P58853 (HIS2_PYRFU) 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:	PF1664

Organism

Pyrococcus furiosus (strain ATCC 43587 / DSM 3638 / JCM 8422 / Vc1)

Taxonomic identifier

186497 [NCBI]

Taxonomic lineage

Archaea › Euryarchaeota › Thermococci › Thermococcales › Thermococcaceae › Pyrococcus

Protein attributes

Sequence length	209 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.
Sequence caution	The sequence AAL81788.1 differs from that shown. Reason: Erroneous initiation.

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 Reference proteome
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 – 209	209	Histidine biosynthesis bifunctional protein HisIE HAMAP MF_01019		PRO_0000136455
Regions
	Region	1 – 123	123	Phosphoribosyl-AMP cyclohydrolase HAMAP MF_01019
	Region	124 – 209	86	Phosphoribosyl-ATP pyrophosphohydrolase HAMAP MF_01019

Sequences

	Sequence		Length	Mass (Da)
	P58853 [UniParc]. Last modified June 6, 2002. Version 1. Checksum: E7F1BF99CCF2C5E8	FASTA	209	24,236
	10 20 30 40 50 60 MEIEKLLEQV NWEKNNGIVP VIVQDEKGEV LTLAYMNKEA LRKTLETGIA HYYSRSKGRI 70 80 90 100 110 120 RMKGEVSGNI QTVKEIKIDC DNDALLLIVS PKGPACHTGN YSCFYRKLGE PERVLPIDYS 130 140 150 160 170 180 LSILKELEEI IKRRKETPVE GSYTSKLFKE GREKIYKKFG EEAIEVLVAE KRERIIYEVA 190 200 DLLYHLLVLL TYNDISLGEV MNELRRRRK

References

[1]

"Divergence of the hyperthermophilic archaea Pyrococcus furiosus and P. horikoshii inferred from complete genomic sequences." Maeder D.L., Weiss R.B., Dunn D.M., Cherry J.L., Gonzalez J.M., DiRuggiero J., Robb F.T. Genetics 152:1299-1305(1999) [PubMed: 10430560] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 43587 / DSM 3638 / JCM 8422 / Vc1.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AE009950 Genomic DNA. Translation: AAL81788.1. Different initiation.
RefSeq	NP_579393.1. NC_003413.1.
3D structure databases
ProteinModelPortal	P58853.
ModBase	Search...
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	EBPYRT00000004715; EBPYRP00000004576; EBPYRG00000004715.
GeneID	1469541.
GenomeReviews	Gene locus PF1664 in contig AE009950_GR.
KEGG	pfu:PF1664.
NMPDR	fig|186497.1.peg.1712.
Phylogenomic databases
GeneTree	EBGT00050000023414.
HOGENOM	HBG294308.
OMA	VMACKDD.
PhylomeDB	P58853.
ProtClustDB	PRK02759.
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_PYRFU

Accession

Primary (citable) accession number: P58853

Entry history

Integrated into UniProtKB/Swiss-Prot:	June 6, 2002
Last sequence update:	June 6, 2002
Last modified:	December 14, 2011
This is version 61 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program