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Protein

Histidinol dehydrogenase

Gene

hisD

Organism
Burkholderia multivorans (strain ATCC 17616 / 249)
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), ATP phosphoribosyltransferase regulatory subunit (hisZ)
  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. Histidinol-phosphate aminotransferase (hisC), 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 sitei138NADUniRule annotation1
Binding sitei199NADUniRule annotation1
Binding sitei222NADUniRule annotation1
Binding sitei245SubstrateUniRule annotation1
Metal bindingi267ZincUniRule annotation1
Binding sitei267SubstrateUniRule annotation1
Metal bindingi270ZincUniRule annotation1
Binding sitei270SubstrateUniRule annotation1
Active sitei335Proton acceptorUniRule annotation1
Active sitei336Proton acceptorUniRule annotation1
Binding sitei336SubstrateUniRule annotation1
Metal bindingi369ZincUniRule annotation1
Binding sitei369SubstrateUniRule annotation1
Binding sitei423SubstrateUniRule annotation1
Metal bindingi428ZincUniRule annotation1
Binding sitei428SubstrateUniRule 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:Bmul_0328, BMULJ_02926
OrganismiBurkholderia multivorans (strain ATCC 17616 / 249)
Taxonomic identifieri395019 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaBetaproteobacteriaBurkholderialesBurkholderiaceaeBurkholderiaBurkholderia cepacia complex
Proteomesi
  • UP000008815 Componenti: Chromosome 1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001357491 – 438Histidinol dehydrogenaseAdd BLAST438

Interactioni

Protein-protein interaction databases

STRINGi395019.BMULJ_02926.

Structurei

3D structure databases

ProteinModelPortaliQ845V3.
SMRiQ845V3.
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.

Q845V3-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSITIRKLDS TSEGFDAALR AVLAFEASED EAIERSVAQI LADVKSRGDA
60 70 80 90 100
AVLEYTNRFD RLNADSVAAL ELPQDALQAA LDGLEPKARA ALEAAAARVR
110 120 130 140 150
GYHEKQKIEC GTHSWQYTES DGTVLGQKIT PLDRVGLYVP GGKAAYPSSV
160 170 180 190 200
LMNAIPARVA GVGEIVMVVP TPDGVKNDLV LAAALLGGVD RVFTIGGAQA
210 220 230 240 250
VGALAYGTAT VPAVDKICGP GNAYVASAKR RVFGTVGIDM IAGPSEILVL
260 270 280 290 300
CDGTTDPSWV AMDLFSQAEH DELAQSILLC PDASFIERVE KAIAELLPSM
310 320 330 340 350
PRQDVIRASL EGRGALIKVR DMTEACRIAN DIAPEHLEIS ALEPQQWSQQ
360 370 380 390 400
IRHAGAIFLG RYTSESLGDY CAGPNHVLPT SRTARFSSPL GVYDFIKRSS
410 420 430
LIEVSAEGAH TLGEIAAELA YGEGLQAHAK SAEFRMKG
Length:438
Mass (Da):46,515
Last modified:September 2, 2008 - v2
Checksum:i8F702C8C7E014B1D
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti90 – 101AALEA…ARVRG → GRAGSGCRTRAR in BAC65270 (PubMed:12754231).CuratedAdd BLAST12

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB091436 Genomic DNA. Translation: BAC65270.1.
CP000868 Genomic DNA. Translation: ABX14023.1.
AP009385 Genomic DNA. Translation: BAG44811.1.
RefSeqiWP_006400584.1. NC_010804.1.

Genome annotation databases

EnsemblBacteriaiABX14023; ABX14023; Bmul_0328.
BAG44811; BAG44811; BMULJ_02926.
GeneIDi24998977.
KEGGibmj:BMULJ_02926.
bmu:Bmul_0328.
PATRICi19167814. VBIBurMul203716_3956.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB091436 Genomic DNA. Translation: BAC65270.1.
CP000868 Genomic DNA. Translation: ABX14023.1.
AP009385 Genomic DNA. Translation: BAG44811.1.
RefSeqiWP_006400584.1. NC_010804.1.

3D structure databases

ProteinModelPortaliQ845V3.
SMRiQ845V3.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi395019.BMULJ_02926.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiABX14023; ABX14023; Bmul_0328.
BAG44811; BAG44811; BMULJ_02926.
GeneIDi24998977.
KEGGibmj:BMULJ_02926.
bmu:Bmul_0328.
PATRICi19167814. VBIBurMul203716_3956.

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_BURM1
AccessioniPrimary (citable) accession number: Q845V3
Secondary accession number(s): A9AE01
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 13, 2004
Last sequence update: September 2, 2008
Last modified: November 2, 2016
This is version 92 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

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.