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Protein

Histidinol dehydrogenase

Gene

hisD

Organism
Escherichia coli (strain K12)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

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+1 PublicationNote: Binds 1 zinc ion per subunit.1 Publication

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 sitei130NAD1 Publication1
Binding sitei188NAD1 Publication1
Binding sitei211NAD1 Publication1
Binding sitei237Substrate1 Publication1
Metal bindingi259Zinc1 Publication1
Binding sitei259Substrate1 Publication1
Metal bindingi262Zinc1 Publication1
Binding sitei262Substrate1 Publication1
Active sitei326Proton acceptor1 Publication1
Active sitei327Proton acceptor1 Publication1
Binding sitei327Substrate1 Publication1
Metal bindingi360Zinc1 Publication1
Binding sitei360Substrate1 Publication1
Binding sitei414Substrate1 Publication1
Metal bindingi419Zinc1 Publication1
Binding sitei419Substrate1 Publication1

GO - Molecular functioni

  • histidinol dehydrogenase activity Source: EcoCyc
  • manganese ion binding Source: EcoCyc
  • metal ion binding Source: EcoCyc
  • NAD binding Source: InterPro
  • zinc ion binding Source: UniProtKB-HAMAP

GO - Biological processi

  • histidine biosynthetic process Source: EcoCyc
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

BioCyciEcoCyc:HISTDEHYD-MONOMER.
ECOL316407:JW2002-MONOMER.
MetaCyc:HISTDEHYD-MONOMER.
BRENDAi1.1.1.23. 2026.
UniPathwayiUPA00031; UER00014.

Names & Taxonomyi

Protein namesi
Recommended name:
Histidinol dehydrogenaseUniRule annotation (EC:1.1.1.23UniRule annotation)
Short name:
HDHUniRule annotation
Gene namesi
Name:hisD1 PublicationUniRule annotation
Ordered Locus Names:b2020, JW2002
OrganismiEscherichia coli (strain K12)
Taxonomic identifieri83333 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacteralesEnterobacteriaceaeEscherichia
Proteomesi
  • UP000000318 Componenti: Chromosome
  • UP000000625 Componenti: Chromosome

Organism-specific databases

EcoGeneiEG10447. hisD.

Subcellular locationi

GO - Cellular componenti

  • cytosol Source: EcoCyc
Complete GO annotation...

Pathology & Biotechi

Chemistry databases

ChEMBLiCHEMBL2366464.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemoved1 Publication
ChainiPRO_00001357702 – 434Histidinol dehydrogenaseAdd BLAST433

Proteomic databases

EPDiP06988.
PaxDbiP06988.
PRIDEiP06988.

2D gel databases

SWISS-2DPAGEP06988.

Interactioni

Subunit structurei

Homodimer.UniRule annotation

Protein-protein interaction databases

BioGridi4260403. 18 interactors.
IntActiP06988. 7 interactors.
STRINGi511145.b2020.

Structurei

Secondary structure

1434
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi5 – 8Combined sources4
Helixi9 – 11Combined sources3
Helixi14 – 20Combined sources7
Helixi30 – 54Combined sources25
Beta strandi57 – 59Combined sources3
Beta strandi64 – 67Combined sources4
Helixi70 – 79Combined sources10
Helixi82 – 100Combined sources19
Beta strandi107 – 112Combined sources6
Beta strandi115 – 123Combined sources9
Beta strandi125 – 130Combined sources6
Beta strandi134 – 136Combined sources3
Helixi140 – 152Combined sources13
Beta strandi155 – 161Combined sources7
Helixi167 – 175Combined sources9
Beta strandi180 – 183Combined sources4
Helixi186 – 195Combined sources10
Beta strandi198 – 200Combined sources3
Beta strandi204 – 207Combined sources4
Helixi212 – 223Combined sources12
Beta strandi225 – 227Combined sources3
Beta strandi229 – 231Combined sources3
Beta strandi238 – 243Combined sources6
Helixi249 – 260Combined sources12
Beta strandi267 – 273Combined sources7
Helixi275 – 289Combined sources15
Helixi295 – 302Combined sources8
Beta strandi306 – 309Combined sources4
Helixi313 – 323Combined sources11
Beta strandi326 – 332Combined sources7
Helixi335 – 338Combined sources4
Helixi339 – 341Combined sources3
Beta strandi346 – 351Combined sources6
Helixi356 – 361Combined sources6
Beta strandi363 – 365Combined sources3
Helixi374 – 376Combined sources3
Helixi383 – 386Combined sources4
Beta strandi387 – 395Combined sources9
Helixi397 – 413Combined sources17
Helixi417 – 433Combined sources17

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1K75X-ray1.75A/B1-434[»]
1KAEX-ray1.70A/B1-434[»]
1KAHX-ray2.10A/B1-434[»]
1KARX-ray2.10A/B1-434[»]
ProteinModelPortaliP06988.
SMRiP06988.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP06988.

Family & Domainsi

Sequence similaritiesi

Belongs to the histidinol dehydrogenase family.UniRule annotationCurated

Phylogenomic databases

eggNOGiENOG4105CEK. Bacteria.
COG0141. LUCA.
HOGENOMiHOG000243914.
InParanoidiP06988.
KOiK00013.
OMAiGGTARFY.
PhylomeDBiP06988.

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.

