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P06988 (HISX_ECOLI) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 135. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Histidinol dehydrogenase
Short name=HDH
EC=1.1.1.23
Gene names
Name:hisD
Ordered Locus Names:b2020, JW2002
OrganismEscherichia coli (strain K12) [Reference proteome] [HAMAP]
Taxonomic identifier83333 [NCBI]
Taxonomic lineageBacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia ›

Protein attributes

Sequence length434 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Catalyzes the sequential NAD-dependent oxidations of L-histidinol to L-histidinaldehyde and then to L-histidine. HAMAP-Rule MF_01024

Catalytic activity

L-histidinol + H2O + 2 NAD+ = L-histidine + 2 NADH. HAMAP-Rule MF_01024

Cofactor

Binds 1 zinc ion per subunit.

Pathway

Amino-acid biosynthesis; L-histidine biosynthesis; L-histidine from 5-phospho-alpha-D-ribose 1-diphosphate: step 9/9. HAMAP-Rule MF_01024

Subunit structure

Homodimer.

Sequence similarities

Belongs to the histidinol dehydrogenase family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.8
Chain2 – 434433Histidinol dehydrogenase HAMAP-Rule MF_01024
PRO_0000135770

Sites

Active site3261Proton acceptor
Active site3271Proton acceptor
Metal binding2591Zinc
Metal binding2621Zinc
Metal binding3601Zinc
Metal binding4191Zinc
Binding site1301NAD
Binding site1881NAD
Binding site2111NAD
Binding site2371Substrate
Binding site2591Substrate
Binding site2621Substrate
Binding site3271Substrate
Binding site3601Substrate
Binding site4141Substrate
Binding site4191Substrate

Experimental info

Sequence conflict151E → V Ref.1
Sequence conflict151E → V Ref.2
Sequence conflict221M → T in CAA27610. Ref.2
Sequence conflict1501S → R Ref.1
Sequence conflict1501S → R Ref.2
Sequence conflict1571V → A in CAA36882. Ref.3
Sequence conflict3131L → S Ref.1
Sequence conflict3131L → S Ref.2
Sequence conflict4031L → V Ref.1
Sequence conflict4031L → V Ref.2

Secondary structure

1 .............................................................................. 434
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P06988 [UniParc].

Last modified January 23, 2007. Version 5.
Checksum: 4B4F2EA00C9BEA4E

FASTA43446,110
        10         20         30         40         50         60 
MSFNTIIDWN SCTAEQQRQL LMRPAISASE SITRTVNDIL DNVKARGDEA LREYSAKFDK 

        70         80         90        100        110        120 
TTVTALKVSA EEIAAASERL SDELKQAMAV AVKNIETFHT AQKLPPVDVE TQPGVRCQQV 

       130        140        150        160        170        180 
TRPVASVGLY IPGGSAPLFS TVLMLATPAS IAGCKKVVLC SPPPIADEIL YAAQLCGVQD 

       190        200        210        220        230        240 
VFNVGGAQAI AALAFGTESV PKVDKIFGPG NAFVTEAKRQ VSQRLDGAAI DMPAGPSEVL 

       250        260        270        280        290        300 
VIADSGATPD FVASDLLSQA EHGPDSQVIL LTPAADMARR VAEAVERQLA ELPRAETARQ 

       310        320        330        340        350        360 
ALNASRLIVT KDLAQCVEIS NQYGPEHLII QTRNARELVD SITSAGSVFL GDWSPESAGD 

       370        380        390        400        410        420 
YASGTNHVLP TYGYTATCSS LGLADFQKRM TVQELSKEGF SALASTIETL AAAERLTAHK 

       430 
NAVTLRVNAL KEQA

« Hide

References

« Hide 'large scale' references
[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]"A 460-kb DNA sequence of the Escherichia coli K-12 genome corresponding to the 40.1-50.0 min region on the linkage map."
Itoh T., Aiba H., Baba T., Fujita K., Hayashi K., Inada T., Isono K., Kasai H., Kimura S., Kitakawa M., Kitagawa M., Makino K., Miki T., Mizobuchi K., Mori H., Mori T., Motomura K., Nakade S. expand/collapse author list , Nakamura Y., Nashimoto H., Nishio Y., Oshima T., Saito N., Sampei G., Seki Y., Sivasundaram S., Tagami H., Takeda J., Takemoto K., Wada C., Yamamoto Y., Horiuchi T.
DNA Res. 3:379-392(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[5]"The complete genome sequence of Escherichia coli K-12."
Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V., Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F., Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B., Shao Y.
Science 277:1453-1474(1997) [PubMed] [Europe PMC] [Abstract]
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.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		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.
PIRDEECHT. C64967.
RefSeqNP_416524.1. NC_000913.2.
YP_490263.1. NC_007779.1.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1K75X-ray1.75A/B1-434[»]
1KAEX-ray1.70A/B1-434[»]
1KAHX-ray2.10A/B1-434[»]
1KARX-ray2.10A/B1-434[»]
ProteinModelPortalP06988.
SMRP06988. Positions 1-434.
ModBaseSearch...

Protein-protein interaction databases

IntActP06988. 6 interactions.
STRING511145.b2020.

2D gel databases

SWISS-2DPAGEP06988.

Proteomic databases

PaxDbP06988.
PRIDEP06988.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAC75081; AAC75081; b2020.
BAA15851; BAA15851; BAA15851.
GeneID12931409.
946531.
KEGGecj:Y75_p1983.
eco:b2020.
PATRIC32119375. VBIEscCol129921_2097.

Organism-specific databases

EchoBASEEB0442.
EcoGeneEG10447. hisD.

Phylogenomic databases

eggNOGCOG0141.
HOGENOMHOG000243914.
KOK00013.
OMAPTYGYSR.
ProtClustDBPRK00877.

Enzyme and pathway databases

BioCycEcoCyc:HISTDEHYD-MONOMER.
ECOL316407:JW2002-MONOMER.
MetaCyc:HISTDEHYD-MONOMER.
UniPathwayUPA00031; UER00014.

Gene expression databases

GenevestigatorP06988.

Family and domain databases

HAMAPMF_01024. HisD.
InterProIPR016161. Ald_DH/histidinol_DH.
IPR001692. Histidinol_DH_CS.
IPR022695. Histidinol_DH_monofunct.
IPR012131. Hstdl_DH.
[Graphical view]
PfamPF00815. Histidinol_dh. 1 hit.
[Graphical view]
PIRSFPIRSF000099. Histidinol_dh. 1 hit.
PRINTSPR00083. HOLDHDRGNASE.
SUPFAMSSF53720. Aldehyde_DH/Histidinol_DH. 1 hit.
TIGRFAMsTIGR00069. hisD. 1 hit.
PROSITEPS00611. HISOL_DEHYDROGENASE. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP06988.

Entry information

Entry nameHISX_ECOLI
AccessionPrimary (citable) accession number: P06988
Secondary accession number(s): O08506, P78076, Q47254
Entry history
Integrated into UniProtKB/Swiss-Prot: April 1, 1988
Last sequence update: January 23, 2007
Last modified: May 1, 2013
This is version 135 of the entry and version 5 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

Escherichia coli

Escherichia coli (strain K12): entries and cross-references to EcoGene

PATHWAY comments

Index of metabolic and biosynthesis pathways

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents