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Protein

Histidinol dehydrogenase

Gene

hisD

Organism
Listeria monocytogenes serotype 4b (strain F2365)
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 (hisG), ATP phosphoribosyltransferase regulatory subunit (hisZ)
  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 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 (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 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

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:LMOf2365_0596
OrganismiListeria monocytogenes serotype 4b (strain F2365)
Taxonomic identifieri265669 [NCBI]
Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesListeriaceaeListeria

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001357921 – 427Histidinol dehydrogenaseAdd BLAST427

Structurei

3D structure databases

ProteinModelPortaliQ722Y3.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the histidinol dehydrogenase family.UniRule annotation

Phylogenomic databases

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.

Q722Y3-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MKILTGTVNE LLNELKIETD TNTSIQVETE VKTIIEKVKT AGDQALFDFT
60 70 80 90 100
SKFDGVGLTE LRVPAADIQA ASAKIEPAFL DALQQAKVNI ESFHSKQKQH
110 120 130 140 150
AFLDSEKDGV IRGQLIRPLE TVGVYVPGGT AAYPSSVLMN VLPAKIAGVK
160 170 180 190 200
RIVMITPPGE NGINPYVLAS AQLAGVDEIY QVGGAHGIAA LAHGTESIPK
210 220 230 240 250
VDKIVGPGNI YVATAKREVF GLVDIDMIAG PSEIVVLADE NANPAFIAAD
260 270 280 290 300
LLSQAEHDIL ARAILITTSK KIAEETQNEI DKQLENLPRK AIAQKSIETR
310 320 330 340 350
GKIIIAATTQ EMFDIMNEIA PEHLEVQLEN PMNYLYQIKN AGSIFLGSYA
360 370 380 390 400
SEPLGDYFAG PNHVLPTSGT AKFFSPLGVE DFTKRSAFIS YTKEALAKEK
410 420
DAIVLLAKKE GLDAHAKAIQ IRFEEEN
Length:427
Mass (Da):46,147
Last modified:July 5, 2004 - v1
Checksum:i015FC5F410CC90A3
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE017262 Genomic DNA. Translation: AAT03378.1.
RefSeqiWP_003725469.1. NC_002973.6.

Genome annotation databases

EnsemblBacteriaiAAT03378; AAT03378; LMOf2365_0596.
KEGGilmf:LMOf2365_0596.
PATRICi20322395. VBILisMon105049_0595.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE017262 Genomic DNA. Translation: AAT03378.1.
RefSeqiWP_003725469.1. NC_002973.6.

3D structure databases

ProteinModelPortaliQ722Y3.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAT03378; AAT03378; LMOf2365_0596.
KEGGilmf:LMOf2365_0596.
PATRICi20322395. VBILisMon105049_0595.

Phylogenomic databases

HOGENOMiHOG000243914.
KOiK00013.
OMAiGGTARFY.

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_LISMF
AccessioniPrimary (citable) accession number: Q722Y3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 7, 2004
Last sequence update: July 5, 2004
Last modified: September 7, 2016
This is version 83 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

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.