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Protein

Histidinol dehydrogenase

Gene

hisD

Organism
Pyrococcus furiosus (strain ATCC 43587 / DSM 3638 / JCM 8422 / Vc1)
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.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

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.
Proteins known to be involved in the 9 steps of the subpathway in this organism are:
  1. ATP phosphoribosyltransferase (hisG)
  2. Histidine biosynthesis bifunctional protein HisIE (hisI)
  3. Histidine biosynthesis bifunctional protein HisIE (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 sitei99NADBy similarity1
Binding sitei159NADBy similarity1
Binding sitei181NADBy similarity1
Binding sitei204SubstrateBy similarity1
Metal bindingi226ZincBy similarity1
Binding sitei226SubstrateBy similarity1
Metal bindingi229ZincBy similarity1
Binding sitei229SubstrateBy similarity1
Active sitei274Proton acceptorBy similarity1
Active sitei275Proton acceptorBy similarity1
Binding sitei275SubstrateBy similarity1
Metal bindingi308ZincBy similarity1
Binding sitei308SubstrateBy similarity1
Binding sitei362SubstrateBy similarity1
Metal bindingi367ZincBy similarity1
Binding sitei367SubstrateBy similarity1

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 dehydrogenase (EC:1.1.1.23)
Short name:
HDH
Gene namesi
Name:hisD
Ordered Locus Names:PF1659
OrganismiPyrococcus furiosus (strain ATCC 43587 / DSM 3638 / JCM 8422 / Vc1)
Taxonomic identifieri186497 [NCBI]
Taxonomic lineageiArchaeaEuryarchaeotaThermococciThermococcalesThermococcaceaePyrococcus
Proteomesi
  • UP000001013 Componenti: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001359031 – 375Histidinol dehydrogenaseAdd BLAST375

Proteomic databases

PRIDEiO59626.

Interactioni

Protein-protein interaction databases

STRINGi186497.PF1659.

Structurei

3D structure databases

ProteinModelPortaliO59626.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the histidinol dehydrogenase family.Curated

Phylogenomic databases

eggNOGiarCOG04352. Archaea.
COG0141. LUCA.
HOGENOMiHOG000243914.
KOiK00013.
OMAiNAGAIYL.

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. 2 hits.
[Graphical view]
PRINTSiPR00083. HOLDHDRGNASE.
SUPFAMiSSF53720. SSF53720. 1 hit.
TIGRFAMsiTIGR00069. hisD. 1 hit.
PROSITEiPS00611. HISOL_DEHYDROGENASE. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

O59626-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MDIEEYVREI LKDIRERGLE AIREYSKKFD GYEGPFEVSK EEFKEAEERI
60 70 80 90 100
PERDKEIIKR TLKRIEKYHR KQLKQDILYI ENGSLYGLIY KPLKRIGIYV
110 120 130 140 150
PGGKPLPSTL MMVGVPARVA GVKEIVVTNP PKDGKVNPYI LYIAKLLKIE
160 170 180 190 200
EVYKLGGIQA IAAMAYGIGM KKVQKIFGPG NKFVNEAKRQ VFGIVGIDSL
210 220 230 240 250
AGPSEIAVIA DESADKDFVL YDLLSQLEHG KDSKAWLLTT SKELADYCNR
260 270 280 290 300
EGITVIVCSS LEECCKKANE IAPEHLEIIT REPLKLVDLI ENAGAIYLGL
310 320 330 340 350
YTPVPAADYF LGVNHVLPTG GAAKFMGVLT VWDFMKPISI AMVSREEFIS
360 370
ERELGIRLAE IEGIELHKKS LEVRK
Length:375
Mass (Da):42,178
Last modified:April 3, 2002 - v2
Checksum:iF8874116A40B1A1B
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti97G → R in BAA25804 (Ref. 1) Curated1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB013080 Genomic DNA. Translation: BAA25804.1.
AE009950 Genomic DNA. Translation: AAL81783.1.
RefSeqiWP_011012805.1. NC_003413.1.

Genome annotation databases

EnsemblBacteriaiAAL81783; AAL81783; PF1659.
GeneIDi1469536.
KEGGipfu:PF1659.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB013080 Genomic DNA. Translation: BAA25804.1.
AE009950 Genomic DNA. Translation: AAL81783.1.
RefSeqiWP_011012805.1. NC_003413.1.

3D structure databases

ProteinModelPortaliO59626.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi186497.PF1659.

Proteomic databases

PRIDEiO59626.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAL81783; AAL81783; PF1659.
GeneIDi1469536.
KEGGipfu:PF1659.

Phylogenomic databases

eggNOGiarCOG04352. Archaea.
COG0141. LUCA.
HOGENOMiHOG000243914.
KOiK00013.
OMAiNAGAIYL.

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. 2 hits.
[Graphical view]
PRINTSiPR00083. HOLDHDRGNASE.
SUPFAMiSSF53720. SSF53720. 1 hit.
TIGRFAMsiTIGR00069. hisD. 1 hit.
PROSITEiPS00611. HISOL_DEHYDROGENASE. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiHISX_PYRFU
AccessioniPrimary (citable) accession number: O59626
Entry historyi
Integrated into UniProtKB/Swiss-Prot: September 26, 2001
Last sequence update: April 3, 2002
Last modified: September 7, 2016
This is version 109 of the entry and version 2 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.