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Q31GY9 (HISX_THICR) 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:Tcr_0989
OrganismThiomicrospira crunogena (strain XCL-2) [Complete proteome] [HAMAP]
Taxonomic identifier317025 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaThiotrichalesPiscirickettsiaceaeThiomicrospira

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
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 HAMAP-Rule MF_01024
PRO_0000229867

Sites

Active site3301Proton acceptor By similarity
Active site3311Proton acceptor By similarity
Metal binding2621Zinc By similarity
Metal binding2651Zinc By similarity
Metal binding3641Zinc By similarity
Metal binding4231Zinc By similarity
Binding site1331NAD By similarity
Binding site1941NAD By similarity
Binding site2171NAD By similarity
Binding site2401Substrate By similarity
Binding site2621Substrate By similarity
Binding site2651Substrate By similarity
Binding site3311Substrate By similarity
Binding site3641Substrate By similarity
Binding site4181Substrate By similarity
Binding site4231Substrate By similarity

Sequences

Sequence LengthMass (Da)Tools
Q31GY9 [UniParc].

Last modified December 6, 2005. Version 1.
Checksum: FFD6A52F32331691

FASTA43346,827
        10         20         30         40         50         60 
MLNIRKLSAN ADGFKAELEA LLAWETVSND SVNEIVKDVL KNVRERGDEA LLEYTAKFDR 

        70         80         90        100        110        120 
LTLAKGSDLE IPKSELEAAL KRIPKDQRDG LELSAQRVKD YHEKQVMKSW SYTEDDGTFL 

       130        140        150        160        170        180 
GQQVTCLDRV GLYVPGGKAA YPSSVIMNAI PAKVAGVPEL IMVVPTPDGE VNDMVLAAAA 

       190        200        210        220        230        240 
ICGVDRVFTL GGAQAVAALA YGTETVPPVD KVVGPGNIFV ATAKREVFGT VGIDMIAGPS 

       250        260        270        280        290        300 
EILVYCDGKT NPDWIAMDLF SQAEHDEDAQ SILVTQDAEF AEKVYLSMNK LVKTLPREEI 

       310        320        330        340        350        360 
ITKAITDRGA IIVVDNEDQA IELINYIAPE HLELSIDEPK ALLPKIKHAG AIFMGRFTAE 

       370        380        390        400        410        420 
ALGDYCAGPN HVLPTSRTAR FSSPLGVYDF QKRSSLIMCS AEGANMLGQV AGVLADGEGL 

       430 
QAHAASARYR VKD 

« Hide

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000109 Genomic DNA. Translation: ABB41584.1.
RefSeqYP_391258.1. NC_007520.2.

3D structure databases

ProteinModelPortalQ31GY9.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING317025.Tcr_0989.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABB41584; ABB41584; Tcr_0989.
GeneID3762167.
KEGGtcx:Tcr_0989.
PATRIC23973952. VBIThiCru83387_1031.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0141.
HOGENOMHOG000243914.
KOK00013.
OMAPSEILII.
OrthoDBEOG6CVVCR.

Enzyme and pathway databases

BioCycTCRU317025:GHE8-1010-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_THICR
AccessionPrimary (citable) accession number: Q31GY9
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