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Protein

Histidinol dehydrogenase

Gene

hisD

Organism
Corynebacterium diphtheriae (strain ATCC 700971 / NCTC 13129 / Biotype gravis)
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 sitei135NADUniRule annotation1
Binding sitei199NADUniRule annotation1
Binding sitei229NADUniRule annotation1
Binding sitei252SubstrateUniRule annotation1
Metal bindingi274ZincUniRule annotation1
Binding sitei274SubstrateUniRule annotation1
Metal bindingi277ZincUniRule annotation1
Binding sitei277SubstrateUniRule annotation1
Active sitei343Proton acceptorUniRule annotation1
Active sitei344Proton acceptorUniRule annotation1
Binding sitei344SubstrateUniRule annotation1
Metal bindingi377ZincUniRule annotation1
Binding sitei377SubstrateUniRule annotation1
Binding sitei431SubstrateUniRule annotation1
Metal bindingi436ZincUniRule annotation1
Binding sitei436SubstrateUniRule 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:DIP1566
OrganismiCorynebacterium diphtheriae (strain ATCC 700971 / NCTC 13129 / Biotype gravis)
Taxonomic identifieri257309 [NCBI]
Taxonomic lineageiBacteriaActinobacteriaCorynebacterialesCorynebacteriaceaeCorynebacterium
Proteomesi
  • UP000002198 Componenti: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001357591 – 449Histidinol dehydrogenaseAdd BLAST449

Structurei

3D structure databases

ProteinModelPortaliP60858.
SMRiP60858.
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.

P60858-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MRKRKIMLNV IDLRGHVPTT SELRRTLPRG GTDINSVLPI VEPVVTDVKN
60 70 80 90 100
RGAAAALDYG EKFDHVRPTS IRVPQDVIDQ ALDSLDPNVI EALKESIARV
110 120 130 140 150
RAVHSEQLPA QHTTSFGEGA TITEKFIPVS RVGLYAPGGN AVYPSSVIMN
160 170 180 190 200
VVPAQEAGVE SLVVASPPQK DHGGWPHPTI LAAAKLLGVT EVWAMGGAQA
210 220 230 240 250
VALLAYGDDT QQNSAEVLEP VDMITGPGNI FVTAAKRLVR GVVGIDSEAG
260 270 280 290 300
PTEIAIVADA QANPVWIAYD LISQAEHDVL AASVLITDSE ELAQRVNEEV
310 320 330 340 350
AARYSVTRNA DRVSEALKGQ QSGIVLVDDL PTAVIVADAY AAEHLEIHTA
360 370 380 390 400
ESHKVAEQIR NAGAIFVGGY SPVPLGDYSA GSNHVLPTSG SARYSSGLST
410 420 430 440
HTFLKPVNVI YYDEVALKEI SDTVITLADA EDLPAHGEAI RTRFENLGN
Length:449
Mass (Da):47,762
Last modified:April 13, 2004 - v1
Checksum:i002BB36B98F433FB
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BX248358 Genomic DNA. Translation: CAE50091.1.

Genome annotation databases

EnsemblBacteriaiCAE50091; CAE50091; DIP1566.
KEGGicdi:DIP1566.
PATRICi21484340. VBICorDip47633_1546.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BX248358 Genomic DNA. Translation: CAE50091.1.

3D structure databases

ProteinModelPortaliP60858.
SMRiP60858.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiCAE50091; CAE50091; DIP1566.
KEGGicdi:DIP1566.
PATRICi21484340. VBICorDip47633_1546.

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_CORDI
AccessioniPrimary (citable) accession number: P60858
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 13, 2004
Last sequence update: April 13, 2004
Last modified: November 2, 2016
This is version 91 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.