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Q9C5U8 (HIS8_ARATH) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 105. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Histidinol dehydrogenase, chloroplastic

Short name=HDH
EC=1.1.1.23
Alternative name(s):
Protein HISTIDINE BIOSYNTHESIS 8
Gene names
Name:HISN8
Synonyms:HDH
Ordered Locus Names:At5g63890
ORF Names:MGI19.9
OrganismArabidopsis thaliana (Mouse-ear cress) [Reference proteome]
Taxonomic identifier3702 [NCBI]
Taxonomic lineageEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis

Protein attributes

Sequence length466 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at transcript level

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

Subcellular location

Plastidchloroplast HAMAP-Rule MF_01024.

Sequence similarities

Belongs to the histidinol dehydrogenase family.

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q9C5U8-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
Isoform 2 (identifier: Q9C5U8-2)

The sequence of this isoform differs from the canonical sequence as follows:
     1-25: MSLNLSRLSLLSSPRISISTHAPRK → MNEFVDQLRFT
Note: No experimental confirmation available.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Transit peptide1 – 3030Chloroplast By similarity
Chain31 – 466436Histidinol dehydrogenase, chloroplastic HAMAP-Rule MF_01024
PRO_0000007215

Sites

Active site3561Proton acceptor By similarity
Active site3571Proton acceptor By similarity
Metal binding2881Zinc By similarity
Metal binding2911Zinc By similarity
Metal binding3901Zinc By similarity
Metal binding4491Zinc By similarity
Binding site1551NAD By similarity
Binding site2171NAD By similarity
Binding site2401NAD By similarity
Binding site2661Substrate By similarity
Binding site2881Substrate By similarity
Binding site2911Substrate By similarity
Binding site3571Substrate By similarity
Binding site3901Substrate By similarity
Binding site4441Substrate By similarity
Binding site4491Substrate By similarity

Natural variations

Alternative sequence1 – 2525MSLNL…HAPRK → MNEFVDQLRFT in isoform 2.
VSP_047341

Experimental info

Sequence conflict251K → KA in BAB11037. Ref.2

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified June 1, 2001. Version 1.
Checksum: 1175DEA979244595

FASTA46650,323
        10         20         30         40         50         60 
MSLNLSRLSL LSSPRISIST HAPRKGYVCC SMKSYRLSEL SSSQVDSLKS RPRIDFSSIF 

        70         80         90        100        110        120 
ATVNPIIDAV RSNGDNAVKE YTERFDKVQL NKVVEDMSEL SVPELDSNVK EAFDVAYDNI 

       130        140        150        160        170        180 
YAFHLAQKST EKSVENMKGV RCKRVSRSIG SVGLYVPGGT AVLPSTALML AIPAQIAGCK 

       190        200        210        220        230        240 
TVVLATPPSK DGSICKEVLY CAKRAGVTHI LKAGGAQAIA AMAWGTDSCP KVEKIFGPGN 

       250        260        270        280        290        300 
QYVTAAKMIL QNSEAMVSID MPAGPSEVLV IADEHASPVY IAADLLSQAE HGPDSQVVLV 

       310        320        330        340        350        360 
VVGDSVDLNA IEEEIAKQCK SLPRGEFASK ALSHSFTVFA RDMIEAISFS NLYAPEHLII 

       370        380        390        400        410        420 
NVKDAEKWEG LIENAGSVFI GPWTPESVGD YASGTNHVLP TYGYARMYSG VSLDSFLKFM 

       430        440        450        460 
TVQSLTEEGL RNLGPYVATM AEIEGLDAHK RAVTLRLKDI EAKQLA 

« Hide

Isoform 2 [UniParc].

Checksum: 7DC0EAB6B02866F9
Show »

FASTA45248,957

References

« Hide 'large scale' references
[1]"Isolation of Arabidopsis cDNA for histidinol dehydrogenase."
Fujimori K.
Submitted (MAY-1999) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
[2]"Structural analysis of Arabidopsis thaliana chromosome 5. III. Sequence features of the regions of 1,191,918 bp covered by seventeen physically assigned P1 clones."
Nakamura Y., Sato S., Kaneko T., Kotani H., Asamizu E., Miyajima N., Tabata S.
DNA Res. 4:401-414(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: cv. Columbia.
[3]The Arabidopsis Information Resource (TAIR)
Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases
Cited for: GENOME REANNOTATION.
Strain: cv. Columbia.
[4]"Empirical analysis of transcriptional activity in the Arabidopsis genome."
Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M., Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G., Liu S.X., Lam B., Sakano H., Wu T., Yu G. expand/collapse author list , Miranda M., Quach H.L., Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C., Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J., Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A., Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C., Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X., Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M., Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K., Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A., Ecker J.R.
Science 302:842-846(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
Strain: cv. Columbia.
[5]"Full-length cDNA from Arabidopsis thaliana."
Brover V.V., Troukhan M.E., Alexandrov N.A., Lu Y.-P., Flavell R.B., Feldmann K.A.
Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
[6]"Histidine biosynthesis in plants."
Stepansky A., Leustek T.
Amino Acids 30:127-142(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: GENE FAMILY, NOMENCLATURE.
[7]"Genetic dissection of histidine biosynthesis in Arabidopsis."
Muralla R., Sweeney C., Stepansky A., Leustek T., Meinke D.
Plant Physiol. 144:890-903(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: GENE FAMILY, NOMENCLATURE.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AB027709 mRNA. Translation: BAB40445.1.
AB007646 Genomic DNA. Translation: BAB11037.1.
CP002688 Genomic DNA. Translation: AED97811.1.
CP002688 Genomic DNA. Translation: AED97812.1.
AY039881 mRNA. Translation: AAK63985.1.
AY143900 mRNA. Translation: AAN28839.1.
AY087987 mRNA. Translation: AAM65533.1.
RefSeqNP_568981.2. NM_125784.3. [Q9C5U8-1]
NP_851260.1. NM_180929.3. [Q9C5U8-2]
UniGeneAt.20645.
At.66745.

3D structure databases

ProteinModelPortalQ9C5U8.
SMRQ9C5U8. Positions 41-463.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid21751. 1 interaction.
STRING3702.AT5G63890.2-P.

Proteomic databases

PaxDbQ9C5U8.
PRIDEQ9C5U8.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblPlantsAT5G63890.2; AT5G63890.2; AT5G63890. [Q9C5U8-1]
GeneID836509.
KEGGath:AT5G63890.

Organism-specific databases

TAIRAT5G63890.

Phylogenomic databases

eggNOGCOG0141.
HOGENOMHOG000243914.
InParanoidQ9C5U8.
KOK00013.
OMAYAAKLCG.
PhylomeDBQ9C5U8.

Enzyme and pathway databases

BioCycARA:GQT-2426-MONOMER.
UniPathwayUPA00031; UER00014.

Gene expression databases

GenevestigatorQ9C5U8.

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...

Other

PROQ9C5U8.

Entry information

Entry nameHIS8_ARATH
AccessionPrimary (citable) accession number: Q9C5U8
Secondary accession number(s): F4KC60, Q8LA77, Q9FN00
Entry history
Integrated into UniProtKB/Swiss-Prot: March 28, 2003
Last sequence update: June 1, 2001
Last modified: May 14, 2014
This is version 105 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways

Arabidopsis thaliana

Arabidopsis thaliana: entries and gene names