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Protein

Histidinol dehydrogenase

Gene

hisD

Organism
Thermus thermophilus (strain HB8 / ATCC 27634 / DSM 579)
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. Histidine biosynthesis bifunctional protein HisIE (hisI)
  3. Histidine biosynthesis bifunctional protein HisIE (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 sitei118NADUniRule annotation1
Binding sitei176NADUniRule annotation1
Binding sitei199NADUniRule annotation1
Binding sitei222SubstrateUniRule annotation1
Metal bindingi244ZincUniRule annotation1
Binding sitei244SubstrateUniRule annotation1
Metal bindingi247ZincUniRule annotation1
Binding sitei247SubstrateUniRule annotation1
Active sitei311Proton acceptorUniRule annotation1
Active sitei312Proton acceptorUniRule annotation1
Binding sitei312SubstrateUniRule annotation1
Metal bindingi345ZincUniRule annotation1
Binding sitei345SubstrateUniRule annotation1
Binding sitei399SubstrateUniRule annotation1
Metal bindingi404ZincUniRule annotation1
Binding sitei404SubstrateUniRule annotation1

GO - Molecular functioni

GO - Biological processi

Keywordsi

Molecular functionOxidoreductase
Biological processAmino-acid biosynthesis, Histidine biosynthesis
LigandMetal-binding, NAD, Zinc

Enzyme and pathway databases

BioCyciTTHE300852:G1GKC-739-MONOMER
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:TTHA0722
OrganismiThermus thermophilus (strain HB8 / ATCC 27634 / DSM 579)
Taxonomic identifieri300852 [NCBI]
Taxonomic lineageiBacteriaDeinococcus-ThermusDeinococciThermalesThermaceaeThermus
Proteomesi
  • UP000000532 Componenti: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001358711 – 412Histidinol dehydrogenaseAdd BLAST412

Proteomic databases

PRIDEiQ5SKC1

Interactioni

Protein-protein interaction databases

STRINGi300852.TTHA0722

Structurei

3D structure databases

ProteinModelPortaliQ5SKC1
SMRiQ5SKC1
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the histidinol dehydrogenase family.UniRule annotation

Phylogenomic databases

eggNOGiENOG4105CEK Bacteria
COG0141 LUCA
HOGENOMiHOG000243914
KOiK00013
OMAiQAEHDPM
PhylomeDBiQ5SKC1

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.

Q5SKC1-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MIYAAEEVRA RFARRGLSFD PTVEEIVRGI LEAVREEGDE ALDRFSRDLD
60 70 80 90 100
GYPVEEVPKR AWREAYEDLD EDLRDALETA RERIEAFYRE EARGGFLRAE
110 120 130 140 150
GGGVLAQLVR PLERVGVYVP GGSAPLLSTL LMTVVPAKVA GVREVIVASP
160 170 180 190 200
PKVHPGVLAA AWVAGADRLF AMGGAQAIAA LAYGTGRVPR VDKIVGPGNR
210 220 230 240 250
YVVAAKRLVY GTVGIDGLAG PTETMIIADG SASPRLLAAD LLAQAEHGPD
260 270 280 290 300
SEPWLLSPDR ALLERVEAEL SWQLQDLPRA EVARQALEKG GLVLTKDLEE
310 320 330 340 350
AFALANLYAP EHLSLALSDP LPWLEKVQNA GGVFLGEGSP EALGDYIAGP
360 370 380 390 400
SHVMPTSGTA RFQGGLAVRD FLKVIPVVGL SEGAARELAK KGALLARAEG
410
LEGHARSLDL RR
Length:412
Mass (Da):44,123
Last modified:December 21, 2004 - v1
Checksum:i4A4BBDC4F9027A3E
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AP008226 Genomic DNA Translation: BAD70545.1
RefSeqiWP_011228145.1, NC_006461.1
YP_143988.1, NC_006461.1

Genome annotation databases

EnsemblBacteriaiBAD70545; BAD70545; BAD70545
GeneIDi3170022
KEGGittj:TTHA0722
PATRICifig|300852.9.peg.715

Similar proteinsi

Entry informationi

Entry nameiHISX_THET8
AccessioniPrimary (citable) accession number: Q5SKC1
Entry historyiIntegrated into UniProtKB/Swiss-Prot: January 10, 2006
Last sequence update: December 21, 2004
Last modified: May 23, 2018
This is version 90 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, Reference proteome

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. SIMILARITY comments
    Index of protein domains and families

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