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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

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.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)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei197 – 1971SubstrateUniRule annotation
Metal bindingi218 – 2181ZincUniRule annotation
Binding sitei218 – 2181SubstrateUniRule annotation
Metal bindingi221 – 2211ZincUniRule annotation
Binding sitei221 – 2211SubstrateUniRule annotation
Active sitei276 – 2761Proton acceptorUniRule annotation
Active sitei277 – 2771Proton acceptorUniRule annotation
Binding sitei277 – 2771SubstrateUniRule annotation
Metal bindingi306 – 3061ZincUniRule annotation
Binding sitei306 – 3061SubstrateUniRule annotation
Binding sitei358 – 3581SubstrateUniRule annotation
Metal bindingi363 – 3631ZincUniRule annotation
Binding sitei363 – 3631SubstrateUniRule annotation

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

BioCyciPAER178306:GCEO-707-MONOMER.
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
ProteomesiUP000002439 Componenti: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 368368Histidinol dehydrogenasePRO_0000135902Add
BLAST

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

eggNOGiCOG0141.
HOGENOMiHOG000243914.
InParanoidiQ8ZY17.
KOiK00013.
OMAiPEHLEVW.

Family and domain databases

HAMAPiMF_01024. HisD.
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.
RefSeqiNP_558997.1. NC_003364.1.
WP_011007651.1. NC_003364.1.

Genome annotation databases

EnsemblBacteriaiAAL63179; AAL63179; PAE0988.
GeneIDi1465414.
KEGGipai:PAE0988.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE009441 Genomic DNA. Translation: AAL63179.1.
RefSeqiNP_558997.1. NC_003364.1.
WP_011007651.1. NC_003364.1.

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.
GeneIDi1465414.
KEGGipai:PAE0988.

Phylogenomic databases

eggNOGiCOG0141.
HOGENOMiHOG000243914.
InParanoidiQ8ZY17.
KOiK00013.
OMAiPEHLEVW.

Enzyme and pathway databases

UniPathwayiUPA00031; UER00014.
BioCyciPAER178306:GCEO-707-MONOMER.

Family and domain databases

HAMAPiMF_01024. HisD.
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...

Publicationsi

  1. "Genome sequence of the hyperthermophilic crenarchaeon Pyrobaculum aerophilum."
    Fitz-Gibbon S.T., Ladner H., Kim U.-J., Stetter K.O., Simon M.I., Miller J.H.
    Proc. Natl. Acad. Sci. U.S.A. 99:984-989(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 51768 / IM2 / DSM 7523 / JCM 9630 / NBRC 100827.

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: April 29, 2015
This is version 90 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

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.