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P28736 (HISX_MYCSM) 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
OrganismMycobacterium smegmatis
Taxonomic identifier1772 [NCBI]
Taxonomic lineageBacteriaActinobacteriaActinobacteridaeActinomycetalesCorynebacterineaeMycobacteriaceaeMycobacterium

Protein attributes

Sequence length445 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
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 – 445445Histidinol dehydrogenase HAMAP-Rule MF_01024
PRO_0000135798

Sites

Active site3421Proton acceptor By similarity
Active site3431Proton acceptor By similarity
Metal binding2731Zinc By similarity
Metal binding2761Zinc By similarity
Metal binding3761Zinc By similarity
Metal binding4351Zinc By similarity
Binding site1361NAD By similarity
Binding site2001NAD By similarity
Binding site2281NAD By similarity
Binding site2511Substrate By similarity
Binding site2731Substrate By similarity
Binding site2761Substrate By similarity
Binding site3431Substrate By similarity
Binding site3761Substrate By similarity
Binding site4301Substrate By similarity
Binding site4351Substrate By similarity

Sequences

Sequence LengthMass (Da)Tools
P28736 [UniParc].

Last modified December 1, 1992. Version 1.
Checksum: 19996D28D4591170

FASTA44546,703
        10         20         30         40         50         60 
MNMMAKFQMS RIDLRNRVLS AAQLRSALPR GGVDVDAVVP KVRPIVDAVA QRGAQAALEY 

        70         80         90        100        110        120 
GESFDGIRPE TVRVPRELLS QALENLDADV RAALQVSIDR ARAVHADQRR TDTTTTLAPG 

       130        140        150        160        170        180 
ATVTERWVPV ERVGLYVPGG NAVYPSSVVM NVVPAQTAGV DSMVIASPPQ GQFGGRPHPT 

       190        200        210        220        230        240 
ILAAAALLGV DEVWAVGGAQ AVALLAYGGT DTDGAELAPV DMITGPGNIY VTAAKRICRS 

       250        260        270        280        290        300 
QVGIDAEAGP TEIAILADHT ADPVHVAADL ISQAEHDEMA ASVLVTDSET LAEATDRELA 

       310        320        330        340        350        360 
NQLATTKHVE RVTAALSGKQ SAIVLVDDID AGVRTVNAYA AEHLEIQTVD APGVAGRIRS 

       370        380        390        400        410        420 
AGAIFVGAWS PVSLGDYCAG SNHVLPTAGC ARHSSGLSVQ TFLRGIHVVE YDEAALKDVS 

       430        440 
GHVITLSKAE DLPAHGEAVR RRFER 

« Hide

References

[1]"Cloning of mycobacterial histidine synthesis genes by complementation of a Mycobacterium smegmatis auxotroph."
Hinshelwood S., Stoker N.G.
Mol. Microbiol. 6:2887-2895(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: ATCC 607 / DSM 43465 / JCM 20379 / NBRC 3207 / NRRL B-692.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X65542 Genomic DNA. Translation: CAA46509.1.
PIRS26209.

3D structure databases

ProteinModelPortalP28736.
ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

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_MYCSM
AccessionPrimary (citable) accession number: P28736
Entry history
Integrated into UniProtKB/Swiss-Prot: December 1, 1992
Last sequence update: December 1, 1992
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