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Protein

Histidinol dehydrogenase

Gene

hisD

Organism
Yersinia pseudotuberculosis serotype I (strain IP32953)
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 HisH (hisH), Imidazole glycerol phosphate synthase subunit HisF (hisF)
  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 sitei133NADUniRule annotation1
Binding sitei191NADUniRule annotation1
Binding sitei214NADUniRule annotation1
Binding sitei240SubstrateUniRule annotation1
Metal bindingi262ZincUniRule annotation1
Binding sitei262SubstrateUniRule annotation1
Metal bindingi265ZincUniRule annotation1
Binding sitei265SubstrateUniRule annotation1
Active sitei329Proton acceptorUniRule annotation1
Active sitei330Proton acceptorUniRule annotation1
Binding sitei330SubstrateUniRule annotation1
Metal bindingi363ZincUniRule annotation1
Binding sitei363SubstrateUniRule annotation1
Binding sitei417SubstrateUniRule annotation1
Metal bindingi422ZincUniRule annotation1
Binding sitei422SubstrateUniRule 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:YPTB1561
OrganismiYersinia pseudotuberculosis serotype I (strain IP32953)
Taxonomic identifieri273123 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacteralesYersiniaceaeYersinia
Proteomesi
  • UP000001011 Componenti: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001358881 – 443Histidinol dehydrogenaseAdd BLAST443

Interactioni

Subunit structurei

Homodimer.UniRule annotation

Structurei

3D structure databases

ProteinModelPortaliQ66C49.
SMRiQ66C49.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the histidinol dehydrogenase family.UniRule annotation

Phylogenomic databases

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.

Q66C49-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MQPTNFNTLI NWQQCSEEQQ KALLSRPAIN ASERITATVS DILDRVKAEG
60 70 80 90 100
DSALRDFSQR FDHVQVADIR ITASEIAAAS ARLSDDVKHA MAQAVRNIEI
110 120 130 140 150
FHNAQKMPVV DVETQPGVRC QQITRPIASV GLYIPGGSAP LPSTVLMLGT
160 170 180 190 200
PARIAGCQRV VLCSPPPIAD EILYAAQLCG IQEVFQIGGA QAIAAMAFGS
210 220 230 240 250
ESVPKVHKIF GPGNAYVTEA KRQVSQRLDG AAIDMPAGPS EVLVIADSGA
260 270 280 290 300
TPAFIAADLL SQAEHGPDSQ VILLTPDAAI AQAVAVEVEQ QLALLSRADI
310 320 330 340 350
ARQALESSRL IVTNDLQQCI DISNAYGPEH LILQIRQPEE IIDQIDNAGS
360 370 380 390 400
VFMGDWSPES AGDYASGTNH VLPTYGYTST YSSLGLADFV KRMTVQQLTP
410 420 430 440
QGLLGLASTI ETLAQAEQLT AHKNAVTLRV TALNNALTAV NKE
Length:443
Mass (Da):47,263
Last modified:October 11, 2004 - v1
Checksum:iC8AF3D43698CF00D
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BX936398 Genomic DNA. Translation: CAH20800.1.
RefSeqiWP_011192122.1. NZ_CP009712.1.

Genome annotation databases

EnsemblBacteriaiCAH20800; CAH20800; YPTB1561.
KEGGiypo:BZ17_954.
yps:YPTB1561.
PATRICi18641747. VBIYerPse22266_1940.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BX936398 Genomic DNA. Translation: CAH20800.1.
RefSeqiWP_011192122.1. NZ_CP009712.1.

3D structure databases

ProteinModelPortaliQ66C49.
SMRiQ66C49.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiCAH20800; CAH20800; YPTB1561.
KEGGiypo:BZ17_954.
yps:YPTB1561.
PATRICi18641747. VBIYerPse22266_1940.

Phylogenomic databases

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_YERPS
AccessioniPrimary (citable) accession number: Q66C49
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 7, 2004
Last sequence update: October 11, 2004
Last modified: November 2, 2016
This is version 89 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.