5NTD_VIBPA
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 03-AUG-2022, entry version 148.
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; Proteobacteria; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC 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}.
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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; NP_797127.1; NC_004603.1.
DR RefSeq; WP_005481350.1; NC_004603.1.
DR AlphaFoldDB; P22848; -.
DR SMR; P22848; -.
DR STRING; 223926.28805734; -.
DR EnsemblBacteria; BAC59011; BAC59011; BAC59011.
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 OMA; VQPFTNM; -.
DR Proteomes; UP000002493; Chromosome 1.
DR GO; GO:0009279; C:cell outer membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0000166; F:nucleotide binding; IEA:UniProtKB-KW.
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.
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
