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Q8R882 (HISX_THETN) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 85. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
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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.

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_0000135867

Sites

Active site3261Proton acceptor By similarity
Active site3271Proton acceptor By similarity
Metal binding2581Zinc By similarity
Metal binding2611Zinc By similarity
Metal binding3601Zinc By similarity
Metal binding4191Zinc By similarity
Binding site1291NAD By similarity
Binding site1901NAD By similarity
Binding site2131NAD By similarity
Binding site2361Substrate By similarity
Binding site2581Substrate By similarity
Binding site2611Substrate By similarity
Binding site3271Substrate By similarity
Binding site3601Substrate By similarity
Binding site4141Substrate By similarity
Binding site4191Substrate By similarity

Sequences

Sequence LengthMass (Da)Tools
Q8R882 [UniParc].

Last modified June 1, 2002. Version 1.
Checksum: BA4DB51BA0557DB3

FASTA43047,674
        10         20         30         40         50         60 
MIEMFDFTKE VDIGIFNKIQ NRSKLENKEI AKRVEDIIEN VRERKDKALF EYTYMYDGIN 

        70         80         90        100        110        120 
LNSETVKVKE EEIKRAYEEV KEDFLKALDK AIKNITEFHE KQKEKTWMDF KEGIVYGQVL 

       130        140        150        160        170        180 
RPLSSVGIYV PGGTASYPSS VLMNGIPAKV AGVERIVMVS PAGKKGISPY VLVAADKIGI 

       190        200        210        220        230        240 
KEIYKIGGAQ AVAALAFGTE SIPKVDKIVG PGNIYVAMAK RALYGYVDID MVAGPSEILV 

       250        260        270        280        290        300 
IADESASPKY VAADLLSQAE HDVMASSILV TTSKELAEKV KKEIERQMEY LERKEIIAES 

       310        320        330        340        350        360 
LKNFGAIIVI DNLKEAIGIA NEIAPEHLEL VIENPFEILG EIKNAGAVFL GEFSPEPLGD 

       370        380        390        400        410        420 
YLAGPNHVLP TSGTARFFSP LSVRDFVKKM NVLYYSKEAL SSVKDDVITL AEAEELTAHA 

       430 
NSVKVRFYND 

« Hide

References

[1]"A complete sequence of the T. tengcongensis genome."
Bao Q., Tian Y., Li W., Xu Z., Xuan Z., Hu S., Dong W., Yang J., Chen Y., Xue Y., Xu Y., Lai X., Huang L., Dong X., Ma Y., Ling L., Tan H., Chen R. expand/collapse author list , Wang J., Yu J., Yang H.
Genome Res. 12:689-700(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: DSM 15242 / JCM 11007 / NBRC 100824 / MB4.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AE008691 Genomic DNA. Translation: AAM25303.1.
RefSeqNP_623699.1. NC_003869.1.

3D structure databases

ProteinModelPortalQ8R882.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING273068.TTE2138.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAM25303; AAM25303; TTE2138.
GeneID997457.
KEGGtte:TTE2138.
PATRIC23899019. VBITheTen82880_2146.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0141.
HOGENOMHOG000243914.
KOK00013.
OMAGFLFHAN.
OrthoDBEOG6CVVCR.

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_THETN
AccessionPrimary (citable) accession number: Q8R882
Entry history
Integrated into UniProtKB/Swiss-Prot: March 25, 2003
Last sequence update: June 1, 2002
Last modified: May 14, 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