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Protein

Histidinol dehydrogenase

Gene

hisD

Organism
Brucella canis (strain ATCC 23365 / NCTC 10854)
Status
Unreviewed-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 annotationSAAS annotation

Catalytic activityi

L-histidinol + H2O + 2 NAD+ = L-histidine + 2 NADH.UniRule annotationSAAS 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 annotationSAAS 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 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 sitei130NADUniRule annotation1
Binding sitei191NADUniRule annotation1
Binding sitei214NADUniRule annotation1
Binding sitei237SubstrateUniRule annotation1
Metal bindingi259ZincUniRule annotation1
Binding sitei259SubstrateUniRule annotation1
Metal bindingi262ZincUniRule annotation1
Binding sitei262SubstrateUniRule 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

Keywordsi

Molecular functionOxidoreductaseUniRule annotationSAAS annotation
Biological processAmino-acid biosynthesis, Histidine biosynthesisUniRule annotationSAAS annotation
LigandMetal-bindingUniRule annotationSAAS annotation, NADUniRule annotationSAAS annotation, ZincUniRule annotationSAAS annotation

Enzyme and pathway databases

UniPathwayiUPA00031; UER00014.

Names & Taxonomyi

Protein namesi
Recommended name:
Histidinol dehydrogenaseUniRule annotationSAAS annotation (EC:1.1.1.23UniRule annotationSAAS annotation)
Short name:
HDHUniRule annotation
Gene namesi
Name:hisDUniRule annotationImported
Ordered Locus Names:BCAN_A0256Imported
OrganismiBrucella canis (strain ATCC 23365 / NCTC 10854)Imported
Taxonomic identifieri483179 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaAlphaproteobacteriaRhizobialesBrucellaceaeBrucella
Proteomesi
  • UP000001385 Componenti: Chromosome I

Structurei

3D structure databases

ProteinModelPortaliA9M7T9.
SMRiA9M7T9.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the histidinol dehydrogenase family.UniRule annotationSAAS annotation

Phylogenomic databases

HOGENOMiHOG000243914.
KOiK00013.
OMAiQAEHDPM.

Family and domain databases

CDDicd06572. Histidinol_dh. 1 hit.
HAMAPiMF_01024. HisD. 1 hit.
InterProiView protein in InterPro
IPR016161. Ald_DH/histidinol_DH.
IPR001692. Histidinol_DH_CS.
IPR022695. Histidinol_DH_monofunct.
IPR012131. Hstdl_DH.
PfamiView protein in Pfam
PF00815. Histidinol_dh. 1 hit.
PIRSFiPIRSF000099. Histidinol_dh. 1 hit.
PRINTSiPR00083. HOLDHDRGNASE.
SUPFAMiSSF53720. SSF53720. 1 hit.
TIGRFAMsiTIGR00069. hisD. 1 hit.
PROSITEiView protein in PROSITE
PS00611. HISOL_DEHYDROGENASE. 1 hit.

Sequencei

Sequence statusi: Complete.

A9M7T9-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MVTTLRQTDP DFEQKFAAFL SGKREVSEDV DRAVREIVDR VRREGDSALL
60 70 80 90 100
DYSRRFDRID LEKTGIAVTE AEIDAAFDAA PASTVEALKL ARDRIEKHHA
110 120 130 140 150
RQLPKDDRYT DALGVELGSR WTAIEAVGLY VPGGTASYPS SVLMNAMPAK
160 170 180 190 200
VAGVDRIVMV VPAPDGNLNP LVLVAARLAG VSEIYRVGGA QAIAALAYGT
210 220 230 240 250
ETIRPVAKIV GPGNAYVAAA KRIVFGTVGI DMIAGPSEVL IVADKDNNPD
260 270 280 290 300
WIAADLLAQA EHDTAAQSIL MTNDEAFAHA VEEAVERQLH TLARTETASA
310 320 330 340 350
SWRDFGAVIL VKDFEDAIPL ANRIAAEHLE IAVADAEAFV PRIRNAGSIF
360 370 380 390 400
IGGYTPEVIG DYVGGCNHVL PTARSARFSS GLSVLDYMKR TSLLKLGSEQ
410 420 430
LRALGPAAIE IARAEGLDAH AQSVAIRLNL
Length:430
Mass (Da):46,072
Last modified:February 5, 2008 - v1
Checksum:i2752FA59731001E0
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000872 Genomic DNA. Translation: ABX61349.1.
RefSeqiWP_004687945.1. NC_010103.1.

Genome annotation databases

EnsemblBacteriaiABX61349; ABX61349; BCAN_A0256.
KEGGibcs:BCAN_A0256.

Similar proteinsi

Entry informationi

Entry nameiA9M7T9_BRUC2
AccessioniPrimary (citable) accession number: A9M7T9
Entry historyiIntegrated into UniProtKB/TrEMBL: February 5, 2008
Last sequence update: February 5, 2008
Last modified: June 7, 2017
This is version 78 of the entry and version 1 of the sequence. See complete history.
Entry statusiUnreviewed (UniProtKB/TrEMBL)

Miscellaneousi

Keywords - Technical termi

Complete proteomeImported