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P10370

- HISX_SALTY

UniProt

P10370 - HISX_SALTY

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Protein

Histidinol dehydrogenase

Gene
hisD, STM2072
Organism
Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)
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. At high pH manganese can replace zinc.1 Publication

Enzyme regulationi

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

Pathwayi

Sites

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

GO - Molecular functioni

  1. histidinol dehydrogenase activity Source: UniProtKB-HAMAP
  2. NAD binding Source: InterPro
  3. zinc ion binding Source: UniProtKB-HAMAP

GO - Biological processi

  1. histidine biosynthetic process Source: UniProtKB-HAMAP
Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Biological processi

Amino-acid biosynthesis, Histidine biosynthesis

Keywords - Ligandi

Manganese, Metal-binding, NAD, Zinc

Enzyme and pathway databases

BioCyciSENT99287:GCTI-2084-MONOMER.
SABIO-RKP10370.
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:STM2072
OrganismiSalmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)
Taxonomic identifieri99287 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeSalmonella
ProteomesiUP000001014: Chromosome

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi99 – 991H → N: Slight decrease in activity. 1 Publication
Mutagenesisi117 – 1171C → A or S: Almost no change in activity. 1 Publication
Mutagenesisi154 – 1541C → A or S: Almost no change in activity. 1 Publication
Mutagenesisi262 – 2621H → N: 7000-fold decrease in activity. 1 Publication
Mutagenesisi327 – 3271H → N: 500-fold decrease in activity. 1 Publication
Mutagenesisi367 – 3671H → N: Slight decrease in activity. 1 Publication
Mutagenesisi419 – 4191H → Q: 20-fold decrease in activity. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed1 Publication
Chaini2 – 434433Histidinol dehydrogenaseUniRule annotationPRO_0000135840Add
BLAST

Proteomic databases

PRIDEiP10370.

Interactioni

Subunit structurei

Homodimer.1 Publication

Protein-protein interaction databases

STRINGi99287.STM2072.

Structurei

3D structure databases

ProteinModelPortaliP10370.
SMRiP10370. Positions 1-434.

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

HOGENOMiHOG000243914.
KOiK00013.
OMAiYAAKLCG.
OrthoDBiEOG6CVVCR.
PhylomeDBiP10370.

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.

P10370-1 [UniParc]FASTAAdd to Basket

« Hide

MSFNTLIDWN SCSPEQQRAL LTRPAISASD SITRTVSDIL DNVKTRGDDA    50
LREYSAKFDK TEVTALRVTP EEIAAAGARL SDELKQAMTA AVKNIETFHS 100
AQTLPPVDVE TQPGVRCQQV TRPVSSVGLY IPGGSAPLFS TVLMLATPAR 150
IAGCQKVVLC SPPPIADEIL YAAQLCGVQE IFNVGGAQAI AALAFGSESV 200
PKVDKIFGPG NAFVTEAKRQ VSQRLDGAAI DMPAGPSEVL VIADSGATPD 250
FVASDLLSQA EHGPDSQVIL LTPDADIARK VAEAVERQLA ELPRADTARQ 300
ALSASRLIVT KDLAQCVAIS NQYGPEHLII QTRNARDLVD AITSAGSVFL 350
GDWSPESAGD YASGTNHVLP TYGYTATCSS LGLADFQKRM TVQELSKAGF 400
SALASTIETL AAAERLTAHK NAVTLRVNAL KEQA 434
Length:434
Mass (Da):45,889
Last modified:January 23, 2007 - v3
Checksum:i744EDDCDAB5DF6CE
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
X13464 Genomic DNA. Translation: CAA31823.1.
J01804 Genomic DNA. Translation: AAA88615.1.
AE006468 Genomic DNA. Translation: AAL20976.1.
PIRiJS0157. DEEBHT.
RefSeqiNP_461017.1. NC_003197.1.

Genome annotation databases

EnsemblBacteriaiAAL20976; AAL20976; STM2072.
GeneIDi1253593.
KEGGistm:STM2072.
PATRICi32382727. VBISalEnt20916_2194.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
X13464 Genomic DNA. Translation: CAA31823.1 .
J01804 Genomic DNA. Translation: AAA88615.1 .
AE006468 Genomic DNA. Translation: AAL20976.1 .
PIRi JS0157. DEEBHT.
RefSeqi NP_461017.1. NC_003197.1.

3D structure databases

ProteinModelPortali P10370.
SMRi P10370. Positions 1-434.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 99287.STM2072.

Proteomic databases

PRIDEi P10370.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai AAL20976 ; AAL20976 ; STM2072 .
GeneIDi 1253593.
KEGGi stm:STM2072.
PATRICi 32382727. VBISalEnt20916_2194.

Phylogenomic databases

HOGENOMi HOG000243914.
KOi K00013.
OMAi YAAKLCG.
OrthoDBi EOG6CVVCR.
PhylomeDBi P10370.

Enzyme and pathway databases

UniPathwayi UPA00031 ; UER00014 .
BioCyci SENT99287:GCTI-2084-MONOMER.
SABIO-RK P10370.

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: 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. 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. 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.

Entry informationi

Entry nameiHISX_SALTY
AccessioniPrimary (citable) accession number: P10370
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 1, 1989
Last sequence update: January 23, 2007
Last modified: July 9, 2014
This is version 127 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Caution

1 Publication originally reported Cys-117 to be the active site. 1 Publication has shown this to be wrong.

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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