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

Q5ZW87 (HISX_LEGPH) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 73. 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:lpg1199
OrganismLegionella pneumophila subsp. pneumophila (strain Philadelphia 1 / ATCC 33152 / DSM 7513) [Complete proteome] [HAMAP]
Taxonomic identifier272624 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaLegionellalesLegionellaceaeLegionella

Protein attributes

Sequence length431 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 – 431431Histidinol dehydrogenase HAMAP-Rule MF_01024
PRO_0000135786

Sites

Active site3251Proton acceptor By similarity
Active site3261Proton acceptor By similarity
Metal binding2581Zinc By similarity
Metal binding2611Zinc By similarity
Metal binding3591Zinc By similarity
Metal binding4181Zinc By similarity
Binding site1241NAD By similarity
Binding site1871NAD By similarity
Binding site2101NAD By similarity
Binding site2361Substrate By similarity
Binding site2581Substrate By similarity
Binding site2611Substrate By similarity
Binding site3261Substrate By similarity
Binding site3591Substrate By similarity
Binding site4131Substrate By similarity
Binding site4181Substrate By similarity

Sequences

Sequence LengthMass (Da)Tools
Q5ZW87 [UniParc].

Last modified November 23, 2004. Version 1.
Checksum: A9B4D2B3857D6529

FASTA43146,714
        10         20         30         40         50         60 
MLTIKNWQLL SENDKKLCLS RPRQSSAIKE NVLEIINQVQ LSGDKALYDL TKQFDRVNLQ 

        70         80         90        100        110        120 
YLQVPQEKIE QANIPKNALN AITQAIGTIS SYHQSLLPEN TEISTASGIT IRNVYRPIQK 

       130        140        150        160        170        180 
VGLYVPGGNK TPLVSSLLMQ AIPAKVAGCP IKVLCTPPDA EGEINEHILV AARLCGIDTI 

       190        200        210        220        230        240 
YAIGGAQAIA AMAYGTESVI KVDKIFGPGN SYVTQAKTLV AIDADGAAID MPAGPSEVMI 

       250        260        270        280        290        300 
LADTEANPEF IAADLLAQAE HGPDSQVILI CDECELANQV NQQLEIQMSY LSRIEFIKRS 

       310        320        330        340        350        360 
LANSRIIICS NQSEQLDIIN SYAPEHLIIN RKNPEPWVEK IVAAGTVFLG SWAAETMGDY 

       370        380        390        400        410        420 
VTGSNHVLPT SGFARNHSGL STLDFMTRFT VQAINQEAIR NLGPAAMTLA ELEGLDAHAN 

       430 
AVQIRLNTLG D 

« Hide

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AE017354 Genomic DNA. Translation: AAU27284.1.
RefSeqYP_095231.1. NC_002942.5.

3D structure databases

ProteinModelPortalQ5ZW87.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING272624.lpg1199.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAU27284; AAU27284; lpg1199.
GeneID3080215.
KEGGlpn:lpg1199.
PATRIC22329472. VBILegPne29832_1261.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0141.
HOGENOMHOG000243914.
KOK00013.
OMAYAAKLCG.
OrthoDBEOG6CVVCR.

Enzyme and pathway databases

BioCycLPNE272624:GHDI-1198-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_LEGPH
AccessionPrimary (citable) accession number: Q5ZW87
Entry history
Integrated into UniProtKB/Swiss-Prot: January 10, 2006
Last sequence update: November 23, 2004
Last modified: May 14, 2014
This is version 73 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