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Protein

Histidinol dehydrogenase

Gene

hisD

Organism
Shigella flexneri
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 (hisG), ATP phosphoribosyltransferase (hisG)
  2. Histidine biosynthesis bifunctional protein HisIE (hisI), Histidine biosynthesis bifunctional protein HisIE (hisI), Histidine biosynthesis bifunctional protein HisIE (hisI), Histidine biosynthesis bifunctional protein HisIE (hisI)
  3. Histidine biosynthesis bifunctional protein HisIE (hisI), Histidine biosynthesis bifunctional protein HisIE (hisI), Histidine biosynthesis bifunctional protein HisIE (hisI), Histidine biosynthesis bifunctional protein HisIE (hisI)
  4. 1-(5-phosphoribosyl)-5-[(5-phosphoribosylamino)methylideneamino] imidazole-4-carboxamide isomerase (hisA), 1-(5-phosphoribosyl)-5-[(5-phosphoribosylamino)methylideneamino] imidazole-4-carboxamide isomerase (hisA), 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 HisH (hisH), Imidazole glycerol phosphate synthase subunit HisH (hisH), Imidazole glycerol phosphate synthase subunit HisF (hisF), Imidazole glycerol phosphate synthase subunit HisF (hisF), Imidazole glycerol phosphate synthase subunit HisF (hisF), Imidazole glycerol phosphate synthase subunit HisH (hisH), Imidazole glycerol phosphate synthase subunit HisF (hisF)
  6. Histidine biosynthesis bifunctional protein HisB (hisB), Histidine biosynthesis bifunctional protein HisB (hisB), Histidine biosynthesis bifunctional protein HisB (hisB)
  7. Histidinol-phosphate aminotransferase (hisC), Histidinol-phosphate aminotransferase (hisC), Histidinol-phosphate aminotransferase (hisC), Histidinol-phosphate aminotransferase (hisC)
  8. Histidine biosynthesis bifunctional protein HisB (hisB), Histidine biosynthesis bifunctional protein HisB (hisB), Histidine biosynthesis bifunctional protein HisB (hisB)
  9. Histidinol dehydrogenase (hisD), Histidinol dehydrogenase (hisD), Histidinol dehydrogenase (hisD), 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 sitei188NADUniRule annotation1
Binding sitei211NADUniRule annotation1
Binding sitei237SubstrateUniRule annotation1
Metal bindingi259ZincUniRule annotation1
Binding sitei259SubstrateUniRule annotation1
Metal bindingi262ZincUniRule annotation1
Binding sitei262SubstrateUniRule annotation1
Active sitei326Proton acceptorUniRule annotation1
Active sitei327Proton acceptorUniRule annotation1
Binding sitei327SubstrateUniRule annotation1
Metal bindingi360ZincUniRule annotation1
Binding sitei360SubstrateUniRule annotation1
Binding sitei414SubstrateUniRule annotation1
Metal bindingi419ZincUniRule annotation1
Binding sitei419SubstrateUniRule annotation1

GO - Molecular functioni

GO - Biological processi

Keywordsi

Molecular functionOxidoreductase
Biological processAmino-acid biosynthesis, Histidine biosynthesis
LigandMetal-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:SF2082, S2203
OrganismiShigella flexneri
Taxonomic identifieri623 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacteralesEnterobacteriaceaeShigella
Proteomesi
  • UP000002673 Componenti: Chromosome
  • UP000001006 Componenti: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemovedBy similarity
ChainiPRO_00001358442 – 434Histidinol dehydrogenaseAdd BLAST433

Proteomic databases

PaxDbiP59401.
PRIDEiP59401.

Interactioni

Subunit structurei

Homodimer.UniRule annotation

Structurei

3D structure databases

ProteinModelPortaliP59401.
SMRiP59401.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the histidinol dehydrogenase family.UniRule annotation

Phylogenomic databases

eggNOGiENOG4105CEK. Bacteria.
COG0141. LUCA.
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.

Sequence processingi: The displayed sequence is further processed into a mature form.

P59401-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSFNTIIDWN SCTAEQQRQL LMRPAISASE SITRTVNDIL DNVKTRGDEA
60 70 80 90 100
LREYSAKFDK TTVTALKVSA DEIAAASERL SDELKQAMAV AVKSIETFHT
110 120 130 140 150
AQKLPPVDVE TQLGVRCQQV TRPVASVGLY IPGGSAPLFS TVLMLATPAR
160 170 180 190 200
IAGCKKVVLC SPPPIADEIL YAAQLCDVQD VFNVGGAQAI AALAFGTESV
210 220 230 240 250
PKVDKIFGPG NAFVTEAKRQ VSQRLDGAAI DMPAGPSEVL VIADSGATPD
260 270 280 290 300
FVASDLLSQA EHGPDSQVIL LTPDADMARR VAEAVERQLA ELPRAETTRQ
310 320 330 340 350
ALNASRLIVT KDLAQCVEIS NQYGPEHLII QTRNARELVD GITSAGSVFL
360 370 380 390 400
GDWSPESAGD YASGTNHVLP TYGYTATCSS LGLADFQKRM TVQELSKEGF
410 420 430
SALASTIETL AAAERLTAHK NAVTLRVNVL KEQA
Length:434
Mass (Da):46,315
Last modified:January 23, 2007 - v2
Checksum:i43D31484E37781D2
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE005674 Genomic DNA. Translation: AAN43622.2.
AE014073 Genomic DNA. Translation: AAP17450.1.
RefSeqiNP_707915.2. NC_004337.2.
WP_000009597.1. NZ_NMXZ01000030.1.

Genome annotation databases

EnsemblBacteriaiAAN43622; AAN43622; SF2082.
AAP17450; AAP17450; S2203.
GeneIDi1025296.
KEGGisfl:SF2082.
sfx:S2203.
PATRICifig|198214.7.peg.2491.

Similar proteinsi

Entry informationi

Entry nameiHISX_SHIFL
AccessioniPrimary (citable) accession number: P59401
Entry historyiIntegrated into UniProtKB/Swiss-Prot: March 25, 2003
Last sequence update: January 23, 2007
Last modified: November 22, 2017
This is version 110 of the entry and version 2 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