Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Histidinol dehydrogenase

Gene

hisD

Organism
Corynebacterium jeikeium (strain K411)
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 sitei135NADUniRule annotation1
Binding sitei197NADUniRule annotation1
Binding sitei225NADUniRule annotation1
Binding sitei248SubstrateUniRule annotation1
Metal bindingi270ZincUniRule annotation1
Binding sitei270SubstrateUniRule annotation1
Metal bindingi273ZincUniRule annotation1
Binding sitei273SubstrateUniRule annotation1
Active sitei339Proton acceptorUniRule annotation1
Active sitei340Proton acceptorUniRule annotation1
Binding sitei340SubstrateUniRule annotation1
Metal bindingi373ZincUniRule annotation1
Binding sitei373SubstrateUniRule annotation1
Binding sitei427SubstrateUniRule annotation1
Metal bindingi432ZincUniRule annotation1
Binding sitei432SubstrateUniRule 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:jk0786
OrganismiCorynebacterium jeikeium (strain K411)
Taxonomic identifieri306537 [NCBI]
Taxonomic lineageiBacteriaActinobacteriaCorynebacterialesCorynebacteriaceaeCorynebacterium
Proteomesi
  • UP000000545 Componenti: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001357621 – 450Histidinol dehydrogenaseAdd BLAST450

Proteomic databases

PRIDEiQ4JW59.

Interactioni

Protein-protein interaction databases

STRINGi306537.jk0786.

Structurei

3D structure databases

ProteinModelPortaliQ4JW59.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the histidinol dehydrogenase family.UniRule annotation

Phylogenomic databases

eggNOGiENOG4105CEK. Bacteria.
COG0141. LUCA.
HOGENOMiHOG000243914.
KOiK00013.
OMAiGGTARFY.
OrthoDBiPOG091H03YX.

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.

Q4JW59-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MTSAQLDFSR IDLRGQAPTT AELRHRLPRG GTDVDSVIPT VAPIVDQVRE
60 70 80 90 100
GGARAALEIG QRFDGVTPDS VRVPAEVIDA AVGTLADDVI AALEEAIKRV
110 120 130 140 150
RAFHSAIRPE DKQVEVAPGG IVTERFIPVQ RVGLYAPGGN AVYPSSVIMN
160 170 180 190 200
VVPAQEAGVE SLVVASPPQE GGWPHPTVLA ACKLLGVDEV WAVGGAQAVA
210 220 230 240 250
LLAHGSTAEG GEELEPVDMV TGPGNIFVTA AKRLCRSVVG IDSEAGPTEI
260 270 280 290 300
AVLADESANA VEIAYDLISQ AEHDTMAASV LITDSEKLAD EVVAEMNERY
310 320 330 340 350
HITENSERVA EALSGQQSGV VLVDDIAAGI RAANAYGAEH LEIHTEDAHG
360 370 380 390 400
VAAQITNAGA IFIGRFSPVP LGDYAAGSNH VLPTSGTARH SSGLSTLTFL
410 420 430 440 450
KSVHVIDYNE EGLRGVADTV ITLSKSEGLP AHGEAISART STANTNGTEV
Length:450
Mass (Da):46,775
Last modified:August 2, 2005 - v1
Checksum:i2BED7B5FA2E531C5
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CR931997 Genomic DNA. Translation: CAI36948.1.
RefSeqiWP_011273391.1. NC_007164.1.

Genome annotation databases

EnsemblBacteriaiCAI36948; CAI36948; jk0786.
GeneIDi3433179.
KEGGicjk:jk0786.
PATRICi21512466. VBICorJei31838_0795.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CR931997 Genomic DNA. Translation: CAI36948.1.
RefSeqiWP_011273391.1. NC_007164.1.

3D structure databases

ProteinModelPortaliQ4JW59.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi306537.jk0786.

Proteomic databases

PRIDEiQ4JW59.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiCAI36948; CAI36948; jk0786.
GeneIDi3433179.
KEGGicjk:jk0786.
PATRICi21512466. VBICorJei31838_0795.

Phylogenomic databases

eggNOGiENOG4105CEK. Bacteria.
COG0141. LUCA.
HOGENOMiHOG000243914.
KOiK00013.
OMAiGGTARFY.
OrthoDBiPOG091H03YX.

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_CORJK
AccessioniPrimary (citable) accession number: Q4JW59
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 10, 2006
Last sequence update: August 2, 2005
Last modified: November 2, 2016
This is version 81 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.