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Reviewed, UniProtKB/Swiss-Prot P24226 (HISX_BRAOC)

Last modified June 16, 2009. Version 60. 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, chloroplastic
      Short name=HDH
    EC=1.1.1.23
Gene names
Name: HDH
OrganismBrassica oleracea var. capitata (Cabbage)
Taxonomic identifier3716 [NCBI]
Taxonomic lineageEukaryota › Viridiplantae › Streptophyta › Embryophyta › Tracheophyta › Spermatophyta › Magnoliophyta › eudicotyledons › core eudicotyledons › rosids › eurosids II › Brassicales › Brassicaceae › Brassica

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Protein attributes

Sequence length469 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level.

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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.

Subcellular location

Plastid › chloroplast.

Miscellaneous

Cabbage may contain multiple HDH isozymes encoded by different genes.

Sequence similarities

Belongs to the histidinol dehydrogenase family.

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Ontologies

Keywords
   Biological processAmino-acid biosynthesis
Histidine biosynthesis
   Cellular componentChloroplast
Plastid
   DomainTransit peptide
   LigandMetal-binding
NAD
Zinc
   Molecular functionOxidoreductase
   Technical termDirect protein sequencing
Gene Ontology (GO)
   Biological processhistidine biosynthetic process

Inferred from electronic annotation. Source: UniProtKB-KW

oxidation reduction

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular componentchloroplast

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular functionNAD or NADH binding

Inferred from electronic annotation. Source: InterPro

histidinol dehydrogenase activity

Inferred from electronic annotation. Source: EC

zinc ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

Complete GO annotation...

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Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Transit peptide1 – 3131Chloroplast
Chain32 – 469438Histidinol dehydrogenase, chloroplastic
PRO_0000007216

Sites

Active site3571Proton acceptor By similarity
Active site3581Proton acceptor By similarity
Metal binding2891Zinc By similarity
Metal binding2921Zinc By similarity
Metal binding3911Zinc By similarity
Metal binding4501Zinc By similarity
Binding site1561NAD By similarity
Binding site2181NAD By similarity
Binding site2411NAD By similarity
Binding site2671Substrate By similarity
Binding site2891Substrate By similarity
Binding site2921Substrate By similarity
Binding site3581Substrate By similarity
Binding site3911Substrate By similarity
Binding site4451Substrate By similarity
Binding site4501Substrate By similarity

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Sequences

Sequence LengthMass (Da)Tools
P24226-1 [UniParc].

Last modified March 1, 1992. Version 1.
Checksum: EC63FA4B7B2E19CA

FASTA46950,959
        10         20         30         40         50         60 
MSFDLSRLSL TSSPRLSFLT RTATKKGFVR CSMKSYRLSE LSFSQVENLK ARPRIDFSSI 

        70         80         90        100        110        120 
FTTVNPIIDA VRSKGDTAVK EYTERFDKVQ LNKVVEDVSE LDIPELDSAV KEAFDVAYDN 

       130        140        150        160        170        180 
IYAFHFAQMS TEKSVENMKG VRCKRVSRSI GSVGLYVPGG TAVLPSTALM LAIPAQIAGC 

       190        200        210        220        230        240 
KTVVLATPPT KEGSICKEVL YCAKRAGVTH ILKAGGAQAI AAMAWGTDSC PKVEKIFGPG 

       250        260        270        280        290        300 
NQYVTAAKMI LQNSEAMVSI DMPAGPSEVL VIADEHASPV YIAADLLSQA EHGPDSQVVL 

       310        320        330        340        350        360 
VVVGDGVNLK AIEEEIAKQC KSLPRGEFAS KALSHSFTVF ARDMIEAITF SNLYAPEHLI 

       370        380        390        400        410        420 
INVKDAEKWE GLIENAGSVF IGPWTPESVG DYASGTNHVL PTYGYARMYS GVSLDSFLKF 

       430        440        450        460 
MTVQSLTEEG LRNLGPYVAT MAEIEGLDAH KRAVTLRLKD IEAKQTQTK

« Hide

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References

[1]"Structural and functional conservation of histidinol dehydrogenase between plants and microbes."
Nagai A., Ward E., Beck J., Tada S., Chang J.-Y., Scheidegger A., Ryals J.
Proc. Natl. Acad. Sci. U.S.A. 88:4133-4137(1991) [PubMed: 2034659] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE.

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Cross-references

Sequence databases

M60466 mRNA. Translation: AAA32991.1.
PIRA39358.

3D structure databases

HSSPHSSP built from PDB template 1K75 based on UniProtKB P06988.
ModBaseSearch...

Enzyme and pathway databases

BRENDA1.1.1.23. 289288.

Family and domain databases

InterProIPR001692. Histidinol_DH_CS.
IPR012131. Hstdl_DH_prok-type.
[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_BRAOC
AccessionPrimary (citable) accession number: P24226
Entry history
Integrated into UniProtKB/Swiss-Prot: March 1, 1992
Last sequence update: March 1, 1992
Last modified: June 16, 2009
This is version 60 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectPPAP (Plant Proteome Annotation Project)

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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