ID 5NTD_VIBPA Reviewed; 560 AA. AC P22848; DT 01-AUG-1991, integrated into UniProtKB/Swiss-Prot. DT 04-APR-2003, sequence version 2. DT 02-SEP-2026, entry version 164. DE RecName: Full=5'-nucleotidase; DE EC=3.1.3.5; DE Flags: Precursor; GN Name=nutA; OrderedLocusNames=VP0748; OS Vibrio parahaemolyticus serotype O3:K6 (strain RIMD 2210633). OC Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria; Vibrionales; OC Vibrionaceae; Vibrio. OX NCBI_TaxID=223926; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=AQ3334; RX PubMed=2016269; DOI=10.1093/oxfordjournals.jbchem.a123345; RA Tamao Y., Noguchi K., Sakai-Tomita Y., Hama H., Shimamoto T., Kanazawa H., RA Tsuda M., Tsuchiya T.; RT "Sequence analysis of nutA gene encoding membrane-bound Cl(-)-dependent 5'- RT nucleotidase of Vibrio parahaemolyticus."; RL J. Biochem. 109:24-29(1991). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=RIMD 2210633; RX PubMed=12620739; DOI=10.1016/s0140-6736(03)12659-1; RA Makino K., Oshima K., Kurokawa K., Yokoyama K., Uda T., Tagomori K., RA Iijima Y., Najima M., Nakano M., Yamashita A., Kubota Y., Kimura S., RA Yasunaga T., Honda T., Shinagawa H., Hattori M., Iida T.; RT "Genome sequence of Vibrio parahaemolyticus: a pathogenic mechanism RT distinct from that of V. cholerae."; RL Lancet 361:743-749(2003). CC -!- FUNCTION: Degradation of extracellular 5'-nucleotides for nutritional CC needs. 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=chloride; Xref=ChEBI:CHEBI:17996; CC Note=Chloride.; CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; CC -!- SUBCELLULAR LOCATION: Cell outer membrane {ECO:0000305}; Lipid-anchor CC {ECO:0000305}. CC -!- SIMILARITY: Belongs to the 5'-nucleotidase family. {ECO:0000305}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; X57711; CAA40882.1; -; Genomic_DNA. DR EMBL; D00910; BAA00756.1; -; Genomic_DNA. DR EMBL; BA000031; BAC59011.1; -; Genomic_DNA. DR PIR; JX0153; JX0153. DR RefSeq; WP_005481350.1; NC_004603.1. DR AlphaFoldDB; P22848; -. DR SMR; P22848; -. DR GeneID; 1188243; -. DR KEGG; vpa:VP0748; -. DR PATRIC; fig|223926.6.peg.715; -. DR eggNOG; COG0737; Bacteria. DR HOGENOM; CLU_005854_7_0_6; -. DR Proteomes; UP000002493; Chromosome 1. DR GO; GO:0009279; C:cell outer membrane; IEA:UniProtKB-SubCell. DR GO; GO:0030288; C:outer membrane-bounded periplasmic space; IEA:TreeGrafter. DR GO; GO:0008253; F:5'-nucleotidase activity; IEA:UniProtKB-EC. DR GO; GO:0046872; F:metal ion binding; IEA:InterPro. DR GO; GO:0000166; F:nucleotide binding; IEA:InterPro. DR GO; GO:0008768; F:UDP-sugar diphosphatase activity; IEA:TreeGrafter. DR GO; GO:0009166; P:nucleotide catabolic process; IEA:InterPro. DR FunFam; 3.60.21.10:FF:000025; Protein UshA; 1. DR FunFam; 3.90.780.10:FF:000003; Protein UshA; 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. DR InterPro; IPR029052; Metallo-depent_PP-like. DR