ID   5NTD_LUTLO              Reviewed;         572 AA.
AC   Q9XZ43;
DT   11-JAN-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1999, sequence version 1.
DT   27-MAR-2024, entry version 100.
DE   RecName: Full=Protein 5NUC;
DE   Includes:
DE     RecName: Full=UDP-sugar hydrolase;
DE              EC=3.6.1.45;
DE     AltName: Full=UDP-sugar diphosphatase;
DE     AltName: Full=UDP-sugar pyrophosphatase;
DE   Includes:
DE     RecName: Full=5'-nucleotidase;
DE              Short=5'-NT;
DE              EC=3.1.3.5;
DE   Flags: Precursor;
GN   Name=5NUC;
OS   Lutzomyia longipalpis (Sand fly).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Diptera; Nematocera; Psychodoidea; Psychodidae;
OC   Lutzomyia; Lutzomyia.
OX   NCBI_TaxID=7200;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=Jacobina; TISSUE=Salivary gland;
RX   PubMed=10611354; DOI=10.1073/pnas.96.26.15155;
RA   Charlab R., Valenzuela J.G., Rowton E.D., Ribeiro J.M.;
RT   "Toward an understanding of the biochemical and pharmacological complexity
RT   of the saliva of a hematophagous sand fly Lutzomyia longipalpis.";
RL   Proc. Natl. Acad. Sci. U.S.A. 96:15155-15160(1999).
RN   [2]
RP   CHARACTERIZATION.
RC   TISSUE=Salivary gland;
RX   PubMed=10727894; DOI=10.1016/s0965-1748(99)00123-x;
RA   Ribeiro J.M.C., Rowton E.D., Charlab R.;
RT   "The salivary 5'-nucleotidase/phosphodiesterase of the hematophagus sand
RT   fly, Lutzomyia longipalpis.";
RL   Insect Biochem. Mol. Biol. 30:279-285(2000).
RN   [3]
RP   ERRATUM OF PUBMED:10727894.
RA   Ribeiro J.M.C., Rowton E.D., Charlab R.;
RL   Insect Biochem. Mol. Biol. 30:609-609(2000).
CC   -!- FUNCTION: Degradation of external UDP-glucose to uridine monophosphate
CC       and glucose-1-phosphate, which can then be used by the cell.
CC       {ECO:0000250}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=UDP-sugar + H2O = UMP + alpha-D-aldose 1-phosphate.;
CC         EC=3.6.1.45;
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a ribonucleoside 5'-phosphate + H2O = a ribonucleoside +
CC         phosphate; Xref=Rhea:RHEA:12484, ChEBI:CHEBI:15377,
CC         ChEBI:CHEBI:18254, ChEBI:CHEBI:43474, ChEBI:CHEBI:58043; EC=3.1.3.5;
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250};
CC   -!- SIMILARITY: Belongs to the 5'-nucleotidase family. {ECO:0000305}.
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DR   EMBL; AF132510; AAD32190.1; -; mRNA.
DR   AlphaFoldDB; Q9XZ43; -.
DR   SMR; Q9XZ43; -.
DR   GlyCosmos; Q9XZ43; 3 sites, No reported glycans.
DR   VEuPathDB; VectorBase:LLOJ009119; -.
DR   Proteomes; UP000092461; Unassembled WGS sequence.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0000166; F:nucleotide binding; IEA:UniProtKB-KW.
DR   GO; GO:0008768; F:UDP-sugar diphosphatase activity; IEA:UniProtKB-EC.
DR   GO; GO:0106411; F:XMP 5'-nucleosidase activity; IEA:UniProtKB-EC.
DR   GO; GO:0009166; P:nucleotide catabolic process; IEA:InterPro.
DR   CDD; cd07409; MPP_CD73_N; 1.
DR   Gene3D; 3.60.21.10; -; 1.
DR   Gene3D; 3.90.780.10; 5'-Nucleotidase, C-terminal domain; 1.
