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Protein

Histidinol dehydrogenase

Gene

hisD

Organism
Lactobacillus plantarum (strain ATCC BAA-793 / NCIMB 8826 / WCFS1)
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 (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)DescriptionActionsGraphical viewLength
Binding sitei125NADUniRule annotation1
Binding sitei186NADUniRule annotation1
Binding sitei209NADUniRule annotation1
Binding sitei232SubstrateUniRule annotation1
Metal bindingi254ZincUniRule annotation1
Binding sitei254SubstrateUniRule annotation1
Metal bindingi257ZincUniRule annotation1
Binding sitei257SubstrateUniRule annotation1
Active sitei322Proton acceptorUniRule annotation1
Active sitei323Proton acceptorUniRule annotation1
Binding sitei323SubstrateUniRule annotation1
Metal bindingi356ZincUniRule annotation1
Binding sitei356SubstrateUniRule annotation1
Binding sitei410SubstrateUniRule annotation1
Metal bindingi415ZincUniRule annotation1
Binding sitei415SubstrateUniRule 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

BioCyciLPLA220668:G137Z-2196-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:lp_2559
OrganismiLactobacillus plantarum (strain ATCC BAA-793 / NCIMB 8826 / WCFS1)
Taxonomic identifieri220668 [NCBI]
Taxonomic lineageiBacteriaFirmicutesBacilliLactobacillalesLactobacillaceaeLactobacillus
Proteomesi
  • UP000000432 Componenti: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001357821 – 428Histidinol dehydrogenaseAdd BLAST428

Interactioni

Protein-protein interaction databases

STRINGi220668.lp_2559.

Structurei

3D structure databases

ProteinModelPortaliP59399.
SMRiP59399.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the histidinol dehydrogenase family.UniRule annotation

Phylogenomic databases

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

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.

P59399-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MKIINEDLAS LKRLVQTKTQ QLTDLKVESA VREIIANVIK NGDAAVKDYE
60 70 80 90 100
TQFDKVTLTD FKLSQTVIDD AYNNLDPQVK DALLLAKRNI TSFHEKEKAT
110 120 130 140 150
GFIDAEQPGV LRGQKLMPLN RVGLYVPGGT AAYPSTLLMS ALPAKIAGVN
160 170 180 190 200
EVIMVTPPQV DGINPAVLAA AKIAGVDAIY QVGGAQAIAA LAYGTESIPA
210 220 230 240 250
VDKIIGPGNI FVATAKKQVF GQVAIDMVAG PSEIGILADD SADPRQLAAD
260 270 280 290 300
LLSQAEHDRR ARPILITDSA DLAQAVSDNV TSQLKVLPRE AIATDAVNEK
310 320 330 340 350
GFIAVVAKIE EMFDLMNTVA PEHLEVQLKN PTQYLNLIKN AGSVFLGRYA
360 370 380 390 400
SEPLGDYVAG PNHILPTSGT ARFSSPLGVY DFVKRTSFIQ YTKDALAKEA
410 420
PAITTLARVE GLEGHARAIE SRFDTYYD
Length:428
Mass (Da):45,986
Last modified:March 25, 2003 - v1
Checksum:i9DE9DDE6D8487D2C
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AL935263 Genomic DNA. Translation: CCC79714.1.
RefSeqiWP_011101827.1. NC_004567.2.
YP_004890228.1. NC_004567.2.

Genome annotation databases

EnsemblBacteriaiCCC79714; CCC79714; lp_2559.
GeneIDi1062752.
KEGGilpl:lp_2559.
PATRICi22251085. VBILacPla27411_2150.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AL935263 Genomic DNA. Translation: CCC79714.1.
RefSeqiWP_011101827.1. NC_004567.2.
YP_004890228.1. NC_004567.2.

3D structure databases

ProteinModelPortaliP59399.
SMRiP59399.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi220668.lp_2559.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiCCC79714; CCC79714; lp_2559.
GeneIDi1062752.
KEGGilpl:lp_2559.
PATRICi22251085. VBILacPla27411_2150.

Phylogenomic databases

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

Enzyme and pathway databases

UniPathwayiUPA00031; UER00014.
BioCyciLPLA220668:G137Z-2196-MONOMER.

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_LACPL
AccessioniPrimary (citable) accession number: P59399
Secondary accession number(s): F9UR75
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 25, 2003
Last sequence update: March 25, 2003
Last modified: November 2, 2016
This is version 94 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.