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Protein

Histidinol dehydrogenase

Gene

hisD

Organism
Geobacillus thermodenitrificans (strain NG80-2)
Status
Unreviewed-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 annotationSAAS annotation

Catalytic activityi

L-histidinol + H2O + 2 NAD+ = L-histidine + 2 NADH.UniRule annotationSAAS 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 annotationSAAS 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 HisH (hisH), Imidazole glycerol phosphate synthase subunit HisF (hisF)
  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 sitei220NADUniRule annotation1
Binding sitei243SubstrateUniRule annotation1
Metal bindingi265ZincUniRule annotation1
Binding sitei265SubstrateUniRule annotation1
Metal bindingi268ZincUniRule annotation1
Binding sitei268SubstrateUniRule annotation1
Active sitei333Proton acceptorUniRule annotation1
Active sitei334Proton acceptorUniRule annotation1
Binding sitei334SubstrateUniRule annotation1
Metal bindingi367ZincUniRule annotation1
Binding sitei367SubstrateUniRule annotation1
Binding sitei421SubstrateUniRule annotation1
Metal bindingi426ZincUniRule annotation1
Binding sitei426SubstrateUniRule annotation1

GO - Molecular functioni

GO - Biological processi

Keywordsi

Molecular functionOxidoreductaseUniRule annotationSAAS annotation
Biological processAmino-acid biosynthesis, Histidine biosynthesisUniRule annotationSAAS annotation
LigandMetal-bindingUniRule annotationSAAS annotation, NADUniRule annotationSAAS annotation, ZincUniRule annotationSAAS annotation

Enzyme and pathway databases

UniPathwayiUPA00031; UER00014

Names & Taxonomyi

Protein namesi
Recommended name:
Histidinol dehydrogenaseUniRule annotationSAAS annotation (EC:1.1.1.23UniRule annotationSAAS annotation)
Short name:
HDHUniRule annotation
Gene namesi
Name:hisDUniRule annotation
Ordered Locus Names:GTNG_3025Imported
OrganismiGeobacillus thermodenitrificans (strain NG80-2)Imported
Taxonomic identifieri420246 [NCBI]
Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesBacillaceaeGeobacillus
Proteomesi
  • UP000001578 Componenti: Chromosome

Interactioni

Protein-protein interaction databases

STRINGi420246.GTNG_3025

Structurei

3D structure databases

ProteinModelPortaliA4ISR6
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Coiled coil

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Coiled coili420 – 440Sequence analysisAdd BLAST21

Sequence similaritiesi

Belongs to the histidinol dehydrogenase family.UniRule annotationSAAS annotation

Keywords - Domaini

Coiled coilSequence analysis

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.

A4ISR6-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MDENRWTSQK GERTMKIERV QGGVSLRRTI ESGTDEQRRA VLDIIAAVRA
60 70 80 90 100
RGDAALKEYT EQFDGVKLET LQVTEEEMKR AHAALSPEML AVIREAATNI
110 120 130 140 150
RDYHERQKRQ SWWMTKEDGT ILGQKVTPLD AVGLYVPGGT AAYPSSVLMN
160 170 180 190 200
VIPAQVAGVK RIVIASPPNA DGSLPDGVLA AAYELGVTEV YKVGGAQAIA
210 220 230 240 250
ALAYGTETIR PVDKIFGPGN IYVALAKREV FGHVAIDMIA GPSEIVVLAD
260 270 280 290 300
ETAYADEIAA DLLSQAEHDV RASAILVTPS MKLALAVASE VERQLETLPR
310 320 330 340 350
REIAQAALET YGAIYVTETL DEAVDVVNEL APEHLEVMTA EPMALLGKLR
360 370 380 390 400
HAGAMFFGRF SSEPVGDYFA GPNHVLPTNG TARFSSGLSV DEFVKKSSVI
410 420 430 440
VYSEAALREH GKDIAAFARL EGLEAHARAI EVRLKKERGE R
Length:441
Mass (Da):47,862
Last modified:May 1, 2007 - v1
Checksum:i463946FB50E2044C
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000557 Genomic DNA Translation: ABO68370.1

Genome annotation databases

EnsemblBacteriaiABO68370; ABO68370; GTNG_3025
KEGGigtn:GTNG_3025

Similar proteinsi

Entry informationi

Entry nameiA4ISR6_GEOTN
AccessioniPrimary (citable) accession number: A4ISR6
Entry historyiIntegrated into UniProtKB/TrEMBL: May 1, 2007
Last sequence update: May 1, 2007
Last modified: March 28, 2018
This is version 91 of the entry and version 1 of the sequence. See complete history.
Entry statusiUnreviewed (UniProtKB/TrEMBL)

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteomeImported

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