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P06988

- HISX_ECOLI

UniProt

P06988 - HISX_ECOLI

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Protein
Histidinol dehydrogenase
Gene
hisD, b2020, JW2002
Organism
Escherichia coli (strain K12)
Status
Reviewed - 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

Binds 1 zinc ion per subunit.

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei130 – 1301NAD
Binding sitei188 – 1881NAD
Binding sitei211 – 2111NAD
Binding sitei237 – 2371Substrate
Metal bindingi259 – 2591Zinc
Binding sitei259 – 2591Substrate
Metal bindingi262 – 2621Zinc
Binding sitei262 – 2621Substrate
Active sitei326 – 3261Proton acceptor
Active sitei327 – 3271Proton acceptor
Binding sitei327 – 3271Substrate
Metal bindingi360 – 3601Zinc
Binding sitei360 – 3601Substrate
Binding sitei414 – 4141Substrate
Metal bindingi419 – 4191Zinc
Binding sitei419 – 4191Substrate

GO - Molecular functioni

  1. NAD binding Source: InterPro
  2. histidinol dehydrogenase activity Source: EcoCyc
  3. manganese ion binding Source: EcoCyc
  4. metal ion binding Source: EcoCyc
  5. zinc ion binding Source: UniProtKB-HAMAP

GO - Biological processi

  1. 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.
UniPathwayiUPA00031; UER00014.

Names & Taxonomyi

Protein namesi
Recommended name:
Histidinol dehydrogenase (EC:1.1.1.23)
Short name:
HDH
Gene namesi
Name:hisD
Ordered Locus Names:b2020, JW2002
OrganismiEscherichia coli (strain K12)
Taxonomic identifieri83333 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
ProteomesiUP000000318: Chromosome, UP000000625: Chromosome

Organism-specific databases

EcoGeneiEG10447. hisD.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed1 Publication
Chaini2 – 434433Histidinol dehydrogenaseUniRule annotation
PRO_0000135770Add
BLAST

Proteomic databases

PaxDbiP06988.
PRIDEiP06988.

2D gel databases

SWISS-2DPAGEP06988.

Expressioni

Gene expression databases

GenevestigatoriP06988.

Interactioni

Subunit structurei

Homodimer.

Protein-protein interaction databases

IntActiP06988. 7 interactions.
STRINGi511145.b2020.

Structurei

Secondary structure

Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi5 – 84
Helixi9 – 113
Helixi14 – 207
Helixi30 – 5425
Beta strandi57 – 593
Beta strandi64 – 674
Helixi70 – 7910
Helixi82 – 10019
Beta strandi107 – 1126
Beta strandi115 – 1239
Beta strandi125 – 1306
Beta strandi134 – 1363
Helixi140 – 15213
Beta strandi155 – 1617
Helixi167 – 1759
Beta strandi180 – 1834
Helixi186 – 19510
Beta strandi198 – 2003
Beta strandi204 – 2074
Helixi212 – 22312
Beta strandi225 – 2273
Beta strandi229 – 2313
Beta strandi238 – 2436
Helixi249 – 26012
Beta strandi267 – 2737
Helixi275 – 28915
Helixi295 – 3028
Beta strandi306 – 3094
Helixi313 – 32311
Beta strandi326 – 3327
Helixi335 – 3384
Helixi339 – 3413
Beta strandi346 – 3516
Helixi356 – 3616
Beta strandi363 – 3653
Helixi374 – 3763
Helixi383 – 3864
Beta strandi387 – 3959
Helixi397 – 41317
Helixi417 – 43317

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1K75X-ray1.75A/B1-434[»]
1KAEX-ray1.70A/B1-434[»]
1KAHX-ray2.10A/B1-434[»]
1KARX-ray2.10A/B1-434[»]
ProteinModelPortaliP06988.

Miscellaneous databases

EvolutionaryTraceiP06988.

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

eggNOGiCOG0141.
HOGENOMiHOG000243914.
KOiK00013.
OMAiYAAKLCG.
OrthoDBiEOG6CVVCR.
PhylomeDBiP06988.

Family and domain databases

HAMAPiMF_01024. HisD.
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

MSFNTIIDWN SCTAEQQRQL LMRPAISASE SITRTVNDIL DNVKARGDEA    50
LREYSAKFDK TTVTALKVSA EEIAAASERL SDELKQAMAV AVKNIETFHT 100
AQKLPPVDVE TQPGVRCQQV TRPVASVGLY IPGGSAPLFS TVLMLATPAS 150
IAGCKKVVLC SPPPIADEIL YAAQLCGVQD VFNVGGAQAI AALAFGTESV 200
PKVDKIFGPG NAFVTEAKRQ VSQRLDGAAI DMPAGPSEVL VIADSGATPD 250
FVASDLLSQA EHGPDSQVIL LTPAADMARR VAEAVERQLA ELPRAETARQ 300
ALNASRLIVT KDLAQCVEIS NQYGPEHLII QTRNARELVD SITSAGSVFL 350
GDWSPESAGD YASGTNHVLP TYGYTATCSS LGLADFQKRM TVQELSKEGF 400
SALASTIETL AAAERLTAHK NAVTLRVNAL KEQA 434
Length:434
Mass (Da):46,110
Last modified:January 23, 2007 - v5
Checksum:i4B4F2EA00C9BEA4E
GO

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti15 – 151E → V1 Publication
Sequence conflicti15 – 151E → V1 Publication
Sequence conflicti22 – 221M → T in CAA27610. 1 Publication
Sequence conflicti150 – 1501S → R1 Publication
Sequence conflicti150 – 1501S → R1 Publication
Sequence conflicti157 – 1571V → A in CAA36882. 1 Publication
Sequence conflicti313 – 3131L → S1 Publication
Sequence conflicti313 – 3131L → S1 Publication
Sequence conflicti403 – 4031L → V1 Publication
Sequence conflicti403 – 4031L → V1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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.
YP_490263.1. NC_007779.1.

