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Protein

Histidinol dehydrogenase 1

Gene

hisD1

Organism
Bacillus clausii (strain KSM-K16)
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. 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. no protein annotated in this organism
  9. Histidinol dehydrogenase 1 (hisD1), Histidinol dehydrogenase 2 (hisD2)
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 sitei121NADUniRule annotation1
Binding sitei182NADUniRule annotation1
Binding sitei205NADUniRule annotation1
Binding sitei228SubstrateUniRule annotation1
Metal bindingi250ZincUniRule annotation1
Binding sitei250SubstrateUniRule annotation1
Metal bindingi253ZincUniRule annotation1
Binding sitei253SubstrateUniRule annotation1
Active sitei318Proton acceptorUniRule annotation1
Active sitei319Proton acceptorUniRule annotation1
Binding sitei319SubstrateUniRule annotation1
Metal bindingi352ZincUniRule annotation1
Binding sitei352SubstrateUniRule annotation1
Binding sitei406SubstrateUniRule annotation1
Metal bindingi411ZincUniRule annotation1
Binding sitei411SubstrateUniRule 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 dehydrogenase 1UniRule annotation (EC:1.1.1.23UniRule annotation)
Short name:
HDH 1UniRule annotation
Gene namesi
Name:hisD1UniRule annotation
Ordered Locus Names:ABC1168
OrganismiBacillus clausii (strain KSM-K16)
Taxonomic identifieri66692 [NCBI]
Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesBacillaceaeBacillus
Proteomesi
  • UP000001168 Componenti: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001357241 – 424Histidinol dehydrogenase 1Add BLAST424

Interactioni

Protein-protein interaction databases

STRINGi66692.ABC1168.

Structurei

3D structure databases

ProteinModelPortaliQ5WIU9.
SMRiQ5WIU9.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the histidinol dehydrogenase family.UniRule annotation

Phylogenomic databases

eggNOGiENOG4105CEK. Bacteria.
COG0141. LUCA.
HOGENOMiHOG000243914.
KOiK15509.
OMAiTKKAGRY.
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.

Q5WIU9-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAQYIKQGKS ESELKDSHGK VEQTVASLIA RIEKEGETAV RELSRQFDNW
60 70 80 90 100
DPEQFRLSAE EIEKIVRSVP DQVKADICFA QEQIRHFAEQ QRASIQDIEV
110 120 130 140 150
ETRPGVFLGH KNIPVNSVGC YIPGGRYPMV ASSHMSILTA KVAGVKRVIG
160 170 180 190 200
CTPPINGEIP AATVTAMHFA GADEIYILGG VQAMTAMAVG TETIEAVDML
210 220 230 240 250
VGPGNAFVAE AKRQLFGRVG IDLFAGPTEV LIIADDTADG EMVATDLLGQ
260 270 280 290 300
AEHGPTSPAA LITTSKKLAE ETVAEIERQL QTLPTADVAK VAWEEHGMII
310 320 330 340 350
LVDDLAEAVV EADKLAYEHV QVLTENPNYF LDHMTNYGAL FLGPETNVAY
360 370 380 390 400
GDKVIGTNHT LPTKKAAKYT GGLWVGKFLK NCTYQRCTPE ASAEIGRIAE
410 420
RLCELEGFIG HKAQASLRVK RYGK
Length:424
Mass (Da):46,122
Last modified:November 23, 2004 - v1
Checksum:i6131743AA063022E
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AP006627 Genomic DNA. Translation: BAD63706.1.
RefSeqiWP_011246020.1. NC_006582.1.

Genome annotation databases

EnsemblBacteriaiBAD63706; BAD63706; ABC1168.
KEGGibcl:ABC1168.
PATRICi18921728. VBIBacCla58185_1252.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AP006627 Genomic DNA. Translation: BAD63706.1.
RefSeqiWP_011246020.1. NC_006582.1.

3D structure databases

ProteinModelPortaliQ5WIU9.
SMRiQ5WIU9.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi66692.ABC1168.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiBAD63706; BAD63706; ABC1168.
KEGGibcl:ABC1168.
PATRICi18921728. VBIBacCla58185_1252.

Phylogenomic databases

eggNOGiENOG4105CEK. Bacteria.
COG0141. LUCA.
HOGENOMiHOG000243914.
KOiK15509.
OMAiTKKAGRY.
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 nameiHISX1_BACSK
AccessioniPrimary (citable) accession number: Q5WIU9
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 10, 2006
Last sequence update: November 23, 2004
Last modified: November 2, 2016
This is version 81 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.