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Protein

Histidinol dehydrogenase

Gene

hisD

Organism
Bordetella parapertussis (strain 12822 / ATCC BAA-587 / NCTC 13253)
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 HisF (hisF), Imidazole glycerol phosphate synthase subunit HisH (hisH)
  6. Imidazoleglycerol-phosphate dehydratase (hisB)
  7. Histidinol-phosphate aminotransferase 1 (hisC1), Histidinol-phosphate aminotransferase 2 (hisC2)
  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

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:BPP4267
OrganismiBordetella parapertussis (strain 12822 / ATCC BAA-587 / NCTC 13253)
Taxonomic identifieri257311 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaBetaproteobacteriaBurkholderialesAlcaligenaceaeBordetella
Proteomesi
  • UP000001421 Componenti: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001357371 – 440Histidinol dehydrogenaseAdd BLAST440

Structurei

3D structure databases

ProteinModelPortaliQ7W2Y4.
SMRiQ7W2Y4.
ModBaseiSearch...
MobiDBiSearch...

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.

Q7W2Y4-1 [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
BX640436 Genomic DNA. Translation: CAE39546.1.

Genome annotation databases

EnsemblBacteriaiCAE39546; CAE39546; BPP4267.
KEGGibpa:BPP4267.
PATRICi21152644. VBIBorPar43418_4478.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BX640436 Genomic DNA. Translation: CAE39546.1.

3D structure databases

ProteinModelPortaliQ7W2Y4.
SMRiQ7W2Y4.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiCAE39546; CAE39546; BPP4267.
KEGGibpa:BPP4267.
PATRICi21152644. VBIBorPar43418_4478.

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 nameiHISX_BORPA
AccessioniPrimary (citable) accession number: Q7W2Y4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 13, 2004
Last sequence update: October 1, 2003
Last modified: November 2, 2016
This is version 87 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

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.