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Q92S26 (HISX1_RHIME) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 85. 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 1

Short name=HDH 1
EC=1.1.1.23
Gene names
Name:hisD1
Ordered Locus Names:R00611
ORF Names:SMc02307
OrganismRhizobium meliloti (strain 1021) (Ensifer meliloti) (Sinorhizobium meliloti) [Complete proteome] [HAMAP]
Taxonomic identifier266834 [NCBI]
Taxonomic lineageBacteriaProteobacteriaAlphaproteobacteriaRhizobialesRhizobiaceaeSinorhizobium/Ensifer groupSinorhizobium

Protein attributes

Sequence length434 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
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 – 434434Histidinol dehydrogenase 1 HAMAP-Rule MF_01024
PRO_0000135832

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

Sequences

Sequence LengthMass (Da)Tools
Q92S26 [UniParc].

Last modified December 1, 2001. Version 1.
Checksum: BEC67BD413535616

FASTA43445,555
        10         20         30         40         50         60 
MAIRLNYLDT SFERDFAAFL TTKREVSEDV NAVVRAIIDD VRARGDAALA DYSARFDGID 

        70         80         90        100        110        120 
FTVTGMAVTS AEIDAAIHAV APEVLGALKV AATRIEAHHR RQLPKDDIYE DQMGVGLGSR 

       130        140        150        160        170        180 
WTPIDAVGLY VPGGTASYPS SVLMNALPAK VAGVPRIVMV VPASGGSINP AVLAAARLAG 

       190        200        210        220        230        240 
VEEIYRIGGA QAVAALAYGT ETIEPVAKIV GPGNAYVAAA KRQVFGTVGI DMIAGPSEVL 

       250        260        270        280        290        300 
VIADRDNDPD WIAADLLAQA EHDAGAQAIL ITDDAAFGDA VEKAVERQLK TLPRAETAAA 

       310        320        330        340        350        360 
SWRDFGAVIL VPDFDKAVPL ANRIAPEHLE LATADPDAMV PAIRNAGAIF IGRHTPEVIG 

       370        380        390        400        410        420 
DYVGGSNHVL PTARSARFSS GLGVLDYVKR TSILRLGPDQ LRILGPAAIA LARSEGLEAH 

       430 
ARSVAIRLNL GEEG 

« Hide

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AL591688 Genomic DNA. Translation: CAC45183.1.
RefSeqNP_384717.1. NC_003047.1.

3D structure databases

ProteinModelPortalQ92S26.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING266834.SMc02307.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaCAC45183; CAC45183; SMc02307.
GeneID1232249.
KEGGsme:SMc02307.
PATRIC23630435. VBISinMel96828_1984.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0141.
HOGENOMHOG000243914.
KOK00013.
OMAPSEILII.
OrthoDBEOG6CVVCR.
ProtClustDBPRK00877.

Enzyme and pathway databases

BioCycSMEL266834:GJF6-627-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 nameHISX1_RHIME
AccessionPrimary (citable) accession number: Q92S26
Entry history
Integrated into UniProtKB/Swiss-Prot: March 25, 2003
Last sequence update: December 1, 2001
Last modified: February 19, 2014
This is version 85 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