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Q9XZ43 (5NTD_LUTLO) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 77. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | 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:
Protein 5NUC

Including the following 2 domains:

  1. UDP-sugar hydrolase
    EC=3.6.1.45
    Alternative name(s):
    UDP-sugar diphosphatase
    UDP-sugar pyrophosphatase
  2. 5'-nucleotidase
    Short name=5'-NT
    EC=3.1.3.5
Gene names
Name:5NUC
OrganismLutzomyia longipalpis (Sand fly)
Taxonomic identifier7200 [NCBI]
Taxonomic lineageEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaDipteraNematoceraPsychodoideaPsychodidaeLutzomyiaLutzomyia

Protein attributes

Sequence length572 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Degradation of external UDP-glucose to uridine monophosphate and glucose-1-phosphate, which can then be used by the cell By similarity.

Catalytic activity

UDP-sugar + H2O = UMP + alpha-D-aldose 1-phosphate.

A 5'-ribonucleotide + H2O = a ribonucleoside + phosphate.

Cofactor

Zinc By similarity.

Sequence similarities

Belongs to the 5'-nucleotidase family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2525 Potential
Chain26 – 572547Protein 5NUC
PRO_0000000023

Regions

Region512 – 5187Substrate binding By similarity

Sites

Metal binding391Zinc 1 By similarity
Metal binding411Zinc 1 By similarity
Metal binding931Zinc 1 By similarity
Metal binding931Zinc 2 By similarity
Metal binding1251Zinc 2 By similarity
Metal binding2271Zinc 2 By similarity
Metal binding2501Zinc 2 By similarity
Binding site3611Substrate By similarity
Binding site3991Substrate By similarity
Binding site4041Substrate By similarity
Binding site4271Substrate By similarity
Site1261Transition state stabilizer By similarity
Site1291Transition state stabilizer By similarity

Amino acid modifications

Glycosylation821N-linked (GlcNAc...) Potential
Glycosylation4541N-linked (GlcNAc...) Potential
Glycosylation4901N-linked (GlcNAc...) Potential
Disulfide bond54 ↔ 64 By similarity
Disulfide bond360 ↔ 365 By similarity
Disulfide bond488 ↔ 491 By similarity

Sequences

Sequence LengthMass (Da)Tools
Q9XZ43 [UniParc].

Last modified November 1, 1999. Version 1.
Checksum: 69A652338C04536D

FASTA57263,354
        10         20         30         40         50         60 
MLFFLNFFVL VFSIELALLT ASAAAEDGSY EIIILHTNDM HARFDQTNAG SNKCQEKDKI 

        70         80         90        100        110        120 
ASKCYGGFAR VSTMVKKFRE ENGSSVLFLN AGDTYTGTPW FTLYKETIAT EMMNILRPDA 

       130        140        150        160        170        180 
ASLGNHEFDK GVEGLVPFLN GVTFPILTAN LDTSQEPTMT NAKNLKRSMI FTVSGHRVGV 

       190        200        210        220        230        240 
IGYLTPDTKF LSDVGKVNFI PEVEAINTEA QRLKKEENAE IIIVVGHSGL IKDREIAEKC 

       250        260        270        280        290        300 
PLVDIIVGGH SHTFLYTGSQ PDREVPVDVY PVVVTQSSGK KVPIVQAYCF TKYLGYFKVT 

       310        320        330        340        350        360 
INGKGNVVGW TGQPILLNNN IPQDQEVLTA LEKYRERVEN YGNRVIGVSR VILNGGHTEC 

       370        380        390        400        410        420 
RFHECNMGNL ITDAFVYANV ISTPMSTNAW TDASVVLYQS GGIRAPIDPR TAAGSITRLE 

       430        440        450        460        470        480 
LDNVLPFGNA LYVVKVPGNV LRKALEHSVH RYSNTSGWGE FPQVSGLKIR FNVNEEIGKR 

       490        500        510        520        530        540 
VKSVKVLCSN CSQPEYQPLR NKKTYNVIMD SFMKDGGDGY SMFKPLKIIK TLPLGDIETV 

       550        560        570 
EAYIEKMGPI FPAVEGRITV LGGLQKSDED WH 

« Hide

References

[1]"Toward an understanding of the biochemical and pharmacological complexity of the saliva of a hematophagous sand fly Lutzomyia longipalpis."
Charlab R., Valenzuela J.G., Rowton E.D., Ribeiro J.M.
Proc. Natl. Acad. Sci. U.S.A. 96:15155-15160(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Strain: Jacobina.
Tissue: Salivary gland.
[2]"The salivary 5'-nucleotidase/phosphodiesterase of the hematophagus sand fly, Lutzomyia longipalpis."
Ribeiro J.M.C., Rowton E.D., Charlab R.
Insect Biochem. Mol. Biol. 30:279-285(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: CHARACTERIZATION.
Tissue: Salivary gland.
[3]Erratum
Ribeiro J.M.C., Rowton E.D., Charlab R.
Insect Biochem. Mol. Biol. 30:609-609(2000)

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF132510 mRNA. Translation: AAD32190.1.

3D structure databases

ProteinModelPortalQ9XZ43.
ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Family and domain databases

Gene3D3.60.21.10. 1 hit.
3.90.780.10. 1 hit.
InterProIPR008334. 5'-Nucleotdase_C.
IPR006146. 5'-Nucleotdase_CS.
IPR006179. 5_nucleotidase/apyrase.
IPR004843. Calcineurin-like_PHP_apaH.
IPR029052. Metallo-depent_PP-like.
[Graphical view]
PANTHERPTHR11575. PTHR11575. 1 hit.
PfamPF02872. 5_nucleotid_C. 1 hit.
PF00149. Metallophos. 1 hit.
[Graphical view]
PRINTSPR01607. APYRASEFAMLY.
SUPFAMSSF55816. SSF55816. 1 hit.
SSF56300. SSF56300. 1 hit.
PROSITEPS00785. 5_NUCLEOTIDASE_1. 1 hit.
PS00786. 5_NUCLEOTIDASE_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry name5NTD_LUTLO
AccessionPrimary (citable) accession number: Q9XZ43
Entry history
Integrated into UniProtKB/Swiss-Prot: January 11, 2001
Last sequence update: November 1, 1999
Last modified: June 11, 2014
This is version 77 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)

Relevant documents

SIMILARITY comments

Index of protein domains and families