ExPASy logo ExPASy Home page Site Map Search ExPASy Contact us Swiss-Prot
Notice: This page will be replaced with www.uniprot.org. Please send us your feedback!
Search for

UniProtKB/Swiss-Prot entry Q5HSJ3

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

Note: most headings are clickable, even if they don't appear as links. They link to the user manual or other documents.
Entry information
Entry name HISX_CAMJR
Primary accession number Q5HSJ3
Secondary accession numbers None
Integrated into Swiss-Prot on January 10, 2006
Sequence was last modified on February 15, 2005 (Sequence version 1)
Annotations were last modified on    July 22, 2008 (Entry version 26)
Name and origin of the protein
Protein name Histidinol dehydrogenase
Synonyms HDH
EC 1.1.1.23
Gene name
Name: hisD
OrderedLocusNames: CJE1770
From
Campylobacter jejuni (strain RM1221) [TaxID: 195099] [HAMAP proteome]
Taxonomy Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales; Campylobacteraceae; Campylobacter.
Protein existence 3: Inferred from homology;
References
[1]
 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
DOI=10.1371/journal.pbio.0030015; PubMed=15660156 [NCBI, ExPASy, EBI, Israel, Japan]
Fouts D.E., Mongodin E.F., Mandrell R.E., Miller W.G., Rasko D.A., Ravel J., Brinkac L.M., DeBoy R.T., Parker C.T., Daugherty S.C., Dodson R.J., Durkin A.S., Madupu R., Sullivan S.A., Shetty J.U., Ayodeji M.A., Shvartsbeyn A., Schatz M.C., Badger J.H., Fraser C.M., Nelson K.E.;
"Major structural differences and novel potential virulence mechanisms from the genomes of multiple Campylobacter species.";
PLoS Biol. 3:72-85(2005).
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
CP000025; AAW36194.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
RefSeq YP_179742.1; -.
3D structure databases
ModBase Q5HSJ3.
Enzyme and pathway databases
BioCyc CJEJ195099:CJE_1770-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 Q5HSJ3.
Genome annotation databases
GeneID 3232397; -.
GenomeReviews CP000025_GR; CJE1770.
KEGG cjr:CJE1770; -.
NMPDR fig|195099.3.peg.1298; -.
TIGR CJE1770; -.
Phylogenomic databases
HOGENOM Q5HSJ3; -.
Other
ProtoNet Q5HSJ3.
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_0000135752
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: 46430 Da [This is the MW of the unprocessed precursor] CRC64: EF20C2265EBABBE6 [This is a checksum on the sequence] 
        10         20         30         40         50         60 
MQILVYDNLD EKQKEEALKR PAISAKDEIS KIVSSIIKEV QEKGDEALIE QALKFDKAEI 

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

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

       190        200        210        220        230        240 
MGGAGAIAAL AYGTQSVLKV 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
Q5HSJ3 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
Report form for errors/updates in this UniProtKB/Swiss-Prot entry

BLAST logo BLAST submission on ExPASy/SIB
or at NCBI (USA) 		Tools Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
PROSITE logo ScanProsite, MotifScan SWISS-MODEL Submit a homology modeling request to SWISS-MODEL
NPSA logo NPSA Sequence analysis tools

ExPASy logo ExPASy Home page Site Map Search ExPASy Contact us Swiss-Prot
Hosted by ca flag CBR Canada Mirror sites: Australia Brazil China Korea Switzerland
Notice: This page will be replaced with www.uniprot.org. Please send us your feedback!