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Q6A8L5 (HISX_PROAC) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 75. 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:PPA1152
OrganismPropionibacterium acnes (strain KPA171202 / DSM 16379) [Complete proteome] [HAMAP]
Taxonomic identifier267747 [NCBI]
Taxonomic lineageBacteriaActinobacteriaActinobacteridaeActinomycetalesPropionibacterineaePropionibacteriaceaePropionibacterium

Protein attributes

Sequence length439 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 – 439439Histidinol dehydrogenase HAMAP-Rule MF_01024
PRO_0000135817

Sites

Active site3361Proton acceptor By similarity
Active site3371Proton acceptor By similarity
Metal binding2671Zinc By similarity
Metal binding2701Zinc By similarity
Metal binding3701Zinc By similarity
Metal binding4291Zinc By similarity
Binding site1291NAD By similarity
Binding site1931NAD By similarity
Binding site2221NAD By similarity
Binding site2451Substrate By similarity
Binding site2671Substrate By similarity
Binding site2701Substrate By similarity
Binding site3371Substrate By similarity
Binding site3701Substrate By similarity
Binding site4241Substrate By similarity
Binding site4291Substrate By similarity

Sequences

Sequence LengthMass (Da)Tools
Q6A8L5 [UniParc].

Last modified September 13, 2004. Version 1.
Checksum: F1B7C0C567681677

FASTA43946,098
        10         20         30         40         50         60 
MLRIVDVTSE TTDDLRCAVP RADFDVDAAM AAVIPVCSAV RDRGVEALRE YSEKFDHVVP 

        70         80         90        100        110        120 
EHLRVPVEAL ATAAANLDGT LRRAFSESIR RRRQVCQEAE VETSSQPVEV AGGARVSQRI 

       130        140        150        160        170        180 
VPVGRVGLYV PGGFAPLASS VIMNVVPAQE AGVSSIAVAS PPQAEFGGLP HPSILALCHL 

       190        200        210        220        230        240 
LGVNEVYAVG GAQAIAMFAY GVEGSDEADS CPRVDMVTGP GNIYVVAAKR CLRGTVGIDS 

       250        260        270        280        290        300 
EAGPTEIAIL ADETADPRHI AADLMSQAEH DTLAAAVLVT DSTTLAEAVQ RELAPMVSAT 

       310        320        330        340        350        360 
LHSERIRTSL TSKQSAIVMV RDIDQGLEVV NAYAAEHLEI QTADAAAVAA RVWNAGAIFV 

       370        380        390        400        410        420 
GPWAPVSLGD YSAGSTHVLP TAGAACHSSG LSVRSFMRAV HVIDYTEDAL LELADSVEAF 

       430 
ALAENLPGHA NAITVRRSR 

« Hide

References

[1]"The complete genome sequence of Propionibacterium acnes, a commensal of human skin."
Brueggemann H., Henne A., Hoster F., Liesegang H., Wiezer A., Strittmatter A., Hujer S., Duerre P., Gottschalk G.
Science 305:671-673(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: KPA171202 / DSM 16379.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AE017283 Genomic DNA. Translation: AAT82901.1.
RefSeqYP_055859.1. NC_006085.1.

3D structure databases

ProteinModelPortalQ6A8L5.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING267747.PPA1152.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAT82901; AAT82901; PPA1152.
GeneID2932004.
KEGGpac:PPA1152.
PATRIC23037039. VBIProAcn64440_1188.

Organism-specific databases

CMRSearch...

Phylogenomic databases

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

Enzyme and pathway databases

BioCycPACN267747:GHO9-1165-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_PROAC
AccessionPrimary (citable) accession number: Q6A8L5
Entry history
Integrated into UniProtKB/Swiss-Prot: December 7, 2004
Last sequence update: September 13, 2004
Last modified: February 19, 2014
This is version 75 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