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

P06988-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSFNTIIDWN SCTAEQQRQL LMRPAISASE SITRTVNDIL DNVKARGDEA
60 70 80 90 100
LREYSAKFDK TTVTALKVSA EEIAAASERL SDELKQAMAV AVKNIETFHT
110 120 130 140 150
AQKLPPVDVE TQPGVRCQQV TRPVASVGLY IPGGSAPLFS TVLMLATPAS
160 170 180 190 200
IAGCKKVVLC SPPPIADEIL YAAQLCGVQD VFNVGGAQAI AALAFGTESV
210 220 230 240 250
PKVDKIFGPG NAFVTEAKRQ VSQRLDGAAI DMPAGPSEVL VIADSGATPD
260 270 280 290 300
FVASDLLSQA EHGPDSQVIL LTPAADMARR VAEAVERQLA ELPRAETARQ
310 320 330 340 350
ALNASRLIVT KDLAQCVEIS NQYGPEHLII QTRNARELVD SITSAGSVFL
360 370 380 390 400
GDWSPESAGD YASGTNHVLP TYGYTATCSS LGLADFQKRM TVQELSKEGF
410 420 430
SALASTIETL AAAERLTAHK NAVTLRVNAL KEQA
Length:434
Mass (Da):46,110
Last modified:January 23, 2007 - v5
Checksum:i4B4F2EA00C9BEA4E
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti15E → V (PubMed:3062174).Curated1
Sequence conflicti15E → V (PubMed:3018428).Curated1
Sequence conflicti22M → T in CAA27610 (PubMed:3018428).Curated1
Sequence conflicti150S → R (PubMed:3062174).Curated1
Sequence conflicti150S → R (PubMed:3018428).Curated1
Sequence conflicti157V → A in CAA36882 (PubMed:2194167).Curated1
Sequence conflicti313L → S (PubMed:3062174).Curated1
Sequence conflicti313L → S (PubMed:3018428).Curated1
Sequence conflicti403L → V (PubMed:3062174).Curated1
Sequence conflicti403L → V (PubMed:3018428).Curated1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X13462 Genomic DNA. Translation: CAA31812.1.
X03972 Genomic DNA. Translation: CAA27610.1.
X52656 Genomic DNA. Translation: CAA36882.1.
U00096 Genomic DNA. Translation: AAC75081.1.
AP009048 Genomic DNA. Translation: BAA15851.1.
M10483 Genomic DNA. Translation: AAA23962.1.
PIRiC64967. DEECHT.
RefSeqiNP_416524.1. NC_000913.3.
WP_000009594.1. NZ_LN832404.1.

Genome annotation databases

EnsemblBacteriaiAAC75081; AAC75081; b2020.
BAA15851; BAA15851; BAA15851.
GeneIDi946531.
KEGGiecj:JW2002.
eco:b2020.
PATRICi32119375. VBIEscCol129921_2097.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X13462 Genomic DNA. Translation: CAA31812.1.
X03972 Genomic DNA. Translation: CAA27610.1.
X52656 Genomic DNA. Translation: CAA36882.1.
U00096 Genomic DNA. Translation: AAC75081.1.
AP009048 Genomic DNA. Translation: BAA15851.1.
M10483 Genomic DNA. Translation: AAA23962.1.
PIRiC64967. DEECHT.
RefSeqiNP_416524.1. NC_000913.3.
WP_000009594.1. NZ_LN832404.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1K75X-ray1.75A/B1-434[»]
1KAEX-ray1.70A/B1-434[»]
1KAHX-ray2.10A/B1-434[»]
1KARX-ray2.10A/B1-434[»]
ProteinModelPortaliP06988.
SMRiP06988.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi4260403. 18 interactors.
IntActiP06988. 7 interactors.
STRINGi511145.b2020.

Chemistry databases

ChEMBLiCHEMBL2366464.

2D gel databases

SWISS-2DPAGEP06988.

Proteomic databases

EPDiP06988.
PaxDbiP06988.
PRIDEiP06988.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAC75081; AAC75081; b2020.
BAA15851; BAA15851; BAA15851.
GeneIDi946531.
KEGGiecj:JW2002.
eco:b2020.
PATRICi32119375. VBIEscCol129921_2097.

Organism-specific databases

EchoBASEiEB0442.
EcoGeneiEG10447. hisD.

Phylogenomic databases

eggNOGiENOG4105CEK. Bacteria.
COG0141. LUCA.
HOGENOMiHOG000243914.
InParanoidiP06988.
KOiK00013.
OMAiGGTARFY.
PhylomeDBiP06988.

Enzyme and pathway databases

UniPathwayiUPA00031; UER00014.
BioCyciEcoCyc:HISTDEHYD-MONOMER.
ECOL316407:JW2002-MONOMER.
MetaCyc:HISTDEHYD-MONOMER.
BRENDAi1.1.1.23. 2026.

Miscellaneous databases

EvolutionaryTraceiP06988.
PROiP06988.

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_ECOLI
AccessioniPrimary (citable) accession number: P06988
Secondary accession number(s): O08506, P78076, Q47254
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 1, 1988
Last sequence update: January 23, 2007
Last modified: November 2, 2016
This is version 160 of the entry and version 5 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Escherichia coli
    Escherichia coli (strain K12): entries and cross-references to EcoGene
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  3. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. 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.