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P16245 (HISX_STRCO) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 110. 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:SCO2054
ORF Names:SC4G6.23c
OrganismStreptomyces coelicolor (strain ATCC BAA-471 / A3(2) / M145) [Reference proteome] [HAMAP]
Taxonomic identifier100226 [NCBI]
Taxonomic lineageBacteriaActinobacteriaActinobacteridaeActinomycetalesStreptomycineaeStreptomycetaceaeStreptomyces

Protein attributes

Sequence length441 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 – 441441Histidinol dehydrogenase HAMAP-Rule MF_01024
PRO_0000135860

Sites

Active site3321Proton acceptor By similarity
Active site3331Proton acceptor By similarity
Metal binding2621Zinc By similarity
Metal binding2651Zinc By similarity
Metal binding3661Zinc By similarity
Metal binding4251Zinc By similarity
Binding site2401Substrate By similarity
Binding site2621Substrate By similarity
Binding site2651Substrate By similarity
Binding site3331Substrate By similarity
Binding site3661Substrate By similarity
Binding site4201Substrate By similarity
Binding site4251Substrate By similarity

Experimental info

Sequence conflict2621Q → L in CAA45767. Ref.2

Sequences

Sequence LengthMass (Da)Tools
P16245 [UniParc].

Last modified December 1, 2000. Version 3.
Checksum: 3B0B26BA17F91743

FASTA44146,493
        10         20         30         40         50         60 
MISRIDLRGD ALPEGPALRD LLPRADFDVS VALEKVRPIC EAVHHRGDAA LIDFTEQFDG 

        70         80         90        100        110        120 
VRLERVRVPA EELTRALEGL DPEVRAALEE SIRRARLVHR EQRRATHTTQ VVPGGSVTEK 

       130        140        150        160        170        180 
WVPVERVGLY VPGGRSVYPS SVVMNVVPAQ EAGVGSIALA SPAQAEFGGI PHPTILAACA 

       190        200        210        220        230        240 
LLGVDEVYAA GGATAVAMFA YGTESCPPAN MVTGPGNIWV AAAKRFFTGK IGIDAEAGPT 

       250        260        270        280        290        300 
EIAVLADSTA DPVHVASDLI SQAEHDPLAA AVLVTDSAEL ADAVEKELQP QVEATKHIED 

       310        320        330        340        350        360 
RIRPALAGRQ SAIVLVDGLD EGLRVVDAYG AEHLEIQTAD AAAVADRVKN AGAIFVGPWA 

       370        380        390        400        410        420 
PVSLGDYAAG SNHVLPTGGC ACHSSGLSVQ SFLRGIHIVD YTRDALAEVA RHVVTLAEAE 

       430        440 
DLPAHGAAIK ARFEWKVPES K 

« Hide

References

« Hide 'large scale' references
[1]"Complete genome sequence of the model actinomycete Streptomyces coelicolor A3(2)."
Bentley S.D., Chater K.F., Cerdeno-Tarraga A.-M., Challis G.L., Thomson N.R., James K.D., Harris D.E., Quail M.A., Kieser H., Harper D., Bateman A., Brown S., Chandra G., Chen C.W., Collins M., Cronin A., Fraser A., Goble A. expand/collapse author list , Hidalgo J., Hornsby T., Howarth S., Huang C.-H., Kieser T., Larke L., Murphy L.D., Oliver K., O'Neil S., Rabbinowitsch E., Rajandream M.A., Rutherford K.M., Rutter S., Seeger K., Saunders D., Sharp S., Squares R., Squares S., Taylor K., Warren T., Wietzorrek A., Woodward J.R., Barrell B.G., Parkhill J., Hopwood D.A.
Nature 417:141-147(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC BAA-471 / A3(2) / M145.
[2]"Further characterization of the histidine gene cluster of Streptomyces coelicolor A3(2): nucleotide sequence and transcriptional analysis of hisD."
Limauro D., Avitabile A., Puglia A.M., Bruni C.B.
Res. Microbiol. 143:683-693(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-288.
Strain: A3(2) / NRRL B-16638.
[3]"Cloning and characterization of the histidine biosynthetic gene cluster of Streptomyces coelicolor A3(2)."
Limauro D., Avitabile A., Cappellano M., Puglia A.M., Bruni C.B.
Gene 90:31-41(1990) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 287-441.
Strain: A3(2) / NRRL B-16638.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AL939111 Genomic DNA. Translation: CAB51446.1.
X64420 Genomic DNA. Translation: CAA45767.1.
M31628 Genomic DNA. Translation: AAA26755.1.
PIRT35083.
RefSeqNP_626314.1. NC_003888.3.

3D structure databases

ProteinModelPortalP16245.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING100226.SCO2054.

Proteomic databases

PRIDEP16245.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaCAB51446; CAB51446; CAB51446.
GeneID1097488.
KEGGsco:SCO2054.
PATRIC23733754. VBIStrCoe124346_2086.

Phylogenomic databases

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

Enzyme and pathway databases

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_STRCO
AccessionPrimary (citable) accession number: P16245
Secondary accession number(s): Q59834, Q9S2T5
Entry history
Integrated into UniProtKB/Swiss-Prot: August 1, 1990
Last sequence update: December 1, 2000
Last modified: February 19, 2014
This is version 110 of the entry and version 3 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