Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

Q57MS3

- HISX_SALCH

UniProt

Q57MS3 - HISX_SALCH

(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Protein

Histidinol dehydrogenase

Gene

hisD

Organism
Salmonella choleraesuis (strain SC-B67)
Status
Reviewed - 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

Binds 1 zinc ion per subunit.UniRule annotation

Pathwayi

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

  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

Metal-binding, NAD, Zinc

Enzyme and pathway databases

BioCyciSENT321314:GJCS-2178-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:SCH_2082
OrganismiSalmonella choleraesuis (strain SC-B67)
Taxonomic identifieri321314 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeSalmonella
ProteomesiUP000000538: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 434434Histidinol dehydrogenasePRO_0000135836Add
BLAST

Proteomic databases

PaxDbiQ57MS3.
PRIDEiQ57MS3.

Interactioni

Subunit structurei

Homodimer.UniRule annotation

Protein-protein interaction databases

STRINGi321314.SC2082.

Structurei

3D structure databases

ProteinModelPortaliQ57MS3.
SMRiQ57MS3. Positions 1-434.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the histidinol dehydrogenase family.UniRule annotation

Phylogenomic databases

eggNOGiCOG0141.
OMAiYAAKLCG.
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.

Q57MS3 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MSFNTLINWN SCSPEQQRAL LTRPAISASD SITRTVSDIL DNVKTRGDDA
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
IAGCQNVVLC 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):45,828
Last modified:May 10, 2005 - v1
Checksum:iEBE439C77A42BCC9
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AE017220 Genomic DNA. Translation: AAX65988.1.
RefSeqiYP_217069.1. NC_006905.1.

Genome annotation databases

EnsemblBacteriaiAAX65988; AAX65988; SCH_2082.
PATRICi32325089. VBISalEnt136302_2523.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AE017220 Genomic DNA. Translation: AAX65988.1 .
RefSeqi YP_217069.1. NC_006905.1.

3D structure databases

ProteinModelPortali Q57MS3.
SMRi Q57MS3. Positions 1-434.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 321314.SC2082.

Proteomic databases

PaxDbi Q57MS3.
PRIDEi Q57MS3.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai AAX65988 ; AAX65988 ; SCH_2082 .
PATRICi 32325089. VBISalEnt136302_2523.

Phylogenomic databases

eggNOGi COG0141.
OMAi YAAKLCG.
OrthoDBi EOG6CVVCR.

Enzyme and pathway databases

UniPathwayi UPA00031 ; UER00014 .
BioCyci SENT321314:GJCS-2178-MONOMER.

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

  1. "The genome sequence of Salmonella enterica serovar Choleraesuis, a highly invasive and resistant zoonotic pathogen."
    Chiu C.-H., Tang P., Chu C., Hu S., Bao Q., Yu J., Chou Y.-Y., Wang H.-S., Lee Y.-S.
    Nucleic Acids Res. 33:1690-1698(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: SC-B67.

Entry informationi

Entry nameiHISX_SALCH
AccessioniPrimary (citable) accession number: Q57MS3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 10, 2006
Last sequence update: May 10, 2005
Last modified: October 1, 2014
This is version 70 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