Q7U635 (HIS2_SYNPX) 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:	SYNW1505

Organism

Synechococcus sp. (strain WH8102) [Complete proteome] [HAMAP]

Taxonomic identifier

84588 [NCBI]

Taxonomic lineage

cellular organisms › Bacteria › Cyanobacteria › Oscillatoriophycideae › Chroococcales › Synechococcus

Protein attributes

Sequence length	222 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-Rule MF_01019 1-(5-phosphoribosyl)-AMP + H2O = 1-(5-phosphoribosyl)-5-((5-phosphoribosylamino)methylideneamino)imidazole-4-carboxamide. HAMAP-Rule MF_01019
Pathway	Amino-acid biosynthesis; L-histidine biosynthesis; L-histidine from 5-phospho-alpha-D-ribose 1-diphosphate: step 2/9. HAMAP-Rule 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: UniProtKB-UniPathway
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 – 222	222	Histidine biosynthesis bifunctional protein HisIE HAMAP-Rule MF_01019		PRO_0000136439
Regions
	Region	1 – 128	128	Phosphoribosyl-AMP cyclohydrolase HAMAP-Rule MF_01019
	Region	129 – 222	94	Phosphoribosyl-ATP pyrophosphohydrolase HAMAP-Rule MF_01019

Sequences

	Sequence		Length	Mass (Da)
	Q7U635 [UniParc]. Last modified October 1, 2003. Version 1. Checksum: 36F5CDFBCB2251F5	FASTA	222	24,704
	10 20 30 40 50 60 MQPLSPAFID QLRFNEAGLI PAIAQDWLDG AVLMVAWMNR ESIQQTLNSG EAHYWSRSRQ 70 80 90 100 110 120 ELWHKGATSG HTQTLRSIRY DCDADVLLLT IEQRGDIACH TGARSCFYEG GDQRSDGGSN 130 140 150 160 170 180 ALSPPADACT ELFRVIESRR DNPEEGSYTN KLLEGGDNKI LKKIGEESAE FVMACKDDNP 190 200 210 220 EEIAGEAADI LFHMQVALAH HGVSWRQVQE VLAARRGAPR RH

References

[1]

"The genome of a motile marine Synechococcus." Palenik B., Brahamsha B., Larimer F.W., Land M.L., Hauser L., Chain P., Lamerdin J.E., Regala W., Allen E.E., McCarren J., Paulsen I.T., Dufresne A., Partensky F., Webb E.A., Waterbury J. Nature 424:1037-1042(2003) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: WH8102.

Cross-references

Sequence databases
EMBL GenBank DDBJ	BX569693 Genomic DNA. Translation: CAE08020.1.
RefSeq	NP_897598.1. NC_005070.1.
3D structure databases
ProteinModelPortal	Q7U635.
SMR	Q7U635. Positions 11-111.
ModBase	Search...
Protein-protein interaction databases
STRING	84588.SYNW1505.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	CAE08020; CAE08020; SYNW1505.
GeneID	1730396.
KEGG	syw:SYNW1505.
PATRIC	23834634. VBISynSp27240_1617.
Organism-specific databases
CMR	Search...
Phylogenomic databases
eggNOG	COG0140.
HOGENOM	HOG000277503.
KO	K11755.
OMA	SITPDCD.
ProtClustDB	PRK02759.
Enzyme and pathway databases
UniPathway	UPA00031; UER00007. UPA00031; UER00008.
Family and domain databases
HAMAP	MF_01019. HisIE.
InterPro	IPR023019. His_synth_HisIE. IPR026660. PRA-CH. IPR008179. PRib-ATP_PPHydrolase. IPR021130. PRib-ATP_PPHydrolase-like. IPR002496. PRib_AMP_CycHydrolase_dom. [Graphical view]
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_SYNPX

Accession

Primary (citable) accession number: Q7U635

Entry history

Integrated into UniProtKB/Swiss-Prot:	March 15, 2004
Last sequence update:	October 1, 2003
Last modified:	May 1, 2013
This is version 64 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program