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Q2YZB4 (HISX_STAAB) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 65. 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:SAB2554c
OrganismStaphylococcus aureus (strain bovine RF122 / ET3-1) [Complete proteome] [HAMAP]
Taxonomic identifier273036 [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_0000229866

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
Q2YZB4 [UniParc].

Last modified December 20, 2005. Version 1.
Checksum: D05A097D8E2860C5

FASTA41646,206
        10         20         30         40         50         60 
MLNAQQFLNQ FSLEAPLDES LYPIIRDICQ EVKVHGDKAL KMYNLTFDHT KTDHLEISHE 

        70         80         90        100        110        120 
QIKAAFDTLD EKTKQALQQS YERIKAYQES IKQTNQQLEK 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 ELARTYVISE DAQVLKDLES RITKALPNVD RYDIVSKSIA NQHYLIHASN 

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

       370        380        390        400        410 
RTARFTNGLS VNDFLTRNTV IHLSKDTFEQ IADSAQHIAH VEALYNHQQS ILIRQS 

« Hide

References

[1]"Molecular correlates of host specialization in Staphylococcus aureus."
Herron-Olson L., Fitzgerald J.R., Musser J.M., Kapur V.
PLoS ONE 2:E1120-E1120(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: bovine RF122 / ET3-1.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AJ938182 Genomic DNA. Translation: CAI82242.1.
RefSeqYP_417997.1. NC_007622.1.

3D structure databases

ProteinModelPortalQ2YZB4.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING273036.SAB2554c.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaCAI82242; CAI82242; SAB2554c.
GeneID3794915.
KEGGsab:SAB2554c.
PATRIC19526193. VBIStaAur92441_2692.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0141.
HOGENOMHOG000243914.
KOK00013.
OMAICGPGNK.
OrthoDBEOG6CVVCR.

Enzyme and pathway databases

BioCycSAUR273036:GJVS-2627-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_STAAB
AccessionPrimary (citable) accession number: Q2YZB4
Entry history
Integrated into UniProtKB/Swiss-Prot: April 4, 2006
Last sequence update: December 20, 2005
Last modified: May 14, 2014
This is version 65 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