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Q7UX39 (HISX_RHOBA) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 79. 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:RB1584
OrganismRhodopirellula baltica (strain SH1) [Reference proteome] [HAMAP]
Taxonomic identifier243090 [NCBI]
Taxonomic lineageBacteriaPlanctomycetesPlanctomycetiaPlanctomycetalesPlanctomycetaceaeRhodopirellula

Protein attributes

Sequence length460 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
Reference 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 – 460460Histidinol dehydrogenase HAMAP-Rule MF_01024
PRO_0000135834

Sites

Active site3581Proton acceptor By similarity
Active site3591Proton acceptor By similarity
Metal binding2911Zinc By similarity
Metal binding2941Zinc By similarity
Metal binding3921Zinc By similarity
Metal binding4511Zinc By similarity
Binding site2691Substrate By similarity
Binding site2911Substrate By similarity
Binding site2941Substrate By similarity
Binding site3591Substrate By similarity
Binding site3921Substrate By similarity
Binding site4461Substrate By similarity
Binding site4511Substrate By similarity

Sequences

Sequence LengthMass (Da)Tools
Q7UX39 [UniParc].

Last modified October 1, 2003. Version 1.
Checksum: 507E4E5DAE69E1BF

FASTA46048,514
        10         20         30         40         50         60 
MFRIVAVPEF SIQTVDARDP SSSEAAETLA ALREKLSPRG DLVSPRGREL TLKVFGKALS 

        70         80         90        100        110        120 
PIEVVETICK DVQSQGTEAL LRYTKSLDGA ELTADTLRVP EEDLKAAHAV ADPKLIETIG 

       130        140        150        160        170        180 
RIRDNIATFQ SAILHRDVTI TPRPGVSLTQ RYVPIPRVGI CVPGGAAAYP STVMMTAIPA 

       190        200        210        220        230        240 
QVAGVDEIAV VAPPTPFGAY NTDMLATCHE LGIKEVYRCG GAQAVAAMAY GCDALPAVDK 

       250        260        270        280        290        300 
IVGPGNLFVA LAKKHVFGTV DIDSFAGPSE VIVIADESAN AAFVASDLLA QAEHSPGSAI 

       310        320        330        340        350        360 
LITWDESLLT SVQAELSRQL GELERGDLAR DALSDFGALV LARDADHACE LTDSFAPEHL 

       370        380        390        400        410        420 
QIETREPESL IAKIRHSGAA FLGHHTPVAL GDYAAGPSHV LPTGGTCRWA AGLSANSFLR 

       430        440        450        460 
SGSVTQFDQS ALSAIAQDVI TVAEKEGLTA HARSISIRTE 

« Hide

References

[1]"Complete genome sequence of the marine planctomycete Pirellula sp. strain 1."
Gloeckner F.O., Kube M., Bauer M., Teeling H., Lombardot T., Ludwig W., Gade D., Beck A., Borzym K., Heitmann K., Rabus R., Schlesner H., Amann R., Reinhardt R.
Proc. Natl. Acad. Sci. U.S.A. 100:8298-8303(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: SH1.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
BX294135 Genomic DNA. Translation: CAD72173.1.
RefSeqNP_864492.1. NC_005027.1.

3D structure databases

ProteinModelPortalQ7UX39.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING243090.RB1584.

Proteomic databases

PRIDEQ7UX39.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaCAD72173; CAD72173; RB1584.
GeneID1789901.
KEGGrba:RB1584.
PATRIC23242901. VBIRhoBal59814_0740.

Phylogenomic databases

eggNOGCOG0141.
HOGENOMHOG000243914.
KOK00013.
OMAPSEILII.
OrthoDBEOG6CVVCR.
ProtClustDBCLSK2758609.

Enzyme and pathway databases

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_RHOBA
AccessionPrimary (citable) accession number: Q7UX39
Entry history
Integrated into UniProtKB/Swiss-Prot: April 13, 2004
Last sequence update: October 1, 2003
Last modified: February 19, 2014
This is version 79 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