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Q9CC57 (HISX_MYCLE) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 91. 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:ML1257
ORF Names:MLCB1610.20
OrganismMycobacterium leprae (strain TN) [Complete proteome] [HAMAP]
Taxonomic identifier272631 [NCBI]
Taxonomic lineageBacteriaActinobacteriaActinobacteridaeActinomycetalesCorynebacterineaeMycobacteriaceaeMycobacterium

Protein attributes

Sequence length449 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.

Sequence caution

The sequence CAB43166.1 differs from that shown. Reason: Erroneous initiation.

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 – 449449Histidinol dehydrogenase HAMAP-Rule MF_01024
PRO_0000135796

Sites

Active site3461Proton acceptor By similarity
Active site3471Proton acceptor By similarity
Metal binding2771Zinc By similarity
Metal binding2801Zinc By similarity
Metal binding3801Zinc By similarity
Metal binding4391Zinc By similarity
Binding site1361NAD By similarity
Binding site2041NAD By similarity
Binding site2321NAD By similarity
Binding site2551Substrate By similarity
Binding site2771Substrate By similarity
Binding site2801Substrate By similarity
Binding site3471Substrate By similarity
Binding site3801Substrate By similarity
Binding site4341Substrate By similarity
Binding site4391Substrate By similarity

Sequences

Sequence LengthMass (Da)Tools
Q9CC57 [UniParc].

Last modified June 1, 2001. Version 1.
Checksum: 241D7CC6DF3AF171

FASTA44946,828
        10         20         30         40         50         60 
MSITPPFLLA CIDLRGAELT ATQLRATLPR GGADVEAVLP TVWPIVQAVA ECGADAALEF 

        70         80         90        100        110        120 
GALFDGVRPP TVRVPDAALD AALAGLDPDV RDALQVMIER TRVVHADQRR TDVTTALGPG 

       130        140        150        160        170        180 
ATVTERWVPV ERVGLYVPGG NAVYPSSVVM NVVPAQTAGV DSLVVASPPQ FTSGGRFHGL 

       190        200        210        220        230        240 
PHPTILAAAR LLGVDEVWAV GGAQAVALLA YGGTDSDDCE LAPVDMITGP GNIYVTAAKR 

       250        260        270        280        290        300 
LCRSRVGIDG EAGPTEIAIL ADHTADPAHV AADMISQAEH DEMAASVLVT PSTDLADATD 

       310        320        330        340        350        360 
AELAAQLRTT VHRKRVVAAL GGRQSAIILV DDLEAGVKVV NLYAAEHLEI QTAEASRVAS 

       370        380        390        400        410        420 
RIRCAGAIFV GPWAPVSLGD YCAGSNHVLP TAGFARHSGG LSVQTFLRGI HVVNYTKTAL 

       430        440 
KDISGHVITL AKAEDLPAHG EAVRRRFAR 

« Hide

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AL049913 Genomic DNA. Translation: CAB43166.1. Different initiation.
AL583921 Genomic DNA. Translation: CAC31638.1.
PIRC87066.
T45246.
RefSeqNP_301906.1. NC_002677.1.

3D structure databases

ProteinModelPortalQ9CC57.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING272631.ML1257.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaCAC31638; CAC31638; CAC31638.
GeneID910363.
KEGGmle:ML1257.
PATRIC18054758. VBIMycLep78757_2318.

Organism-specific databases

LepromaML1257.
CMRSearch...

Phylogenomic databases

eggNOGCOG0141.
HOGENOMHOG000243914.
KOK00013.
OMAYAAKLCG.
OrthoDBEOG6CVVCR.

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_MYCLE
AccessionPrimary (citable) accession number: Q9CC57
Secondary accession number(s): Q9X7B7
Entry history
Integrated into UniProtKB/Swiss-Prot: August 14, 2001
Last sequence update: June 1, 2001
Last modified: May 14, 2014
This is version 91 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