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Q5V574 (HISX_HALMA) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 70. 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:rrnAC0272
OrganismHaloarcula marismortui (strain ATCC 43049 / DSM 3752 / JCM 8966 / VKM B-1809) (Halobacterium marismortui) [Complete proteome] [HAMAP]
Taxonomic identifier272569 [NCBI]
Taxonomic lineageArchaeaEuryarchaeotaHalobacteriaHalobacterialesHalobacteriaceaeHaloarcula

Protein attributes

Sequence length422 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 – 422422Histidinol dehydrogenase HAMAP-Rule MF_01024
PRO_0000135891

Sites

Active site3201Proton acceptor By similarity
Active site3211Proton acceptor By similarity
Metal binding2511Zinc By similarity
Metal binding2541Zinc By similarity
Metal binding3541Zinc By similarity
Metal binding4131Zinc By similarity
Binding site1231NAD By similarity
Binding site1831NAD By similarity
Binding site2061NAD By similarity
Binding site2291Substrate By similarity
Binding site2511Substrate By similarity
Binding site2541Substrate By similarity
Binding site3211Substrate By similarity
Binding site3541Substrate By similarity
Binding site4081Substrate By similarity
Binding site4131Substrate By similarity

Sequences

Sequence LengthMass (Da)Tools
Q5V574 [UniParc].

Last modified December 7, 2004. Version 1.
Checksum: B04AC7EF3AA246D8

FASTA42244,466
        10         20         30         40         50         60 
MNVRTIADLG PDERAAFFDR DAGVDAVRDD VRDIVSQVHE EGDVALRRFA EEFDDVSVGN 

        70         80         90        100        110        120 
IDITDAAERA YEEIDDDVRE AIEDAAANIR AFHERQVPED WRDDFEGREL GRRFRPLDSA 

       130        140        150        160        170        180 
GVYAPGGTAA YPSSALMGVI PAKVAGVEHV AVATPPAEEV NPVTLAAIHV AGADAVYQVG 

       190        200        210        220        230        240 
GAQAIAALAY GTETVSATDI VVGPGNRWVT AAKAEVRGDV AIDFLAGPSE VMVVADGDAD 

       250        260        270        280        290        300 
PELVAADLIA QAEHDENASV VAVTDDADLA EQVVDAVDEQ ADGREREAVI RAALDNDTSG 

       310        320        330        340        350        360 
VLLARSMSEA VLFAEEYAAE HLSIQAADDE SLLERIPSAG SVFLGPYSPV AAGDYATGTN 

       370        380        390        400        410        420 
HVLPTGGNAR VTGGLSVDTF VRSTTVQRLS EDSLGDIADT ITTLAEAEGL DAHAESVRKR 


FE 

« Hide

References

[1]"Genome sequence of Haloarcula marismortui: a halophilic archaeon from the Dead Sea."
Baliga N.S., Bonneau R., Facciotti M.T., Pan M., Glusman G., Deutsch E.W., Shannon P., Chiu Y., Weng R.S., Gan R.R., Hung P., Date S.V., Marcotte E., Hood L., Ng W.V.
Genome Res. 14:2221-2234(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 43049 / DSM 3752 / JCM 8966 / VKM B-1809.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AY596297 Genomic DNA. Translation: AAV45328.1.
RefSeqYP_135034.1. NC_006396.1.

3D structure databases

ProteinModelPortalQ5V574.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING272569.rrnAC0272.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAV45328; AAV45328; rrnAC0272.
GeneID3129583.
KEGGhma:rrnAC0272.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0141.
HOGENOMHOG000243914.
KOK00013.
OMANAMSILL.

Enzyme and pathway databases

BioCycHMAR272569:GJDH-247-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_HALMA
AccessionPrimary (citable) accession number: Q5V574
Entry history
Integrated into UniProtKB/Swiss-Prot: January 10, 2006
Last sequence update: December 7, 2004
Last modified: May 14, 2014
This is version 70 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