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UniProtKB/Swiss-Prot entry Q7TUC7


[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

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Entry information
Entry name HIS2_PROMP
Primary accession number Q7TUC7
Secondary accession numbers None
Integrated into Swiss-Prot on March 15, 2004
Sequence was last modified on October 1, 2003 (Sequence version 1)
Annotations were last modified on    July 22, 2008 (Entry version 33)
Name and origin of the protein
Protein name Histidine biosynthesis bifunctional protein hisIE
Synonyms None
Includes Phosphoribosyl-AMP cyclohydrolase
     (PRA-CH)
     (EC 3.5.4.19)
Phosphoribosyl-ATP pyrophosphatase
     (PRA-PH)
     (EC 3.6.1.31)
Gene name
Name: hisI
Synonyms: hisIE
OrderedLocusNames: PMM0578
From
Prochlorococcus marinus subsp. pastoris (strain CCMP1378 / MED4) [TaxID: 59919] [HAMAP proteome]
Taxonomy Bacteria; Cyanobacteria; Prochlorales; Prochlorococcaceae; Prochlorococcus.
Protein existence 3: Inferred from homology;
References
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
DOI=10.1038/nature01947; PubMed=12917642 [NCBI, ExPASy, EBI, Israel, Japan]
Rocap G., Larimer F.W., Lamerdin J.E., Malfatti S., Chain P., Ahlgren N.A., Arellano A., Coleman M., Hauser L., Hess W.R., Johnson Z.I., Land M.L., Lindell D., Post A.F., Regala W., Shah M., Shaw S.L., Steglich C., Sullivan M.B., Ting C.S., Tolonen A., Webb E.A., Zinser E.R., Chisholm S.W.;
"Genome divergence in two Prochlorococcus ecotypes reflects oceanic niche differentiation.";
Nature 424:1042-1047(2003).
Comments
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
Sequence databases
EMBL
BX548174; CAE19037.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
RefSeq NP_892696.1; -.
3D structure databases
ModBase Q7TUC7.
Enzyme and pathway databases
BioCyc PMAR167540:PMM0578-MON; -.
Ontologies
GO
GO:0005737; Cellular component: cytoplasm (inferred from electronic annotation from HAMAP).
GO:0004635; Molecular function: phosphoribosyl-AMP cyclohydrolase activity (inferred from electronic annotation from HAMAP).
GO:0004636; Molecular function: phosphoribosyl-ATP diphosphatase activity (inferred from electronic annotation from HAMAP).
GO:0000105; Biological process: histidine biosynthetic process (inferred from electronic annotation from HAMAP).
QuickGo view.
Family and domain databases
HAMAP MF_01019; -; 1.
PBIL [Tree]
InterPro IPR002496; PRA_CycOHase.
IPR008179; PRib-ATP_pyrophosphohydrolase.
Graphical view of domain structure.
Pfam PF01502; PRA-CH; 1.
PF01503; PRA-PH; 1.
Pfam graphical view of domain structure.
ProDom PD002610; PRA_cyclohydro; 1.
PD002611; Pra_PH/CH; 1.
[Domain structure / List of seq. sharing at least 1 domain]
TIGRFAMs TIGR03188; histidine_hisI; 1.
BLOCKS Q7TUC7.
ProtoNet Q7TUC7.
Genome annotation databases
GeneID 1726317; -.
GenomeReviews BX548174_GR; PMM0578.
KEGG pmm:PMM0578; -.
NMPDR fig|59919.1.peg.575; -.
Phylogenomic databases
HOGENOM Q7TUC7; -.
Genome annotation databases
CMR Q7TUC7; PMM0578.
Other
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
Amino-acid biosynthesis; Complete proteome; Cytoplasm; Histidine biosynthesis; Hydrolase; Multifunctional enzyme.
Features
SEVIEWER logo Feature table viewer FT aligner logo Feature aligner
KeyFrom   To Length Description FTId
CHAIN   1   221  221     Histidine biosynthesis bifunctional protein hisIE. PRO_0000136425
REGION   1   129  129     Phosphoribosyl-AMP cyclohydrolase. 
REGION   130   221  92     Phosphoribosyl-ATP pyrophosphohydrolase. 
Sequence information
Length: 221 AA [This is the length of the unprocessed precursor] Molecular weight: 25197 Da [This is the MW of the unprocessed precursor] CRC64: E7E3F7C964AE14C6 [This is a checksum on the sequence]
        10         20         30         40         50         60 
MAYSKNFSIE ELRFDNKGLI PAIAQDWLDG SILMLAWMNK ESLNKTLETR NVHYWSRSRS 

        70         80         90        100        110        120 
EIWRKGATSG STQFLKEIRF DCDNDALVLS IEQNGSGACH TGEKSCFFNE IDSISMNKTA 

       130        140        150        160        170        180 
KKTSPFSNIC SELFDTLHER SINPLEKSYT NHLLTKGSNT ILKKIGEETA EFIMACKDND 

       190        200        210        220 
KDEIANEASD IIYHLQVALI YKGVKWRDVL NVLESRRGKN N 

Q7TUC7 in FASTA format

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BLAST logo BLAST submission on ExPASy/SIB
or at NCBI (USA)
Tools Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
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NPSA logo NPSA Sequence analysis tools

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