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Protein

Histidinol dehydrogenase

Gene

hisD

Organism
Buchnera aphidicola subsp. Baizongia pistaciae (strain Bp)
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. Histidine biosynthesis bifunctional protein HisIE (hisI)
  3. Histidine biosynthesis bifunctional protein HisIE (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. Histidine biosynthesis bifunctional protein HisB (hisB)
  7. Histidinol-phosphate aminotransferase (hisC)
  8. Histidine biosynthesis bifunctional protein HisB (hisB)
  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 sitei131NADUniRule annotation1
Binding sitei189NADUniRule annotation1
Binding sitei212NADUniRule annotation1
Binding sitei238SubstrateUniRule annotation1
Metal bindingi260ZincUniRule annotation1
Binding sitei260SubstrateUniRule annotation1
Metal bindingi263ZincUniRule annotation1
Binding sitei263SubstrateUniRule annotation1
Active sitei327Proton acceptorUniRule annotation1
Active sitei328Proton acceptorUniRule annotation1
Binding sitei328SubstrateUniRule annotation1
Metal bindingi361ZincUniRule annotation1
Binding sitei361SubstrateUniRule annotation1
Binding sitei415SubstrateUniRule annotation1
Metal bindingi420ZincUniRule annotation1
Binding sitei420SubstrateUniRule 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:bbp_094
OrganismiBuchnera aphidicola subsp. Baizongia pistaciae (strain Bp)
Taxonomic identifieri224915 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacteralesErwiniaceaeBuchnera
Proteomesi
  • UP000000601 Componenti: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001357431 – 435Histidinol dehydrogenaseAdd BLAST435

Interactioni

Subunit structurei

Homodimer.UniRule annotation

Protein-protein interaction databases

STRINGi224915.bbp094.

Structurei

3D structure databases

ProteinModelPortaliP59398.
SMRiP59398.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the histidinol dehydrogenase family.UniRule annotation

Phylogenomic databases

eggNOGiENOG4105CEK. Bacteria.
COG0141. LUCA.
KOiK00013.
OMAiNAGAIYL.
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.

P59398-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MEVYIPIIYW KSCSEKEKRE ILFRPVVNDN SQIKEVVKEI ITNVKNSGDK
60 70 80 90 100
ALYDYTKTFD KIRLESIQVS YGEIVDSDSF VNEEIQKSIS VAKNNIKIFH
110 120 130 140 150
EKQTHNVVNI EIQPGVFCRQ IIRPIQSVGL YIPGGCAPLV STVLMLAIPA
160 170 180 190 200
KIVGCKNIIL CSPPPITKEI LYASKICGIH NIFQVGGAQA IAAMAFGTKT
210 220 230 240 250
IPKVNKIFGP GNVYVTEAKL QINALLNDLS IDMLAGPSEI LIIADFKANA
260 270 280 290 300
CIIASDFLSQ MEHGIYSQAI LVTPSYDLAC NVIFEINIQL KNLSRKKVIN
310 320 330 340 350
KSLKYSRIIV TKTLLECFEI SNLYAPEHLI IQCENSNRLL VYVINAGSIF
360 370 380 390 400
LGRWSAVASG DYVTGTNHVL PTYGSAIVNS GLTVMDFQKI ISVQKLDQQG
410 420 430
LIDVSSSIIS LSEVERMDAH TNSIKQRLIA LQDVK
Length:435
Mass (Da):48,185
Last modified:March 25, 2003 - v1
Checksum:i8A2F3ED2073D73F2
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE016826 Genomic DNA. Translation: AAO26829.1.
RefSeqiWP_011091230.1. NC_004545.1.

Genome annotation databases

EnsemblBacteriaiAAO26829; AAO26829; bbp_094.
KEGGibab:bbp_094.
PATRICi21244967. VBIBucAph80364_0091.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE016826 Genomic DNA. Translation: AAO26829.1.
RefSeqiWP_011091230.1. NC_004545.1.

3D structure databases

ProteinModelPortaliP59398.
SMRiP59398.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi224915.bbp094.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAO26829; AAO26829; bbp_094.
KEGGibab:bbp_094.
PATRICi21244967. VBIBucAph80364_0091.

Phylogenomic databases

eggNOGiENOG4105CEK. Bacteria.
COG0141. LUCA.
KOiK00013.
OMAiNAGAIYL.
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_BUCBP
AccessioniPrimary (citable) accession number: P59398
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 25, 2003
Last sequence update: March 25, 2003
Last modified: November 2, 2016
This is version 102 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.