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Q318Q4 (HISX_PROM9) 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 namesRecommended name:
Histidinol dehydrogenase

Short name=HDH
EC=1.1.1.23
Gene names
Name:hisD
Ordered Locus Names:PMT9312_1581
OrganismProchlorococcus marinus (strain MIT 9312) [Complete proteome] [HAMAP]
Taxonomic identifier74546 [NCBI]
Taxonomic lineageBacteriaCyanobacteriaProchloralesProchlorococcaceaeProchlorococcus

Protein attributes

Sequence length440 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 – 440440Histidinol dehydrogenase HAMAP-Rule MF_01024
PRO_0000229861

Sites

Active site3371Proton acceptor By similarity
Active site3381Proton acceptor By similarity
Metal binding2691Zinc By similarity
Metal binding2721Zinc By similarity
Metal binding3711Zinc By similarity
Metal binding4301Zinc By similarity
Binding site1391NAD By similarity
Binding site2011NAD By similarity
Binding site2241NAD By similarity
Binding site2471Substrate By similarity
Binding site2691Substrate By similarity
Binding site2721Substrate By similarity
Binding site3381Substrate By similarity
Binding site3711Substrate By similarity
Binding site4251Substrate By similarity
Binding site4301Substrate By similarity

Sequences

Sequence LengthMass (Da)Tools
Q318Q4 [UniParc].

Last modified December 6, 2005. Version 1.
Checksum: 5D93F6C85EBF6D0F

FASTA44048,592
        10         20         30         40         50         60 
MGREPFNLKN LEMRIINNKK DAIQELKRIS SRTNSENNNK INLIVEEILQ EVKTYGDIAV 

        70         80         90        100        110        120 
EKYTKKFDGF NPDPMQISED HLKDAWDEID SNLKRSLEVA HKRIKKFHEK EIPQSFTIKG 

       130        140        150        160        170        180 
EHGDTVQRRW RPVKNAGIYI PGGRAAYPST VLMNAIPAKV AGVEEIIMVS PGNKEGEINK 

       190        200        210        220        230        240 
TVLAAAHLSG IKKVFRIGGA QAIGALAFGT NQINKVDVIT GPGNIYVTTA KKLIYGSTGI 

       250        260        270        280        290        300 
DSLAGPSEIL VIADETAQST HIASDLLAQA EHDPLASSIL LTTSKNQAKE VLEELYKKID 

       310        320        330        340        350        360 
DHPRKEICMQ SIKNWGLIVI CENYELCIEL SNNFAPEHLE ILALDSKKIL EGIENAGAIF 

       370        380        390        400        410        420 
LGKWTPEAVG DYLAGPNHTL PTSGNSRFSG SLGVETFMKN TSIIEFNEES LKVNSLDIIN 

       430        440 
LAESEGLHSH ANSVKIRFED 

« Hide

References

[1]"Complete sequence of Prochlorococcus marinus str. MIT 9312."
US DOE Joint Genome Institute
Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T., Hammon N., Israni S., Pitluck S., Thiel J., Schmutz J., Larimer F., Land M., Kyrpides N., Lykidis A., Richardson P.
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: MIT 9312.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000111 Genomic DNA. Translation: ABB50641.1.
RefSeqYP_398077.1. NC_007577.1.

3D structure databases

ProteinModelPortalQ318Q4.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING74546.PMT9312_1581.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABB50641; ABB50641; PMT9312_1581.
GeneID3766398.
KEGGpmi:PMT9312_1581.
PATRIC23007178. VBIProMar70153_1752.

Organism-specific databases

CMRSearch...

Phylogenomic databases

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

Enzyme and pathway databases

BioCycPMAR74546:GHRG-1618-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_PROM9
AccessionPrimary (citable) accession number: Q318Q4
Entry history
Integrated into UniProtKB/Swiss-Prot: April 4, 2006
Last sequence update: December 6, 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