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Q8X8T3 (HISX_ECO57) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 89. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | 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

Names and origin

Protein namesRecommended name:
Histidinol dehydrogenase

Short name=HDH
EC=1.1.1.23
Gene names
Name:hisD
Ordered Locus Names:Z3182, ECs2821
OrganismEscherichia coli O157:H7 [Complete proteome] [HAMAP]
Taxonomic identifier83334 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia

Protein attributes

Sequence length434 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceInferred from homology

General annotation (Comments)

Function

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

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 By similarity. HAMAP-Rule MF_01024

Sequence similarities

Belongs to the histidinol dehydrogenase family.

Ontologies

Keywords
   Biological processAmino-acid biosynthesis
Histidine biosynthesis
   LigandMetal-binding
NAD
Zinc
   Molecular functionOxidoreductase
   Technical termComplete proteome
Gene Ontology (GO)
   Biological_processhistidine biosynthetic process

Inferred from electronic annotation. Source: UniProtKB-HAMAP

   Molecular_functionNAD binding

Inferred from electronic annotation. Source: InterPro

histidinol dehydrogenase activity

Inferred from electronic annotation. Source: UniProtKB-HAMAP

zinc ion binding

Inferred from electronic annotation. Source: UniProtKB-HAMAP

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed By similarity
Chain2 – 434433Histidinol dehydrogenase HAMAP-Rule MF_01024
PRO_0000135771

Sites

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

Sequences

Sequence LengthMass (Da)Tools
Q8X8T3 [UniParc].

Last modified January 23, 2007. Version 3.
Checksum: A280AE06E39689C8

FASTA43446,074
        10         20         30         40         50         60 
MSFNTIIDWN SCTAKQQRQL LMRPAISASE SITRTVNDIL DSVKARGDDA LREYSAKFDK 

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

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

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

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

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

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

       430 
NAVTLRVNAL KEQA 

« Hide

References

« Hide 'large scale' references
[1]"Analysis of the genes responsible for the O-antigen synthesis in enterohaemorrhagic Escherichia coli O157."
Shimizu T., Yamasaki S., Tsukamoto T., Takeda Y.
Microb. Pathog. 26:235-247(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: O157:H- / 184 / EHEC.
[2]"Genome sequence of enterohaemorrhagic Escherichia coli O157:H7."
Perna N.T., Plunkett G. III, Burland V., Mau B., Glasner J.D., Rose D.J., Mayhew G.F., Evans P.S., Gregor J., Kirkpatrick H.A., Posfai G., Hackett J., Klink S., Boutin A., Shao Y., Miller L., Grotbeck E.J., Davis N.W. expand/collapse author list , Lim A., Dimalanta E.T., Potamousis K., Apodaca J., Anantharaman T.S., Lin J., Yen G., Schwartz D.C., Welch R.A., Blattner F.R.
Nature 409:529-533(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: O157:H7 / EDL933 / ATCC 700927 / EHEC.
[3]"Complete genome sequence of enterohemorrhagic Escherichia coli O157:H7 and genomic comparison with a laboratory strain K-12."
Hayashi T., Makino K., Ohnishi M., Kurokawa K., Ishii K., Yokoyama K., Han C.-G., Ohtsubo E., Nakayama K., Murata T., Tanaka M., Tobe T., Iida T., Takami H., Honda T., Sasakawa C., Ogasawara N., Yasunaga T. expand/collapse author list , Kuhara S., Shiba T., Hattori M., Shinagawa H.
DNA Res. 8:11-22(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: O157:H7 / Sakai / RIMD 0509952 / EHEC.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AB008676 Genomic DNA. Translation: BAA77745.1.
AE005174 Genomic DNA. Translation: AAG57079.1.
BA000007 Genomic DNA. Translation: BAB36244.1.
PIRC85827.
E90981.
RefSeqNP_288525.1. NC_002655.2.
NP_310848.1. NC_002695.1.

3D structure databases

ProteinModelPortalQ8X8T3.
SMRQ8X8T3. Positions 1-434.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING155864.Z3182.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAG57079; AAG57079; Z3182.
BAB36244; BAB36244; BAB36244.
GeneID912702.
962078.
KEGGece:Z3182.
ecs:ECs2821.
PATRIC18355030. VBIEscCol44059_2716.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0141.
HOGENOMHOG000243914.
KOK00013.
OMAYAAKLCG.
OrthoDBEOG6CVVCR.

Enzyme and pathway databases

BioCycECOL386585:GJFA-2785-MONOMER.
ECOO157:HISD-MONOMER.
UniPathwayUPA00031; UER00014.

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. SSF53720. 1 hit.
TIGRFAMsTIGR00069. hisD. 1 hit.
PROSITEPS00611. HISOL_DEHYDROGENASE. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameHISX_ECO57
AccessionPrimary (citable) accession number: Q8X8T3
Secondary accession number(s): Q9WX45
Entry history
Integrated into UniProtKB/Swiss-Prot: March 25, 2003
Last sequence update: January 23, 2007
Last modified: May 14, 2014
This is version 89 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways