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Protein

Histidinol dehydrogenase

Gene

hisD

Organism
Nitrobacter winogradskyi (strain Nb-255 / ATCC 25391)
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:iL-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)
  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 1 (hisH1), Imidazole glycerol phosphate synthase subunit HisH 2 (hisH2), 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)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei130 – 1301NADUniRule annotation
Binding sitei191 – 1911NADUniRule annotation
Binding sitei214 – 2141NADUniRule annotation
Binding sitei237 – 2371SubstrateUniRule annotation
Metal bindingi259 – 2591ZincUniRule annotation
Binding sitei259 – 2591SubstrateUniRule annotation
Metal bindingi262 – 2621ZincUniRule annotation
Binding sitei262 – 2621SubstrateUniRule annotation
Active sitei327 – 3271Proton acceptorUniRule annotation
Active sitei328 – 3281Proton acceptorUniRule annotation
Binding sitei328 – 3281SubstrateUniRule annotation
Metal bindingi361 – 3611ZincUniRule annotation
Binding sitei361 – 3611SubstrateUniRule annotation
Binding sitei415 – 4151SubstrateUniRule annotation
Metal bindingi420 – 4201ZincUniRule annotation
Binding sitei420 – 4201SubstrateUniRule 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

BioCyciNWIN323098:GJEG-252-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:Nwi_0247
OrganismiNitrobacter winogradskyi (strain Nb-255 / ATCC 25391)
Taxonomic identifieri323098 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaAlphaproteobacteriaRhizobialesBradyrhizobiaceaeNitrobacter
ProteomesiUP000002531 Componenti: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 429429Histidinol dehydrogenasePRO_0000135803Add
BLAST

Interactioni

Protein-protein interaction databases

STRINGi323098.Nwi_0247.

Structurei

3D structure databases

ProteinModelPortaliQ3SW26.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the histidinol dehydrogenase family.UniRule annotation

Phylogenomic databases

eggNOGiCOG0141.
HOGENOMiHOG000243914.
KOiK00013.
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.

Q3SW26-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MPIRIDSRNA DFVPRFKAFL ATKREVSADI EAATRAIVDD VAARGDAALI
60 70 80 90 100
EATCKFDRLS VDAAGLRFTA AEIDAAVAAC DAATLDALKL ARDRIETFHR
110 120 130 140 150
RQLPKDDRFI DALGVELGSR WTAIEAVGLY VPGGSAAYPS SVLMNAVPAM
160 170 180 190 200
VAGVARVVMV VPSPAGRINP LVLAAARLGG VSEIYRVGGA QAVAALAYGT
210 220 230 240 250
ATIAPVAKIV GPGNAYVAAA KRQVFGKVGI DMIAGPSEVL VIADQTGNAG
260 270 280 290 300
WIAADLLAQA EHDANAQSIL ITDSEALAAD VERAVETQLA TLPRAGIARA
310 320 330 340 350
SWNDFGAVIL VTDLDEAVVL ADSIAAEHLE IMTADPEGLA ARIRNAGAIF
360 370 380 390 400
LGPHTPEAIG DYVGGSNHVL PTARSARFSS GLGVLDFMKR TSILKCGPDQ
410 420
LRALGPAAMT LGKAEGLDAH ARSVGVRLN
Length:429
Mass (Da):44,496
Last modified:January 10, 2006 - v2
Checksum:iAED2E80E595F7F0C
GO

Sequence cautioni

The sequence ABA03515.1 differs from that shown. Reason: Erroneous initiation. Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000115 Genomic DNA. Translation: ABA03515.1. Different initiation.
RefSeqiWP_041344641.1. NC_007406.1.

Genome annotation databases

EnsemblBacteriaiABA03515; ABA03515; Nwi_0247.
KEGGinwi:Nwi_0247.
PATRICi22696844. VBINitWin102302_0273.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000115 Genomic DNA. Translation: ABA03515.1. Different initiation.
RefSeqiWP_041344641.1. NC_007406.1.

3D structure databases

ProteinModelPortaliQ3SW26.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi323098.Nwi_0247.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiABA03515; ABA03515; Nwi_0247.
KEGGinwi:Nwi_0247.
PATRICi22696844. VBINitWin102302_0273.

Phylogenomic databases

eggNOGiCOG0141.
HOGENOMiHOG000243914.
KOiK00013.
OrthoDBiEOG6CVVCR.

Enzyme and pathway databases

UniPathwayiUPA00031; UER00014.
BioCyciNWIN323098:GJEG-252-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. "Genome sequence of the chemolithoautotrophic nitrite-oxidizing bacterium Nitrobacter winogradskyi Nb-255."
    Starkenburg S.R., Chain P.S.G., Sayavedra-Soto L.A., Hauser L., Land M.L., Larimer F.W., Malfatti S.A., Klotz M.G., Bottomley P.J., Arp D.J., Hickey W.J.
    Appl. Environ. Microbiol. 72:2050-2063(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: Nb-255 / ATCC 25391.

Entry informationi

Entry nameiHISX_NITWN
AccessioniPrimary (citable) accession number: Q3SW26
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 10, 2006
Last sequence update: January 10, 2006
Last modified: July 22, 2015
This is version 70 of the entry and version 2 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.