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Protein

Histidinol dehydrogenase, chloroplastic

Gene

HISN8

Organism
Arabidopsis thaliana (Mouse-ear cress)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at transcript leveli

Functioni

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

Catalytic activityi

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

Cofactori

Zn2+By similarityNote: Binds 1 zinc ion per subunit.By similarity

Pathway: L-histidine biosynthesis

This protein is involved in step 9 of the subpathway that synthesizes L-histidine from 5-phospho-alpha-D-ribose 1-diphosphate.
Proteins known to be involved in the 9 steps of the subpathway in this organism are:
  1. ATP phosphoribosyltransferase 1, chloroplastic (HISN1A), ATP phosphoribosyltransferase 2, chloroplastic (HISN1B)
  2. Histidine biosynthesis bifunctional protein hisIE, chloroplastic (HISN2)
  3. Histidine biosynthesis bifunctional protein hisIE, chloroplastic (HISN2)
  4. 1-(5-phosphoribosyl)-5-[(5-phosphoribosylamino)methylideneamino] imidazole-4-carboxamide isomerase, chloroplastic (HISN3)
  5. Imidazole glycerol phosphate synthase hisHF, chloroplastic (HISN4)
  6. Imidazoleglycerol-phosphate dehydratase 2, chloroplastic (HISN5B), Imidazoleglycerol-phosphate dehydratase (HISN5B), Imidazoleglycerol-phosphate dehydratase (At3g22425), Imidazoleglycerol-phosphate dehydratase 1, chloroplastic (HISN5A), Imidazoleglycerol-phosphate dehydratase (HISN5B)
  7. Histidinol-phosphate aminotransferase 2, chloroplastic (HISN6B), Histidinol-phosphate aminotransferase 1, chloroplastic (HISN6A)
  8. Bifunctional phosphatase IMPL2, chloroplastic (HISN7)
  9. Histidinol dehydrogenase, chloroplastic (HISN8)
This subpathway is part of the pathway L-histidine biosynthesis, which is itself part of Amino-acid biosynthesis.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes L-histidine from 5-phospho-alpha-D-ribose 1-diphosphate, the pathway L-histidine biosynthesis and in Amino-acid biosynthesis.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei155 – 1551NADBy similarity
Binding sitei217 – 2171NADBy similarity
Binding sitei240 – 2401NADBy similarity
Binding sitei266 – 2661SubstrateBy similarity
Metal bindingi288 – 2881ZincBy similarity
Binding sitei288 – 2881SubstrateBy similarity
Metal bindingi291 – 2911ZincBy similarity
Binding sitei291 – 2911SubstrateBy similarity
Active sitei356 – 3561Proton acceptorBy similarity
Active sitei357 – 3571Proton acceptorBy similarity
Binding sitei357 – 3571SubstrateBy similarity
Metal bindingi390 – 3901ZincBy similarity
Binding sitei390 – 3901SubstrateBy similarity
Binding sitei444 – 4441SubstrateBy similarity
Metal bindingi449 – 4491ZincBy similarity
Binding sitei449 – 4491SubstrateBy similarity

GO - Molecular functioni

  • histidinol dehydrogenase activity Source: TAIR
  • NAD binding Source: InterPro
  • zinc ion binding Source: InterPro

GO - Biological processi

  • histidine biosynthetic process Source: UniProtKB-UniPathway
  • pollen development Source: TAIR
  • response to UV Source: TAIR
Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Biological processi

Amino-acid biosynthesis, Histidine biosynthesis

Keywords - Ligandi

Metal-binding, NAD, Zinc

Enzyme and pathway databases

BioCyciARA:GQT-2426-MONOMER.
UniPathwayiUPA00031; UER00014.

Names & Taxonomyi

Protein namesi
Recommended name:
Histidinol dehydrogenase, chloroplastic (EC:1.1.1.23)
Short name:
HDH
Alternative name(s):
Protein HISTIDINE BIOSYNTHESIS 8
Gene namesi
Name:HISN8
Synonyms:HDH
Ordered Locus Names:At5g63890
ORF Names:MGI19.9
OrganismiArabidopsis thaliana (Mouse-ear cress)
Taxonomic identifieri3702 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis
ProteomesiUP000006548 Componenti: Chromosome 5

Organism-specific databases

TAIRiAT5G63890.

Subcellular locationi

GO - Cellular componenti

  • chloroplast Source: TAIR
  • chloroplast stroma Source: TAIR
Complete GO annotation...

Keywords - Cellular componenti

Chloroplast, Plastid

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transit peptidei1 – 3030ChloroplastBy similarityAdd
BLAST
Chaini31 – 466436Histidinol dehydrogenase, chloroplasticPRO_0000007215Add
BLAST

Proteomic databases

PaxDbiQ9C5U8.
PRIDEiQ9C5U8.

Interactioni

Protein-protein interaction databases

BioGridi21751. 1 interaction.
STRINGi3702.AT5G63890.2.

Structurei

3D structure databases

ProteinModelPortaliQ9C5U8.
SMRiQ9C5U8. Positions 41-463.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the histidinol dehydrogenase family.Curated

Keywords - Domaini

Transit peptide

Phylogenomic databases

eggNOGiCOG0141.
HOGENOMiHOG000243914.
InParanoidiQ9C5U8.
KOiK00013.
OMAiLSVQSFL.
PhylomeDBiQ9C5U8.

