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Protein

Histidinol dehydrogenase

Gene

hisD

Organism
Deinococcus radiodurans (strain ATCC 13939 / DSM 20539 / JCM 16871 / LMG 4051 / NBRC 15346 / NCIMB 9279 / R1 / VKM B-1422)
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

Pathway: 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. Probable histidinol-phosphatase (hisK)
  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)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei135 – 1351NADUniRule annotation
Binding sitei197 – 1971NADUniRule annotation
Binding sitei220 – 2201NADUniRule annotation
Binding sitei243 – 2431SubstrateUniRule annotation
Metal bindingi265 – 2651ZincUniRule annotation
Binding sitei265 – 2651SubstrateUniRule annotation
Metal bindingi268 – 2681ZincUniRule annotation
Binding sitei268 – 2681SubstrateUniRule annotation
Active sitei334 – 3341Proton acceptorUniRule annotation
Active sitei335 – 3351Proton acceptorUniRule annotation
Binding sitei335 – 3351SubstrateUniRule annotation
Metal bindingi368 – 3681ZincUniRule annotation
Binding sitei368 – 3681SubstrateUniRule annotation
Binding sitei422 – 4221SubstrateUniRule annotation
Metal bindingi427 – 4271ZincUniRule annotation
Binding sitei427 – 4271SubstrateUniRule annotation

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

BioCyciDRAD243230:GH46-2183-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:DR_2140
OrganismiDeinococcus radiodurans (strain ATCC 13939 / DSM 20539 / JCM 16871 / LMG 4051 / NBRC 15346 / NCIMB 9279 / R1 / VKM B-1422)
Taxonomic identifieri243230 [NCBI]
Taxonomic lineageiBacteriaDeinococcus-ThermusDeinococciDeinococcalesDeinococcaceaeDeinococcus
ProteomesiUP000002524 Componenti: Chromosome I

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 436436Histidinol dehydrogenasePRO_0000135766Add
BLAST

Interactioni

Protein-protein interaction databases

STRINGi243230.DR_2140.

Structurei

3D structure databases

ProteinModelPortaliQ9RSI4.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the histidinol dehydrogenase family.UniRule annotation

Phylogenomic databases

eggNOGiCOG0141.
HOGENOMiHOG000243914.
InParanoidiQ9RSI4.
KOiK00013.
OMAiLSVQSFL.
OrthoDBiEOG6CVVCR.

Family and domain databases

HAMAPiMF_01024. HisD.
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.

Q9RSI4-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MQVLQGAEAR AALTRTFSQI PVPDAVLSRI EQTFGERLTP EQVVERILLD
60 70 80 90 100
VRARGDDALR DWTERLDGPR PAELEVPAAE LEAAQVAPEL HAAIRLAAER
110 120 130 140 150
VRAFYRQQPA HGFLEHGPDG ALGQLVRPLG RVGVYVPGGL APLISTLMHT
160 170 180 190 200
AVPAQVAGVP DIVVTTPPGK DGQVHPAILV AARELGLSRV FKVGGAQAIA
210 220 230 240 250
ALAYGTASVP AVDKIAGPGN LFVVIAKRLV YGQTGIESLP GPTETLVVAD
260 270 280 290 300
DSASPRYVAA DLLAQAEHNG AEPVLVSVSR ELLLAVQAEL NEQLENLPEP
310 320 330 340 350
NRSWARDSVG ARMKVVLADS LDEALDLANL YAPEHLCLLT RDPWSLLGQV
360 370 380 390 400
RRAGGVFVGE ASMEALGDYV AGPSHVMPTG GTARFMSPVN VRDFQNIISV
410 420 430
VGVNEETLRR IGPAAATLAR AEGLEAHARA VESRLK
Length:436
Mass (Da):46,273
Last modified:May 1, 2000 - v1
Checksum:iFB3A68DF7457E6B2
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE000513 Genomic DNA. Translation: AAF11684.1.
PIRiA75311.
RefSeqiNP_295863.1. NC_001263.1.
WP_010888771.1. NC_001263.1.

Genome annotation databases

EnsemblBacteriaiAAF11684; AAF11684; DR_2140.
GeneIDi1800305.
KEGGidra:DR_2140.
PATRICi21631956. VBIDeiRad64572_2363.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE000513 Genomic DNA. Translation: AAF11684.1.
PIRiA75311.
RefSeqiNP_295863.1. NC_001263.1.
WP_010888771.1. NC_001263.1.

3D structure databases

ProteinModelPortaliQ9RSI4.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi243230.DR_2140.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAF11684; AAF11684; DR_2140.
GeneIDi1800305.
KEGGidra:DR_2140.
PATRICi21631956. VBIDeiRad64572_2363.

Phylogenomic databases

eggNOGiCOG0141.
HOGENOMiHOG000243914.
InParanoidiQ9RSI4.
KOiK00013.
OMAiLSVQSFL.
OrthoDBiEOG6CVVCR.

Enzyme and pathway databases

UniPathwayiUPA00031; UER00014.
BioCyciDRAD243230:GH46-2183-MONOMER.

Family and domain databases

HAMAPiMF_01024. HisD.
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...

Publicationsi

  1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 13939 / DSM 20539 / JCM 16871 / LMG 4051 / NBRC 15346 / NCIMB 9279 / R1 / VKM B-1422.

Entry informationi

Entry nameiHISX_DEIRA
AccessioniPrimary (citable) accession number: Q9RSI4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 25, 2003
Last sequence update: May 1, 2000
Last modified: May 27, 2015
This is version 99 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, Reference proteome

Documents

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

External Data

Dasty 3

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 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.