Reviewed, UniProtKB/Swiss-Prot Q8ZFY1 (HIS2_YERPE)

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:	YPO1542, y2628, YP_1431

Organism

Yersinia pestis [Complete proteome] [HAMAP]

Taxonomic identifier

632 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Yersinia

Protein attributes

Sequence length	204 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: 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 – 204	204	Histidine biosynthesis bifunctional protein hisIE HAMAP MF_01019		PRO_0000136454
Regions
	Region	1 – 114	114	Phosphoribosyl-AMP cyclohydrolase HAMAP MF_01019
	Region	115 – 204	90	Phosphoribosyl-ATP pyrophosphohydrolase HAMAP MF_01019

Sequences

	Sequence		Length	Mass (Da)
	Q8ZFY1-1 [UniParc]. Last modified March 1, 2002. Version 1. Checksum: BF3328DF1C0A8C79	FASTA	204	22,807
	10 20 30 40 50 60 MLTEQQINQL DWEKVDHLMP AIVQHAVSGE VLMMGYMNQE ALAVTEKTGK VTFFSRTKQR 70 80 90 100 110 120 LWTKGESSGH FLNVVNIYPD CDNDTLLILV KPIGPTCHLG NSSCFAPAAS DWSFLYQLEQ 130 140 150 160 170 180 LLASRKSADP ASSYTAKLYA SGTKRIAQKV GEEGVETALA ATVNDREELT NEASDLMYHL 190 200 LVLLQDQDLD FSTVIGRLRE RHEK

References

[1]	"Genome sequence of Yersinia pestis, the causative agent of plague." Parkhill J., Wren B.W., Thomson N.R., Titball R.W., Holden M.T.G., Prentice M.B., Sebaihia M., James K.D., Churcher C.M., Mungall K.L., Baker S., Basham D., Bentley S.D., Brooks K., Cerdeno-Tarraga A.-M., Chillingworth T., Cronin A., Davies R.M. , Davis P., Dougan G., Feltwell T., Hamlin N., Holroyd S., Jagels K., Karlyshev A.V., Leather S., Moule S., Oyston P.C.F., Quail M.A., Rutherford K.M., Simmonds M., Skelton J., Stevens K., Whitehead S., Barrell B.G. Nature 413:523-527(2001) [PubMed: 11586360] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: CO-92 / Biovar Orientalis.
[2]	"Genome sequence of Yersinia pestis KIM." Deng W., Burland V., Plunkett G. III, Boutin A., Mayhew G.F., Liss P., Perna N.T., Rose D.J., Mau B., Zhou S., Schwartz D.C., Fetherston J.D., Lindler L.E., Brubaker R.R., Plano G.V., Straley S.C., McDonough K.A., Nilles M.L. , Matson J.S., Blattner F.R., Perry R.D. J. Bacteriol. 184:4601-4611(2002) [PubMed: 12142430] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: KIM5 / Biovar Mediaevalis.
[3]	"Complete genome sequence of Yersinia pestis strain 91001, an isolate avirulent to humans." Song Y., Tong Z., Wang J., Wang L., Guo Z., Han Y., Zhang J., Pei D., Zhou D., Qin H., Pang X., Han Y., Zhai J., Li M., Cui B., Qi Z., Jin L., Dai R. , Chen F., Li S., Ye C., Du Z., Lin W., Wang J., Yu J., Yang H., Wang J., Huang P., Yang R. DNA Res. 11:179-197(2004) [PubMed: 15368893] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: 91001 / Biovar Mediaevalis.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AL590842 Genomic DNA. Translation: CAL20188.1. AE009952 Genomic DNA. Translation: AAM86182.1. AE017042 Genomic DNA. Translation: AAS61672.1.
PIR	AB0188.
RefSeq	NP_669931.1. NP_992795.1. YP_002346558.1.
3D structure databases
SMR	Q8ZFY1. Positions 15-109, 114-203.
ModBase	Search...
Genome annotation databases
GeneID	1147575. 1174381. 2765682.
GenomeReviews	Gene locus y2628 in contig AE009952_GR. Gene locus YP_1431 in contig AE017042_GR. Gene locus YPO1542 in contig AL590842_GR.
KEGG	ype:YPO1542. ypk:y2628. ypm:YP_1431.
Organism-specific databases
CMR	Search...
Phylogenomic databases
HOGENOM	HBG294308.
OMA	VHYWSRS.
Enzyme and pathway databases
BioCyc	YPES187410:Y2628-MONOMER. YPES214092:YPO1542-MONOMER. YPES229193:YP1431-MONOMER.
BRENDA	3.5.4.19. 142588. 3.6.1.31. 142588.
Family and domain databases
HAMAP	MF_01019. HisIE. [Tree]
InterPro	IPR002496. PRA_CycHdrlase. IPR008179. PRib-ATP_pyrophosphohydrolase. IPR021130. PRib-ATP_pyroPHydrolase-like. [Graphical view]
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_YERPE

Accession

Primary (citable) accession number: Q8ZFY1
Secondary accession number(s): Q0WGN0

Entry history

Integrated into UniProtKB/Swiss-Prot:	June 6, 2002
Last sequence update:	March 1, 2002
Last modified:	February 9, 2010
This is version 64 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)