Skip Header

 
Contribute Send feedback
Read comments (0) or add your own

Reviewed, UniProtKB/Swiss-Prot Q7VD07 (HIS2_PROMA)

Last modified November 3, 2009. Version 39. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended 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: Pro_0582
OrganismProchlorococcus marinus [Complete proteome] [HAMAP]
Taxonomic identifier1219 [NCBI]
Taxonomic lineageBacteriaCyanobacteriaProchlorophytesProchlorococcaceaeProchlorococcus

Protein attributes

Sequence length226 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
Protein existenceInferred 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.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 226226Histidine biosynthesis bifunctional protein hisIE HAMAP MF_01019
PRO_0000136423

Regions

Region1 – 131131Phosphoribosyl-AMP cyclohydrolase HAMAP MF_01019
Region132 – 22695Phosphoribosyl-ATP pyrophosphohydrolase HAMAP MF_01019

Sequences

Sequence LengthMass (Da)Tools
Q7VD07-1 [UniParc].

Last modified October 1, 2003. Version 1.
Checksum: 9BEEC8B333134B2B

FASTA22626,026
        10         20         30         40         50         60 
MMPMNQEFIQ KLRFNEKGLI PAIAQDWLDG AILMMAWMNK ESLEKTLITG EVHYWSRSRE 

        70         80         90        100        110        120 
KLWHKGETSG HFQILKGIRF DCDSDVMLLS IEQVGSIACH TGARSCFFQE VEENIPDLEQ 

       130        140        150        160        170        180 
NSTFNRPLSN TCSELFEVIK DRSSNPQKNS YTNSLLKDGD NKILKKIGEE GSEFVMACKD 

       190        200        210        220 
NDHESISNEA ADLIFHIQVA LKYHKVEWRD VLEVLAKRRQ SKSNPK 

« Hide

References

[1]"Genome sequence of the cyanobacterium Prochlorococcus marinus SS120, a nearly minimal oxyphototrophic genome."
Dufresne A., Salanoubat M., Partensky F., Artiguenave F., Axmann I.M., Barbe V., Duprat S., Galperin M.Y., Koonin E.V., Le Gall F., Makarova K.S., Ostrowski M., Oztas S., Robert C., Rogozin I.B., Scanlan D.J., Tandeau de Marsac N., Weissenbach J. expand/collapse author list , Wincker P., Wolf Y.I., Hess W.R.
Proc. Natl. Acad. Sci. U.S.A. 100:10020-10025(2003) [PubMed: 12917486] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: SARG / CCMP1375 / SS120.

Cross-references

Sequence databases

AE017126 Genomic DNA. Translation: AAP99627.1.
RefSeqNP_874975.1.

3D structure databases

ModBaseSearch...

Genome annotation databases

GeneID1461964.
GenomeReviewsGene locus Pro_0582 in contig AE017126_GR.
KEGGpma:Pro0582.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMQ7VD07.
OMAVHYWSRS.

Enzyme and pathway databases

BioCycPMAR167539:PRO_0582-MON.
BRENDA3.5.4.19. 141456.
3.6.1.31. 141456.

Family and domain databases

HAMAPMF_01019.
[Tree]
InterProIPR002496. PRA_CycHdrlase.
IPR008179. PRib-ATP_pyrophosphohydrolase.
[Graphical view]
PfamPF01502. PRA-CH. 1 hit.
PF01503. PRA-PH. 1 hit.
[Graphical view]
ProDomPD002610. PRA_cyclohydro. 1 hit.
PD002611. Pra_PH/CH. 1 hit.
[Graphical view] [Entries sharing at least one domain]
TIGRFAMsTIGR03188. histidine_hisI. 1 hit.
ProtoNetSearch...

Entry information

Entry nameHIS2_PROMA
AccessionPrimary (citable) accession number: Q7VD07
Entry history
Integrated into UniProtKB/Swiss-Prot: March 15, 2004
Last sequence update: October 1, 2003
Last modified: November 3, 2009
This is version 39 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)

Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents