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Protein

Histidinol dehydrogenase

Gene

hisD

Organism
Bacillus cereus (strain ZK / E33L)
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 HisH (hisH), Imidazole glycerol phosphate synthase subunit HisF (hisF)
  6. Imidazoleglycerol-phosphate dehydratase (hisB)
  7. Histidinol-phosphate aminotransferase 2 (hisC2), Histidinol-phosphate aminotransferase 1 (hisC1)
  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 sitei127NADUniRule annotation1
Binding sitei188NADUniRule annotation1
Binding sitei211NADUniRule annotation1
Binding sitei234SubstrateUniRule annotation1
Metal bindingi256ZincUniRule annotation1
Binding sitei256SubstrateUniRule annotation1
Metal bindingi259ZincUniRule annotation1
Binding sitei259SubstrateUniRule annotation1
Active sitei324Proton acceptorUniRule annotation1
Active sitei325Proton acceptorUniRule annotation1
Binding sitei325SubstrateUniRule annotation1
Metal bindingi358ZincUniRule annotation1
Binding sitei358SubstrateUniRule annotation1
Binding sitei412SubstrateUniRule annotation1
Metal bindingi417ZincUniRule annotation1
Binding sitei417SubstrateUniRule 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:BCE33L1291
OrganismiBacillus cereus (strain ZK / E33L)
Taxonomic identifieri288681 [NCBI]
Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesBacillaceaeBacillusBacillus cereus group
Proteomesi
  • UP000002612 Componenti: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001357231 – 429Histidinol dehydrogenaseAdd BLAST429

Structurei

3D structure databases

ProteinModelPortaliQ63DX2.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the histidinol dehydrogenase family.UniRule annotation

Phylogenomic databases

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.

Q63DX2-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MEIVCEDFQK ALTKIKLLRE NANIIEETVQ RSVREIVQNV RESRDEALSF
60 70 80 90 100
YTKKFDGVEI KDVRVSEEEI KQASMFVESS FLEALQEAKK NIISYHEKQK
110 120 130 140 150
RQSMFDCTSK GIIRGQIIRP LENIGVYVPG GTASYPSSVL MNVLPAKLAG
160 170 180 190 200
VKKIVMVTPP RAGGIDPHIL VAASLAGVDE IYMIGGAQAI AALAYGTESI
210 220 230 240 250
PKVDKIVGPG NLYVALAKRE VYGIVNIDMI AGPSEIVVIA DETGNAKYIA
260 270 280 290 300
ADLLSQAEHD ERATAICITT NIELAKEVEK EIERQLETLP RSEIARESIN
310 320 330 340 350
RNGAIFIVPS IDEALQLSNE IAPEHLELHI KEPMNALAYV KHAGSIFLGP
360 370 380 390 400
YAPEPLGDYL AGPNHVLPTS GTARFFSPLS VDDFVKKSSF LSYTEEALRD
410 420
VKHHIVELAN KEGLHAHARS IQIRFGEEE
Length:429
Mass (Da):47,271
Last modified:October 25, 2004 - v1
Checksum:iEBF5F9843321CD2C
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000001 Genomic DNA. Translation: AAU18958.1.
RefSeqiWP_000406993.1. NZ_CP009968.1.

Genome annotation databases

EnsemblBacteriaiAAU18958; AAU18958; BCE33L1291.
KEGGibcz:BCE33L1291.
PATRICi18886046. VBIBacCer95304_1362.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000001 Genomic DNA. Translation: AAU18958.1.
RefSeqiWP_000406993.1. NZ_CP009968.1.

3D structure databases

ProteinModelPortaliQ63DX2.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAU18958; AAU18958; BCE33L1291.
KEGGibcz:BCE33L1291.
PATRICi18886046. VBIBacCer95304_1362.

Phylogenomic databases

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_BACCZ
AccessioniPrimary (citable) accession number: Q63DX2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 10, 2006
Last sequence update: October 25, 2004
Last modified: November 2, 2016
This is version 89 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

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.