Reviewed, UniProtKB/Swiss-Prot O24714 (HIS2_KLEPN)

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

Klebsiella pneumoniae

Taxonomic identifier

573 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Klebsiella

Protein attributes

Sequence length	198 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 – 198	198	Histidine biosynthesis bifunctional protein hisIE HAMAP MF_01019		PRO_0000136417
Regions
	Region	1 – 110	110	Phosphoribosyl-AMP cyclohydrolase HAMAP MF_01019
	Region	111 – 198	88	Phosphoribosyl-ATP pyrophosphohydrolase HAMAP MF_01019

Sequences

	Sequence		Length	Mass (Da)
	O24714-1 [UniParc]. Last modified January 1, 1998. Version 1. Checksum: 3762428287C25D00	FASTA	198	22,046
	10 20 30 40 50 60 MLTEQLDWEK TDGMMPAIVQ HAVSGEVLML GYMNKEALEK TEATGKVTFY SRTKQRLWTK 70 80 90 100 110 120 GETSGNVLNV VSITPDCDND TLLVLVNPIG PTCHKGTTSC FGETGHQWLF LYQLEQLLAE 130 140 150 160 170 180 RKHADPESSY TAKLYASGTK RIAQKVGEEG VETALAATVN DRFELKNEAS DLMYHLLVLL 190 QDQGLDLGEV IDNLKSRH

References

[1]

"Evolutionary relationship among rfb gene clusters synthesizing mannose homopolymer as O-specific polysaccharides in Escherichia coli and Klebsiella." Sugiyama T., Kido N., Kato Y., Koide N., Yoshida T., Yokochi T. Gene 198:111-113(1997) [PubMed: 9370271] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: K53 / Serotype O3.

Cross-references

Sequence databases
EMBLGenBankDDBJ	AB000126 Genomic DNA. Translation: BAA23229.1.
3D structure databases
ModBase	Search...
Enzyme and pathway databases
BRENDA	3.5.4.19. 758. 3.6.1.31. 758.
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_KLEPN

Accession

Primary (citable) accession number: O24714

Entry history

Integrated into UniProtKB/Swiss-Prot:	December 15, 1998
Last sequence update:	January 1, 1998
Last modified:	June 16, 2009
This is version 53 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)