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Protein

Histidinol dehydrogenase

Gene

hisD

Organism
Staphylococcus epidermidis (strain ATCC 12228)
Status
Reviewed-Annotation score: -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. 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. 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 sitei116NADUniRule annotation1
Binding sitei177NADUniRule annotation1
Binding sitei200NADUniRule annotation1
Binding sitei223SubstrateUniRule annotation1
Metal bindingi245ZincUniRule annotation1
Binding sitei245SubstrateUniRule annotation1
Metal bindingi248ZincUniRule annotation1
Binding sitei248SubstrateUniRule annotation1
Active sitei313Proton acceptorUniRule annotation1
Active sitei314Proton acceptorUniRule annotation1
Binding sitei314SubstrateUniRule annotation1
Metal bindingi347ZincUniRule annotation1
Binding sitei347SubstrateUniRule annotation1
Binding sitei401SubstrateUniRule annotation1
Metal bindingi406ZincUniRule annotation1
Binding sitei406SubstrateUniRule annotation1

GO - Molecular functioni

GO - Biological processi

Keywordsi

Molecular functionOxidoreductase
Biological processAmino-acid biosynthesis, Histidine biosynthesis
LigandMetal-binding, NAD, Zinc

Enzyme and pathway databases

BioCyciSEPI176280:G1G05-274-MONOMER
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:SE_0272
OrganismiStaphylococcus epidermidis (strain ATCC 12228)
Taxonomic identifieri176280 [NCBI]
Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesStaphylococcaceaeStaphylococcus
Proteomesi
  • UP000001411 Componenti: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001358551 – 414Histidinol dehydrogenaseAdd BLAST414

Proteomic databases

PRIDEiQ8CQ95

Interactioni

Protein-protein interaction databases

STRINGi176280.SE0272

Structurei

3D structure databases

ProteinModelPortaliQ8CQ95
SMRiQ8CQ95
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the histidinol dehydrogenase family.UniRule annotation

Phylogenomic databases

eggNOGiENOG4105CEK Bacteria
COG0141 LUCA
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
PANTHERiPTHR21256 PTHR21256, 1 hit
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.

Q8CQ95-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MLSAQQFLKE FNNVESLNES LYEIVSHICE EVKLQGDKAL KNYNLQFDQV
60 70 80 90 100
ETEKLELEQS QLKNAYDMLD NETRDALEQS YQRIKVYQEN IKVKQESSQQ
110 120 130 140 150
TECYERYHPI ERVGIYVPGG KASYPSTVLM TATLAQVAGV NEITVVTPPQ
160 170 180 190 200
NNGICQEVLA ACYITGVHHV YQVGGAQSIA ALTYGTETIK KVDKIVGPGN
210 220 230 240 250
QYVAYAKKFV FGQVGIDQIA GPTEIALIID ESADLDAIAY DVFAQAEHDE
260 270 280 290 300
MACTYVISEN EKVLNQLNTI IQEKLQYVER QDIISQSIAN HHYLILAQDT
310 320 330 340 350
EEACLIMNTI APEHASIQTR APEMYIDKVK YVGALFLGHF SPEVIGDYMA
360 370 380 390 400
GPSHVLPTNQ TARFTNGLSV NDFMTRHSVI HLSQKTFNEV AESAEHIAHI
410
ESLFNHEKSI HVRR
Length:414
Mass (Da):46,494
Last modified:March 1, 2003 - v1
Checksum:i5D96007ECE4E1843
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE015929 Genomic DNA Translation: AAO03869.1
RefSeqiNP_763827.1, NC_004461.1
WP_001829419.1, NC_004461.1

Genome annotation databases

EnsemblBacteriaiAAO03869; AAO03869; SE_0272
GeneIDi1058081
KEGGisep:SE0272
PATRICifig|176280.10.peg.250

Similar proteinsi

Entry informationi

Entry nameiHISX_STAES
AccessioniPrimary (citable) accession number: Q8CQ95
Entry historyiIntegrated into UniProtKB/Swiss-Prot: March 25, 2003
Last sequence update: March 1, 2003
Last modified: May 23, 2018
This is version 104 of the entry and version 1 of the sequence. See 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

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