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P62456 (HISX_BACC1) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 65. Feed History...

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

Protein namesRecommended name:
Histidinol dehydrogenase
Short name=HDH
EC=1.1.1.23
Gene names
Name:hisD
Ordered Locus Names:BCE_1526
OrganismBacillus cereus (strain ATCC 10987) [Complete proteome] [HAMAP]
Taxonomic identifier222523 [NCBI]
Taxonomic lineageBacteria › Firmicutes › Bacillales › Bacillaceae › Bacillus › Bacillus cereus group

Protein attributes

Sequence length429 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 MF_01024

Catalytic activity

L-histidinol + H2O + 2 NAD+ = L-histidine + 2 NADH. HAMAP MF_01024

Cofactor

Binds 1 zinc ion per subunit By similarity. HAMAP MF_01024

Pathway

Amino-acid biosynthesis; L-histidine biosynthesis; L-histidine from 5-phospho-alpha-D-ribose 1-diphosphate: step 9/9. HAMAP 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-KW

   Molecular functionNAD binding

Inferred from electronic annotation. Source: InterPro

histidinol dehydrogenase activity

Inferred from electronic annotation. Source: EC

zinc ion binding

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 429429Histidinol dehydrogenase HAMAP MF_01024
PRO_0000135721

Sites

Active site3241Proton acceptor By similarity
Active site3251Proton acceptor By similarity
Metal binding2561Zinc By similarity
Metal binding2591Zinc By similarity
Metal binding3581Zinc By similarity
Metal binding4171Zinc By similarity
Binding site1271NAD By similarity
Binding site1881NAD By similarity
Binding site2111NAD By similarity
Binding site2341Substrate By similarity
Binding site2561Substrate By similarity
Binding site2591Substrate By similarity
Binding site3251Substrate By similarity
Binding site3581Substrate By similarity
Binding site4121Substrate By similarity
Binding site4171Substrate By similarity

Sequences

Sequence LengthMass (Da)Tools
P62456 [UniParc].

Last modified July 5, 2004. Version 1.
Checksum: FBA64A1F6C18A30A

FASTA42947,360
        10         20         30         40         50         60 
MEIVFEDFQK ALSKIKLLRE NANIIEETVQ RNVSEIVRNV RESGDEALSF YTKKFDGVKI 

        70         80         90        100        110        120 
KEFRVSEEEE KRASMFVENS FLEALQEAKK NIISYHEKQK RQSMFDCASE GIIRGQIIRP 

       130        140        150        160        170        180 
LENVGVYVPG GTASYPSSVL MNVLPAKLAG VKKIVMVTPP REGGIDPHIL VAASLAGVDE 

       190        200        210        220        230        240 
IYTIGGAQAI AALAYGTESI PKVDKIVGPG NLYVALAKRE VYGIVNIDMI AGPSEIVVIA 

       250        260        270        280        290        300 
DETGNAKYIA ADLLSQAEHD ERATAICITT NIELAKKVEK EIERQLETLP RSEIARESIN 

       310        320        330        340        350        360 
RNGAIFIVPS IDEALQLSNE IAPEHLELHI KEPMNALAYV KHAGSIFLGP YAPEPLGDYL 

       370        380        390        400        410        420 
AGPNHVLPTS GTARFFSPLS VDDFVKKSSF LSYTEEALRD VQHHIVELAN KEGLHAHARA 


IQIRFEEEE

« Hide

References

[1]"The genome sequence of Bacillus cereus ATCC 10987 reveals metabolic adaptations and a large plasmid related to Bacillus anthracis pXO1."
Rasko D.A., Ravel J., Oekstad O.A., Helgason E., Cer R.Z., Jiang L., Shores K.A., Fouts D.E., Tourasse N.J., Angiuoli S.V., Kolonay J.F., Nelson W.C., Kolstoe A.-B., Fraser C.M., Read T.D.
Nucleic Acids Res. 32:977-988(2004) [PubMed: 14960714] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 10987.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		AE017194 Genomic DNA. Translation: AAS40455.1.
RefSeqNP_977847.1. NC_003909.8.

3D structure databases

ProteinModelPortalP62456.
ModBaseSearch...

Protein-protein interaction databases

STRINGP62456.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaEBBACT00000024785; EBBACP00000024135; EBBACG00000024776.
GeneID2748395.
GenomeReviewsGene locus BCE_1526 in contig AE017194_GR.
KEGGbca:BCE_1526.
NMPDRfig|222523.1.peg.1519.
PATRIC18851896. VBIBacCer118379_1452.
TIGRBCE_1526.

Phylogenomic databases

eggNOGCOG0141.
GeneTreeEBGT00050000002843.
HOGENOMHBG329596.
OMANRYVTEA.
ProtClustDBPRK00877.

Enzyme and pathway databases

BioCycBCER405917:BCE_1526-MONOMER.

Family and domain databases

HAMAPMF_01024. HisD.
[Tree]
InterProIPR016161. Ald_DH/histidinol_DH.
IPR001692. Histidinol_DH_CS.
IPR022695. Histidinol_DH_monofunct.
IPR012131. Hstdl_DH.
[Graphical view]
KOK00013.
PANTHERPTHR21256:SF2. Hstdl_DH_prok. 1 hit.
PfamPF00815. Histidinol_dh. 1 hit.
[Graphical view]
PIRSFPIRSF000099. Histidinol_dh. 1 hit.
PRINTSPR00083. HOLDHDRGNASE.
SUPFAMSSF53720. Aldehyde_DH/Histidinol_DH. 1 hit.
TIGRFAMsTIGR00069. HisD. 1 hit.
PROSITEPS00611. HISOL_DEHYDROGENASE. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameHISX_BACC1
AccessionPrimary (citable) accession number: P62456
Entry history
Integrated into UniProtKB/Swiss-Prot: July 5, 2004
Last sequence update: July 5, 2004
Last modified: January 25, 2012
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

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

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