Genome annotation databases

EnsemblBacteriaiAAC75081; AAC75081; b2020.
BAA15851; BAA15851; BAA15851.
GeneIDi12931409.
946531.
KEGGiecj:Y75_p1983.
eco:b2020.
PATRICi32119375. VBIEscCol129921_2097.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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 .
PIRi C64967. DEECHT.
RefSeqi NP_416524.1. NC_000913.3.
YP_490263.1. NC_007779.1.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1K75 X-ray 1.75 A/B 1-434 [» ]
1KAE X-ray 1.70 A/B 1-434 [» ]
1KAH X-ray 2.10 A/B 1-434 [» ]
1KAR X-ray 2.10 A/B 1-434 [» ]
ProteinModelPortali P06988.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

IntActi P06988. 7 interactions.
STRINGi 511145.b2020.

2D gel databases

SWISS-2DPAGE P06988.

Proteomic databases

PaxDbi P06988.
PRIDEi P06988.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai AAC75081 ; AAC75081 ; b2020 .
BAA15851 ; BAA15851 ; BAA15851 .
GeneIDi 12931409.
946531.
KEGGi ecj:Y75_p1983.
eco:b2020.
PATRICi 32119375. VBIEscCol129921_2097.

Organism-specific databases

EchoBASEi EB0442.
EcoGenei EG10447. hisD.

Phylogenomic databases

eggNOGi COG0141.
HOGENOMi HOG000243914.
KOi K00013.
OMAi YAAKLCG.
OrthoDBi EOG6CVVCR.
PhylomeDBi P06988.

Enzyme and pathway databases

UniPathwayi UPA00031 ; UER00014 .
BioCyci EcoCyc:HISTDEHYD-MONOMER.
ECOL316407:JW2002-MONOMER.
MetaCyc:HISTDEHYD-MONOMER.

Miscellaneous databases

EvolutionaryTracei P06988.
PROi P06988.

Gene expression databases

Genevestigatori P06988.

Family and domain databases

HAMAPi MF_01024. HisD.
InterProi IPR016161. Ald_DH/histidinol_DH.
IPR001692. Histidinol_DH_CS.
IPR022695. Histidinol_DH_monofunct.
IPR012131. Hstdl_DH.
[Graphical view ]
Pfami PF00815. Histidinol_dh. 1 hit.
[Graphical view ]
PIRSFi PIRSF000099. Histidinol_dh. 1 hit.
PRINTSi PR00083. HOLDHDRGNASE.
SUPFAMi SSF53720. SSF53720. 1 hit.
TIGRFAMsi TIGR00069. hisD. 1 hit.
PROSITEi PS00611. HISOL_DEHYDROGENASE. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Structure and function of the Salmonella typhimurium and Escherichia coli K-12 histidine operons."
    Carlomagno M.S., Chiariotti L., Alifano P., Nappo A.G., Bruni C.B.
    J. Mol. Biol. 203:585-606(1988) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: K12.
  2. "Nucleotide sequence of the Escherichia coli hisD gene and of the Escherichia coli and Salmonella typhimurium hisIE region."
    Chiariotti L., Alifano P., Carlomagno M.S., Bruni C.B.
    Mol. Gen. Genet. 203:382-388(1986) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  3. "Nucleotide and amino acid polymorphism in the gene for L-histidinol dehydrogenase of Escherichia coli K12."
    Savic D.J., Jovanovic G., Kostic T.
    Nucleic Acids Res. 18:3634-3634(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: K12 / W3100 / ATCC 14948 / DSM 6302.
  4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
  5. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / MG1655 / ATCC 47076.
  6. "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110."
    Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.
    Mol. Syst. Biol. 2:E1-E5(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
  7. "Structural and physiological studies of the Escherichia coli histidine operon inserted into plasmid vectors."
    Bruni C.B., Musti A.M., Frunzio R., Blasi F.
    J. Bacteriol. 142:32-42(1980) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 296-319.
  8. "Comparing the predicted and observed properties of proteins encoded in the genome of Escherichia coli K-12."
    Link A.J., Robison K., Church G.M.
    Electrophoresis 18:1259-1313(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 2-13.
    Strain: K12 / EMG2.
  9. "Mechanism of action and NAD+-binding mode revealed by the crystal structure of L-histidinol dehydrogenase."
    Barbosa J.A.R.G., Sivaraman J., Li Y., Larocque R., Matte A., Schrag J.D., Cygler M.
    Proc. Natl. Acad. Sci. U.S.A. 99:1859-1864(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS).
    Strain: K12 / MC1061 / ATCC 53338 / DSM 7140.

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: September 3, 2014
This is version 145 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

External Data

Dasty 3

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