NCBIfam; NF007109; PRK09558.1; 1. DR PANTHER; PTHR11575; 5'-NUCLEOTIDASE-RELATED; 1. DR PANTHER; PTHR11575:SF46; PROTEIN USHA; 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. DR PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1. PE 3: Inferred from homology; KW Cell outer membrane; Hydrolase; Lipoprotein; Magnesium; Membrane; KW Metal-binding; Nucleotide-binding; Palmitate; Reference proteome; Signal. FT SIGNAL 1..21 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00303" FT CHAIN 22..560 FT /note="5'-nucleotidase" FT /id="PRO_0000000029" FT BINDING 45 FT /ligand="a divalent metal cation" FT /ligand_id="ChEBI:CHEBI:60240" FT /ligand_label="1" FT /evidence="ECO:0000250" FT BINDING 47 FT /ligand="a divalent metal cation" FT /ligand_id="ChEBI:CHEBI:60240" FT /ligand_label="1" FT /evidence="ECO:0000250" FT BINDING 88 FT /ligand="a divalent metal cation" FT /ligand_id="ChEBI:CHEBI:60240" FT /ligand_label="1" FT /evidence="ECO:0000250" FT BINDING 88 FT /ligand="a divalent metal cation" FT /ligand_id="ChEBI:CHEBI:60240" FT /ligand_label="2" FT /evidence="ECO:0000250" FT BINDING 120 FT /ligand="a divalent metal cation" FT /ligand_id="ChEBI:CHEBI:60240" FT /ligand_label="2" FT /evidence="ECO:0000250" FT BINDING 221 FT /ligand="a divalent metal cation" FT /ligand_id="ChEBI:CHEBI:60240" FT /ligand_label="2" FT /evidence="ECO:0000250" FT BINDING 256 FT /ligand="a divalent metal cation" FT /ligand_id="ChEBI:CHEBI:60240" FT /ligand_label="2" FT /evidence="ECO:0000250" FT BINDING 258 FT /ligand="a divalent metal cation" FT /ligand_id="ChEBI:CHEBI:60240" FT /ligand_label="1" FT /evidence="ECO:0000250" FT BINDING 432 FT /ligand="substrate" FT /evidence="ECO:0000250" FT BINDING 501..507 FT /ligand="substrate" FT /evidence="ECO:0000250" FT SITE 121 FT /note="Transition state stabilizer" FT /evidence="ECO:0000250" FT SITE 124 FT /note="Transition state stabilizer" FT /evidence="ECO:0000250" FT LIPID 22 FT /note="N-palmitoyl cysteine" FT /evidence="ECO:0000305" FT LIPID 22 FT /note="S-diacylglycerol cysteine" FT /evidence="ECO:0000305" FT CONFLICT 198 FT /note="V -> A (in Ref. 1; CAA40882/BAA00756)" FT /evidence="ECO:0000305" SQ SEQUENCE 560 AA; 62175 MW; F82E6B4095403D05 CRC64; MNQRLIIKTA LSAAILASLA GCASQPAHEW NADTTYKLTV LHTNDHHGRF WQNKHGEYGM AARKTLIDDL RDEIQAEGGS VLLLSGGDIN TGVPESDLQD AEPDFKGMSK IGYDAMALGN HEFDNPLDVL FKQQDWANFP MLSANIYDKK TGKRLFQPYA MFNKQGIKIA VIGLTTEDTA KLGNPEFIGQ VDFRDPKVEA KELIAELKKT ENPDLIFAVT HMGHYENGNR GINAPGDVAL ARYLNEGDLD MIVGGHSQEP VCMEGPNVIK KNFKPGDECQ PDQQNGTYIV QAHEWGKYVG RADYEFRNGE LSMVSYDLIP VNLKKKINVD GQSQRVFVQD EITQDKAMLD FLRPFQEKGQ SQLNVKIAES NGKLEGDRDV VRFQQTNLGR LIATAHMERA KADFAVMNSG GVRDSIEAGD ITYKDVLTVQ PFGNMVSYVD MSGQEVLDYL NIVATKPVDS GAYAQFAGIS MRIENDKVTN VFIGNKQLRL DGRYRFTVPS YNASGGDGYP KIDTHPGYVN TGFTDAEVLK DYLESHSPID VNEYAPSGEV MYQTNNVVNQ //