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UniProtKB/Swiss-Prot entry Q9PM76

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

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Entry information
Entry name HIS7_CAMJE
Primary accession number Q9PM76
Secondary accession number Q0P829
Integrated into Swiss-Prot on June 24, 2002
Sequence was last modified on October 1, 2000 (Sequence version 1)
Annotations were last modified on    November 4, 2008 (Entry version 45)
Name and origin of the protein
Protein name Histidine biosynthesis bifunctional protein hisB
Synonyms None
Includes Histidinol-phosphatase
     (EC 3.1.3.15)
Imidazoleglycerol-phosphate dehydratase
     (IGPD)
     (EC 4.2.1.19)
Gene name
Name: hisB
OrderedLocusNames: Cj1599
From
Campylobacter jejuni [TaxID: 197] [HAMAP proteome]
Taxonomy Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales; Campylobacteraceae; Campylobacter.
Protein existence 3: Inferred from homology;
References
[1]
 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=NCTC 11168 / Serotype O:2;
DOI=10.1038/35001088; PubMed=10688204 [NCBI, ExPASy, EBI, Israel, Japan]
Parkhill J., Wren B.W., Mungall K.L., Ketley J.M., Churcher C.M., Basham D., Chillingworth T., Davies R.M., Feltwell T., Holroyd S., Jagels K., Karlyshev A.V., Moule S., Pallen M.J., Penn C.W., Quail M.A., Rajandream M.A., Rutherford K.M., van Vliet A.H.M., Whitehead S., Barrell B.G.;
"The genome sequence of the food-borne pathogen Campylobacter jejuni reveals hypervariable sequences.";
Nature 403:665-668(2000).
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
AL111168; CAL35696.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
PIR E81255; E81255.
3D structure databases
ModBase Q9PM76.
Protein-protein interaction databases
IntAct Q9PM76; -.
Enzyme and pathway databases
BioCyc CJEJ192222:CJ1599-MON; -.
Ontologies
GO
GO:0005737; Cellular component: cytoplasm (inferred from electronic annotation from HAMAP).
GO:0004401; Molecular function: histidinol-phosphatase activity (inferred from electronic annotation from HAMAP).
GO:0004424; Molecular function: imidazoleglycerol-phosphate dehydratase 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_01022; -; 1.
PBIL [Tree]
InterPro IPR006549; HAD-SF_hydro_IIIA.
IPR005954; HisB_N.
IPR006543; Histidinol-phos.
IPR000807; Imidazole_glycer-P_deHydtase.
IPR013954; PNK3P_central-region.
Graphical view of domain structure.
PANTHER PTHR23133:SF2; Imidazole-GPD; 1.
Pfam PF00475; IGPD; 1.
PF08645; PNK3P; 1.
Pfam graphical view of domain structure.
ProDom PD002282; IGPD; 1.
[Domain structure / List of seq. sharing at least 1 domain]
TIGRFAMs TIGR01662; HAD-SF-IIIA; 1.
TIGR01261; hisB_Nterm; 1.
TIGR01656; Histidinol-ppas; 1.
PROSITE PS00954; IGP_DEHYDRATASE_1; 1.
PS00955; IGP_DEHYDRATASE_2; 1.
ProtoNet Q9PM76.
Genome annotation databases
GenomeReviews AL111168_GR; Cj1599.
KEGG cje:Cj1599; -.
CMR Q9PM76; Cj1599.
Other
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
Amino-acid biosynthesis; Complete proteome; Cytoplasm; Histidine biosynthesis; Hydrolase; Lyase; Multifunctional enzyme.
Features
SEVIEWER logo Feature table viewer FT aligner logo Feature aligner
KeyFrom   To Length Description FTId
CHAIN   1   352  352     Histidine biosynthesis bifunctional protein hisB. PRO_0000158204
REGION   1   164  164     Histidinol-phosphatase. 
REGION   165   352  188     Imidazoleglycerol-phosphate dehydratase. 
Sequence information
Length: 352 AA [This is the length of the unprocessed precursor] Molecular weight: 39580 Da [This is the MW of the unprocessed precursor] CRC64: 522FDD31CC01A656 [This is a checksum on the sequence] 
        10         20         30         40         50         60 
MSQKILFIDR DGTLIEEPKS DFQIDTLEKL RFEKDAIPTL LKLKKFGFKF VMVSNQDGLG 

        70         80         90        100        110        120 
TPSFPKENFE IAHEKMLDIL KSCGIEFQDI FICPHFENEN CACRKPKTAM LEEYIKHELY 

       130        140        150        160        170        180 
DKEQSFVIGD RESDMILASN LGVRGLKYGE LSWKEIENEI LSSFRSASYQ RTTKETDIKV 

       190        200        210        220        230        240 
KVCLNGGKVS IKTGIDFFDH MLEQIAVHGG IGLEISCKGD LEIDEHHSVE DVALALGACI 

       250        260        270        280        290        300 
KKALGDKIGI ARYGFALPMD ECLASCAMDF CNRPHLVYKA KFKKSHLGAL STEMIEHFFY 

       310        320        330        340        350 
SLSYAMGVSL HLKVKGKNDH HKAEGLFKAF AKALKMAVKI ESENLASSKG VI
Q9PM76 in FASTA format

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