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Reviewed, UniProtKB/Swiss-Prot Q7P0F6 (HISX_CHRVO)

Last modified November 25, 2008. Version 43. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

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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: CV_0611
OrganismChromobacterium violaceum [Complete proteome] [HAMAP]
Taxonomic identifier536 [NCBI]
Taxonomic lineageBacteria › Proteobacteria › Betaproteobacteria › Neisseriales › Neisseriaceae › Chromobacterium

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Protein attributes

Sequence length434 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
Protein existenceInferred from homology.

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General annotation (Comments)

Function

Catalyzes the sequential NAD-dependent oxidations of L-histidinol to L-histidinaldehyde and then to L-histidine By similarity.

Catalytic activity

L-histidinol + 2 NAD(+) = L-histidine + 2 NADH.

Cofactor

Binds 1 zinc ion per subunit By similarity.

Pathway

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

Sequence similarities

Belongs to the histidinol dehydrogenase family.

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Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 434434Histidinol dehydrogenase
PRO_0000135755

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

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Sequences

Sequence LengthMass (Da)Tools
Q7P0F6-1 [UniParc].

Last modified December 15, 2003. Version 1.
Checksum: D240002A51339F53

FASTA43446,030
        10         20         30         40         50         60 
MLKLSSSQPD FAERLKALLA FETAQDPAVD AAVASICADV HHRGDAALVE HTNRFDRMQA 

        70         80         90        100        110        120 
AGMADLTLSR EQLEAAWLRL PADVRDALSA AAERVRRYHE KQLAHSWSYE DEDGTLLGQQ 

       130        140        150        160        170        180 
VTPLDRVGIY VPGGKAAYPS SVLMNALPAK VAGVGEIIMV VPTPGGERND LVLAAAYIAG 

       190        200        210        220        230        240 
VDKVFTVGGA QAVAALAYGT ETVPQVDKIT GPGNAYVAAA KRRVFGVVGI DMVAGPSEIL 

       250        260        270        280        290        300 
VICDGATDPD WVAMDLFSQA EHDEIAQAIL LCPSADYIAQ VEASIAKLLP SMPRRAIIEA 

       310        320        330        340        350        360 
SLAGRGALIQ VSDLAEACEI SNYIAPEHLE LSVADPDALL PQLRHAGAIF MGRFTSESLG 

       370        380        390        400        410        420 
DYCAGPNHVL PTSRTARFAS PLGVYDFQKR SSLIRVSQAG AQKLGRIASL LAHGEGLTAH 

       430 
ARAAELRLED GTPR

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References

[1]"The complete genome sequence of Chromobacterium violaceum reveals remarkable and exploitable bacterial adaptability."
Vasconcelos A.T.R., de Almeida D.F., Hungria M., Guimaraes C.T., Antonio R.V., Almeida F.C., de Almeida L.G.P., de Almeida R., Alves-Gomes J.A., Andrade E.M., Araripe J., de Araujo M.F.F., Astolfi-Filho S., Azevedo V., Baptista A.J., Bataus L.A.M., Batista J.S., Belo A. expand/collapse author list , van den Berg C., Bogo M., Bonatto S., Bordignon J., Brigido M.M., Brito C.A., Brocchi M., Burity H.A., Camargo A.A., Cardoso D.D.P., Carneiro N.P., Carraro D.M., Carvalho C.M.B., Cascardo J.C.M., Cavada B.S., Chueire L.M.O., Creczynski-Pasa T.B., Cunha-Junior N.C., Fagundes N., Falcao C.L., Fantinatti F., Farias I.P., Felipe M.S.S., Ferrari L.P., Ferro J.A., Ferro M.I.T., Franco G.R., Freitas N.S.A., Furlan L.R., Gazzinelli R.T., Gomes E.A., Goncalves P.R., Grangeiro T.B., Grattapaglia D., Grisard E.C., Hanna E.S., Jardim S.N., Laurino J., Leoi L.C.T., Lima L.F.A., Loureiro M.F., Lyra M.C.C.P., Madeira H.M.F., Manfio G.P., Maranhao A.Q., Martins W.S., di Mauro S.M.Z., de Medeiros S.R.B., Meissner R.V., Moreira M.A.M., Nascimento F.F., Nicolas M.F., Oliveira J.G., Oliveira S.C., Paixao R.F.C., Parente J.A., Pedrosa F.O., Pena S.D.J., Pereira J.O., Pereira M., Pinto L.S.R.C., Pinto L.S., Porto J.I.R., Potrich D.P., Ramalho-Neto C.E., Reis A.M.M., Rigo L.U., Rondinelli E., Santos E.B.P., Santos F.R., Schneider M.P.C., Seuanez H.N., Silva A.M.R., da Silva A.L.C., Silva D.W., Silva R., Simoes I.C., Simon D., Soares C.M.A., Soares R.B.A., Souza E.M., Souza K.R.L., Souza R.C., Steffens M.B.R., Steindel M., Teixeira S.R., Urmenyi T., Vettore A., Wassem R., Zaha A., Simpson A.J.G.
Proc. Natl. Acad. Sci. U.S.A. 100:11660-11665(2003) [PubMed: 14500782] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 12472 / DSM 30191 / IFO 12614 / JCM 1249 / NCIB 9131.

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Cross-references

Sequence databases

AE016825 Genomic DNA. Translation: AAQ58287.1.
RefSeqNP_900281.1.

3D structure databases

ModBaseSearch...

Genome annotation databases

GeneID2548270.
GenomeReviewsGene locus CV_0611 in contig AE016825_GR.
KEGGcvi:CV_0611.
NMPDRfig|243365.1.peg.611.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMQ7P0F6.

Enzyme and pathway databases

BioCycCVIO243365:CV_0611-MON.

Family and domain databases

HAMAPMF_01024.
[Tree]
InterProIPR001692. Histidinol_DHase.
IPR012131. Hstdl_DHase_prok.
[Graphical view]
PANTHERPTHR21256:SF2. Hstdl_DH_prok. 1 hit.
PfamPF00815. Histidinol_dh. 1 hit.
[Graphical view]
PRINTSPR00083. HOLDHDRGNASE.
ProDomPD002680. Histidinol_dh. 1 hit.
[Graphical view] [Entries sharing at least one domain]
TIGRFAMsTIGR00069. hisD. 1 hit.
PROSITEPS00611. HISOL_DEHYDROGENASE. 1 hit.
[Graphical view]
ProtoNetSearch...

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Entry information

Entry nameHISX_CHRVO
AccessionPrimary (citable) accession number: Q7P0F6
Entry history
Integrated into UniProtKB/Swiss-Prot: April 13, 2004
Last sequence update: December 15, 2003
Last modified: November 25, 2008
This is version 43 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)

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Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents