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Q8UHX1 (HISX_AGRT5) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 89. 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:Atu0537
ORF Names:AGR_C_948
OrganismAgrobacterium tumefaciens (strain C58 / ATCC 33970) [Reference proteome] [HAMAP]
Taxonomic identifier176299 [NCBI]
Taxonomic lineageBacteriaProteobacteriaAlphaproteobacteriaRhizobialesRhizobiaceaeRhizobium/Agrobacterium groupAgrobacteriumAgrobacterium tumefaciens complex

Protein attributes

Sequence length432 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 – 432432Histidinol dehydrogenase HAMAP-Rule MF_01024
PRO_0000135714

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
Q8UHX1 [UniParc].

Last modified June 1, 2002. Version 1.
Checksum: B1A794B64953518F

FASTA43245,806
        10         20         30         40         50         60 
MAIWLERASA DFEQKFAAFL TTKREVSEDV NATVRDIIND VRHRGDAALA HYSQKFDGID 

        70         80         90        100        110        120 
FTRVSMRVTA DEIDAAFSAV DRAVIEALEL AARRIEKHHA RQMPKDDIYE DDIGVGLGSR 

       130        140        150        160        170        180 
WTAIEAVGLY VPGGTASYPS SVLMNAVPAK VAGVERIVMV VPANGGAVNP AVLAAARIAG 

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

       250        260        270        280        290        300 
VIADKDNDPD WLAADLLAQA EHDRGAQSIL ITDNADLGKA VGAAVERQLK LLSRSETAAA 

       310        320        330        340        350        360 
SWADFGAIIL VEKLTDAIPL ANRIAAEHLE LAVDDPDALM AHIRNAGAIF VGRHTPEVIG 

       370        380        390        400        410        420 
DYVGGSNHVL PTARSARFSS GLSVLDFVKR TSILRLGPEQ LRQLAPAAIT LAHSEGLDAH 

       430 
ARSVSIRLNP ES 

« Hide

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AE007869 Genomic DNA. Translation: AAK86351.1.
PIRAE2642.
F97424.
RefSeqNP_353566.1. NC_003062.2.

3D structure databases

ProteinModelPortalQ8UHX1.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING176299.Atu0537.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAK86351; AAK86351; Atu0537.
GeneID1132575.
KEGGatu:Atu0537.
PATRIC20810779. VBIAgrTum91616_0535.

Phylogenomic databases

eggNOGCOG0141.
HOGENOMHOG000243914.
KOK00013.
OMACAIANRI.
OrthoDBEOG6CVVCR.

Enzyme and pathway databases

BioCycAGRO:ATU0537-MONOMER.
RETL1328306-WGS:GSTH-592-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 nameHISX_AGRT5
AccessionPrimary (citable) accession number: Q8UHX1
Entry history
Integrated into UniProtKB/Swiss-Prot: March 25, 2003
Last sequence update: June 1, 2002
Last modified: July 9, 2014
This is version 89 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