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

Q606Q2 (HISX_METCA) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 71. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | 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:MCA1963
OrganismMethylococcus capsulatus (strain ATCC 33009 / NCIMB 11132 / Bath) [Complete proteome] [HAMAP]
Taxonomic identifier243233 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaMethylococcalesMethylococcaceaeMethylococcus

Protein attributes

Sequence length436 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

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 term3D-structure
Complete 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 – 436436Histidinol dehydrogenase HAMAP-Rule MF_01024
PRO_0000135794

Sites

Active site3321Proton acceptor By similarity
Active site3331Proton acceptor By similarity
Metal binding2641Zinc By similarity
Metal binding2671Zinc By similarity
Metal binding3661Zinc By similarity
Metal binding4251Zinc By similarity
Binding site1351NAD By similarity
Binding site1961NAD By similarity
Binding site2191NAD By similarity
Binding site2421Substrate By similarity
Binding site2641Substrate By similarity
Binding site2671Substrate By similarity
Binding site3331Substrate By similarity
Binding site3661Substrate By similarity
Binding site4201Substrate By similarity
Binding site4251Substrate By similarity

Secondary structure

.................................................................... 436
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Q606Q2 [UniParc].

Last modified November 23, 2004. Version 1.
Checksum: 161D3DEAAE8BDE17

FASTA43647,045
        10         20         30         40         50         60 
MTEVKIKRLY TGDADFASQL DRLLAWSESE DTDIHQRVTE IIGCIRRDGD AALVELTARF 

        70         80         90        100        110        120 
DHFVVDTAAA LELPRDVLEA AWQALPAEQA KALREAAERI RAYAERQKLD SWDYREADGT 

       130        140        150        160        170        180 
LLGQKITPLD RVGLYVPGGK AAYPSSVLMN AVPAKVAGVP ELIMAVPAPR GELNALVLAA 

       190        200        210        220        230        240 
AYISGVDRVF RIGGAQAVAA LAYGTETVPR VDKIVGPGNI YVATAKKLVF GQVGIDMVAG 

       250        260        270        280        290        300 
PSEILVISDG RTDPDWIAMD LFSQAEHDED AQAILISPDA AHLEAVQASI ERLLPGMERA 

       310        320        330        340        350        360 
EVIRTSLERR GGMILVDDLE QAAAVANRIA PEHLELSVES PEVLVESIRN AGAIFMGRYT 

       370        380        390        400        410        420 
AEALGDYCAG PNHVLPTSGT ARFSSPLGVY DFQKRSSLIY CSPDGADQLG RTASLLAWGE 

       430 
GLGAHARSAE YRIRHH 

« Hide

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AE017282 Genomic DNA. Translation: AAU92021.1.
RefSeqYP_114396.1. NC_002977.6.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
4GICX-ray2.05A/B1-422[»]
ProteinModelPortalQ606Q2.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING243233.MCA1963.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAU92021; AAU92021; MCA1963.
GeneID3102435.
KEGGmca:MCA1963.
PATRIC22607774. VBIMetCap22254_1995.

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 nameHISX_METCA
AccessionPrimary (citable) accession number: Q606Q2
Entry history
Integrated into UniProtKB/Swiss-Prot: January 10, 2006
Last sequence update: November 23, 2004
Last modified: February 19, 2014
This is version 71 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

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

PATHWAY comments

Index of metabolic and biosynthesis pathways