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P63954 (HISX_STAAW) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 72. 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:MW2597
OrganismStaphylococcus aureus (strain MW2) [Complete proteome] [HAMAP]
Taxonomic identifier196620 [NCBI]
Taxonomic lineageBacteriaFirmicutesBacilliBacillalesStaphylococcus

Protein attributes

Sequence length416 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 – 416416Histidinol dehydrogenase HAMAP-Rule MF_01024
PRO_0000135853

Sites

Active site3141Proton acceptor By similarity
Active site3151Proton acceptor By similarity
Metal binding2461Zinc By similarity
Metal binding2491Zinc By similarity
Metal binding3481Zinc By similarity
Metal binding4071Zinc By similarity
Binding site1171NAD By similarity
Binding site1781NAD By similarity
Binding site2011NAD By similarity
Binding site2241Substrate By similarity
Binding site2461Substrate By similarity
Binding site2491Substrate By similarity
Binding site3151Substrate By similarity
Binding site3481Substrate By similarity
Binding site4021Substrate By similarity
Binding site4071Substrate By similarity

Sequences

Sequence LengthMass (Da)Tools
P63954 [UniParc].

Last modified October 11, 2004. Version 1.
Checksum: EE6639C9B503264A

FASTA41646,161
        10         20         30         40         50         60 
MLNAQQFLNQ FSLEAPLDES LYPIIRDICQ EVKVHGDKAL KMYNLTFDHT KTDHLEISHE 

        70         80         90        100        110        120 
QIKAAFDTLD EKTKQALQQS YERIKAYQES IKQTNQQLEE SVECYEIYHP LESVGIYVPG 

       130        140        150        160        170        180 
GKASYPSTVL MTATLAQVAG VENIVVVTPP QPNGVSQEVL AACYITQVNQ VFQVGGAQSI 

       190        200        210        220        230        240 
AALTYGTETI PKVDKIVGPG NQFVAYAKKY LFGQVGIDQI AGPTEIALII DDTADLDAIV 

       250        260        270        280        290        300 
YDVFAQAEHD ELARTYVIGE DAQVLKDLES RIAKALPNVD RYDIVSKSIA NQHYLIHASN 

       310        320        330        340        350        360 
FDEACHVMNT IAPEHASIQT VNPQPYIEKV KYVGALFIGH YSPEVIGDYV AGPSHVLPTN 

       370        380        390        400        410 
RTARFTNGLS VNDFLTRNTV IHLSKDTFEQ IADSAQHIAH VEALYNHQQS ILIRQS 

« Hide

References

[1]"Genome and virulence determinants of high virulence community-acquired MRSA."
Baba T., Takeuchi F., Kuroda M., Yuzawa H., Aoki K., Oguchi A., Nagai Y., Iwama N., Asano K., Naimi T., Kuroda H., Cui L., Yamamoto K., Hiramatsu K.
Lancet 359:1819-1827(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: MW2.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
BA000033 Genomic DNA. Translation: BAB96462.1.
RefSeqNP_647414.1. NC_003923.1.

3D structure databases

ProteinModelPortalP63954.
SMRP63954. Positions 18-414.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING196620.MW2597.

Proteomic databases

PRIDEP63954.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaBAB96462; BAB96462; BAB96462.
GeneID1004733.
KEGGsam:MW2597.
PATRIC19571948. VBIStaAur44266_2685.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0141.
HOGENOMHOG000243914.
KOK00013.
OMAPSEILII.
OrthoDBEOG6CVVCR.
ProtClustDBPRK13770.

Enzyme and pathway databases

BioCycSAUR196620:GJ9Z-2673-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_STAAW
AccessionPrimary (citable) accession number: P63954
Secondary accession number(s): Q99QW3
Entry history
Integrated into UniProtKB/Swiss-Prot: October 11, 2004
Last sequence update: October 11, 2004
Last modified: February 19, 2014
This is version 72 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