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Protein

Histidinol dehydrogenase

Gene

hisD

Organism
Dehalococcoides mccartyi (strain CBDB1)
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)
  2. no protein annotated in this organism
  3. no protein annotated in this organism
  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 sitei136NADUniRule annotation1
Binding sitei198NADUniRule annotation1
Binding sitei221NADUniRule annotation1
Binding sitei244SubstrateUniRule annotation1
Metal bindingi266ZincUniRule annotation1
Binding sitei266SubstrateUniRule annotation1
Metal bindingi269ZincUniRule annotation1
Binding sitei269SubstrateUniRule annotation1
Active sitei334Proton acceptorUniRule annotation1
Active sitei335Proton acceptorUniRule annotation1
Binding sitei335SubstrateUniRule annotation1
Metal bindingi368ZincUniRule annotation1
Binding sitei368SubstrateUniRule annotation1
Binding sitei422SubstrateUniRule annotation1
Metal bindingi427ZincUniRule annotation1
Binding sitei427SubstrateUniRule 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:cbdbA826
OrganismiDehalococcoides mccartyi (strain CBDB1)
Taxonomic identifieri255470 [NCBI]
Taxonomic lineageiBacteriaChloroflexiDehalococcoidiaDehalococcoidalesDehalococcoidaceaeDehalococcoides

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001357651 – 436Histidinol dehydrogenaseAdd BLAST436

Interactioni

Protein-protein interaction databases

STRINGi255470.cbdb_A826.

Structurei

3D structure databases

ProteinModelPortaliQ3ZXL7.
SMRiQ3ZXL7.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the histidinol dehydrogenase family.UniRule annotation

Phylogenomic databases

eggNOGiENOG4105CEK. Bacteria.
COG0141. LUCA.
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.

Q3ZXL7-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MKIIRGFAQA EKRLSRRDKA GFFLDETERT ELARRLGVDP EKAVNGIIAD
60 70 80 90 100
VRKQGDEAVL GYTLKFDRAN LSKLEVGQPE IQQAASEIPA ELFEALQLAA
110 120 130 140 150
SQIRAYHRFQ KEAVWKTAEI MQGKQLIRPL ERVGLYVPGG KAFYPSTVLM
160 170 180 190 200
TAIPAREAGV KEIILVTPPG ANGKIPAPTL AAAQIAGVDR IFACGGAQAV
210 220 230 240 250
AALAFGTKSI PKVDKICGPG NIFVTLAKKA VFGVVDIDGL QGPSEVLIVA
260 270 280 290 300
DQYANAEYCA SDILAQAEHD ALASSILITT SEDLANRVND IVESKADTCS
310 320 330 340 350
RRDIIKQSLR DNGLIAVVDN INEAIKLANM YAAEHLCLLV KDSEKYLTQI
360 370 380 390 400
NHAGCIFYGE KASVVMGDYV AGPSHALPTS GTARFSSPLN ILDFVKYIDI
410 420 430
VKVDKQDIAK LGQAAATIAK AEGLECHAEA VLKRLE
Length:436
Mass (Da):46,942
Last modified:September 27, 2005 - v1
Checksum:i4FE7208670BA48C6
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AJ965256 Genomic DNA. Translation: CAI82971.1.
RefSeqiWP_011309322.1. NC_007356.1.

Genome annotation databases

EnsemblBacteriaiCAI82971; CAI82971; cbdbA826.
KEGGideh:cbdbA826.
PATRICi21611735. VBIDehSp125902_0698.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AJ965256 Genomic DNA. Translation: CAI82971.1.
RefSeqiWP_011309322.1. NC_007356.1.

3D structure databases

ProteinModelPortaliQ3ZXL7.
SMRiQ3ZXL7.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi255470.cbdb_A826.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiCAI82971; CAI82971; cbdbA826.
KEGGideh:cbdbA826.
PATRICi21611735. VBIDehSp125902_0698.

Phylogenomic databases

eggNOGiENOG4105CEK. Bacteria.
COG0141. LUCA.
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_DEHMC
AccessioniPrimary (citable) accession number: Q3ZXL7
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 10, 2006
Last sequence update: September 27, 2005
Last modified: November 30, 2016
This is version 80 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.