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Protein

Histidinol dehydrogenase

Gene

hisD

Organism
Rhodospirillum rubrum (strain ATCC 11170 / ATH 1.1.1 / DSM 467 / LMG 4362 / NCIB 8255 / S1)
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 regulatory subunit (hisZ), ATP phosphoribosyltransferase (hisG)
  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 (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 sitei130NADUniRule annotation1
Binding sitei191NADUniRule annotation1
Binding sitei214NADUniRule annotation1
Binding sitei237SubstrateUniRule annotation1
Metal bindingi259ZincUniRule annotation1
Binding sitei259SubstrateUniRule annotation1
Metal bindingi262ZincUniRule annotation1
Binding sitei262SubstrateUniRule annotation1
Active sitei328Proton acceptorUniRule annotation1
Active sitei329Proton acceptorUniRule annotation1
Binding sitei329SubstrateUniRule annotation1
Metal bindingi362ZincUniRule annotation1
Binding sitei362SubstrateUniRule annotation1
Binding sitei416SubstrateUniRule annotation1
Metal bindingi421ZincUniRule annotation1
Binding sitei421SubstrateUniRule 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:Rru_A2771
OrganismiRhodospirillum rubrum (strain ATCC 11170 / ATH 1.1.1 / DSM 467 / LMG 4362 / NCIB 8255 / S1)
Taxonomic identifieri269796 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaAlphaproteobacteriaRhodospirillalesRhodospirillaceaeRhodospirillum
Proteomesi
  • UP000001929 Componenti: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00002298651 – 434Histidinol dehydrogenaseAdd BLAST434

Proteomic databases

PRIDEiQ2RQM7

Interactioni

Protein-protein interaction databases

STRINGi269796.Rru_A2771

Structurei

3D structure databases

ProteinModelPortaliQ2RQM7
SMRiQ2RQM7
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.

Q2RQM7-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MPLRLEASSA DFAPAFAALL AGKRESAQDV NDVVSAILAD VRLRGDDALI
60 70 80 90 100
DYTARFDKMT VSAEGLRFSD DEVDTAVALI EPALRDALAL AAKRITRFHE
110 120 130 140 150
RQMPTAISFT DEDGVRLGQR WTAVSAAGLY VPGGLAAYPS SVLMNALPAK
160 170 180 190 200
VAGVERLVMV VPTPAGRINP LVLAAAKLAG VDEIYRVGGA QAVAALAYGT
210 220 230 240 250
RTIAPVDKIV GPGNAYVAAA KRQVFGTVGI DMIAGPSEIL VVADGANDPD
260 270 280 290 300
WIALDLLSQA EHDAAAQSIL ITDDRAFADR VERAVTDRLR TLSRTEIASA
310 320 330 340 350
SWRDHGAIIL VGDLLRDAPA LVDKVAPEHL ELAVADPDAL AARVRHAGAI
360 370 380 390 400
FLGRYTPEAI GDYIAGPNHV LPTSRTARFS SGLGVLDFMK RTTLVGCGAE
410 420 430
SLGAIGPSAV RLARAEGLEA HGLSVAARMN RGWE
Length:434
Mass (Da):45,648
Last modified:January 24, 2006 - v1
Checksum:iBB30BB3A879BB054
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000230 Genomic DNA Translation: ABC23568.1
RefSeqiWP_011390581.1, NC_007643.1
YP_427855.1, NC_007643.1

Genome annotation databases

EnsemblBacteriaiABC23568; ABC23568; Rru_A2771
GeneIDi3836211
KEGGirru:Rru_A2771
PATRICifig|269796.9.peg.2877

Similar proteinsi

Entry informationi

Entry nameiHISX_RHORT
AccessioniPrimary (citable) accession number: Q2RQM7
Entry historyiIntegrated into UniProtKB/Swiss-Prot: April 4, 2006
Last sequence update: January 24, 2006
Last modified: May 23, 2018
This is version 77 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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