Q9CLL8 (HIS2_PASMU) 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:	PM1206

Organism

Pasteurella multocida (strain Pm70) [Complete proteome] [HAMAP]

Taxonomic identifier

272843 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Pasteurellales › Pasteurellaceae › Pasteurella

Protein attributes

Sequence length	201 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: 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 – 201	201	Histidine biosynthesis bifunctional protein HisIE HAMAP MF_01019		PRO_0000136420
Regions
	Region	1 – 111	111	Phosphoribosyl-AMP cyclohydrolase HAMAP MF_01019
	Region	112 – 201	90	Phosphoribosyl-ATP pyrophosphohydrolase HAMAP MF_01019

Sequences

	Sequence		Length	Mass (Da)
	Q9CLL8 [UniParc]. Last modified June 1, 2001. Version 1. Checksum: 64420D0F0152FB82	FASTA	201	22,697
	10 20 30 40 50 60 MKINWQKVDN LLPVIIQNVA TCEVLMLGYM NQEALEKTLA EKRVTFFSRT KNRLWTKGET 70 80 90 100 110 120 SGHFLNVVDM SLDCDNDTLL ILVNPIGETC HTGAESCFYQ FEKTTQPDWI FLSKLERLIA 130 140 150 160 170 180 SRKGADPESS YTAQLYAKGT KRIAQKVGEE GVETALAATV KDKAETICEA ADLVYHLTVL 190 200 LQDADLSWSD VIHKLKERHT K

References

[1]	"Complete genomic sequence of Pasteurella multocida Pm70." May B.J., Zhang Q., Li L.L., Paustian M.L., Whittam T.S., Kapur V. Proc. Natl. Acad. Sci. U.S.A. 98:3460-3465(2001) [PubMed: 11248100] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: Pm70.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AE004439 Genomic DNA. Translation: AAK03290.1.
RefSeq	NP_246143.1. NC_002663.1.
3D structure databases
ProteinModelPortal	Q9CLL8.
ModBase	Search...
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	1244553.
GenomeReviews	Gene locus PM1206 in contig AE004439_GR.
KEGG	pmu:PM1206.
NMPDR	fig|272843.1.peg.1206.
PATRIC	22871663. VBIPasMul88067_1216.
Organism-specific databases
CMR	Search...
Phylogenomic databases
HOGENOM	HBG294308.
OMA	VMACKDD.
ProtClustDB	CLSK2517342.
Enzyme and pathway databases
BioCyc	PMUL272843:PM1206-MONOMER.
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_PASMU

Accession

Primary (citable) accession number: Q9CLL8

Entry history

Integrated into UniProtKB/Swiss-Prot:	June 6, 2002
Last sequence update:	June 1, 2001
Last modified:	January 25, 2012
This is version 60 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program