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Protein

Histidinol dehydrogenase

Gene

hisD

Organism
Cupriavidus pinatubonensis (strain JMP 134 / LMG 1197) (Ralstonia eutropha (strain JMP 134))
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 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 HisH (hisH), Imidazole glycerol phosphate synthase subunit HisF (hisF)
  6. Imidazoleglycerol-phosphate dehydratase (hisB)
  7. Histidinol-phosphate aminotransferase 2 (hisC2), Histidinol-phosphate aminotransferase 1 (hisC1)
  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 sitei144NADUniRule annotation1
Binding sitei205NADUniRule annotation1
Binding sitei228NADUniRule annotation1
Binding sitei251SubstrateUniRule annotation1
Metal bindingi273ZincUniRule annotation1
Binding sitei273SubstrateUniRule annotation1
Metal bindingi276ZincUniRule annotation1
Binding sitei276SubstrateUniRule annotation1
Active sitei341Proton acceptorUniRule annotation1
Active sitei342Proton acceptorUniRule annotation1
Binding sitei342SubstrateUniRule annotation1
Metal bindingi375ZincUniRule annotation1
Binding sitei375SubstrateUniRule annotation1
Binding sitei429SubstrateUniRule annotation1
Metal bindingi434ZincUniRule annotation1
Binding sitei434SubstrateUniRule 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:Reut_A3111
OrganismiCupriavidus pinatubonensis (strain JMP 134 / LMG 1197) (Ralstonia eutropha (strain JMP 134))
Taxonomic identifieri264198 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaBetaproteobacteriaBurkholderialesBurkholderiaceaeCupriavidus
Proteomesi
  • UP000002697 Componenti: Chromosome 1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001358261 – 445Histidinol dehydrogenaseAdd BLAST445

Interactioni

Protein-protein interaction databases

STRINGi264198.Reut_A3111.

Structurei

3D structure databases

ProteinModelPortaliQ46WL2.
SMRiQ46WL2.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the histidinol dehydrogenase family.UniRule annotation

Phylogenomic databases

eggNOGiENOG4105CEK. Bacteria.
COG0141. LUCA.
HOGENOMiHOG000243914.
KOiK00013.
OMAiGGTARFY.
OrthoDBiPOG091H03YX.

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.

Q46WL2-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MNATEMENVS IRRLDSSDPR FAQALREVLA FEAGEDEAID RAVAQILADV
60 70 80 90 100
KDRGDAAVLE YTQRFDRVEA ASMGALEISQ SELEAALEDL EPKRRAALEA
110 120 130 140 150
AAARVRAYHE KQKIECGSHS WEYTEADGTM LGQKVTPLDR VGIYVPGGKA
160 170 180 190 200
AYPSSVLMNA IPARVAGVKE IIMVVPTPGG VRNELVLAAA QIAGVDRVFT
210 220 230 240 250
IGGAQAVGAL AYGTATLPQV DKIVGPGNAY VAAAKRRVFG TVGIDMIAGP
260 270 280 290 300
SEILVICDGT TDPDWVAMDL FSQAEHDELA QSILLCPDAD YIAQVEASIQ
310 320 330 340 350
RQLDSMPRRE VIAASISGRG ALIKVRDMEE ACEIANAIAP EHLEISAENP
360 370 380 390 400
RQWSEKIRHA GAIFLGRYTS ESLGDYCAGP NHVLPTSRTA RFSSPLGVYD
410 420 430 440
FQKRSSLIEV SEGGAQMLGQ IAAELAYGEG LQAHARSAEY RFKRS
Length:445
Mass (Da):47,888
Last modified:September 13, 2005 - v1
Checksum:i4E3DF54A378ADE4B
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000090 Genomic DNA. Translation: AAZ62471.1.
RefSeqiWP_011299254.1. NC_007347.1.

Genome annotation databases

EnsemblBacteriaiAAZ62471; AAZ62471; Reut_A3111.
KEGGireu:Reut_A3111.
PATRICi20231936. VBIRalEut24049_3794.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000090 Genomic DNA. Translation: AAZ62471.1.
RefSeqiWP_011299254.1. NC_007347.1.

3D structure databases

ProteinModelPortaliQ46WL2.
SMRiQ46WL2.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi264198.Reut_A3111.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAZ62471; AAZ62471; Reut_A3111.
KEGGireu:Reut_A3111.
PATRICi20231936. VBIRalEut24049_3794.

Phylogenomic databases

eggNOGiENOG4105CEK. Bacteria.
COG0141. LUCA.
HOGENOMiHOG000243914.
KOiK00013.
OMAiGGTARFY.
OrthoDBiPOG091H03YX.

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_CUPPJ
AccessioniPrimary (citable) accession number: Q46WL2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 10, 2006
Last sequence update: September 13, 2005
Last modified: November 2, 2016
This is version 78 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.