Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

Q48EC9 (HISX_PSE14) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 64. 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 attributes

Sequence length448 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 – 448448Histidinol dehydrogenase HAMAP-Rule MF_01024
PRO_0000135822

Sites

Active site3331Proton acceptor By similarity
Active site3341Proton acceptor By similarity
Metal binding2651Zinc By similarity
Metal binding2681Zinc By similarity
Metal binding3671Zinc By similarity
Metal binding4261Zinc By similarity
Binding site1361NAD By similarity
Binding site1971NAD By similarity
Binding site2201NAD By similarity
Binding site2431Substrate By similarity
Binding site2651Substrate By similarity
Binding site2681Substrate By similarity
Binding site3341Substrate By similarity
Binding site3671Substrate By similarity
Binding site4211Substrate By similarity
Binding site4261Substrate By similarity

Sequences

Sequence LengthMass (Da)Tools
Q48EC9 [UniParc].

Last modified September 13, 2005. Version 1.
Checksum: D44110537C039678

FASTA44848,160
        10         20         30         40         50         60 
MTTPTAIRRL DAADPDFARH LDHLLSWESV SDDSVNQRVL DIIKAVRERG DEALVEFTQK 

        70         80         90        100        110        120 
FDGLQVASMA DLILPRERLE LALTRITPVQ REALEKAAER VRSYHEKQKQ DSWSYTEADG 

       130        140        150        160        170        180 
TVLGQKVTPL DRAGLYVPGG KASYPSSVLM NAIPAKVAGV TEVVMVVPTP RGEINELVLA 

       190        200        210        220        230        240 
AACIAGVDRV FTIGGAQAVA ALAYGTESVP KVDKVVGPGN IYVATAKRHV FGQVGIDMIA 

       250        260        270        280        290        300 
GPSEILVVCD GQTDPDWIAM DLFSQAEHDE DAQAILVSPD ADFLDKVAAS ITRLLPTMER 

       310        320        330        340        350        360 
AAIVETSING RGALIKVADM AQAIEVANRI APEHLELSVA DPEAWLPQIR HAGAIFMGRH 

       370        380        390        400        410        420 
TSEALGDYCA GPNHVLPTSG TARFSSPLGV YDFQKRSSII YCSPQGASEL GKTASVLARG 

       430        440 
ESLSGHARSA EYRITDPDWK AGNTEDGK 

« Hide

References

[1]"Whole-genome sequence analysis of Pseudomonas syringae pv. phaseolicola 1448A reveals divergence among pathovars in genes involved in virulence and transposition."
Joardar V., Lindeberg M., Jackson R.W., Selengut J., Dodson R., Brinkac L.M., Daugherty S.C., DeBoy R.T., Durkin A.S., Gwinn Giglio M., Madupu R., Nelson W.C., Rosovitz M.J., Sullivan S.A., Crabtree J., Creasy T., Davidsen T.M., Haft D.H. expand/collapse author list , Zafar N., Zhou L., Halpin R., Holley T., Khouri H.M., Feldblyum T.V., White O., Fraser C.M., Chatterjee A.K., Cartinhour S., Schneider D., Mansfield J.W., Collmer A., Buell R.
J. Bacteriol. 187:6488-6498(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: 1448A / Race 6.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000058 Genomic DNA. Translation: AAZ37769.1.
RefSeqYP_276259.1. NC_005773.3.

3D structure databases

ProteinModelPortalQ48EC9.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING264730.PSPPH_4137.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAZ37769; AAZ37769; PSPPH_4137.
GeneID3560434.
KEGGpsp:PSPPH_4137.
PATRIC19977743. VBIPseSyr78478_4329.

Organism-specific databases

CMRSearch...

Phylogenomic databases

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

Enzyme and pathway databases

BioCycPSAV264730:GKDE-4141-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_PSE14
AccessionPrimary (citable) accession number: Q48EC9
Entry history
Integrated into UniProtKB/Swiss-Prot: January 10, 2006
Last sequence update: September 13, 2005
Last modified: February 19, 2014
This is version 64 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