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P59398 (HISX_BUCBP) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 73. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
Histidinol dehydrogenase
Short name=HDH
EC=1.1.1.23
Gene names
Name:hisD
Ordered Locus Names:bbp_094
OrganismBuchnera aphidicola subsp. Baizongia pistaciae (strain Bp) [Complete proteome] [HAMAP]
Taxonomic identifier224915 [NCBI]
Taxonomic lineageBacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Buchnera

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 MF_01024

Catalytic activity

L-histidinol + H2O + 2 NAD+ = L-histidine + 2 NADH. HAMAP MF_01024

Cofactor

Binds 1 zinc ion per subunit By similarity. HAMAP MF_01024

Pathway

Amino-acid biosynthesis; L-histidine biosynthesis; L-histidine from 5-phospho-alpha-D-ribose 1-diphosphate: step 9/9. HAMAP MF_01024

Subunit structure

Homodimer By similarity. HAMAP 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-KW

   Molecular functionNAD binding

Inferred from electronic annotation. Source: InterPro

histidinol dehydrogenase activity

Inferred from electronic annotation. Source: EC

zinc ion binding

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 435435Histidinol dehydrogenase HAMAP MF_01024
PRO_0000135743

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
P59398 [UniParc].

Last modified March 25, 2003. Version 1.
Checksum: 8A2F3ED2073D73F2

FASTA43548,185
        10         20         30         40         50         60 
MEVYIPIIYW KSCSEKEKRE ILFRPVVNDN SQIKEVVKEI ITNVKNSGDK ALYDYTKTFD 

        70         80         90        100        110        120 
KIRLESIQVS YGEIVDSDSF VNEEIQKSIS VAKNNIKIFH EKQTHNVVNI EIQPGVFCRQ 

       130        140        150        160        170        180 
IIRPIQSVGL YIPGGCAPLV STVLMLAIPA KIVGCKNIIL CSPPPITKEI LYASKICGIH 

       190        200        210        220        230        240 
NIFQVGGAQA IAAMAFGTKT IPKVNKIFGP GNVYVTEAKL QINALLNDLS IDMLAGPSEI 

       250        260        270        280        290        300 
LIIADFKANA CIIASDFLSQ MEHGIYSQAI LVTPSYDLAC NVIFEINIQL KNLSRKKVIN 

       310        320        330        340        350        360 
KSLKYSRIIV TKTLLECFEI SNLYAPEHLI IQCENSNRLL VYVINAGSIF LGRWSAVASG 

       370        380        390        400        410        420 
DYVTGTNHVL PTYGSAIVNS GLTVMDFQKI ISVQKLDQQG LIDVSSSIIS LSEVERMDAH 

       430 
TNSIKQRLIA LQDVK

« Hide

References

[1]"Reductive genome evolution in Buchnera aphidicola."
van Ham R.C.H.J., Kamerbeek J., Palacios C., Rausell C., Abascal F., Bastolla U., Fernandez J.M., Jimenez L., Postigo M., Silva F.J., Tamames J., Viguera E., Latorre A., Valencia A., Moran F., Moya A.
Proc. Natl. Acad. Sci. U.S.A. 100:581-586(2003) [PubMed: 12522265] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: Bp.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		AE016826 Genomic DNA. Translation: AAO26829.1.
RefSeqNP_777724.1. NC_004545.1.

3D structure databases

ProteinModelPortalP59398.
SMRP59398. Positions 6-433.
ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaEBBUCT00000002410; EBBUCP00000002234; EBBUCG00000002410.
GeneID1058171.
GenomeReviewsGene locus bbp_094 in contig AE016826_GR.
KEGGbab:bbp094.
PATRIC21244967. VBIBucAph80364_0091.

Organism-specific databases

CMRSearch...

Phylogenomic databases

GeneTreeEBGT00050000008005.
HOGENOMHBG329596.
OMAIMTKNPR.
PhylomeDBP59398.

Enzyme and pathway databases

BioCycBAPH224915:BBP_094-MONOMER.

Family and domain databases

HAMAPMF_01024. HisD.
[Tree]
InterProIPR016161. Ald_DH/histidinol_DH.
IPR001692. Histidinol_DH_CS.
IPR022695. Histidinol_DH_monofunct.
IPR012131. Hstdl_DH.
[Graphical view]
KOK00013.
PANTHERPTHR21256:SF2. Hstdl_DH_prok. 1 hit.
PfamPF00815. Histidinol_dh. 1 hit.
[Graphical view]
PIRSFPIRSF000099. Histidinol_dh. 1 hit.
PRINTSPR00083. HOLDHDRGNASE.
SUPFAMSSF53720. Aldehyde_DH/Histidinol_DH. 1 hit.
TIGRFAMsTIGR00069. HisD. 1 hit.
PROSITEPS00611. HISOL_DEHYDROGENASE. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameHISX_BUCBP
AccessionPrimary (citable) accession number: P59398
Entry history
Integrated into UniProtKB/Swiss-Prot: March 25, 2003
Last sequence update: March 25, 2003
Last modified: January 25, 2012
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

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

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