Reviewed, UniProtKB/Swiss-Prot P44434 (HIS2_HAEIN)

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:	HI0475

Organism

Haemophilus influenzae [Complete proteome] [HAMAP]

Taxonomic identifier

727 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Pasteurellales › Pasteurellaceae › Haemophilus

Protein attributes

Sequence length	221 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	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 – 221	221	Histidine biosynthesis bifunctional protein hisIE HAMAP MF_01019		PRO_0000136415
Regions
	Region	1 – 121	121	Phosphoribosyl-AMP cyclohydrolase HAMAP MF_01019
	Region	122 – 221	100	Phosphoribosyl-ATP pyrophosphohydrolase HAMAP MF_01019

Sequences

	Sequence		Length	Mass (Da)
	P44434-1 [UniParc]. Last modified November 1, 1995. Version 1. Checksum: C79C7B68E297B529	FASTA	221	25,097
	10 20 30 40 50 60 MNITKIDWQK VNGLLPVIIQ NISTREVLML GYMNEEALTK TIKERKVTFF SRTKQRLWTK 70 80 90 100 110 120 GEISGNFLNV EEMSLDCDND TLLILVDPIG ATCHTGEYSC FHQFTSPQSE NKKQQFANWA 130 140 150 160 170 180 WFIKLEQHLK EKKNADPSNS YTATLHAKGT KKIAQKVGEE GVETALAAVA QDKAEVISEA 190 200 210 220 TDLVYHLTVL LHNQDLQWYE IIAKLQERHQ GIGLHPEGGN K

References

[1]

"Whole-genome random sequencing and assembly of Haemophilus influenzae Rd." Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., Scott J.D., Shirley R., Liu L.-I. , Glodek A., Kelley J.M., Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., Venter J.C. Science 269:496-512(1995) [PubMed: 7542800] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 51907 / DSM 11121 / KW20 / Rd.

Cross-references

Sequence databases
EMBLGenBankDDBJ	L42023 Genomic DNA. Translation: AAC22134.1.
PIR	A64071.
RefSeq	NP_438636.1.
3D structure databases
ModBase	Search...
Genome annotation databases
GeneID	949566.
GenomeReviews	Gene locus HI0475 in contig L42023_GR.
KEGG	hin:HI0475.
TIGR	HI0475.
Phylogenomic databases
HOGENOM	P44434.
OMA	P44434. VHYWSRS.
Enzyme and pathway databases
BioCyc	HINF71421:HI_0475-MON.
BRENDA	3.5.4.19. 109. 3.6.1.31. 109.
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_HAEIN

Accession

Primary (citable) accession number: P44434

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 1995
Last sequence update:	November 1, 1995
Last modified:	June 16, 2009
This is version 61 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)