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Q8CQ95 (HISX_STAES) 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
Ordered Locus Names:SE_0272
OrganismStaphylococcus epidermidis (strain ATCC 12228) [Complete proteome] [HAMAP]
Taxonomic identifier176280 [NCBI]
Taxonomic lineageBacteriaFirmicutesBacilliBacillalesStaphylococcus

Protein attributes

Sequence length414 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 – 414414Histidinol dehydrogenase HAMAP-Rule MF_01024
PRO_0000135855

Sites

Active site3131Proton acceptor By similarity
Active site3141Proton acceptor By similarity
Metal binding2451Zinc By similarity
Metal binding2481Zinc By similarity
Metal binding3471Zinc By similarity
Metal binding4061Zinc By similarity
Binding site1161NAD By similarity
Binding site1771NAD By similarity
Binding site2001NAD By similarity
Binding site2231Substrate By similarity
Binding site2451Substrate By similarity
Binding site2481Substrate By similarity
Binding site3141Substrate By similarity
Binding site3471Substrate By similarity
Binding site4011Substrate By similarity
Binding site4061Substrate By similarity

Sequences

Sequence LengthMass (Da)Tools
Q8CQ95 [UniParc].

Last modified March 1, 2003. Version 1.
Checksum: 5D96007ECE4E1843

FASTA41446,494
        10         20         30         40         50         60 
MLSAQQFLKE FNNVESLNES LYEIVSHICE EVKLQGDKAL KNYNLQFDQV ETEKLELEQS 

        70         80         90        100        110        120 
QLKNAYDMLD NETRDALEQS YQRIKVYQEN IKVKQESSQQ TECYERYHPI ERVGIYVPGG 

       130        140        150        160        170        180 
KASYPSTVLM TATLAQVAGV NEITVVTPPQ NNGICQEVLA ACYITGVHHV YQVGGAQSIA 

       190        200        210        220        230        240 
ALTYGTETIK KVDKIVGPGN QYVAYAKKFV FGQVGIDQIA GPTEIALIID ESADLDAIAY 

       250        260        270        280        290        300 
DVFAQAEHDE MACTYVISEN EKVLNQLNTI IQEKLQYVER QDIISQSIAN HHYLILAQDT 

       310        320        330        340        350        360 
EEACLIMNTI APEHASIQTR APEMYIDKVK YVGALFLGHF SPEVIGDYMA GPSHVLPTNQ 

       370        380        390        400        410 
TARFTNGLSV NDFMTRHSVI HLSQKTFNEV AESAEHIAHI ESLFNHEKSI HVRR 

« Hide

References

[1]"Genome-based analysis of virulence genes in a non-biofilm-forming Staphylococcus epidermidis strain (ATCC 12228)."
Zhang Y.-Q., Ren S.-X., Li H.-L., Wang Y.-X., Fu G., Yang J., Qin Z.-Q., Miao Y.-G., Wang W.-Y., Chen R.-S., Shen Y., Chen Z., Yuan Z.-H., Zhao G.-P., Qu D., Danchin A., Wen Y.-M.
Mol. Microbiol. 49:1577-1593(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 12228.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AE015929 Genomic DNA. Translation: AAO03869.1.
RefSeqNP_763827.1. NC_004461.1.

3D structure databases

ProteinModelPortalQ8CQ95.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING176280.SE0272.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAO03869; AAO03869; SE_0272.
GeneID1058081.
KEGGsep:SE0272.
PATRIC19606343. VBIStaEpi113981_0250.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0141.
KOK00013.
OMAPSEILII.
OrthoDBEOG6CVVCR.
ProtClustDBPRK13770.

Enzyme and pathway databases

BioCycSEPI176280:GCDG-274-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_STAES
AccessionPrimary (citable) accession number: Q8CQ95
Entry history
Integrated into UniProtKB/Swiss-Prot: March 25, 2003
Last sequence update: March 1, 2003
Last modified: February 19, 2014
This is version 88 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