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Q6D411 (HISX_PECAS) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 74. 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:ECA2583
OrganismPectobacterium atrosepticum (strain SCRI 1043 / ATCC BAA-672) (Erwinia carotovora subsp. atroseptica) [Complete proteome] [HAMAP]
Taxonomic identifier218491 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaePectobacterium

Protein attributes

Sequence length442 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

Subunit structure

Homodimer By similarity. 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 – 442442Histidinol dehydrogenase HAMAP-Rule MF_01024
PRO_0000135769

Sites

Active site3341Proton acceptor By similarity
Active site3351Proton acceptor By similarity
Metal binding2671Zinc By similarity
Metal binding2701Zinc By similarity
Metal binding3681Zinc By similarity
Metal binding4271Zinc By similarity
Binding site1381NAD By similarity
Binding site1961NAD By similarity
Binding site2191NAD By similarity
Binding site2451Substrate By similarity
Binding site2671Substrate By similarity
Binding site2701Substrate By similarity
Binding site3351Substrate By similarity
Binding site3681Substrate By similarity
Binding site4221Substrate By similarity
Binding site4271Substrate By similarity

Sequences

Sequence LengthMass (Da)Tools
Q6D411 [UniParc].

Last modified August 16, 2004. Version 1.
Checksum: 1BE05D0BA8FAC677

FASTA44246,850
        10         20         30         40         50         60 
MADNTNSTGS FSTLVDWQRC SVEEQRQLLT RPAISASDRI TAVVSDILTN VKSRGDGALR 

        70         80         90        100        110        120 
DYSAQFDKVQ VDAIRITDAE IAAASARLGD EVKQAMAIAV RNIETFHNAQ KLPIVDIETQ 

       130        140        150        160        170        180 
PGVRCQQITR PIATVGLYIP GGSAPLPSTV LMLGTPSRIA GCRRVVLCSP PPIADEILYA 

       190        200        210        220        230        240 
AQLCGIKEVF QLGGAQAIAA MAFGTDSVPK VDKIFGPGNA YVTEAKRQVS QQLDGAAIDM 

       250        260        270        280        290        300 
PAGPSEVLVI ADSGATPAFV ASDLLSQAEH GPDSQVILLT PDAVMAKAVA DAVEEQLTQL 

       310        320        330        340        350        360 
SRADIARQAL ASSRVIVARD LAQCIEISNQ YGPEHLIIQT RDAESLVDSI TSAGSVFLGD 

       370        380        390        400        410        420 
WSPESAGDYA SGTNHVLPTY GYTSTYSSLG LADFQKRMTV QQLTPQGLLQ LAPTIEILAQ 

       430        440 
AEQLTAHKNA VTLRVAALKE QA 

« Hide

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
BX950851 Genomic DNA. Translation: CAG75482.1.
RefSeqYP_050674.1. NC_004547.2.

3D structure databases

ProteinModelPortalQ6D411.
SMRQ6D411. Positions 10-442.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING218491.ECA2583.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaCAG75482; CAG75482; ECA2583.
GeneID2882559.
KEGGeca:ECA2583.
PATRIC20480467. VBIPecAtr54885_2617.

Organism-specific databases

CMRSearch...

Phylogenomic databases

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

Enzyme and pathway databases

BioCycPATR218491:GJNB-2626-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_PECAS
AccessionPrimary (citable) accession number: Q6D411
Entry history
Integrated into UniProtKB/Swiss-Prot: December 7, 2004
Last sequence update: August 16, 2004
Last modified: April 16, 2014
This is version 74 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