase. IPR021130. PRib-ATP_PPHydrolase-like. IPR002496. PRib_AMP_CycHydrolase. [Graphical view]
KO	K11755.
Pfam	PF01502. PRA-CH. 1 hit. PF01503. PRA-PH. 1 hit. [Graphical view]
ProDom	PD002610. PRA_CycHdrlase. 1 hit. [Graphical view] [Entries sharing at least one domain]
TIGRFAMs	TIGR03188. Histidine_hisI. 1 hit.
ProtoNet	Search...

Entry information

Entry name

HIS2_HELHP

Accession

Primary (citable) accession number: Q7VJ02

Entry history

Integrated into UniProtKB/Swiss-Prot:	March 15, 2004
Last sequence update:	October 1, 2003
Last modified:	January 25, 2012
This is version 56 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program