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Protein

Histidinol dehydrogenase

Gene

hisD

Organism
Pyrobaculum aerophilum (strain ATCC 51768 / IM2 / DSM 7523 / JCM 9630 / NBRC 100827)
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 HisH (hisH), Imidazole glycerol phosphate synthase subunit HisF (hisF)
  6. Imidazoleglycerol-phosphate dehydratase (hisB)
  7. no protein annotated in this organism
  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 sitei197SubstrateUniRule annotation1
Metal bindingi218ZincUniRule annotation1
Binding sitei218SubstrateUniRule annotation1
Metal bindingi221ZincUniRule annotation1
Binding sitei221SubstrateUniRule annotation1
Active sitei276Proton acceptorUniRule annotation1
Active sitei277Proton acceptorUniRule annotation1
Binding sitei277SubstrateUniRule annotation1
Metal bindingi306ZincUniRule annotation1
Binding sitei306SubstrateUniRule annotation1
Binding sitei358SubstrateUniRule annotation1
Metal bindingi363ZincUniRule annotation1
Binding sitei363SubstrateUniRule 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:PAE0988
OrganismiPyrobaculum aerophilum (strain ATCC 51768 / IM2 / DSM 7523 / JCM 9630 / NBRC 100827)
Taxonomic identifieri178306 [NCBI]
Taxonomic lineageiArchaeaCrenarchaeotaThermoproteiThermoprotealesThermoproteaceaePyrobaculum
Proteomesi
  • UP000002439 Componenti: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001359021 – 368Histidinol dehydrogenaseAdd BLAST368

Interactioni

Protein-protein interaction databases

STRINGi178306.PAE0988.

Structurei

3D structure databases

ProteinModelPortaliQ8ZY17.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the histidinol dehydrogenase family.UniRule annotation

Phylogenomic databases

eggNOGiarCOG04352. Archaea.
COG0141. LUCA.
HOGENOMiHOG000243914.
InParanoidiQ8ZY17.
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.
IPR012131. Hstdl_DH.
[Graphical view]
PfamiPF00815. Histidinol_dh. 1 hit.
[Graphical view]
PRINTSiPR00083. HOLDHDRGNASE.
SUPFAMiSSF53720. SSF53720. 1 hit.
TIGRFAMsiTIGR00069. hisD. 1 hit.
PROSITEiPS00611. HISOL_DEHYDROGENASE. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q8ZY17-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MRGFPREVLE SVWKIVDDVQ SGGLKAALEY SKRLDGVAPE PHLVTPRQGG
60 70 80 90 100
DPEVVSAALA AAKSLEALYS RISPPAAVDF YGGILRQILW KPVRRAALYV
110 120 130 140 150
PARYISTLVM LAVPARLAGV EEVYVVTPPR GVSEELLAVA KELGVKAVLA
160 170 180 190 200
LGGPHGLAYA VFHMGVDVVA GPGGLYVQAA KYILSQYVGI DGIEGPTELV
210 220 230 240 250
IYAEGVPPEV AVRGALAQLE HGPTSFAYLL SPDGELLKKA EELYVRERTS
260 270 280 290 300
SMGPLKVKKV GGIDEAVSFI DEIAPEHLEV WGRREVAYRV RNVGAVSVNM
310 320 330 340 350
PSPYLDYVAG ISHVLPTGGT ARWRGVITPL AFMKPIGIAE AVGELTLREA
360
ARKLAEYEGF KYHGEALR
Length:368
Mass (Da):39,541
Last modified:March 1, 2002 - v1
Checksum:i7346BE8A2B0333EA
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE009441 Genomic DNA. Translation: AAL63179.1.

Genome annotation databases

EnsemblBacteriaiAAL63179; AAL63179; PAE0988.
KEGGipai:PAE0988.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE009441 Genomic DNA. Translation: AAL63179.1.

3D structure databases

ProteinModelPortaliQ8ZY17.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi178306.PAE0988.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAL63179; AAL63179; PAE0988.
KEGGipai:PAE0988.

Phylogenomic databases

eggNOGiarCOG04352. Archaea.
COG0141. LUCA.
HOGENOMiHOG000243914.
InParanoidiQ8ZY17.
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.
IPR012131. Hstdl_DH.
[Graphical view]
PfamiPF00815. Histidinol_dh. 1 hit.
[Graphical view]
PRINTSiPR00083. HOLDHDRGNASE.
SUPFAMiSSF53720. SSF53720. 1 hit.
TIGRFAMsiTIGR00069. hisD. 1 hit.
PROSITEiPS00611. HISOL_DEHYDROGENASE. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiHISX_PYRAE
AccessioniPrimary (citable) accession number: Q8ZY17
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 25, 2003
Last sequence update: March 1, 2002
Last modified: November 2, 2016
This is version 94 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.