Reviewed, UniProtKB/Swiss-Prot Q8DM88 (HIS2_THEEB)

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:	tll0233

Organism

Thermosynechococcus elongatus (strain BP-1) [Complete proteome] [HAMAP]

Taxonomic identifier

197221 [NCBI]

Taxonomic lineage

Bacteria › Cyanobacteria › Chroococcales › Thermosynechococcus

Protein attributes

Sequence length	214 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 – 214	214	Histidine biosynthesis bifunctional protein hisIE HAMAP MF_01019		PRO_0000136438
Regions
	Region	1 – 125	125	Phosphoribosyl-AMP cyclohydrolase HAMAP MF_01019
	Region	126 – 214	89	Phosphoribosyl-ATP pyrophosphohydrolase HAMAP MF_01019

Sequences

	Sequence		Length	Mass (Da)
	Q8DM88-1 [UniParc]. Last modified March 1, 2003. Version 1. Checksum: C41BC7972DD9B89F	FASTA	214	24,440
	10 20 30 40 50 60 MPATALSLPL DEIRYDERGL VPAIVQDYLD GTVLMLAWMN RESLQKTLET GRTWFWSRSR 70 80 90 100 110 120 QELWPKGETS GHVQWVKSIR YDCDSDALLL TVEQVGHIAC HTGERSCFHR HGAKGESIEP 130 140 150 160 170 180 PPADTLSQVY NIVCQRRDFP QLQSYTSSLF TAGDNKILKK LGEETAEVVM ACKDDDPEAI 190 200 210 ASEVADLFYH TLVALAYHRV SLRQVYEQLQ LRRR

References

[1]

"Complete genome structure of the thermophilic cyanobacterium Thermosynechococcus elongatus BP-1." Nakamura Y., Kaneko T., Sato S., Ikeuchi M., Katoh H., Sasamoto S., Watanabe A., Iriguchi M., Kawashima K., Kimura T., Kishida Y., Kiyokawa C., Kohara M., Matsumoto M., Matsuno A., Nakazaki N., Shimpo S., Sugimoto M. , Takeuchi C., Yamada M., Tabata S. DNA Res. 9:123-130(2002) [PubMed: 12240834] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases
EMBLGenBankDDBJ	BA000039 Genomic DNA. Translation: BAC07786.1.
RefSeq	NP_681024.1.
3D structure databases
SMR	Q8DM88. Positions 20-110.
ModBase	Search...
Protein-protein interaction databases
STRING	Q8DM88.
Genome annotation databases
GeneID	1010550.
GenomeReviews	Gene locus tll0233 in contig BA000039_GR.
KEGG	tel:tll0233.
NMPDR	fig|197221.1.peg.233.
Organism-specific databases
CMR	Search...
Phylogenomic databases
HOGENOM	Q8DM88.
Enzyme and pathway databases
BioCyc	TELO197221:TLL0233-MON.
BRENDA	3.5.4.19. 277225. 3.6.1.31. 277225.
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_THEEB

Accession

Primary (citable) accession number: Q8DM88

Entry history

Integrated into UniProtKB/Swiss-Prot:	March 15, 2004
Last sequence update:	March 1, 2003
Last modified:	September 1, 2009
This is version 40 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)