5NTD_VIBVU
ID 5NTD_VIBVU Reviewed; 553 AA.
AC Q8DFG4;
DT 21-NOV-2003, integrated into UniProtKB/Swiss-Prot.
DT 21-NOV-2003, sequence version 2.
DT 03-AUG-2022, entry version 128.
DE RecName: Full=5'-nucleotidase;
DE EC=3.1.3.5;
DE Flags: Precursor;
GN Name=nutA; OrderedLocusNames=VV1_0248;
OS Vibrio vulnificus (strain CMCP6).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC Vibrio.
OX NCBI_TaxID=216895;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CMCP6;
RA Rhee J.H., Kim S.Y., Chung S.S., Kim J.J., Moon Y.H., Jeong H., Choy H.E.;
RT "Complete genome sequence of Vibrio vulnificus CMCP6.";
RL Submitted (DEC-2002) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Degradation of extracellular 5'-nucleotides for nutritional
CC needs. {ECO:0000250}.
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; Evidence={ECO:0000250};
CC Note=Chloride. {ECO:0000250};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
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; AE016795; AAO08784.2; -; Genomic_DNA.
DR RefSeq; WP_011078362.1; NC_004459.3.
DR AlphaFoldDB; Q8DFG4; -.
DR SMR; Q8DFG4; -.
DR EnsemblBacteria; AAO08784; AAO08784; VV1_0248.
DR KEGG; vvu:VV1_0248; -.
DR HOGENOM; CLU_005854_7_0_6; -.
DR OMA; VQPFTNM; -.
DR Proteomes; UP000002275; 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; Signal.
FT SIGNAL 1..21
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00303"
FT CHAIN 22..553
FT /note="5'-nucleotidase"
FT /id="PRO_0000000030"
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"
SQ SEQUENCE 553 AA; 61331 MW; A4A63360A44C27A6 CRC64;
MKQRLIVKTA LSAAILATLA GCATQPTQEW AADTTYKLTV LHTNDHHGRF WQNKYGEYGM
AARKTLIDEL RAEIQAEGGS VLLLSGGDIN TGVPESDLQD AEPDFKGMSK IGYDAMALGN
HEFDNPLDVL MKQKEWANFP MLSANIYDKK TGERMFQAYE MFDKQGIKIA VIGLTTEDTA
KLGNPEFIGA IDFRDPKEEA KKLIAELKET EKPDLIFAVT HMGHYEDGKR GINAPGDVAL
ARYLNEGDLD MIVGGHSQEP VCMEAPNVVK KNFKPADECK PDQQNGTYIV QAHEWGKYVG
RADYEFRNGE LRMVSYDLIP VNLKKKVEVD GKSQRVFIES EIKEDTALLE FLRPYQEKGQ
EQLNVKIADT NGKLEGDRNV VRFQQTNLGR LIAVSHMERA KADFAVMNSG GVRDSIEAGE
VTYKDVLTVQ PFANILTYTD MTGKEVLDYL NVVATKPVDS GAYAQFAGIS MTVANGKVSN
VFIGGKQLRL DETYRFTVPS YNAAGGDGYP KLTGHPGYVN TGFVDAEVLK EFLEKNSPID
VNKFAPNGEI VYK
