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Q47AL5 (HISX_DECAR) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 50. 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:Daro_3387
OrganismDechloromonas aromatica (strain RCB) [Complete proteome] [HAMAP]
Taxonomic identifier159087 [NCBI]
Taxonomic lineageBacteria › Proteobacteria › Betaproteobacteria › Rhodocyclales › Rhodocyclaceae › Dechloromonas

Protein attributes

Sequence length433 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

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 – 433433Histidinol dehydrogenase HAMAP MF_01024
PRO_0000135763

Sites

Active site3301Proton acceptor By similarity
Active site3311Proton acceptor By similarity
Metal binding2621Zinc By similarity
Metal binding2651Zinc By similarity
Metal binding3641Zinc By similarity
Metal binding4231Zinc By similarity
Binding site1331NAD By similarity
Binding site1941NAD By similarity
Binding site2171NAD By similarity
Binding site2401Substrate By similarity
Binding site2621Substrate By similarity
Binding site2651Substrate By similarity
Binding site3311Substrate By similarity
Binding site3641Substrate By similarity
Binding site4181Substrate By similarity
Binding site4231Substrate By similarity

Sequences

Sequence LengthMass (Da)Tools
Q47AL5 [UniParc].

Last modified September 13, 2005. Version 1.
Checksum: A7E2E5E5990A7CCA

FASTA43346,066
        10         20         30         40         50         60 
MVAIKRLATV DADFKAQMDA LLAFEAAQDE GIERTVIGIL ADVKARGDAA VVEYSNKFDR 

        70         80         90        100        110        120 
LTASSMADLE LSKAEMQKAL DGLPADQRQA LEAAAHRVRV YHEKQRMEGW SYTEADGTML 

       130        140        150        160        170        180 
GQMITPLDRV GLYVPGGKAA YPSSVLMNAI PAKVAGVKEL IMVVPTPGGE HNQLVLAAAC 

       190        200        210        220        230        240 
LAGVDRVFTI GGAQAVGALA YGTEAVPQVD KIVGPGNAYV ACAKRRVFGI VGIDMIAGPS 

       250        260        270        280        290        300 
EILVVADGSS DPDWVAMDLF SQAEHDELAQ SILICTDAAY IDRVQASIEK LLPTMPRREV 

       310        320        330        340        350        360 
IETSLTNRGA LILVRDLEEA CAIANRVAPE HLELSLADPD PWVAKIHHAG AIFIGHYTSE 

       370        380        390        400        410        420 
SLGDYCAGPN HVLPTSGSAR FSSPLGVYDF QKRTSLIKVS KAGAQTLGKI ASTLAHGEGL 

       430 
PAHAKSAEFR LEN

« Hide

References

[1]"Complete sequence of Dechloromonas aromatica RCB."
Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T., Hammon N., Israni S., Pitluck S., Di Bartolo G., Trong S., Kellar K., Schmutz J., Larimer F., Land M., Ivanova N., Richardson P.
Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: RCB.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		CP000089 Genomic DNA. Translation: AAZ48116.1.
RefSeqYP_286586.1. NC_007298.1.

3D structure databases

ProteinModelPortalQ47AL5.
ModBaseSearch...

Protein-protein interaction databases

STRINGQ47AL5.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID3567117.
GenomeReviewsGene locus Daro_3387 in contig CP000089_GR.
KEGGdar:Daro_3387.
NMPDRfig|159087.4.peg.3635.
PATRIC21605458. VBIDecAro89105_3372.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0141.
HOGENOMHBG329596.
OMANRYVTEA.
PhylomeDBQ47AL5.
ProtClustDBCLSK2526049.

Enzyme and pathway databases

BioCycDARO159087:DARO_3387-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_DECAR
AccessionPrimary (citable) accession number: Q47AL5
Entry history
Integrated into UniProtKB/Swiss-Prot: January 10, 2006
Last sequence update: September 13, 2005
Last modified: January 25, 2012
This is version 50 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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