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Protein

Histidinol dehydrogenase

Gene

hisD

Organism
Bordetella bronchiseptica (strain ATCC BAA-588 / NCTC 13252 / RB50) (Alcaligenes bronchisepticus)
Status
Reviewed-Annotation score: -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 2 (hisC2), Histidinol-phosphate aminotransferase 1 (hisC1)
  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 sitei139NADUniRule annotation1
Binding sitei200NADUniRule annotation1
Binding sitei223NADUniRule annotation1
Binding sitei246SubstrateUniRule annotation1
Metal bindingi268ZincUniRule annotation1
Binding sitei268SubstrateUniRule annotation1
Metal bindingi271ZincUniRule annotation1
Binding sitei271SubstrateUniRule annotation1
Active sitei336Proton acceptorUniRule annotation1
Active sitei337Proton acceptorUniRule annotation1
Binding sitei337SubstrateUniRule annotation1
Metal bindingi370ZincUniRule annotation1
Binding sitei370SubstrateUniRule annotation1
Binding sitei424SubstrateUniRule annotation1
Metal bindingi429ZincUniRule annotation1
Binding sitei429SubstrateUniRule annotation1

GO - Molecular functioni

GO - Biological processi

Keywordsi

Molecular functionOxidoreductase
Biological processAmino-acid biosynthesis, Histidine biosynthesis
LigandMetal-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:BB4854
OrganismiBordetella bronchiseptica (strain ATCC BAA-588 / NCTC 13252 / RB50) (Alcaligenes bronchisepticus)
Taxonomic identifieri257310 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaBetaproteobacteriaBurkholderialesAlcaligenaceaeBordetella
Proteomesi

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001357361 – 440Histidinol dehydrogenaseAdd BLAST440

Proteomic databases

PRIDEiQ7WDY4

Interactioni

Protein-protein interaction databases

STRINGi257310.BB4854

Structurei

3D structure databases

ProteinModelPortaliQ7WDY4
SMRiQ7WDY4
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the histidinol dehydrogenase family.UniRule annotation

Phylogenomic databases

eggNOGiENOG4105CEK Bacteria
COG0141 LUCA
HOGENOMiHOG000243914
KOiK00013
OMAiQAEHDPM
OrthoDBiPOG091H03YX

Family and domain databases

CDDicd06572 Histidinol_dh, 1 hit
HAMAPiMF_01024 HisD, 1 hit
InterProiView protein in InterPro
IPR016161 Ald_DH/histidinol_DH
IPR001692 Histidinol_DH_CS
IPR022695 Histidinol_DH_monofunct
IPR012131 Hstdl_DH
PANTHERiPTHR21256 PTHR21256, 1 hit
PfamiView protein in Pfam
PF00815 Histidinol_dh, 1 hit
PIRSFiPIRSF000099 Histidinol_dh, 1 hit
PRINTSiPR00083 HOLDHDRGNASE
SUPFAMiSSF53720 SSF53720, 1 hit
TIGRFAMsiTIGR00069 hisD, 1 hit
PROSITEiView protein in PROSITE
PS00611 HISOL_DEHYDROGENASE, 1 hit

Sequencei

Sequence statusi: Complete.

Q7WDY4-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MQYHDAMALI NRLDSRDPGF KTALSQLLAF EAEQDESIDQ AAAGILADVR
60 70 80 90 100
RRGDAALLEY TQRFDRLAVD DATALEIPQA DWHAALDSLP AAQRQALEAA
110 120 130 140 150
AARVRAYHER QRGETWTYTE ADGTMLGQQI TALDRVGLYV PGGKAAYPSS
160 170 180 190 200
VLMNAIPAKV AGVPELIMVT PTPDGVRNPI VLAAAAIAGV DRAFAIGGAQ
210 220 230 240 250
AVGALAYGTA TVPAVDKIVG PGNAYVAAAK RRVFGTVGID MIAGPSEILV
260 270 280 290 300
ICDGKTPADW IAMDLFSQAE HDELAQSILL CPDAAFLAEV EAAIERLLPG
310 320 330 340 350
MPRADILRVS LANRGALILV RDLEEACAIA NDIAPEHLEI STEQPQRWTA
360 370 380 390 400
LIRHAGAIFM GRYSSEALGD YCAGPNHVLP TSRTARFSSP LGVYDFQKRS
410 420 430 440
SLIQVSREGA QTLGRIAAEL ALGEGLQAHA ASAQYRLDQP
Length:440
Mass (Da):46,882
Last modified:October 1, 2003 - v1
Checksum:iD8FC76AF462F129A
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BX640451 Genomic DNA Translation: CAE35217.1

Genome annotation databases

EnsemblBacteriaiCAE35217; CAE35217; BB4854
KEGGibbr:BB4854

Entry informationi

Entry nameiHISX_BORBR
AccessioniPrimary (citable) accession number: Q7WDY4
Entry historyiIntegrated into UniProtKB/Swiss-Prot: April 13, 2004
Last sequence update: October 1, 2003
Last modified: May 23, 2018
This is version 91 of the entry and version 1 of the sequence. See 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

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