DR   InterPro; IPR008334; 5'-Nucleotdase_C.
DR   InterPro; IPR036907; 5'-Nucleotdase_C_sf.
DR   InterPro; IPR006146; 5'-Nucleotdase_CS.
DR   InterPro; IPR006179; 5_nucleotidase/apyrase.
DR   InterPro; IPR004843; Calcineurin-like_PHP_ApaH.
DR   InterPro; IPR029052; Metallo-depent_PP-like.
DR   PANTHER; PTHR11575; 5'-NUCLEOTIDASE-RELATED; 1.
DR   PANTHER; PTHR11575:SF51; ECTO-5'-NUCLEOTIDASE 2, ISOFORM A-RELATED; 1.
DR   Pfam; PF02872; 5_nucleotid_C; 1.
DR   Pfam; PF00149; Metallophos; 1.
DR   PRINTS; PR01607; APYRASEFAMLY.
DR   SUPFAM; SSF55816; 5'-nucleotidase (syn. UDP-sugar hydrolase), C-terminal domain; 1.
DR   SUPFAM; SSF56300; Metallo-dependent phosphatases; 1.
DR   PROSITE; PS00785; 5_NUCLEOTIDASE_1; 1.
DR   PROSITE; PS00786; 5_NUCLEOTIDASE_2; 1.
PE   1: Evidence at protein level;
KW   Disulfide bond; Glycoprotein; Hydrolase; Metal-binding; Nucleotide-binding;
KW   Signal; Zinc.
FT   SIGNAL          1..25
FT                   /evidence="ECO:0000255"
FT   CHAIN           26..572
FT                   /note="Protein 5NUC"
FT                   /id="PRO_0000000023"
FT   BINDING         39
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
FT   BINDING         41
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
FT   BINDING         93
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
FT   BINDING         93
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
FT   BINDING         125
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
FT   BINDING         227
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
FT   BINDING         250
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
FT   BINDING         361
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         399
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         404
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         427
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         512..518
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   SITE            126
FT                   /note="Transition state stabilizer"
FT                   /evidence="ECO:0000250"
FT   SITE            129
FT                   /note="Transition state stabilizer"
FT                   /evidence="ECO:0000250"
FT   CARBOHYD        82
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        454
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        490
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        54..64
FT                   /evidence="ECO:0000250"
FT   DISULFID        360..365
FT                   /evidence="ECO:0000250"
FT   DISULFID        488..491
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   572 AA;  63354 MW;  69A652338C04536D CRC64;
     MLFFLNFFVL VFSIELALLT ASAAAEDGSY EIIILHTNDM HARFDQTNAG SNKCQEKDKI
     ASKCYGGFAR VSTMVKKFRE ENGSSVLFLN AGDTYTGTPW FTLYKETIAT EMMNILRPDA
     ASLGNHEFDK GVEGLVPFLN GVTFPILTAN LDTSQEPTMT NAKNLKRSMI FTVSGHRVGV
     IGYLTPDTKF LSDVGKVNFI PEVEAINTEA QRLKKEENAE IIIVVGHSGL IKDREIAEKC
     PLVDIIVGGH SHTFLYTGSQ PDREVPVDVY PVVVTQSSGK KVPIVQAYCF TKYLGYFKVT
     INGKGNVVGW TGQPILLNNN IPQDQEVLTA LEKYRERVEN YGNRVIGVSR VILNGGHTEC
     RFHECNMGNL ITDAFVYANV ISTPMSTNAW TDASVVLYQS GGIRAPIDPR TAAGSITRLE
     LDNVLPFGNA LYVVKVPGNV LRKALEHSVH RYSNTSGWGE FPQVSGLKIR FNVNEEIGKR
     VKSVKVLCSN CSQPEYQPLR NKKTYNVIMD SFMKDGGDGY SMFKPLKIIK TLPLGDIETV
     EAYIEKMGPI FPAVEGRITV LGGLQKSDED WH
//