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Q8F393 (HISX_LEPIN) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 86. 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:LA_2515
OrganismLeptospira interrogans serogroup Icterohaemorrhagiae serovar Lai (strain 56601) [Reference proteome] [HAMAP]
Taxonomic identifier189518 [NCBI]
Taxonomic lineageBacteriaSpirochaetesSpirochaetalesLeptospiraceaeLeptospira

Protein attributes

Sequence length427 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 – 427427Histidinol dehydrogenase HAMAP-Rule MF_01024
PRO_0000135788

Sites

Active site3251Proton acceptor By similarity
Active site3261Proton acceptor By similarity
Metal binding2561Zinc By similarity
Metal binding2591Zinc By similarity
Metal binding3591Zinc By similarity
Metal binding4191Zinc By similarity
Binding site1251NAD By similarity
Binding site1861NAD By similarity
Binding site2091NAD By similarity
Binding site2341Substrate By similarity
Binding site2561Substrate By similarity
Binding site2591Substrate By similarity
Binding site3261Substrate By similarity
Binding site3591Substrate By similarity
Binding site4131Substrate By similarity
Binding site4191Substrate By similarity

Sequences

Sequence LengthMass (Da)Tools
Q8F393 [UniParc].

Last modified March 1, 2003. Version 1.
Checksum: 2FA9AB963E5D48ED

FASTA42746,380
        10         20         30         40         50         60 
MAIQIFKVGL KDHSVLDPVL KRAREDLSST LALVKPIVED VKNRGDSALR EYTQKFDEVI 

        70         80         90        100        110        120 
PPKSFVLEIS KLNPKIDPKL KTALVKAAKN IRNFHKIQIP ENKEIIIHGN KLGILHTPIE 

       130        140        150        160        170        180 
SVSVYAPGGK ALYPSTILMG VIPAKLAGVK NIQIVTPPRK GTLPDGLIAA AKIAGADRIV 

       190        200        210        220        230        240 
MAGGAQGIAA VSYGTESIPS SEFVVGPGNK FVTAAKVYLS GQGVIGIDSP AGPSEVLIIA 

       250        260        270        280        290        300 
DDSADPMWVA ADLLSQAEHG EDSVAILCTN SLSLAQKVKE EVEKALIERP KRGEMKRKSI 

       310        320        330        340        350        360 
KDHGKIFVFS NLEECFVFSN LFAPEHLEIQ TKNFKKDLKK VKHAGSVFLG NYSPVAMGDY 

       370        380        390        400        410        420 
ISGTNHILPT AGAARIYSSL GVSTFLKRVT WQEVSKKSIQ NLYPHVKVLS EFEGLDEEHG 


NSVRIRR 

« Hide

References

[1]"Unique physiological and pathogenic features of Leptospira interrogans revealed by whole-genome sequencing."
Ren S.-X., Fu G., Jiang X.-G., Zeng R., Miao Y.-G., Xu H., Zhang Y.-X., Xiong H., Lu G., Lu L.-F., Jiang H.-Q., Jia J., Tu Y.-F., Jiang J.-X., Gu W.-Y., Zhang Y.-Q., Cai Z., Sheng H.-H. expand/collapse author list , Yin H.-F., Zhang Y., Zhu G.-F., Wan M., Huang H.-L., Qian Z., Wang S.-Y., Ma W., Yao Z.-J., Shen Y., Qiang B.-Q., Xia Q.-C., Guo X.-K., Danchin A., Saint Girons I., Somerville R.L., Wen Y.-M., Shi M.-H., Chen Z., Xu J.-G., Zhao G.-P.
Nature 422:888-893(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: 56601.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AE010300 Genomic DNA. Translation: AAN49714.1.
RefSeqNP_712696.1. NC_004342.2.

3D structure databases

ProteinModelPortalQ8F393.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING189518.LA2515.

Proteomic databases

PaxDbQ8F393.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAN49714; AAN49714; LA_2515.
GeneID1151858.
KEGGlil:LA_2515.
PATRIC22385862. VBILepInt91350_2497.

Phylogenomic databases

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

Enzyme and pathway databases

BioCycLINT189518:GJBB-2055-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_LEPIN
AccessionPrimary (citable) accession number: Q8F393
Entry history
Integrated into UniProtKB/Swiss-Prot: March 25, 2003
Last sequence update: March 1, 2003
Last modified: February 19, 2014
This is version 86 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