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

Names and origin

Protein names

Recommended name:
    Protein 5NUC
Including the following 2 domains:
    1- Recommended name:
            UDP-sugar hydrolase
              EC=3.6.1.45
        Alternative name(s):
            UDP-sugar pyrophosphatase
            UDP-sugar diphosphatase
    2- Recommended name:
            5'-nucleotidase
                Short name=5'-NT
              EC=3.1.3.5

Gene names

Name:

5NUC

Organism

Lutzomyia longipalpis (Sand fly)

Taxonomic identifier

7200 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Arthropoda › Hexapoda › Insecta › Pterygota › Neoptera › Endopterygota › Diptera › Nematocera › Psychodoidea › Psychodidae › Lutzomyia › Lutzomyia

Protein attributes

Sequence length	572 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence 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.

Ontologies

Keywords
Domain	Signal
Ligand	Metal-binding Nucleotide-binding Zinc
Molecular function	Hydrolase
PTM	Glycoprotein
Gene Ontology (GO)
Biological process	nucleotide catabolic process Inferred from electronic annotation. Source: InterPro
Molecular function	5'-nucleotidase activity Inferred from electronic annotation. Source: EC UDP-sugar diphosphatase activity Inferred from electronic annotation. Source: EC nucleotide binding Inferred from electronic annotation. Source: UniProtKB-KW zinc ion binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Signal peptide	1 – 25	25	Potential
	Chain	26 – 572	547	Protein 5NUC		PRO_0000000023
Regions
	Region	512 – 518	7	Substrate binding By similarity
Sites
	Metal binding	39	1	Zinc 1 By similarity
	Metal binding	41	1	Zinc 1 By similarity
	Metal binding	93	1	Zinc 1 By similarity
	Metal binding	93	1	Zinc 2 By similarity
	Metal binding	125	1	Zinc 2 By similarity
	Metal binding	227	1	Zinc 2 By similarity
	Metal binding	250	1	Zinc 2 By similarity
	Binding site	427	1	Substrate By similarity
	Site	126	1	Transition state stabilizer By similarity
	Site	129	1	Transition state stabilizer By similarity
Amino acid modifications
	Glycosylation	82	1	N-linked (GlcNAc...) Potential
	Glycosylation	454	1	N-linked (GlcNAc...) Potential
	Glycosylation	490	1	N-linked (GlcNAc...) Potential

Sequences

	Sequence		Length	Mass (Da)
	Q9XZ43-1 [UniParc]. Last modified November 1, 1999. Version 1. Checksum: 69A652338C04536D	FASTA	572	63,354
	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

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: 10611354] [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: 10727894] [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
ModBase	Search...
Enzyme and pathway databases
BRENDA	3.1.3.5. 274802. 3.6.1.45. 274802.
Family and domain databases
InterPro	IPR008334. 5'-Nucleotdase_C. IPR006146. 5'-Nucleotdase_CS. IPR006179. 5_nucleotidase/apyrase. IPR004843. M-pesterase. [Graphical view]
Gene3D	G3DSA:3.90.780.10. 5'-Nucleotdase_C. 1 hit.
PANTHER	PTHR11575. 5_nucleotidase. 1 hit.
Pfam	PF02872. 5_nucleotid_C. 1 hit. PF00149. Metallophos. 1 hit. [Graphical view]
PRINTS	PR01607. APYRASEFAMLY.
PROSITE	PS00785. 5_NUCLEOTIDASE_1. 1 hit. PS00786. 5_NUCLEOTIDASE_2. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

5NTD_LUTLO

Accession

Primary (citable) accession number: Q9XZ43

Entry history

Integrated into UniProtKB/Swiss-Prot:	January 11, 2001
Last sequence update:	November 1, 1999
Last modified:	November 24, 2009
This is version 59 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)