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Q9ZHE6 (HISX_BUCAP) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 102. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | 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:BUsg_093
OrganismBuchnera aphidicola subsp. Schizaphis graminum (strain Sg) [Complete proteome] [HAMAP]
Taxonomic identifier198804 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeBuchnera

Protein attributes

Sequence length435 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

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

Chain1 – 435435Histidinol dehydrogenase HAMAP-Rule MF_01024
PRO_0000135746

Sites

Active site3271Proton acceptor By similarity
Active site3281Proton acceptor By similarity
Metal binding2601Zinc By similarity
Metal binding2631Zinc By similarity
Metal binding3611Zinc By similarity
Metal binding4201Zinc By similarity
Binding site1311NAD By similarity
Binding site1891NAD By similarity
Binding site2121NAD By similarity
Binding site2381Substrate By similarity
Binding site2601Substrate By similarity
Binding site2631Substrate By similarity
Binding site3281Substrate By similarity
Binding site3611Substrate By similarity
Binding site4151Substrate By similarity
Binding site4201Substrate By similarity

Sequences

Sequence LengthMass (Da)Tools
Q9ZHE6 [UniParc].

Last modified May 1, 1999. Version 1.
Checksum: CD25387C2B62BDE2

FASTA43547,738
        10         20         30         40         50         60 
MKYFNTIVNW NMLNSNEQKN ILLRPVIKNN NSIKKKVKKI IENIQVLGEK ALREYTILFE 

        70         80         90        100        110        120 
KCHINKFEVS KEKMLSSSLY VNQSLKDAIS TAKKNITSFH TAQILSPIDI ETQVGVRCQQ 

       130        140        150        160        170        180 
IYLPLNSVGI YIPSGIAPLF STVLMLAIPA KIAGCKQIIL CSPPPIDNTI LYAANICGVD 

       190        200        210        220        230        240 
KIFQMGGAQA IAALAFGTKN IPKVDKIFGP GNAYVTEAKL QVSSIFNGPQ IDMLAGPSEL 

       250        260        270        280        290        300 
LIIADEASNA DFIAADLLSQ AEHSISSQVI LLTPSLQLAK KVIISINNQL KNLSKSDDIS 

       310        320        330        340        350        360 
TALDNSVIIL TKDLFECIKI SNIYAPEHLI IQTKEPRLIL KEILNASSIF LGPWSPESAG 

       370        380        390        400        410        420 
DYASGTNHVL PTYGKSVSSS ALGLCDFKKR VLIQELTSQG FINLSNTLKI LSEAEKLEAH 

       430 
KNAVKIRVDF LKEKI 

« Hide

References

« Hide 'large scale' references
[1]"Buchnera aphidicola (Aphid endosymbiont) contains genes encoding enzymes of histidine biosynthesis."
Clark M.A., Baumann L., Baumann P.
Curr. Microbiol. 37:356-358(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]"50 million years of genomic stasis in endosymbiotic bacteria."
Tamas I., Klasson L., Canbaeck B., Naeslund A.K., Eriksson A.-S., Wernegreen J.J., Sandstroem J.P., Moran N.A., Andersson S.G.E.
Science 296:2376-2379(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: Sg.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF067228 Genomic DNA. Translation: AAC97355.1.
AE013218 Genomic DNA. Translation: AAM67663.1.
RefSeqNP_660452.1. NC_004061.1.

3D structure databases

ProteinModelPortalQ9ZHE6.
SMRQ9ZHE6. Positions 5-434.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING198804.BUsg093.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAM67663; AAM67663; BUsg_093.
GeneID1005910.
KEGGbas:BUsg093.
PATRIC21246963. VBIBucAph100086_0096.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0141.
KOK00013.
OMAPSEILII.
OrthoDBEOG6CVVCR.
ProtClustDBPRK00877.

Enzyme and pathway databases

BioCycBAPH198804:GHMG-102-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_BUCAP
AccessionPrimary (citable) accession number: Q9ZHE6
Entry history
Integrated into UniProtKB/Swiss-Prot: May 30, 2000
Last sequence update: May 1, 1999
Last modified: February 19, 2014
This is version 102 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

Buchnera aphidicola (subsp. Schizaphis graminum)

Buchnera aphidicola (subsp. Schizaphis graminum): entries and gene names