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Q9RH05 (HISX_ZYMMO) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 88. 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
Synonyms:hdh
Ordered Locus Names:ZMO1551
OrganismZymomonas mobilis subsp. mobilis (strain ATCC 31821 / ZM4 / CP4) [Complete proteome] [HAMAP]
Taxonomic identifier264203 [NCBI]
Taxonomic lineageBacteriaProteobacteriaAlphaproteobacteriaSphingomonadalesSphingomonadaceaeZymomonas

Protein attributes

Sequence length430 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.

Sequence caution

The sequence AAF18281.1 differs from that shown. Reason: Frameshift at position 10.

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 – 430430Histidinol dehydrogenase HAMAP-Rule MF_01024
PRO_0000135889

Sites

Active site3271Proton acceptor By similarity
Active site3281Proton acceptor By similarity
Metal binding2591Zinc By similarity
Metal binding2621Zinc By similarity
Metal binding3611Zinc By similarity
Metal binding4201Zinc By similarity
Binding site1301NAD By similarity
Binding site1911NAD By similarity
Binding site2141NAD By similarity
Binding site2371Substrate By similarity
Binding site2591Substrate By similarity
Binding site2621Substrate By similarity
Binding site3281Substrate By similarity
Binding site3611Substrate By similarity
Binding site4151Substrate By similarity
Binding site4201Substrate By similarity

Experimental info

Sequence conflict406 – 43025PAAVT…SRLNK → LRL in AAF18281. Ref.1

Sequences

Sequence LengthMass (Da)Tools
Q9RH05 [UniParc].

Last modified March 23, 2010. Version 3.
Checksum: 213A0D3F7609A6C4

FASTA43046,339
        10         20         30         40         50         60 
MLLKLDSRKA DFQADFTRLV DERRESEGDV SRDVSAIIAD VKKRGDVAIA ELTQKFDRHD 

        70         80         90        100        110        120 
LNKGGWQLTQ EEIKKACDSL PSELMDALKL AATRIRYCHE NQLPESSEMT DAAGVRMGVR 

       130        140        150        160        170        180 
WQAVEAAGLY VPGGRAAYCS SVLMNAVPAK VAGVKRLVMV TPTPDGFVNP AVIAAAVISE 

       190        200        210        220        230        240 
VDEIWKIGGA QAVAALALGT EKIKPVDVVV GPGNAWVAEA KRQLYGQVGI DMVAGPSEIV 

       250        260        270        280        290        300 
VVADKDNDPE WLAADLLSQA EHDPTSQSIL ISDSEDLIEK TIEAVGRRLE KLETQKVARE 

       310        320        330        340        350        360 
SWDKHGATIL VQSLDEAPAL VDRLAPEHLE LAVADPDALF ANVHHSGSVF LGRYTPEAIG 

       370        380        390        400        410        420 
DYVGGPNHVL PTGRRARFSS GLSVIDFMKR TTYLNCSQEA LSKIGPAAVT LAKAEGLPAH 

       430 
AESVISRLNK 

« Hide

References

« Hide 'large scale' references
[1]Kang H.L., Kang H.S.
Submitted (AUG-1998) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: ATCC 31821 / ZM4 / CP4.
[2]"The genome sequence of the ethanologenic bacterium Zymomonas mobilis ZM4."
Seo J.-S., Chong H., Park H.S., Yoon K.-O., Jung C., Kim J.J., Hong J.H., Kim H., Kim J.-H., Kil J.-I., Park C.J., Oh H.-M., Lee J.-S., Jin S.-J., Um H.-W., Lee H.-J., Oh S.-J., Kim J.Y. expand/collapse author list , Kang H.L., Lee S.Y., Lee K.J., Kang H.S.
Nat. Biotechnol. 23:63-68(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 31821 / ZM4 / CP4.
[3]"Improved genome annotation for Zymomonas mobilis."
Yang S., Pappas K.M., Hauser L.J., Land M.L., Chen G.L., Hurst G.B., Pan C., Kouvelis V.N., Typas M.A., Pelletier D.A., Klingeman D.M., Chang Y.J., Samatova N.F., Brown S.D.
Nat. Biotechnol. 27:893-894(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: SEQUENCE REVISION.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF088897 Genomic DNA. Translation: AAF18281.1. Frameshift.
AE008692 Genomic DNA. Translation: AAV90175.2.
RefSeqYP_163286.2. NC_006526.2.

3D structure databases

ProteinModelPortalQ9RH05.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING264203.ZMO1551.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAV90175; AAV90175; ZMO1551.
GeneID3188723.
KEGGzmo:ZMO1551.
PATRIC32568356. VBIZymMob102260_1461.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0141.
HOGENOMHOG000243914.
KOK00013.
ProtClustDBPRK00877.

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_ZYMMO
AccessionPrimary (citable) accession number: Q9RH05
Secondary accession number(s): Q5NM85
Entry history
Integrated into UniProtKB/Swiss-Prot: March 25, 2003
Last sequence update: March 23, 2010
Last modified: February 19, 2014
This is version 88 of the entry and version 3 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