Skip Header

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

Protein 5NUC

Gene

5NUC

Organism
Lutzomyia longipalpis (Sand fly)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at protein leveli

Functioni

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

Catalytic activityi

UDP-sugar + H2O = UMP + alpha-D-aldose 1-phosphate.
A 5'-ribonucleotide + H2O = a ribonucleoside + phosphate.

Cofactori

Zn2+By similarity

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi39 – 391Zinc 1By similarity
Metal bindingi41 – 411Zinc 1By similarity
Metal bindingi93 – 931Zinc 1By similarity
Metal bindingi93 – 931Zinc 2By similarity
Metal bindingi125 – 1251Zinc 2By similarity
Sitei126 – 1261Transition state stabilizerBy similarity
Sitei129 – 1291Transition state stabilizerBy similarity
Metal bindingi227 – 2271Zinc 2By similarity
Metal bindingi250 – 2501Zinc 2By similarity
Binding sitei361 – 3611SubstrateBy similarity
Binding sitei399 – 3991SubstrateBy similarity
Binding sitei404 – 4041SubstrateBy similarity
Binding sitei427 – 4271SubstrateBy similarity

GO - Molecular functioni

  1. 5'-nucleotidase activity Source: UniProtKB-EC
  2. metal ion binding Source: UniProtKB-KW
  3. nucleotide binding Source: UniProtKB-KW
  4. UDP-sugar diphosphatase activity Source: UniProtKB-EC

GO - Biological processi

  1. nucleotide catabolic process Source: InterPro
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase

Keywords - Ligandi

Metal-binding, Nucleotide-binding, Zinc

Names & Taxonomyi

Protein namesi
Recommended name:
Protein 5NUC
Including the following 2 domains:
UDP-sugar hydrolase (EC:3.6.1.45)
Alternative name(s):
UDP-sugar diphosphatase
UDP-sugar pyrophosphatase
5'-nucleotidase (EC:3.1.3.5)
Short name:
5'-NT
Gene namesi
Name:5NUC
OrganismiLutzomyia longipalpis (Sand fly)
Taxonomic identifieri7200 [NCBI]
Taxonomic lineageiEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaDipteraNematoceraPsychodoideaPsychodidaeLutzomyiaLutzomyia

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2525Sequence AnalysisAdd
BLAST
Chaini26 – 572547Protein 5NUCPRO_0000000023Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi54 ↔ 64By similarity
Glycosylationi82 – 821N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi360 ↔ 365By similarity
Glycosylationi454 – 4541N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi488 ↔ 491By similarity
Glycosylationi490 – 4901N-linked (GlcNAc...)Sequence Analysis

Keywords - PTMi

Disulfide bond, Glycoprotein

Structurei

3D structure databases

ProteinModelPortaliQ9XZ43.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni512 – 5187Substrate bindingBy similarity

Sequence similaritiesi

Belongs to the 5'-nucleotidase family.Curated

Keywords - Domaini

Signal

Family and domain databases

Gene3Di3.60.21.10. 1 hit.
3.90.780.10. 1 hit.
InterProiIPR008334. 5'-Nucleotdase_C.
IPR006146. 5'-Nucleotdase_CS.
IPR006179. 5_nucleotidase/apyrase.
IPR004843. Calcineurin-like_PHP_apaH.
IPR029052. Metallo-depent_PP-like.
[Graphical view]
PANTHERiPTHR11575. PTHR11575. 1 hit.
PfamiPF02872. 5_nucleotid_C. 1 hit.
PF00149. Metallophos. 1 hit.
[Graphical view]
PRINTSiPR01607. APYRASEFAMLY.
SUPFAMiSSF55816. SSF55816. 1 hit.
SSF56300. SSF56300. 1 hit.
PROSITEiPS00785. 5_NUCLEOTIDASE_1. 1 hit.
PS00786. 5_NUCLEOTIDASE_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q9XZ43-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MLFFLNFFVL VFSIELALLT ASAAAEDGSY EIIILHTNDM HARFDQTNAG
60 70 80 90 100
SNKCQEKDKI ASKCYGGFAR VSTMVKKFRE ENGSSVLFLN AGDTYTGTPW
110 120 130 140 150
FTLYKETIAT EMMNILRPDA ASLGNHEFDK GVEGLVPFLN GVTFPILTAN
160 170 180 190 200
LDTSQEPTMT NAKNLKRSMI FTVSGHRVGV IGYLTPDTKF LSDVGKVNFI
210 220 230 240 250
PEVEAINTEA QRLKKEENAE IIIVVGHSGL IKDREIAEKC PLVDIIVGGH
260 270 280 290 300
SHTFLYTGSQ PDREVPVDVY PVVVTQSSGK KVPIVQAYCF TKYLGYFKVT
310 320 330 340 350
INGKGNVVGW TGQPILLNNN IPQDQEVLTA LEKYRERVEN YGNRVIGVSR
360 370 380 390 400
VILNGGHTEC RFHECNMGNL ITDAFVYANV ISTPMSTNAW TDASVVLYQS
410 420 430 440 450
GGIRAPIDPR TAAGSITRLE LDNVLPFGNA LYVVKVPGNV LRKALEHSVH
460 470 480 490 500
RYSNTSGWGE FPQVSGLKIR FNVNEEIGKR VKSVKVLCSN CSQPEYQPLR
510 520 530 540 550
NKKTYNVIMD SFMKDGGDGY SMFKPLKIIK TLPLGDIETV EAYIEKMGPI
560 570
FPAVEGRITV LGGLQKSDED WH
Length:572
Mass (Da):63,354
Last modified:November 1, 1999 - v1
Checksum:i69A652338C04536D
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF132510 mRNA. Translation: AAD32190.1.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF132510 mRNA. Translation: AAD32190.1.

3D structure databases

ProteinModelPortaliQ9XZ43.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Family and domain databases

Gene3Di3.60.21.10. 1 hit.
3.90.780.10. 1 hit.
InterProiIPR008334. 5'-Nucleotdase_C.
IPR006146. 5'-Nucleotdase_CS.
IPR006179. 5_nucleotidase/apyrase.
IPR004843. Calcineurin-like_PHP_apaH.
IPR029052. Metallo-depent_PP-like.
[Graphical view]
PANTHERiPTHR11575. PTHR11575. 1 hit.
PfamiPF02872. 5_nucleotid_C. 1 hit.
PF00149. Metallophos. 1 hit.
[Graphical view]
PRINTSiPR01607. APYRASEFAMLY.
SUPFAMiSSF55816. SSF55816. 1 hit.
SSF56300. SSF56300. 1 hit.
PROSITEiPS00785. 5_NUCLEOTIDASE_1. 1 hit.
PS00786. 5_NUCLEOTIDASE_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  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(1998) [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(1999) [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(1999)

Entry informationi

Entry namei5NTD_LUTLO
AccessioniPrimary (citable) accession number: Q9XZ43
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 11, 2001
Last sequence update: November 1, 1999
Last modified: November 26, 2014
This is version 79 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)

Miscellaneousi

Documents

  1. 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.