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

Q4J8I8 (HISX_SULAC) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 68. 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:Saci_1579
OrganismSulfolobus acidocaldarius (strain ATCC 33909 / DSM 639 / JCM 8929 / NBRC 15157 / NCIMB 11770) [Complete proteome] [HAMAP]
Taxonomic identifier330779 [NCBI]
Taxonomic lineageArchaeaCrenarchaeotaThermoproteiSulfolobalesSulfolobaceaeSulfolobus

Protein attributes

Sequence length393 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 – 393393Histidinol dehydrogenase HAMAP-Rule MF_01024
PRO_0000135905

Sites

Active site2931Proton acceptor By similarity
Active site2941Proton acceptor By similarity
Metal binding2391Zinc By similarity
Metal binding2421Zinc By similarity
Metal binding3261Zinc By similarity
Metal binding3841Zinc By similarity
Binding site1121NAD By similarity
Binding site1711NAD By similarity
Binding site1941NAD By similarity
Binding site2171Substrate By similarity
Binding site2391Substrate By similarity
Binding site2421Substrate By similarity
Binding site2941Substrate By similarity
Binding site3261Substrate By similarity
Binding site3791Substrate By similarity
Binding site3841Substrate By similarity

Sequences

Sequence LengthMass (Da)Tools
Q4J8I8 [UniParc].

Last modified August 2, 2005. Version 1.
Checksum: 1BD29F2FC3182EB5

FASTA39343,528
        10         20         30         40         50         60 
MIKYEIPKSR PNEFSKVLPL VEQILNQVKE RGDKALLELE EKYDKAKLDS LVENRIDELA 

        70         80         90        100        110        120 
SKIPEEYKAA IDRIYDQLVE FHKTTLPYMV GGGYNGIEFG ILWRAIEKVG IYVPGGLKSY 

       130        140        150        160        170        180 
PSTLLMAAIP ARVAGVSEIY VATPPNRIDS VIAYIAKKLK INALYRIGGA QAIAALAYGT 

       190        200        210        220        230        240 
ESVKKVDKIV GPGNIFVQAS KFLVSKDVAI DGIEGPTELV VIADSSADYR HVILDMRAQA 

       250        260        270        280        290        300 
EHGSTSYIIL VTTSDFLIDK VREELDKEEF TYYIVKVKSI DEAIDVANDI APEHLSLFVN 

       310        320        330        340        350        360 
DPKSYLHKIK NAGAISLGKT PPALIDYAAG PDHILPTNAW SRVRGGLTVY DFLKPISYAN 

       370        380        390 
SVNPDKELVN MAKLIAEYEG FIYHSKSIGA RYE 

« Hide

References

[1]"The genome of Sulfolobus acidocaldarius, a model organism of the Crenarchaeota."
Chen L., Bruegger K., Skovgaard M., Redder P., She Q., Torarinsson E., Greve B., Awayez M., Zibat A., Klenk H.-P., Garrett R.A.
J. Bacteriol. 187:4992-4999(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 33909 / DSM 639 / JCM 8929 / NBRC 15157 / NCIMB 11770.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000077 Genomic DNA. Translation: AAY80892.1.
RefSeqYP_256185.1. NC_007181.1.

3D structure databases

ProteinModelPortalQ4J8I8.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING330779.Saci_1579.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAY80892; AAY80892; Saci_1579.
GeneID3474262.
KEGGsai:Saci_1579.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0141.
HOGENOMHOG000243914.
KOK00013.
OMAFHRQRLP.
ProtClustDBPRK00877.

Enzyme and pathway databases

BioCycSACI330779:GH9J-1551-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_SULAC
AccessionPrimary (citable) accession number: Q4J8I8
Entry history
Integrated into UniProtKB/Swiss-Prot: September 27, 2005
Last sequence update: August 2, 2005
Last modified: February 19, 2014
This is version 68 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