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UniProtKB/Swiss-Prot entry Q9PM77

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

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Entry information
Entry name HISX_CAMJE
Primary accession number Q9PM77
Secondary accession number Q0P830
Integrated into Swiss-Prot on March 25, 2003
Sequence was last modified on October 1, 2000 (Sequence version 1)
Annotations were last modified on    July 22, 2008 (Entry version 45)
Name and origin of the protein
Protein name Histidinol dehydrogenase
Synonyms HDH
EC 1.1.1.23
Gene name
Name: hisD
OrderedLocusNames: Cj1598
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; CAL35695.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
PIR D81255; D81255.
3D structure databases
HSSP P06988; 1K75. [HSSP ENTRY / PDB]
ModBase Q9PM77.
Enzyme and pathway databases
BioCyc CJEJ192222:CJ1598-MON; -.
Ontologies
GO
GO:0004399; Molecular function: histidinol dehydrogenase 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_01024; -; 1.
PBIL [Tree]
InterPro IPR001692; Histidinol_DHase.
IPR012131; Hstdl_DHase_prok.
Graphical view of domain structure.
PANTHER PTHR21256:SF2; Hstdl_DH_prok; 1.
Pfam PF00815; Histidinol_dh; 1.
Pfam graphical view of domain structure.
PRINTS PR00083; HOLDHDRGNASE.
ProDom PD002680; Histidinol_dh; 1.
[Domain structure / List of seq. sharing at least 1 domain]
TIGRFAMs TIGR00069; hisD; 1.
PROSITE PS00611; HISOL_DEHYDROGENASE; 1.
BLOCKS Q9PM77.
Genome annotation databases
GenomeReviews AL111168_GR; Cj1598.
KEGG cje:Cj1598; -.
CMR Q9PM77; Cj1598.
Other
ProtoNet Q9PM77.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
Amino-acid biosynthesis; Complete proteome; Histidine biosynthesis; Metal-binding; NAD; Oxidoreductase; Zinc.
Features
SEVIEWER logo Feature table viewer
KeyFrom   To Length Description FTId
CHAIN   1   428  428     Histidinol dehydrogenase. PRO_0000135751
ACT_SITE   323   323        Proton acceptor (By similarity). 
ACT_SITE   324   324        Proton acceptor (By similarity). 
METAL   256   256        Zinc (By similarity). 
METAL   259   259        Zinc (By similarity). 
METAL   357   357        Zinc (By similarity). 
METAL   416   416        Zinc (By similarity). 
BINDING   234   234        Substrate (By similarity). 
BINDING   256   256        Substrate (By similarity). 
BINDING   259   259        Substrate (By similarity). 
BINDING   324   324        Substrate (By similarity). 
BINDING   357   357        Substrate (By similarity). 
BINDING   411   411        Substrate (By similarity). 
BINDING   416   416        Substrate (By similarity). 
Sequence information
Length: 428 AA [This is the length of the unprocessed precursor] Molecular weight: 46446 Da [This is the MW of the unprocessed precursor] CRC64: 16F08561BF7DB738 [This is a checksum on the sequence] 
        10         20         30         40         50         60 
MQILVYDNLD EKQKEEALKR PAISAKDEIS KIVSSIIKEV QEKGDKALIE QALKFDKAEI 

        70         80         90        100        110        120 
SKIKITQEEI TQASNRLDKD LQEAILVAYE NIKKFHEAQI PHEIALETTK GVKCEVLTRP 

       130        140        150        160        170        180 
IEKVGLYIPG GLAPLFSTVL MLAIPAKIAG CEKIVLASPA KINDAVLFCA KLCGVDEIYQ 

       190        200        210        220        230        240 
MGGAGAIAAL TYGTQSVLKV DKIFGPGNAF VTEAKRQVSS DINGAAIDMQ AGPSEVLVIA 

       250        260        270        280        290        300 
DDLANEKFVA SDLLSQAEHG ADSQVILVCL SQDFAKKASD EVQSQLELLP RKELASKSIA 

       310        320        330        340        350        360 
NSRIIIAKDL NQALEISNLY APEHLIIQTQ NPRELLKGVK HAGSVFLGAY SPESMGDYAS 

       370        380        390        400        410        420 
GTNHVLPTYG LTKTHSSLGL ADFSKRMTVQ ELSKEGFLAL GKSVEILAQN EHLDAHKNAV 


TFRLESLK
Q9PM77 in FASTA format

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