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Q7U635 (HIS2_SYNPX) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 68. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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
OrganismSynechococcus sp. (strain WH8102) [Complete proteome] [HAMAP]
Taxonomic identifier84588 [NCBI]
Taxonomic lineageBacteriaCyanobacteriaOscillatoriophycideaeChroococcalesSynechococcus

Protein attributes

Sequence length222 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Catalytic activity

1-(5-phospho-beta-D-ribosyl)-ATP + H2O = 1-(5-phospho-beta-D-ribosyl)-AMP + diphosphate. HAMAP-Rule MF_01019

1-(5-phospho-beta-D-ribosyl)-AMP + H2O = 1-(5-phospho-beta-D-ribosyl)-5-((5-phospho-beta-D-ribosylamino)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 HAMAP-Rule 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 processAmino-acid biosynthesis
Histidine biosynthesis
   Cellular componentCytoplasm
   LigandATP-binding
Nucleotide-binding
   Molecular functionHydrolase
   Technical termComplete proteome
Multifunctional enzyme
Gene Ontology (GO)
   Biological_processhistidine biosynthetic process

Inferred from electronic annotation. Source: UniProtKB-HAMAP

   Cellular_componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionATP binding

Inferred from electronic annotation. Source: UniProtKB-KW

phosphoribosyl-AMP cyclohydrolase activity

Inferred from electronic annotation. Source: UniProtKB-HAMAP

phosphoribosyl-ATP diphosphatase activity

Inferred from electronic annotation. Source: UniProtKB-HAMAP

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 222222Histidine biosynthesis bifunctional protein HisIE HAMAP-Rule MF_01019
PRO_0000136439

Regions

Region1 – 128128Phosphoribosyl-AMP cyclohydrolase HAMAP-Rule MF_01019
Region129 – 22294Phosphoribosyl-ATP pyrophosphohydrolase HAMAP-Rule MF_01019

Sequences

Sequence LengthMass (Da)Tools
Q7U635 [UniParc].

Last modified October 1, 2003. Version 1.
Checksum: 36F5CDFBCB2251F5

FASTA22224,704
        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 

« Hide

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.
RefSeqNP_897598.1. NC_005070.1.

3D structure databases

ProteinModelPortalQ7U635.
SMRQ7U635. Positions 11-111.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING84588.SYNW1505.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaCAE08020; CAE08020; SYNW1505.
GeneID1730396.
KEGGsyw:SYNW1505.
PATRIC23834634. VBISynSp27240_1617.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0140.
HOGENOMHOG000277503.
KOK11755.
OMASITPDCD.
OrthoDBEOG6PGKB6.
ProtClustDBPRK02759.

Enzyme and pathway databases

UniPathwayUPA00031; UER00007.
UPA00031; UER00008.

Family and domain databases

HAMAPMF_01019. HisIE.
MF_01020. HisE.
MF_01021. HisI.
InterProIPR023019. His_synth_HisIE.
IPR026660. PRA-CH.
IPR008179. PRib-ATP_PPHydrolase.
IPR021130. PRib-ATP_PPHydrolase-like.
IPR002496. PRib_AMP_CycHydrolase_dom.
[Graphical view]
PfamPF01502. PRA-CH. 1 hit.
PF01503. PRA-PH. 1 hit.
[Graphical view]
ProDomPD002610. PRA_CycHdrlase. 1 hit.
[Graphical view] [Entries sharing at least one domain]
TIGRFAMsTIGR03188. histidine_hisI. 1 hit.
ProtoNetSearch...

Entry information

Entry nameHIS2_SYNPX
AccessionPrimary (citable) accession number: Q7U635
Entry history
Integrated into UniProtKB/Swiss-Prot: March 15, 2004
Last sequence update: October 1, 2003
Last modified: February 19, 2014
This is version 68 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways