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Q9PM77 (HISX_CAMJE) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 86. 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:Cj1598
OrganismCampylobacter jejuni subsp. jejuni serotype O:2 (strain NCTC 11168) [Reference proteome] [HAMAP]
Taxonomic identifier192222 [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
Reference 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_0000135751

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
Q9PM77 [UniParc].

Last modified October 1, 2000. Version 1.
Checksum: 16F08561BF7DB738

FASTA42846,446
        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 

« Hide

References

[1]"The genome sequence of the food-borne pathogen Campylobacter jejuni reveals hypervariable sequences."
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. expand/collapse author list , van Vliet A.H.M., Whitehead S., Barrell B.G.
Nature 403:665-668(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: NCTC 11168.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AL111168 Genomic DNA. Translation: CAL35695.1.
PIRD81255.
RefSeqYP_002344967.1. NC_002163.1.

3D structure databases

ProteinModelPortalQ9PM77.
SMRQ9PM77. Positions 3-428.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING192222.Cj1598.

Proteomic databases

PRIDEQ9PM77.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaCAL35695; CAL35695; Cj1598.
GeneID905868.
KEGGcje:Cj1598.
PATRIC20060156. VBICamJej33762_1574.

Phylogenomic databases

eggNOGCOG0141.
HOGENOMHOG000243914.
KOK00013.
OMAPSEILII.
OrthoDBEOG6CVVCR.
ProtClustDBPRK00877.

Enzyme and pathway databases

BioCycCJEJ192222:GJTS-1557-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_CAMJE
AccessionPrimary (citable) accession number: Q9PM77
Secondary accession number(s): Q0P830
Entry history
Integrated into UniProtKB/Swiss-Prot: March 25, 2003
Last sequence update: October 1, 2000
Last modified: February 19, 2014
This is version 86 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