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Q2YPB8 (HISX_BRUA2) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 44. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
Histidinol dehydrogenase
Short name=HDH
EC=1.1.1.23
Gene names
Name:hisD
Ordered Locus Names:BAB1_0285
OrganismBrucella abortus (strain 2308) [Complete proteome] [HAMAP]
Taxonomic identifier359391 [NCBI]
Taxonomic lineageBacteria › Proteobacteria › Alphaproteobacteria › Rhizobiales › Brucellaceae › Brucella

Protein attributes

Sequence length430 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 MF_01024

Catalytic activity

L-histidinol + H2O + 2 NAD+ = L-histidine + 2 NADH. HAMAP MF_01024

Cofactor

Binds 1 zinc ion per subunit By similarity. HAMAP MF_01024

Pathway

Amino-acid biosynthesis; L-histidine biosynthesis; L-histidine from 5-phospho-alpha-D-ribose 1-diphosphate: step 9/9. HAMAP 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-KW

   Molecular functionNAD binding

Inferred from electronic annotation. Source: InterPro

histidinol dehydrogenase activity

Inferred from electronic annotation. Source: EC

zinc ion binding

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 430430Histidinol dehydrogenase HAMAP MF_01024
PRO_0000229851

Sites

Active site3271Proton acceptor By similarity
Active site3281Proton acceptor By similarity
Metal binding2591Zinc By similarity
Metal binding2621Zinc By similarity
Metal binding3611Zinc By similarity
Metal binding4201Zinc By similarity
Binding site1301NAD By similarity
Binding site1911NAD By similarity
Binding site2141NAD By similarity
Binding site2371Substrate By similarity
Binding site2591Substrate By similarity
Binding site2621Substrate By similarity
Binding site3281Substrate By similarity
Binding site3611Substrate By similarity
Binding site4151Substrate By similarity
Binding site4201Substrate By similarity

Sequences

Sequence LengthMass (Da)Tools
Q2YPB8 [UniParc].

Last modified February 7, 2006. Version 1.
Checksum: 43B836B46DDF3580

FASTA43046,102
        10         20         30         40         50         60 
MVTTLRQTDP DFEQKFAAFL SGKREVSEDV DRAVREIVDR VRREGDSALL DYSRRFDRID 

        70         80         90        100        110        120 
LEKTGIAVTE AEIDAAFDAA PASTVEALKL ARDRIEKHHA RQLPKDDRYT DALGVELGSR 

       130        140        150        160        170        180 
WTAIEAVGLY VPGGTASYPS SVLMNAMPAK VAGVDRIVMV VPAPDGNLNP LVLVAARLAG 

       190        200        210        220        230        240 
VSEIYRVGGA QAIAALAYGT ETIRPVAKIV GPGNAYVAAA KRIVFGTVGI DMIAGPSEVL 

       250        260        270        280        290        300 
IVADKDNNPD WIAADLLAQA EHDMAAQSIL MTNDEAFAHA VEEAVERQLH TLARTETASA 

       310        320        330        340        350        360 
SWRDFGAVIL VKDFEDAIPL ANRIAAEHLE IAVADAEAFV PRIRNAGSIF IGGYTPEVIG 

       370        380        390        400        410        420 
DYVGGCNHVL PTARSARFSS GLSVLDYMKR TSLLKLGSEQ LRALGPAAIE IARAEGLDAH 

       430 
AQSVAIRLNL

« Hide

References

[1]"Whole-genome analyses of speciation events in pathogenic Brucellae."
Chain P.S., Comerci D.J., Tolmasky M.E., Larimer F.W., Malfatti S.A., Vergez L.M., Aguero F., Land M.L., Ugalde R.A., Garcia E.
Infect. Immun. 73:8353-8361(2005) [PubMed: 16299333] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: 2308.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		AM040264 Genomic DNA. Translation: CAJ10241.1.
RefSeqYP_413759.1. NC_007618.1.

3D structure databases

ProteinModelPortalQ2YPB8.
ModBaseSearch...

Protein-protein interaction databases

STRINGQ2YPB8.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID3788752.
GenomeReviewsGene locus BAB1_0285 in contig AM040264_GR.
KEGGbmf:BAB1_0285.
PATRIC17843419. VBIBruMel86222_0297.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0141.
HOGENOMHBG329596.
OMAARDRIEF.
ProtClustDBPRK00877.

Enzyme and pathway databases

BioCycBMEL359391:BAB1_0285-MONOMER.

Family and domain databases

HAMAPMF_01024. HisD.
[Tree]
InterProIPR016161. Ald_DH/histidinol_DH.
IPR001692. Histidinol_DH_CS.
IPR022695. Histidinol_DH_monofunct.
IPR012131. Hstdl_DH.
[Graphical view]
KOK00013.
PANTHERPTHR21256:SF2. Hstdl_DH_prok. 1 hit.
PfamPF00815. Histidinol_dh. 1 hit.
[Graphical view]
PIRSFPIRSF000099. Histidinol_dh. 1 hit.
PRINTSPR00083. HOLDHDRGNASE.
SUPFAMSSF53720. Aldehyde_DH/Histidinol_DH. 1 hit.
TIGRFAMsTIGR00069. HisD. 1 hit.
PROSITEPS00611. HISOL_DEHYDROGENASE. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameHISX_BRUA2
AccessionPrimary (citable) accession number: Q2YPB8
Entry history
Integrated into UniProtKB/Swiss-Prot: April 4, 2006
Last sequence update: February 7, 2006
Last modified: January 25, 2012
This is version 44 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

Brucella abortus strain 2308

Brucella abortus (strain 2308): entries and gene names

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

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