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Q845V3 (HISX_BURM1) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 77. 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:Bmul_0328, BMULJ_02926
OrganismBurkholderia multivorans (strain ATCC 17616 / 249) [Complete proteome] [HAMAP]
Taxonomic identifier395019 [NCBI]
Taxonomic lineageBacteriaProteobacteriaBetaproteobacteriaBurkholderialesBurkholderiaceaeBurkholderiaBurkholderia cepacia complex

Protein attributes

Sequence length438 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 – 438438Histidinol dehydrogenase HAMAP-Rule MF_01024
PRO_0000135749

Sites

Active site3351Proton acceptor By similarity
Active site3361Proton acceptor By similarity
Metal binding2671Zinc By similarity
Metal binding2701Zinc By similarity
Metal binding3691Zinc By similarity
Metal binding4281Zinc By similarity
Binding site1381NAD By similarity
Binding site1991NAD By similarity
Binding site2221NAD By similarity
Binding site2451Substrate By similarity
Binding site2671Substrate By similarity
Binding site2701Substrate By similarity
Binding site3361Substrate By similarity
Binding site3691Substrate By similarity
Binding site4231Substrate By similarity
Binding site4281Substrate By similarity

Experimental info

Sequence conflict90 – 10112AALEA…ARVRG → GRAGSGCRTRAR in BAC65270. Ref.1

Sequences

Sequence LengthMass (Da)Tools
Q845V3 [UniParc].

Last modified September 2, 2008. Version 2.
Checksum: 8F702C8C7E014B1D

FASTA43846,515
        10         20         30         40         50         60 
MSITIRKLDS TSEGFDAALR AVLAFEASED EAIERSVAQI LADVKSRGDA AVLEYTNRFD 

        70         80         90        100        110        120 
RLNADSVAAL ELPQDALQAA LDGLEPKARA ALEAAAARVR GYHEKQKIEC GTHSWQYTES 

       130        140        150        160        170        180 
DGTVLGQKIT PLDRVGLYVP GGKAAYPSSV LMNAIPARVA GVGEIVMVVP TPDGVKNDLV 

       190        200        210        220        230        240 
LAAALLGGVD RVFTIGGAQA VGALAYGTAT VPAVDKICGP GNAYVASAKR RVFGTVGIDM 

       250        260        270        280        290        300 
IAGPSEILVL CDGTTDPSWV AMDLFSQAEH DELAQSILLC PDASFIERVE KAIAELLPSM 

       310        320        330        340        350        360 
PRQDVIRASL EGRGALIKVR DMTEACRIAN DIAPEHLEIS ALEPQQWSQQ IRHAGAIFLG 

       370        380        390        400        410        420 
RYTSESLGDY CAGPNHVLPT SRTARFSSPL GVYDFIKRSS LIEVSAEGAH TLGEIAAELA 

       430 
YGEGLQAHAK SAEFRMKG 

« Hide

References

« Hide 'large scale' references
[1]"Distribution and organization of auxotrophic genes on the multichromosomal genome of Burkholderia multivorans ATCC 17616."
Komatsu H., Imura Y., Ohori A., Nagata Y., Tsuda M.
J. Bacteriol. 185:3333-3343(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]"Complete sequence of chromosome 1 of Burkholderia multivorans ATCC 17616."
Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E., Tice H., Pitluck S., Chain P., Malfatti S., Shin M., Vergez L., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N., Kim E., Tiedje J., Richardson P.
Submitted (OCT-2007) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 17616 / 249.
[3]"Complete genome sequence of Burkholderia multivorans ATCC 17616."
Ohtsubo Y., Yamashita A., Kurokawa K., Takami H., Yuhara S., Nishiyama E., Endo R., Miyazaki R., Ono A., Yano K., Ito M., Sota M., Yuji N., Hattori M., Tsuda M.
Submitted (APR-2007) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 17616 / 249.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AB091436 Genomic DNA. Translation: BAC65270.1.
CP000868 Genomic DNA. Translation: ABX14023.1.
AP009385 Genomic DNA. Translation: BAG44811.1.
RefSeqYP_001578520.1. NC_010084.1.
YP_001947347.1. NC_010804.1.

3D structure databases

ProteinModelPortalQ845V3.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING395019.Bmul_0328.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABX14023; ABX14023; Bmul_0328.
BAG44811; BAG44811; BMULJ_02926.
GeneID5765433.
6359505.
KEGGbmj:BMULJ_02926.
bmu:Bmul_0328.
PATRIC19167814. VBIBurMul203716_3956.

Organism-specific databases

CMRSearch...

Phylogenomic databases

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

Enzyme and pathway databases

BioCycBMUL395019:GIYO-2924-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_BURM1
AccessionPrimary (citable) accession number: Q845V3
Secondary accession number(s): A9AE01
Entry history
Integrated into UniProtKB/Swiss-Prot: April 13, 2004
Last sequence update: September 2, 2008
Last modified: February 19, 2014
This is version 77 of the entry and version 2 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