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Protein

Histidinol dehydrogenase

Gene

hisD

Organism
Burkholderia mallei (strain ATCC 23344)
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), 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 HisH (hisH), Imidazole glycerol phosphate synthase subunit HisF (hisF)
  6. Imidazoleglycerol-phosphate dehydratase (hisB)
  7. Histidinol-phosphate aminotransferase 1 (hisC1), Histidinol-phosphate aminotransferase 2 (hisC2)
  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 sitei138NADUniRule annotation1
Binding sitei199NADUniRule annotation1
Binding sitei222NADUniRule annotation1
Binding sitei245SubstrateUniRule annotation1
Metal bindingi267ZincUniRule annotation1
Binding sitei267SubstrateUniRule annotation1
Metal bindingi270ZincUniRule annotation1
Binding sitei270SubstrateUniRule annotation1
Active sitei335Proton acceptorUniRule annotation1
Active sitei336Proton acceptorUniRule annotation1
Binding sitei336SubstrateUniRule annotation1
Metal bindingi369ZincUniRule annotation1
Binding sitei369SubstrateUniRule annotation1
Binding sitei423SubstrateUniRule annotation1
Metal bindingi428ZincUniRule annotation1
Binding sitei428SubstrateUniRule 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:BMA2714
OrganismiBurkholderia mallei (strain ATCC 23344)
Taxonomic identifieri243160 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaBetaproteobacteriaBurkholderialesBurkholderiaceaeBurkholderiapseudomallei group
Proteomesi
  • UP000006693 Componenti: Chromosome 1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001357481 – 445Histidinol dehydrogenaseAdd BLAST445

Interactioni

Protein-protein interaction databases

STRINGi243160.BMA2714.

Structurei

3D structure databases

ProteinModelPortaliQ62GD9.
SMRiQ62GD9.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the histidinol dehydrogenase family.UniRule annotation

Phylogenomic databases

eggNOGiENOG4105CEK. Bacteria.
COG0141. LUCA.
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.

Q62GD9-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAIKIRKLDS AGEGFAAELR AVLAFEASED DAIERAVAQI LADVKARGDA
60 70 80 90 100
AVLDYTNRFD RLNAASVAAL ELPQSELEAA LEGLEPKRRA ALEAAAARVR
110 120 130 140 150
GYHEKQKIEC GSHSWQYTEA DGTVLGQKVT PLDRVGLYVP GGKAAYPSSV
160 170 180 190 200
LMNAIPARVA GVGEIVMVVP TPDGLKNDLV LAAALLGGVD RVFTIGGAQA
210 220 230 240 250
VAALAYGTQT VPAVDKICGP GNAYVASAKR RVFGTVGIDM IAGPSEILVL
260 270 280 290 300
CDGTTDPSWV AMDLFSQAEH DELAQSILLC PDEAFIERVE KAIGELLPTM
310 320 330 340 350
PRQDVIRASL EGRGALVKVR DMAEACRIAN DIAPEHLEIS ALEPHQWGKQ
360 370 380 390 400
IRHAGAIFLG RYTSESLGDY CAGPNHVLPT SRTARFSSPL GVYDFFKRSS
410 420 430 440
LIEVSAEGAH TLGEIASELA YGEGLQAHAK SAEYRMKGAG DRQKG
Length:445
Mass (Da):47,303
Last modified:October 25, 2004 - v1
Checksum:i7755036D7E02348C
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000010 Genomic DNA. Translation: AAU48282.1.
RefSeqiWP_004185201.1. NC_006348.1.
YP_104235.1. NC_006348.1.

Genome annotation databases

EnsemblBacteriaiAAU48282; AAU48282; BMA2714.
GeneIDi3091284.
KEGGibma:BMA2714.
PATRICi19120581. VBIBurMal55007_2784.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000010 Genomic DNA. Translation: AAU48282.1.
RefSeqiWP_004185201.1. NC_006348.1.
YP_104235.1. NC_006348.1.

3D structure databases

ProteinModelPortaliQ62GD9.
SMRiQ62GD9.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi243160.BMA2714.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAU48282; AAU48282; BMA2714.
GeneIDi3091284.
KEGGibma:BMA2714.
PATRICi19120581. VBIBurMal55007_2784.

Phylogenomic databases

eggNOGiENOG4105CEK. Bacteria.
COG0141. LUCA.
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_BURMA
AccessioniPrimary (citable) accession number: Q62GD9
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 7, 2004
Last sequence update: October 25, 2004
Last modified: November 2, 2016
This is version 84 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.