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Protein

Histidinol dehydrogenase

Gene

hisD

Organism
Sulfolobus tokodaii (strain DSM 16993 / JCM 10545 / NBRC 100140 / 7)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Protein inferred from homologyi

Functioni

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

Catalytic activityi

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

Cofactori

Zn2+UniRule annotationNote: Binds 1 zinc ion per subunit.UniRule annotation

Pathwayi: 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.UniRule annotation
Proteins known to be involved in the 9 steps of the subpathway in this organism are:
  1. ATP phosphoribosyltransferase (hisG)
  2. Phosphoribosyl-ATP pyrophosphatase (hisE)
  3. Phosphoribosyl-AMP cyclohydrolase (hisI)
  4. 1-(5-phosphoribosyl)-5-[(5-phosphoribosylamino)methylideneamino] imidazole-4-carboxamide isomerase (hisA)
  5. Imidazole glycerol phosphate synthase subunit HisF (hisF), Imidazole glycerol phosphate synthase subunit HisH (hisH)
  6. Imidazoleglycerol-phosphate dehydratase (hisB)
  7. Histidinol-phosphate aminotransferase (hisC)
  8. no protein annotated in this organism
  9. Histidinol dehydrogenase (hisD)
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)DescriptionActionsGraphical viewLength
Binding sitei113NADUniRule annotation1
Binding sitei172NADUniRule annotation1
Binding sitei195NADUniRule annotation1
Binding sitei218SubstrateUniRule annotation1
Metal bindingi240ZincUniRule annotation1
Binding sitei240SubstrateUniRule annotation1
Metal bindingi243ZincUniRule annotation1
Binding sitei243SubstrateUniRule annotation1
Active sitei294Proton acceptorUniRule annotation1
Active sitei295Proton acceptorUniRule annotation1
Binding sitei295SubstrateUniRule annotation1
Metal bindingi327ZincUniRule annotation1
Binding sitei327SubstrateUniRule annotation1
Binding sitei380SubstrateUniRule annotation1
Metal bindingi385ZincUniRule annotation1
Binding sitei385SubstrateUniRule annotation1

GO - Molecular functioni

GO - Biological processi

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

UniPathwayiUPA00031; UER00014.

Names & Taxonomyi

Protein namesi
Recommended name:
Histidinol dehydrogenaseUniRule annotation (EC:1.1.1.23UniRule annotation)
Short name:
HDHUniRule annotation
Gene namesi
Name:hisDUniRule annotation
Ordered Locus Names:STK_14640
OrganismiSulfolobus tokodaii (strain DSM 16993 / JCM 10545 / NBRC 100140 / 7)
Taxonomic identifieri273063 [NCBI]
Taxonomic lineageiArchaeaCrenarchaeotaThermoproteiSulfolobalesSulfolobaceaeSulfolobus
Proteomesi
  • UP000001015 Componenti: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001359071 – 394Histidinol dehydrogenaseAdd BLAST394

Interactioni

Protein-protein interaction databases

STRINGi273063.ST1464.

Structurei

3D structure databases

ProteinModelPortaliQ970Y9.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the histidinol dehydrogenase family.UniRule annotation

Phylogenomic databases

eggNOGiarCOG04352. Archaea.
COG0141. LUCA.
HOGENOMiHOG000243914.
KOiK00013.
OMAiWRGIITP.

Family and domain databases

CDDicd06572. Histidinol_dh. 1 hit.
HAMAPiMF_01024. HisD. 1 hit.
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]

Sequencei

Sequence statusi: Complete.

Q970Y9-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MILKELPKQR PNDFTKVLQD VEKIISYVKQ KGDEALIELE EKFDKVKLTS
60 70 80 90 100
IKFPEVDKLA SQISQDLKMA IDVIFTQIYE FNNSIKPPNI IGGSANGIDY
110 120 130 140 150
GIMWKSIERV GIYVPGGEKA YPSTLLMAGV PALVAGVKEI YVSSPPTKIN
160 170 180 190 200
SAIAYISLKL GVKEIYAIGG AQAIAAMAYG TQTVKKVDKI VGPGNIYVQA
210 220 230 240 250
AKYLVSSDVG IDGIEGPTEL VIIADETANP SNIILDLKAQ AEHGRSTFLV
260 270 280 290 300
LLSNSDKIIN FVSKELDVDS NIYYVIKVNS IDEAIDIANE IAPEHLSLQI
310 320 330 340 350
SSAREYLPKV KNAGAVTLGN TPPAIIDYSA GPNHILPTNG WAKIRGGISV
360 370 380 390
YDYLKMIMYA STSNPEKKLV EASKILAKYE GFVFHADSIG VRYE
Length:394
Mass (Da):42,933
Last modified:December 1, 2001 - v1
Checksum:iA8606499D3A65AA4
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BA000023 Genomic DNA. Translation: BAB66534.1.
RefSeqiWP_010979512.1. NC_003106.2.

Genome annotation databases

EnsemblBacteriaiBAB66534; BAB66534; STK_14640.
GeneIDi1459498.
KEGGisto:STK_14640.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BA000023 Genomic DNA. Translation: BAB66534.1.
RefSeqiWP_010979512.1. NC_003106.2.

3D structure databases

ProteinModelPortaliQ970Y9.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi273063.ST1464.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiBAB66534; BAB66534; STK_14640.
GeneIDi1459498.
KEGGisto:STK_14640.

Phylogenomic databases

eggNOGiarCOG04352. Archaea.
COG0141. LUCA.
HOGENOMiHOG000243914.
KOiK00013.
OMAiWRGIITP.

Enzyme and pathway databases

UniPathwayiUPA00031; UER00014.

Family and domain databases

CDDicd06572. Histidinol_dh. 1 hit.
HAMAPiMF_01024. HisD. 1 hit.
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...

Entry informationi

Entry nameiHISX_SULTO
AccessioniPrimary (citable) accession number: Q970Y9
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 25, 2003
Last sequence update: December 1, 2001
Last modified: November 2, 2016
This is version 93 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. SIMILARITY comments
    Index of protein domains and families

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 one 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.