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Protein

Histidinol dehydrogenase

Gene

hisD

Organism
Gluconobacter oxydans (strain 621H) (Gluconobacter suboxydans)
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 (GOX0482)
  5. Imidazole glycerol phosphate synthase subunit HisF (hisF), Imidazole glycerol phosphate synthase subunit HisH (hisH)
  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 sitei129NADUniRule annotation1
Binding sitei190NADUniRule annotation1
Binding sitei213NADUniRule annotation1
Binding sitei236SubstrateUniRule annotation1
Metal bindingi258ZincUniRule annotation1
Binding sitei258SubstrateUniRule annotation1
Metal bindingi261ZincUniRule annotation1
Binding sitei261SubstrateUniRule annotation1
Active sitei326Proton acceptorUniRule annotation1
Active sitei327Proton acceptorUniRule annotation1
Binding sitei327SubstrateUniRule annotation1
Metal bindingi360ZincUniRule annotation1
Binding sitei360SubstrateUniRule annotation1
Binding sitei414SubstrateUniRule annotation1
Metal bindingi419ZincUniRule annotation1
Binding sitei419SubstrateUniRule 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:GOX0991
OrganismiGluconobacter oxydans (strain 621H) (Gluconobacter suboxydans)
Taxonomic identifieri290633 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaAlphaproteobacteriaRhodospirillalesAcetobacteraceaeGluconobacter
Proteomesi
  • UP000006375 Componenti: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001357761 – 430Histidinol dehydrogenaseAdd BLAST430

Interactioni

Protein-protein interaction databases

STRINGi290633.GOX0991.

Structurei

3D structure databases

ProteinModelPortaliQ5FS83.
SMRiQ5FS83.
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.

Q5FS83-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MKRLDTSAAG FSEDFATLLA ARGSDERSVA EPVRAILADV RSRGDEALCD
60 70 80 90 100
YTARFDRLTL PAEKLRISAE EIASEAARVP ADLMDALRTA ARRIETFHAA
110 120 130 140 150
QMPKDLDFTD EDGIRLGMRW TPLDAVGLYV PGGKAAYPSS VLMNALPARV
160 170 180 190 200
AGVKRLAMCV PSPDGVLNPL VLAAAQLCGV EEIYRIGGAQ AVGAMAFGTD
210 220 230 240 250
LIAPVDRIVG PGNAYVAEAK RQVFGHVGID SIAGPSEVVV VADGQNDPRL
260 270 280 290 300
VALDLLAQAE HDEQAQAILI TTDAAFAERA AEAVRKELET LPRTAIASKS
310 320 330 340 350
WEDHGAIIVV RSLEEAAEIV NALAPEHLEV MLDAPRDFSA MIRHAGAIFM
360 370 380 390 400
GRYCPEAVGD YVGGPNHVLP TSRTARFASG LSVFDFIKRT TTIEADEAGL
410 420 430
RRIGPAGVAL AKAEGLDAHA LSLSVRLEKN
Length:430
Mass (Da):45,736
Last modified:March 1, 2005 - v1
Checksum:iC00338F3F3F3274F
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000009 Genomic DNA. Translation: AAW60763.1.
RefSeqiWP_011252557.1. NC_006677.1.

Genome annotation databases

EnsemblBacteriaiAAW60763; AAW60763; GOX0991.
KEGGigox:GOX0991.
PATRICi32609758. VBIGluOxy81109_1251.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000009 Genomic DNA. Translation: AAW60763.1.
RefSeqiWP_011252557.1. NC_006677.1.

3D structure databases

ProteinModelPortaliQ5FS83.
SMRiQ5FS83.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi290633.GOX0991.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAW60763; AAW60763; GOX0991.
KEGGigox:GOX0991.
PATRICi32609758. VBIGluOxy81109_1251.

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_GLUOX
AccessioniPrimary (citable) accession number: Q5FS83
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 10, 2006
Last sequence update: March 1, 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, Reference 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.