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P10370 (HISX_SALTY) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 125. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
Histidinol dehydrogenase

Short name=HDH
EC=1.1.1.23
Gene names
Name:hisD
Ordered Locus Names:STM2072
OrganismSalmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720) [Reference proteome] [HAMAP]
Taxonomic identifier99287 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeSalmonella

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. At high pH manganese can replace zinc. Ref.7

Enzyme regulation

Activity is lost when the metal is removed through urea denaturation or chelation, and can be regained by addition of metal. 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. Ref.5

Sequence similarities

Belongs to the histidinol dehydrogenase family.

Caution

Ref.6 originally reported Cys-117 to be the active site. Ref.4 has shown this to be wrong.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.4
Chain2 – 434433Histidinol dehydrogenase HAMAP-Rule MF_01024
PRO_0000135840

Sites

Active site3261Proton acceptor By similarity
Active site3271Proton acceptor By similarity
Metal binding2591Zinc By similarity
Metal binding2621Zinc Probable
Metal binding3601Zinc By similarity
Metal binding4191Zinc Probable
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

Experimental info

Mutagenesis991H → N: Slight decrease in activity. Ref.8
Mutagenesis1171C → A or S: Almost no change in activity. Ref.4
Mutagenesis1541C → A or S: Almost no change in activity. Ref.4
Mutagenesis2621H → N: 7000-fold decrease in activity. Ref.8
Mutagenesis3271H → N: 500-fold decrease in activity. Ref.8
Mutagenesis3671H → N: Slight decrease in activity. Ref.8
Mutagenesis4191H → Q: 20-fold decrease in activity. Ref.8

Sequences

Sequence LengthMass (Da)Tools
P10370 [UniParc].

Last modified January 23, 2007. Version 3.
Checksum: 744EDDCDAB5DF6CE

FASTA43445,889
        10         20         30         40         50         60 
MSFNTLIDWN SCSPEQQRAL LTRPAISASD SITRTVSDIL DNVKTRGDDA LREYSAKFDK 

        70         80         90        100        110        120 
TEVTALRVTP EEIAAAGARL SDELKQAMTA AVKNIETFHS AQTLPPVDVE TQPGVRCQQV 

       130        140        150        160        170        180 
TRPVSSVGLY IPGGSAPLFS TVLMLATPAR IAGCQKVVLC SPPPIADEIL YAAQLCGVQE 

       190        200        210        220        230        240 
IFNVGGAQAI AALAFGSESV PKVDKIFGPG NAFVTEAKRQ VSQRLDGAAI DMPAGPSEVL 

       250        260        270        280        290        300 
VIADSGATPD FVASDLLSQA EHGPDSQVIL LTPDADIARK VAEAVERQLA ELPRADTARQ 

       310        320        330        340        350        360 
ALSASRLIVT KDLAQCVAIS NQYGPEHLII QTRNARDLVD AITSAGSVFL GDWSPESAGD 

       370        380        390        400        410        420 
YASGTNHVLP TYGYTATCSS LGLADFQKRM TVQELSKAGF 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: LT2.
[2]Barnes W.M., Husson R.N., Whittier R.
Submitted (AUG-1989) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: LT2.
[3]"Complete genome sequence of Salmonella enterica serovar Typhimurium LT2."
McClelland M., Sanderson K.E., Spieth J., Clifton S.W., Latreille P., Courtney L., Porwollik S., Ali J., Dante M., Du F., Hou S., Layman D., Leonard S., Nguyen C., Scott K., Holmes A., Grewal N., Mulvaney E. expand/collapse author list , Ryan E., Sun H., Florea L., Miller W., Stoneking T., Nhan M., Waterston R., Wilson R.K.
Nature 413:852-856(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: LT2 / SGSC1412 / ATCC 700720.
[4]"Conserved cysteine residues of histidinol dehydrogenase are not involved in catalysis. Novel chemistry required for enzymatic aldehyde oxidation."
Teng H., Segura E., Grubmeyer C.
J. Biol. Chem. 268:14182-14188(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 2-15, MUTAGENESIS OF CYS-117 AND CYS-154.
[5]"The catalytically active form of histidinol dehydrogenase from Salmonella typhimurium."
Buerger E., Goerisch H., Lingens F.
Biochem. J. 181:771-774(1979) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBUNIT.
Strain: LT2.
[6]"A cysteine residue (cysteine-116) in the histidinol binding site of histidinol dehydrogenase."
Grubmeyer C.T., Gray W.R.
Biochemistry 25:4778-4784(1986) [PubMed] [Europe PMC] [Abstract]
Cited for: PRELIMINARY ACTIVE SITE.
[7]"L-histidinol dehydrogenase, a Zn2+-metalloenzyme."
Grubmeyer C., Skiadopoulos M., Senior A.E.
Arch. Biochem. Biophys. 272:311-317(1989) [PubMed] [Europe PMC] [Abstract]
Cited for: COFACTOR.
[8]"Mutagenesis of histidinol dehydrogenase reveals roles for conserved histidine residues."
Teng H., Grubmeyer C.
Biochemistry 38:7363-7371(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: MUTAGENESIS OF HIS-99; HIS-262; HIS-327; HIS-367 AND HIS-419.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X13464 Genomic DNA. Translation: CAA31823.1.
J01804 Genomic DNA. Translation: AAA88615.1.
AE006468 Genomic DNA. Translation: AAL20976.1.
PIRDEEBHT. JS0157.
RefSeqNP_461017.1. NC_003197.1.

3D structure databases

ProteinModelPortalP10370.
SMRP10370. Positions 1-434.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING99287.STM2072.

Proteomic databases

PRIDEP10370.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAL20976; AAL20976; STM2072.
GeneID1253593.
KEGGstm:STM2072.
PATRIC32382727. VBISalEnt20916_2194.

Phylogenomic databases

HOGENOMHOG000243914.
KOK00013.
OMAPSEILII.
OrthoDBEOG6CVVCR.
ProtClustDBPRK00877.

Enzyme and pathway databases

BioCycSENT99287:GCTI-2084-MONOMER.
SABIO-RKP10370.
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_SALTY
AccessionPrimary (citable) accession number: P10370
Entry history
Integrated into UniProtKB/Swiss-Prot: July 1, 1989
Last sequence update: January 23, 2007
Last modified: February 19, 2014
This is version 125 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