Reviewed, UniProtKB/Swiss-Prot Q9RPQ3 (HIS2_THEP3)

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

Organism

Thermoanaerobacter pseudethanolicus (strain ATCC 33223 / 39E) (Clostridium thermohydrosulfuricum)

Taxonomic identifier

340099 [NCBI]

Taxonomic lineage

Bacteria › Firmicutes › Clostridia › Thermoanaerobacterales › Thermoanaerobacteriaceae › Thermoanaerobacter

Protein attributes

Sequence length	216 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	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 – 216	216	Histidine biosynthesis bifunctional protein hisIE HAMAP MF_01019		PRO_0000136441
Regions
	Region	1 – 132	132	Phosphoribosyl-AMP cyclohydrolase HAMAP MF_01019
	Region	133 – 216	84	Phosphoribosyl-ATP pyrophosphohydrolase HAMAP MF_01019

Sequences

	Sequence		Length	Mass (Da)
	Q9RPQ3-1 [UniParc]. Last modified May 1, 2000. Version 1. Checksum: 1230E351B36C35D5	FASTA	216	25,005
	10 20 30 40 50 60 MENILKELKF DDRGLIPVIT QDYKTNEVLM MAYIMKRPLK KSLETGKVHY FSRSRNKLWL 70 80 90 100 110 120 KGETSGHFQL IKSISIDCDA DTLLIKVEQV EAACHTGHYS CFYREISGNE LKETSDKVFD 130 140 150 160 170 180 EQKVYEAENA KILQEIYDVI VDRTIHPKEG SYTNYLFEKG LDKILKKVGE EAAEVIIGAK 190 200 210 NRDKGEIVYE ISDLIYHLLV LMVERGIKLE DIYEEA

References

[1]	"Organization and sequence of histidine biosynthesis genes hisH, -A, -F, and -IE in Thermoanaerobacter ethanolicus." Erbeznik M., Strobel H.J., Dawson K.A. Curr. Microbiol. 40:140-142(2000) [PubMed: 10594232] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].

Cross-references

Sequence databases
EMBLGenBankDDBJ	AF150930 Genomic DNA. Translation: AAF05095.1.
3D structure databases
ModBase	Search...
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_THEP3

Accession

Primary (citable) accession number: Q9RPQ3

Entry history

Integrated into UniProtKB/Swiss-Prot:	June 6, 2002
Last sequence update:	May 1, 2000
Last modified:	June 16, 2009
This is version 44 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)