Family and domain databases

HAMAPiMF_01024. HisD.
InterProiIPR016161. Ald_DH/histidinol_DH.
IPR001692. Histidinol_DH_CS.
IPR022695. Histidinol_DH_monofunct.
IPR012131. Hstdl_DH.
[Graphical view]
PfamiPF00815. Histidinol_dh. 1 hit.
[Graphical view]
PIRSFiPIRSF000099. Histidinol_dh. 1 hit.
PRINTSiPR00083. HOLDHDRGNASE.
SUPFAMiSSF53720. SSF53720. 1 hit.
TIGRFAMsiTIGR00069. hisD. 1 hit.
PROSITEiPS00611. HISOL_DEHYDROGENASE. 1 hit.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: Q9C5U8-1) [UniParc]FASTAAdd to basket

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.

« Hide

        10         20         30         40         50
MSLNLSRLSL LSSPRISIST HAPRKGYVCC SMKSYRLSEL SSSQVDSLKS
60 70 80 90 100
RPRIDFSSIF ATVNPIIDAV RSNGDNAVKE YTERFDKVQL NKVVEDMSEL
110 120 130 140 150
SVPELDSNVK EAFDVAYDNI YAFHLAQKST EKSVENMKGV RCKRVSRSIG
160 170 180 190 200
SVGLYVPGGT AVLPSTALML AIPAQIAGCK TVVLATPPSK DGSICKEVLY
210 220 230 240 250
CAKRAGVTHI LKAGGAQAIA AMAWGTDSCP KVEKIFGPGN QYVTAAKMIL
260 270 280 290 300
QNSEAMVSID MPAGPSEVLV IADEHASPVY IAADLLSQAE HGPDSQVVLV
310 320 330 340 350
VVGDSVDLNA IEEEIAKQCK SLPRGEFASK ALSHSFTVFA RDMIEAISFS
360 370 380 390 400
NLYAPEHLII NVKDAEKWEG LIENAGSVFI GPWTPESVGD YASGTNHVLP
410 420 430 440 450
TYGYARMYSG VSLDSFLKFM TVQSLTEEGL RNLGPYVATM AEIEGLDAHK
460
RAVTLRLKDI EAKQLA
Length:466
Mass (Da):50,323
Last modified:June 1, 2001 - v1
Checksum:i1175DEA979244595
GO
Isoform 2 (identifier: Q9C5U8-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-25: MSLNLSRLSLLSSPRISISTHAPRK → MNEFVDQLRFT

Note: No experimental confirmation available.
Show »
Length:452
Mass (Da):48,957
Checksum:i7DC0EAB6B02866F9
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti25 – 251K → KA in BAB11037 (PubMed:9501997).Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 2525MSLNL…HAPRK → MNEFVDQLRFT in isoform 2. 1 PublicationVSP_047341Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
RefSeqiNP_568981.2. NM_125784.3. [Q9C5U8-1]
NP_851260.1. NM_180929.3. [Q9C5U8-2]
UniGeneiAt.20645.
At.66745.

Genome annotation databases

EnsemblPlantsiAT5G63890.2; AT5G63890.2; AT5G63890. [Q9C5U8-1]
GeneIDi836509.
KEGGiath:AT5G63890.

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
RefSeqiNP_568981.2. NM_125784.3. [Q9C5U8-1]
NP_851260.1. NM_180929.3. [Q9C5U8-2]
UniGeneiAt.20645.
At.66745.

3D structure databases

ProteinModelPortaliQ9C5U8.
SMRiQ9C5U8. Positions 41-463.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi21751. 1 interaction.
STRINGi3702.AT5G63890.2.

Proteomic databases

PaxDbiQ9C5U8.
PRIDEiQ9C5U8.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblPlantsiAT5G63890.2; AT5G63890.2; AT5G63890. [Q9C5U8-1]
GeneIDi836509.
KEGGiath:AT5G63890.

Organism-specific databases

TAIRiAT5G63890.

Phylogenomic databases

eggNOGiCOG0141.
HOGENOMiHOG000243914.
InParanoidiQ9C5U8.
KOiK00013.
OMAiLSVQSFL.
PhylomeDBiQ9C5U8.

Enzyme and pathway databases

UniPathwayiUPA00031; UER00014.
BioCyciARA:GQT-2426-MONOMER.

Miscellaneous databases

PROiQ9C5U8.

Family and domain databases

HAMAPiMF_01024. HisD.
InterProiIPR016161. Ald_DH/histidinol_DH.
IPR001692. Histidinol_DH_CS.
IPR022695. Histidinol_DH_monofunct.
IPR012131. Hstdl_DH.
[Graphical view]
PfamiPF00815. Histidinol_dh. 1 hit.
[Graphical view]
PIRSFiPIRSF000099. Histidinol_dh. 1 hit.
PRINTSiPR00083. HOLDHDRGNASE.
SUPFAMiSSF53720. SSF53720. 1 hit.
TIGRFAMsiTIGR00069. hisD. 1 hit.
PROSITEiPS00611. HISOL_DEHYDROGENASE. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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.
    , 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. 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.

Entry informationi

Entry nameiHIS8_ARATH
AccessioniPrimary (citable) accession number: Q9C5U8
Secondary accession number(s): F4KC60, Q8LA77, Q9FN00
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 28, 2003
Last sequence update: June 1, 2001
Last modified: June 24, 2015
This is version 109 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Arabidopsis thaliana
    Arabidopsis thaliana: entries and gene names
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.