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Q5LL27 (HISX3_RUEPO) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 69. 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 3

Short name=HDH 3
EC=1.1.1.23
Gene names
Name:hisD3
Ordered Locus Names:SPOA0202
Encoded onPlasmid megaplasmid Spo
OrganismRuegeria pomeroyi (strain ATCC 700808 / DSM 15171 / DSS-3) (Silicibacter pomeroyi) [Complete proteome] [HAMAP]
Taxonomic identifier246200 [NCBI]
Taxonomic lineageBacteriaProteobacteriaAlphaproteobacteriaRhodobacteralesRhodobacteraceaeRuegeria

Protein attributes

Sequence length433 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
Plasmid
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 – 433433Histidinol dehydrogenase 3 HAMAP-Rule MF_01024
PRO_0000135848

Sites

Active site3271Proton acceptor By similarity
Active site3281Proton acceptor By similarity
Metal binding2591Zinc By similarity
Metal binding2621Zinc By similarity
Metal binding3611Zinc By similarity
Metal binding4201Zinc By similarity
Binding site1301NAD By similarity
Binding site1911NAD By similarity
Binding site2141NAD By similarity
Binding site2371Substrate By similarity
Binding site2591Substrate By similarity
Binding site2621Substrate By similarity
Binding site3281Substrate By similarity
Binding site3611Substrate By similarity
Binding site4151Substrate By similarity
Binding site4201Substrate By similarity

Sequences

Sequence LengthMass (Da)Tools
Q5LL27 [UniParc].

Last modified February 1, 2005. Version 1.
Checksum: C15B11CCF2ACC563

FASTA43345,887
        10         20         30         40         50         60 
MPQFLDSRQP DFETAFTALL GAKREDSPDV DAVVAGIIAD VRARGDAAVI ELTERFDRVA 

        70         80         90        100        110        120 
LTPQSLRFST EEIAQAVDEV PAPERAALEL AAARIRAYHE RQMPQDADWT DDTGARLGWR 

       130        140        150        160        170        180 
WSAVSAAGLY VPGGLASYPS SVLMNAIPAK VAGVGRLAIA VPTPDGQVNP LVLLAAQISG 

       190        200        210        220        230        240 
VDEVYRIGGA QAIAALAYGT DTIAPVDKIT GPGNAFVAAA KRRVFGKVGI DMIAGPSEIL 

       250        260        270        280        290        300 
VIADRDNDPD WIALDLLSQA EHDESAQSIL ITDDAAFGRA VAEAVDKRLE TLERRAIAGV 

       310        320        330        340        350        360 
SWRDFGAVIT VSDLDEAAAL SNRIAPEHLE LCVSDPEALA ARTIHAGAIF LGQYTPEAIG 

       370        380        390        400        410        420 
DYVGGPNHVL PTARSARFSS GLSVMDFLKR TTMSRMTPEA LRAIGPAAAQ LARSESLEAH 

       430 
GLSVQARLDR LNG 

« Hide

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000032 Genomic DNA. Translation: AAV97336.1.
RefSeqYP_165031.1. NC_006569.1.

3D structure databases

ProteinModelPortalQ5LL27.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING246200.SPOA0202.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAV97336; AAV97336; SPOA0202.
GeneID3196717.
KEGGsil:SPOA0202.
PATRIC23381738. VBIRuePom114501_4192.

Organism-specific databases

CMRSearch...

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 nameHISX3_RUEPO
AccessionPrimary (citable) accession number: Q5LL27
Entry history
Integrated into UniProtKB/Swiss-Prot: January 10, 2006
Last sequence update: February 1, 2005
Last modified: February 19, 2014
This is version 69 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