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Protein

Histidinol dehydrogenase

Gene

hisD

Organism
Salmonella paratyphi A (strain ATCC 9150 / SARB42)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Protein inferred from homologyi

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

Zn2+UniRule annotationNote: Binds 1 zinc ion per subunit.UniRule annotation

Pathway:iL-histidine biosynthesis

This protein is involved in step 9 of the subpathway that synthesizes L-histidine from 5-phospho-alpha-D-ribose 1-diphosphate.UniRule annotation
Proteins known to be involved in the 9 steps of the subpathway in this organism are:
  1. ATP phosphoribosyltransferase (hisG)
  2. no protein annotated in this organism
  3. no protein annotated in this organism
  4. 1-(5-phosphoribosyl)-5-[(5-phosphoribosylamino)methylideneamino] imidazole-4-carboxamide isomerase (hisA)
  5. Imidazole glycerol phosphate synthase subunit HisH (hisH), Imidazole glycerol phosphate synthase subunit HisF (hisF)
  6. Histidine biosynthesis bifunctional protein HisB (hisB)
  7. Histidinol-phosphate aminotransferase (hisC)
  8. Histidine biosynthesis bifunctional protein HisB (hisB)
  9. Histidinol dehydrogenase (hisD)
This subpathway is part of the pathway L-histidine biosynthesis, which is itself part of Amino-acid biosynthesis.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes L-histidine from 5-phospho-alpha-D-ribose 1-diphosphate, the pathway L-histidine biosynthesis and in Amino-acid biosynthesis.

Sites

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

GO - Molecular functioni

GO - Biological processi

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

BioCyciSENT295319:GJBZ-799-MONOMER.
UniPathwayiUPA00031; UER00014.

Names & Taxonomyi

Protein namesi
Recommended name:
Histidinol dehydrogenaseUniRule annotation (EC:1.1.1.23UniRule annotation)
Short name:
HDHUniRule annotation
Gene namesi
Name:hisDUniRule annotation
Ordered Locus Names:SPA0799
OrganismiSalmonella paratyphi A (strain ATCC 9150 / SARB42)
Taxonomic identifieri295319 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeSalmonella
ProteomesiUP000008185 Componenti: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 434434Histidinol dehydrogenasePRO_0000135838Add
BLAST

Interactioni

Subunit structurei

Homodimer.UniRule annotation

Structurei

3D structure databases

ProteinModelPortaliQ5PDP3.
SMRiQ5PDP3. Positions 1-434.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the histidinol dehydrogenase family.UniRule annotation

Phylogenomic databases

eggNOGiCOG0141.
HOGENOMiHOG000243914.
KOiK00013.
OMAiIETFHNA.
OrthoDBiEOG6CVVCR.

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.

Q5PDP3-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSFNTLIDWN SCSPEQQRAL LTRPAISASD SITRTVSDIL YNVKTRGDDV
60 70 80 90 100
LREYSAKFDK TEVTALRVTP EEIAAAGARL SDELKQAMAA AVKNIETFHS
110 120 130 140 150
AQTLPPVDVE TQPGVRCQQV TRPVASVGLY IPGGSAPLFS TVLMLATPAR
160 170 180 190 200
IAGCQKVVLC SPPPIADEIL YAAQLCGVQE IFNVGGAQAI AALAFGSESV
210 220 230 240 250
PKVDKIFGPG NAFVTEAKRQ VSQRLDGAAI DMPAGPSEVL VIADSGATPD
260 270 280 290 300
FVASDLLSQA EHGPDSQVIL LTPDADIARK VAEAVERQLA ELPRADTARQ
310 320 330 340 350
ALSASRLIVT KDLAQCVAIS NQYGPEHLII QTRNARDLVD AITSAGSVFL
360 370 380 390 400
GDWSPESAGD YASGTNHVLP TYGYTATCSS LGLADFQKRM TVQELSKAGF
410 420 430
SALASTIETL AAAERLTAHK NAVTLRVNAL KEQA
Length:434
Mass (Da):45,919
Last modified:January 4, 2005 - v1
Checksum:i9769526495ED567B
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000026 Genomic DNA. Translation: AAV76792.1.
RefSeqiWP_000009630.1. NC_006511.1.
YP_150104.1. NC_006511.1.

Genome annotation databases

EnsemblBacteriaiAAV76792; AAV76792; SPA0799.
KEGGispt:SPA0799.
PATRICi32350802. VBISalEnt134188_0847.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000026 Genomic DNA. Translation: AAV76792.1.
RefSeqiWP_000009630.1. NC_006511.1.
YP_150104.1. NC_006511.1.

3D structure databases

ProteinModelPortaliQ5PDP3.
SMRiQ5PDP3. Positions 1-434.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAV76792; AAV76792; SPA0799.
KEGGispt:SPA0799.
PATRICi32350802. VBISalEnt134188_0847.

Phylogenomic databases

eggNOGiCOG0141.
HOGENOMiHOG000243914.
KOiK00013.
OMAiIETFHNA.
OrthoDBiEOG6CVVCR.

Enzyme and pathway databases

UniPathwayiUPA00031; UER00014.
BioCyciSENT295319:GJBZ-799-MONOMER.

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]
ProtoNetiSearch...

Publicationsi

  1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 9150 / SARB42.

Entry informationi

Entry nameiHISX_SALPA
AccessioniPrimary (citable) accession number: Q5PDP3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 10, 2006
Last sequence update: January 4, 2005
Last modified: July 22, 2015
This is version 75 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome

Documents

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

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.