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Q5HSJ3 (HISX_CAMJR) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 67. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Histidinol dehydrogenase

Short name=HDH
EC=1.1.1.23
Gene names
Name:hisD
Ordered Locus Names:CJE1770
OrganismCampylobacter jejuni (strain RM1221) [Complete proteome] [HAMAP]
Taxonomic identifier195099 [NCBI]
Taxonomic lineageBacteriaProteobacteriaEpsilonproteobacteriaCampylobacteralesCampylobacteraceaeCampylobacter

Protein attributes

Sequence length428 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Function

Catalyzes the sequential NAD-dependent oxidations of L-histidinol to L-histidinaldehyde and then to L-histidine By similarity. HAMAP-Rule MF_01024

Catalytic activity

L-histidinol + H2O + 2 NAD+ = L-histidine + 2 NADH. HAMAP-Rule MF_01024

Cofactor

Binds 1 zinc ion per subunit By similarity. HAMAP-Rule MF_01024

Pathway

Amino-acid biosynthesis; L-histidine biosynthesis; L-histidine from 5-phospho-alpha-D-ribose 1-diphosphate: step 9/9. HAMAP-Rule MF_01024

Sequence similarities

Belongs to the histidinol dehydrogenase family.

Ontologies

Keywords
   Biological processAmino-acid biosynthesis
Histidine biosynthesis
   LigandMetal-binding
NAD
Zinc
   Molecular functionOxidoreductase
   Technical termComplete proteome
Gene Ontology (GO)
   Biological_processhistidine biosynthetic process

Inferred from electronic annotation. Source: UniProtKB-HAMAP

   Molecular_functionNAD binding

Inferred from electronic annotation. Source: InterPro

histidinol dehydrogenase activity

Inferred from electronic annotation. Source: UniProtKB-HAMAP

zinc ion binding

Inferred from electronic annotation. Source: UniProtKB-HAMAP

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 428428Histidinol dehydrogenase HAMAP-Rule MF_01024
PRO_0000135752

Sites

Active site3231Proton acceptor By similarity
Active site3241Proton acceptor By similarity
Metal binding2561Zinc By similarity
Metal binding2591Zinc By similarity
Metal binding3571Zinc By similarity
Metal binding4161Zinc By similarity
Binding site2341Substrate By similarity
Binding site2561Substrate By similarity
Binding site2591Substrate By similarity
Binding site3241Substrate By similarity
Binding site3571Substrate By similarity
Binding site4111Substrate By similarity
Binding site4161Substrate By similarity

Sequences

Sequence LengthMass (Da)Tools
Q5HSJ3 [UniParc].

Last modified February 15, 2005. Version 1.
Checksum: EF20C2265EBABBE6

FASTA42846,430
        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 

« Hide

References

[1]"Major structural differences and novel potential virulence mechanisms from the genomes of multiple Campylobacter species."
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. expand/collapse author list , Badger J.H., Fraser C.M., Nelson K.E.
PLoS Biol. 3:72-85(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: RM1221.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000025 Genomic DNA. Translation: AAW36194.1.
RefSeqYP_179742.1. NC_003912.7.

3D structure databases

ProteinModelPortalQ5HSJ3.
SMRQ5HSJ3. Positions 3-428.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING195099.CJE1770.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAW36194; AAW36194; CJE1770.
GeneID3232397.
KEGGcjr:CJE1770.
PATRIC20045350. VBICamJej134361_1786.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0141.
HOGENOMHOG000243914.
KOK00013.
OMACAIANRI.
OrthoDBEOG6CVVCR.

Enzyme and pathway databases

BioCycCJEJ195099:GJC0-1800-MONOMER.
UniPathwayUPA00031; UER00014.

Family and domain databases

HAMAPMF_01024. HisD.
InterProIPR016161. Ald_DH/histidinol_DH.
IPR001692. Histidinol_DH_CS.
IPR022695. Histidinol_DH_monofunct.
IPR012131. Hstdl_DH.
[Graphical view]
PfamPF00815. Histidinol_dh. 1 hit.
[Graphical view]
PIRSFPIRSF000099. Histidinol_dh. 1 hit.
PRINTSPR00083. HOLDHDRGNASE.
SUPFAMSSF53720. SSF53720. 1 hit.
TIGRFAMsTIGR00069. hisD. 1 hit.
PROSITEPS00611. HISOL_DEHYDROGENASE. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameHISX_CAMJR
AccessionPrimary (citable) accession number: Q5HSJ3
Entry history
Integrated into UniProtKB/Swiss-Prot: January 10, 2006
Last sequence update: February 15, 2005
Last modified: May 14, 2014
This is version 67 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways