5NTD_LUTLO
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 03-AUG-2022, entry version 97.
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 VEuPathDB; VectorBase:LLOJ009119; -.
DR Proteomes; UP000092461; Unassembled WGS sequence.
DR GO; GO:0110165; C:cellular anatomical entity; IEA:UniProt.
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 Gene3D; 3.60.21.10; -; 1.
DR Gene3D; 3.90.780.10; -; 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; PTHR11575; 1.
DR Pfam; PF02872; 5_nucleotid_C; 1.
DR Pfam; PF00149; Metallophos; 1.
DR PRINTS; PR01607; APYRASEFAMLY.
DR SUPFAM; SSF55816; SSF55816; 1.
DR SUPFAM; SSF56300; SSF56300; 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
