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P60860 (HISX_MYCPA) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 79. 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:MAP_1293
OrganismMycobacterium paratuberculosis (strain ATCC BAA-968 / K-10) [Complete proteome] [HAMAP]
Taxonomic identifier262316 [NCBI]
Taxonomic lineageBacteriaActinobacteriaActinobacteridaeActinomycetalesCorynebacterineaeMycobacteriaceaeMycobacteriumMycobacterium avium complex (MAC)

Protein attributes

Sequence length480 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 – 480480Histidinol dehydrogenase HAMAP-Rule MF_01024
PRO_0000135797

Sites

Active site3771Proton acceptor By similarity
Active site3781Proton acceptor By similarity
Metal binding3081Zinc By similarity
Metal binding3111Zinc By similarity
Metal binding4111Zinc By similarity
Metal binding4701Zinc By similarity
Binding site1521NAD By similarity
Binding site2161NAD By similarity
Binding site2631NAD By similarity
Binding site2861Substrate By similarity
Binding site3081Substrate By similarity
Binding site3111Substrate By similarity
Binding site3781Substrate By similarity
Binding site4111Substrate By similarity
Binding site4651Substrate By similarity
Binding site4701Substrate By similarity

Sequences

Sequence LengthMass (Da)Tools
P60860 [UniParc].

Last modified April 13, 2004. Version 1.
Checksum: D51BE3BAB2ABB107

FASTA48049,373
        10         20         30         40         50         60 
MYRPDIDLSS SGTMDTVSPT PASPMAGIDL RGAELTAARL RSALPRGGAD VETVLPKVRP 

        70         80         90        100        110        120 
IVQAVAERGA DAALEFGASF DGVRPAAVRV PEAALDKALA DLDAAVADAL RVMIDRARAV 

       130        140        150        160        170        180 
HADQRRTDVT TTLGPGATVT ERWVPVERVG LYVPGGNAVY PSSVVMNVVP AQAAGVASLV 

       190        200        210        220        230        240 
VASPPQAQFD GLPHPTILAA ARLLGVDEVW AVGGAQAVAL LAYGGTDTGA EWPGFSSDRA 

       250        260        270        280        290        300 
RSASSPGADA ELVPVDMITG PGNIYVTAAK RLCRSRVGID AEAGPTEIAI LADHTADPAH 

       310        320        330        340        350        360 
VAADLISQAE HDEMAGSVLV TPSEDLAAAT DAELAAQLPT TVHRERVTAA LGGRQSAIIL 

       370        380        390        400        410        420 
VDDLDAGITV VNAYAAEHLE IQTADAAAVA GRIRAAGAVF VGPYSPVSLG DYCAGSNHVL 

       430        440        450        460        470        480 
PTAGSARHSS GLSVQTFLRG IHVVDYTEAA LKDVSGHVIT LAQAEDLPAH GEAIRRRFER 

« Hide

References

[1]"The complete genome sequence of Mycobacterium avium subspecies paratuberculosis."
Li L., Bannantine J.P., Zhang Q., Amonsin A., May B.J., Alt D., Banerji N., Kanjilal S., Kapur V.
Proc. Natl. Acad. Sci. U.S.A. 102:12344-12349(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC BAA-968 / K-10.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AE016958 Genomic DNA. Translation: AAS03610.1.
RefSeqNP_960227.1. NC_002944.2.

3D structure databases

ProteinModelPortalP60860.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING262316.MAP1293.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAS03610; AAS03610; MAP_1293.
GeneID2717805.
KEGGmpa:MAP1293.
PATRIC17995063. VBIMycAvi108102_1362.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0141.
KOK00013.
OMAPSEILII.
OrthoDBEOG6CVVCR.
ProtClustDBPRK00877.

Enzyme and pathway databases

BioCycMAVI262316:GCQR-1313-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_MYCPA
AccessionPrimary (citable) accession number: P60860
Entry history
Integrated into UniProtKB/Swiss-Prot: April 13, 2004
Last sequence update: April 13, 2004
Last modified: February 19, 2014
This is version 79 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