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Protein

Histidinol dehydrogenase

Gene

hisD

Organism
Corynebacterium efficiens (strain DSM 44549 / YS-314 / AJ 12310 / JCM 11189 / NBRC 100395)
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)
  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 sitei129NADUniRule annotation1
Binding sitei193NADUniRule annotation1
Binding sitei218NADUniRule annotation1
Binding sitei241SubstrateUniRule annotation1
Metal bindingi263ZincUniRule annotation1
Binding sitei263SubstrateUniRule annotation1
Metal bindingi266ZincUniRule annotation1
Binding sitei266SubstrateUniRule annotation1
Active sitei332Proton acceptorUniRule annotation1
Active sitei333Proton acceptorUniRule annotation1
Binding sitei333SubstrateUniRule annotation1
Metal bindingi366ZincUniRule annotation1
Binding sitei366SubstrateUniRule annotation1
Binding sitei420SubstrateUniRule annotation1
Metal bindingi425ZincUniRule annotation1
Binding sitei425SubstrateUniRule 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:CE2003
OrganismiCorynebacterium efficiens (strain DSM 44549 / YS-314 / AJ 12310 / JCM 11189 / NBRC 100395)
Taxonomic identifieri196164 [NCBI]
Taxonomic lineageiBacteriaActinobacteriaCorynebacterialesCorynebacteriaceaeCorynebacterium
Proteomesi
  • UP000001409 Componenti: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001357601 – 451Histidinol dehydrogenaseAdd BLAST451

Proteomic databases

PRIDEiQ8FNZ0.

Interactioni

Protein-protein interaction databases

STRINGi196164.HMPREF0290_2035.

Structurei

3D structure databases

ProteinModelPortaliQ8FNZ0.
SMRiQ8FNZ0.
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.

Q8FNZ0-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MLNVTDLRGH TPSKSDIRRA LPRGGTDVVS VLPIVEPVVD DVQNRGAEAA
60 70 80 90 100
LDYGEKFDHI RPASVRVPAE VLKAAEDTLD PRVREAIEES IRRVRKVHAD
110 120 130 140 150
QKPREHTTEL APGGTVTERF LPIDRVGLYV PGGNAVYPSS VIMNAVPAQE
160 170 180 190 200
AGVGTLVVAS PPQADHGGWP HPTILAACSI LGVDEVWAVG GAQAVALLAF
210 220 230 240 250
GDDSADLEPV DIITGPGNIF VTAAKRLVRG VVGTDSEAGP TEIAILADDT
260 270 280 290 300
ANPVNVAYDL ISQAEHDVMA ASVLITDSEQ LARDVNREIE ARYAITRNAD
310 320 330 340 350
RVAEALRGKQ SGIVLVDDIE VGIAVADQYA AEHLEVHTAN AREVSERISN
360 370 380 390 400
AGAIFVGDFS PVPLGDYSAG SNHVLPTSGT ARFSAGLSTH TFLRPVNLIE
410 420 430 440 450
YDEAALKDIS EVVINFADAE DLPAHGEAIR ARFETLPTTT ADTTDTPDAT

A
Length:451
Mass (Da):47,770
Last modified:March 1, 2003 - v1
Checksum:i5A2D5AA7B990ECCF
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BA000035 Genomic DNA. Translation: BAC18813.1.
RefSeqiWP_006768001.1. NZ_GG700683.1.

Genome annotation databases

EnsemblBacteriaiBAC18813; BAC18813; BAC18813.
KEGGicef:CE2003.
PATRICi21490139. VBICorEff9312_1984.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BA000035 Genomic DNA. Translation: BAC18813.1.
RefSeqiWP_006768001.1. NZ_GG700683.1.

3D structure databases

ProteinModelPortaliQ8FNZ0.
SMRiQ8FNZ0.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi196164.HMPREF0290_2035.

Proteomic databases

PRIDEiQ8FNZ0.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiBAC18813; BAC18813; BAC18813.
KEGGicef:CE2003.
PATRICi21490139. VBICorEff9312_1984.

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_COREF
AccessioniPrimary (citable) accession number: Q8FNZ0
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 25, 2003
Last sequence update: March 1, 2003
Last modified: November 2, 2016
This is version 96 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.