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Protein

Histidinol dehydrogenase

Gene

hisD

Organism
Sulfolobus islandicus (strain Y.N.15.51 / Yellowstone #2)
Status
Unreviewed-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. no protein annotated in this organism
  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 sitei114NADUniRule annotation1
Binding sitei176NADUniRule annotation1
Binding sitei199NADUniRule annotation1
Binding sitei222SubstrateUniRule annotation1
Metal bindingi244ZincUniRule annotation1
Binding sitei244SubstrateUniRule annotation1
Metal bindingi247ZincUniRule annotation1
Binding sitei247SubstrateUniRule annotation1
Active sitei298Proton acceptorUniRule annotation1
Active sitei299Proton acceptorUniRule annotation1
Binding sitei299SubstrateUniRule annotation1
Metal bindingi331ZincUniRule annotation1
Binding sitei331SubstrateUniRule annotation1
Binding sitei384SubstrateUniRule annotation1
Metal bindingi389ZincUniRule annotation1
Binding sitei389SubstrateUniRule annotation1

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

OxidoreductaseUniRule annotationImported

Keywords - Biological processi

Amino-acid biosynthesis, Histidine biosynthesisUniRule annotation

Keywords - Ligandi

Metal-bindingUniRule annotation, NADUniRule annotation, ZincUniRule annotation

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:YN1551_1297Imported
OrganismiSulfolobus islandicus (strain Y.N.15.51 / Yellowstone #2)Imported
Taxonomic identifieri419942 [NCBI]
Taxonomic lineageiArchaeaCrenarchaeotaThermoproteiSulfolobalesSulfolobaceaeSulfolobus
Proteomesi
  • UP000006818 Componenti: Chromosome

Family & Domainsi

Sequence similaritiesi

Belongs to the histidinol dehydrogenase family.UniRule annotation

Phylogenomic databases

HOGENOMiHOG000243914.
KOiK00013.
OMAiGGTARFY.

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.

C3NGY2-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MISYSLPNER PNDFSRVIPV VRDIIESVKA RGDNALYQLT EKLDKVKINN
60 70 80 90 100
IKVSEEELKT QASKLDPKVK QAIDVAYEQL KAFHEMLVPP NIGGGYQGIS
110 120 130 140 150
FGVVWRSIEK IGIYVPSGKY SYPSTLLMAG IPAKVAKVKE IYVASPPNQE
160 170 180 190 200
GSVNPALAYV AIKLGVNDVY KVGGAQAIAA LAYGTESVRK VYKIVGPGNV
210 220 230 240 250
YVQAAKFLVS NVVGIDGIEG PTELVIIADE TAKAEHVVLD MKAQAEHGPD
260 270 280 290 300
TYIVLLSNDD ELLKKVEEKI MDDKKIYYII KTKNIDEAIE IANKIAPEHL
310 320 330 340 350
SLYVKDAYTL MDKIVNAGAI SLGNTPPAII DYVAGPNHIL PTNGWARIRG
360 370 380 390
GVTVYDFIKP TMYANVRDIN KQLLEASISL ANYEGFVIHG KSIGVRYE
Length:398
Mass (Da):43,606
Last modified:June 16, 2009 - v1
Checksum:i5642CBB806FA93FB
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP001404 Genomic DNA. Translation: ACP48392.1.
RefSeqiWP_012717403.1. NC_012623.1.

Genome annotation databases

EnsemblBacteriaiACP48392; ACP48392; YN1551_1297.
GeneIDi7810082.
KEGGisin:YN1551_1297.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP001404 Genomic DNA. Translation: ACP48392.1.
RefSeqiWP_012717403.1. NC_012623.1.

3D structure databases

ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiACP48392; ACP48392; YN1551_1297.
GeneIDi7810082.
KEGGisin:YN1551_1297.

Phylogenomic databases

HOGENOMiHOG000243914.
KOiK00013.
OMAiGGTARFY.

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 nameiC3NGY2_SULIN
AccessioniPrimary (citable) accession number: C3NGY2
Entry historyi
Integrated into UniProtKB/TrEMBL: June 16, 2009
Last sequence update: June 16, 2009
Last modified: November 2, 2016
This is version 58 of the entry and version 1 of the sequence. [Complete history]
Entry statusiUnreviewed (UniProtKB/TrEMBL)

Miscellaneousi

Keywords - Technical termi

Complete proteomeImported

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.