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Q3B5E3 (HISX_PELLD) 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:Plut_0554
OrganismPelodictyon luteolum (strain DSM 273) (Chlorobium luteolum (strain DSM 273)) [Complete proteome] [HAMAP]
Taxonomic identifier319225 [NCBI]
Taxonomic lineageBacteriaChlorobiChlorobiaChlorobialesChlorobiaceaeChlorobium/Pelodictyon groupPelodictyon

Protein attributes

Sequence length443 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 – 443443Histidinol dehydrogenase HAMAP-Rule MF_01024
PRO_0000229860

Sites

Active site3391Proton acceptor By similarity
Active site3401Proton acceptor By similarity
Metal binding2711Zinc By similarity
Metal binding2741Zinc By similarity
Metal binding3731Zinc By similarity
Metal binding4321Zinc By similarity
Binding site1411NAD By similarity
Binding site2031NAD By similarity
Binding site2261NAD By similarity
Binding site2491Substrate By similarity
Binding site2711Substrate By similarity
Binding site2741Substrate By similarity
Binding site3401Substrate By similarity
Binding site3731Substrate By similarity
Binding site4271Substrate By similarity
Binding site4321Substrate By similarity

Sequences

Sequence LengthMass (Da)Tools
Q3B5E3 [UniParc].

Last modified November 22, 2005. Version 1.
Checksum: 7A4C8C653019BE3F

FASTA44348,062
        10         20         30         40         50         60 
MSPVHYRTST STIVAVLKLY RFLDDRDALF RQIGRSVDFD PEVQRAVTDI LEAVRLRGDM 

        70         80         90        100        110        120 
AVLEYTERFQ GAVLTSMQVP EEDILRAREE ADPAFIRVLE EAWENILRFH RHEVENSFFY 

       130        140        150        160        170        180 
EGEGGVVLGQ RVTPMDRAML YVPGGKASYP SSVLMNAAPA RVAGVGEIFM TTPCDASGAV 

       190        200        210        220        230        240 
SPHILAAASV AGVTSVYRLG GAQAVAAFAY GTQTIPKVDI ITGPGNKYVA LAKKQVFGHV 

       250        260        270        280        290        300 
AIDSIAGPSE VVVVADDDAD AEFITMDLFA QAEHDPDASS VLITPSMRLA EEVRDLAAAR 

       310        320        330        340        350        360 
VGSMLRGEVI AEALSNNGAI VVVADIEEAC RVSDMIAPEH LELHVLHPWE LLASIRHAGA 

       370        380        390        400        410        420 
VFMGGYSCET VGDYYAGPNH TLPTNGTARF FSPLSVRDFV KHTSIISYTR RQIMACGERI 

       430        440 
ASFADHEGLE AHAEAVRARL KKG 

« Hide

References

[1]"Complete sequence of Pelodictyon luteolum DSM 273."
US DOE Joint Genome Institute
Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T., Hammon N., Israni S., Pitluck S., Bryant D., Schmutz J., Larimer F., Land M., Kyrpides N., Ivanova N., Richardson P.
Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: DSM 273.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000096 Genomic DNA. Translation: ABB23438.1.
RefSeqYP_374481.1. NC_007512.1.

3D structure databases

ProteinModelPortalQ3B5E3.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING319225.Plut_0554.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABB23438; ABB23438; Plut_0554.
GeneID3746220.
KEGGplt:Plut_0554.
PATRIC21378590. VBIChlLut1287_0577.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0141.
HOGENOMHOG000243914.
KOK00013.
OMAYAAKLCG.
OrthoDBEOG6CVVCR.

Enzyme and pathway databases

BioCycPLUT319225:GHDM-565-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_PELLD
AccessionPrimary (citable) accession number: Q3B5E3
Entry history
Integrated into UniProtKB/Swiss-Prot: April 4, 2006
Last sequence update: November 22, 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