Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

Q8Z5K0 (HISX_SALTI) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 92. 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:STY2281, t0801
OrganismSalmonella typhi [Complete proteome] [HAMAP]
Taxonomic identifier90370 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeSalmonella

Protein attributes

Sequence length434 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
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

Subunit structure

Homodimer By similarity. 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

Initiator methionine11Removed By similarity
Chain2 – 434433Histidinol dehydrogenase HAMAP-Rule MF_01024
PRO_0000135839

Sites

Active site3261Proton acceptor By similarity
Active site3271Proton acceptor By similarity
Metal binding2591Zinc By similarity
Metal binding2621Zinc By similarity
Metal binding3601Zinc By similarity
Metal binding4191Zinc By similarity
Binding site1301NAD By similarity
Binding site1881NAD By similarity
Binding site2111NAD By similarity
Binding site2371Substrate By similarity
Binding site2591Substrate By similarity
Binding site2621Substrate By similarity
Binding site3271Substrate By similarity
Binding site3601Substrate By similarity
Binding site4141Substrate By similarity
Binding site4191Substrate By similarity

Experimental info

Sequence conflict2481T → I in AAN39867. Ref.3

Sequences

Sequence LengthMass (Da)Tools
Q8Z5K0 [UniParc].

Last modified January 23, 2007. Version 3.
Checksum: E159F95D01850C47

FASTA43445,833
        10         20         30         40         50         60 
MSFNTLIDWN SCSPEQQRAL LTRPAISASD SITRTVSDIL YNVKTRGDDA LREYSAKFDK 

        70         80         90        100        110        120 
TEVTALRVTP EEIAAAGARL SDELKQAMAA AVKNIETFHS AQTLPPVDVE TQPGVRCQQV 

       130        140        150        160        170        180 
TRPVASVGLY IPGGSAPLFS TVLMLATPAR IAGCQKVVLC SPPPIADEIL YAAQLCGVQE 

       190        200        210        220        230        240 
IFNVGGAQAI AALAFGSESV PKVDKIFGPG NAFVTEAKRQ VSQRLDGAAI DMPAGPSEVL 

       250        260        270        280        290        300 
VIADSGATPD FVASDLLSQA EHGPDSQVIL LTPDADIARK VAEAVERQLA ELPRAGTARQ 

       310        320        330        340        350        360 
ALSASRLIVT KDLAQCVAIS NQYGPEHLII QTRNARDLVD AITSAGSVFL GDWSPESAGD 

       370        380        390        400        410        420 
YASGTNHVLP TYGYTATCSS LGLADFQKRM TVQELSKAGF SALASTIETL AAAERLTAHK 

       430 
NAVTLRVNAL KEQA 

« Hide

References

« Hide 'large scale' references
[1]"Complete genome sequence of a multiple drug resistant Salmonella enterica serovar Typhi CT18."
Parkhill J., Dougan G., James K.D., Thomson N.R., Pickard D., Wain J., Churcher C.M., Mungall K.L., Bentley S.D., Holden M.T.G., Sebaihia M., Baker S., Basham D., Brooks K., Chillingworth T., Connerton P., Cronin A., Davis P. expand/collapse author list , Davies R.M., Dowd L., White N., Farrar J., Feltwell T., Hamlin N., Haque A., Hien T.T., Holroyd S., Jagels K., Krogh A., Larsen T.S., Leather S., Moule S., O'Gaora P., Parry C., Quail M.A., Rutherford K.M., Simmonds M., Skelton J., Stevens K., Whitehead S., Barrell B.G.
Nature 413:848-852(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: CT18.
[2]"Comparative genomics of Salmonella enterica serovar Typhi strains Ty2 and CT18."
Deng W., Liou S.-R., Plunkett G. III, Mayhew G.F., Rose D.J., Burland V., Kodoyianni V., Schwartz D.C., Blattner F.R.
J. Bacteriol. 185:2330-2337(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 700931 / Ty2.
[3]"Salmonella typhi, the causative agent of typhoid fever, is approximately 50,000 years old."
Kidgell C., Reichard U., Wain J., Linz B., Torpdahl M., Dougan G., Achtman M.
Infect. Genet. Evol. 2:39-45(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 152-318.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AL513382 Genomic DNA. Translation: CAD02434.1.
AE014613 Genomic DNA. Translation: AAO68492.1.
AY142232 Genomic DNA. Translation: AAN39867.1.
AY142233 Genomic DNA. Translation: AAN39868.1.
RefSeqNP_456620.1. NC_003198.1.
NP_804643.1. NC_004631.1.

3D structure databases

ProteinModelPortalQ8Z5K0.
SMRQ8Z5K0. Positions 1-434.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING220341.STY2281.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAO68492; AAO68492; t0801.
CAD02434; CAD02434; CAD02434.
GeneID1248616.
KEGGsty:STY2281.
PATRIC18542503. VBISalEnt120419_2301.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0141.
HOGENOMHOG000243914.
KOK00013.
OMAYAAKLCG.
OrthoDBEOG6CVVCR.

Enzyme and pathway databases

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_SALTI
AccessionPrimary (citable) accession number: Q8Z5K0
Secondary accession number(s): Q8GKY3, Q8GKY4
Entry history
Integrated into UniProtKB/Swiss-Prot: March 25, 2003
Last sequence update: January 23, 2007
Last modified: May 14, 2014
This is version 92 of the entry and version 3 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