5NTD_VIBCH
ID 5NTD_VIBCH Reviewed; 553 AA.
AC Q9KQ30;
DT 20-JUN-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 134.
DE RecName: Full=5'-nucleotidase;
DE EC=3.1.3.5;
DE Flags: Precursor;
GN Name=nutA; OrderedLocusNames=VC_2174;
OS Vibrio cholerae serotype O1 (strain ATCC 39315 / El Tor Inaba N16961).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC Vibrio.
OX NCBI_TaxID=243277;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 39315 / El Tor Inaba N16961;
RX PubMed=10952301; DOI=10.1038/35020000;
RA Heidelberg J.F., Eisen J.A., Nelson W.C., Clayton R.A., Gwinn M.L.,
RA Dodson R.J., Haft D.H., Hickey E.K., Peterson J.D., Umayam L.A., Gill S.R.,
RA Nelson K.E., Read T.D., Tettelin H., Richardson D.L., Ermolaeva M.D.,
RA Vamathevan J.J., Bass S., Qin H., Dragoi I., Sellers P., McDonald L.A.,
RA Utterback T.R., Fleischmann R.D., Nierman W.C., White O., Salzberg S.L.,
RA Smith H.O., Colwell R.R., Mekalanos J.J., Venter J.C., Fraser C.M.;
RT "DNA sequence of both chromosomes of the cholera pathogen Vibrio
RT cholerae.";
RL Nature 406:477-483(2000).
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:0000250}; Lipid-anchor
CC {ECO:0000255|PROSITE-ProRule:PRU00303}.
CC -!- SIMILARITY: Belongs to the 5'-nucleotidase family. {ECO:0000305}.
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DR EMBL; AE003852; AAF95319.1; -; Genomic_DNA.
DR PIR; E82108; E82108.
DR RefSeq; NP_231805.1; NC_002505.1.
DR RefSeq; WP_000809002.1; NZ_LT906614.1.
DR AlphaFoldDB; Q9KQ30; -.
DR SMR; Q9KQ30; -.
DR STRING; 243277.VC_2174; -.
DR DNASU; 2613310; -.
DR EnsemblBacteria; AAF95319; AAF95319; VC_2174.
DR GeneID; 57740786; -.
DR KEGG; vch:VC_2174; -.
DR PATRIC; fig|243277.26.peg.2072; -.
DR eggNOG; COG0737; Bacteria.
DR HOGENOM; CLU_005854_7_0_6; -.
DR OMA; VQPFTNM; -.
DR BioCyc; VCHO:VC2174-MON; -.
DR Proteomes; UP000000584; Chromosome 1.
DR GO; GO:0009279; C:cell outer membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0030288; C:outer membrane-bounded periplasmic space; IBA:GO_Central.
DR GO; GO:0008253; F:5'-nucleotidase activity; IBA:GO_Central.
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; IBA:GO_Central.
DR GO; GO:0106411; F:XMP 5'-nucleosidase activity; IEA:UniProtKB-EC.
DR GO; GO:0009166; P:nucleotide catabolic process; IBA:GO_Central.
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..553
FT /note="5'-nucleotidase"
FT /id="PRO_0000000028"
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; 60903 MW; 5AA621C27526B311 CRC64;
MKQGLILKSV LSAAIIASLA GCATAPAQQW EADKTYKLTI LHTNDHHGRF WQNQYGEYGM
AARKTLIDQL RADIEAQGGS VLLLSGGDIN TGVPESDLQD AEPDFKGMSK IGYDAMALGN
HEFDNPLEVL FKQKEWANFP MLSANIYDKA TGKRLFEPYH IFDKQGIKIA VIGLTTEDTA
KIGNPEYIGG IDFRDPKEEA KKVIAELKKK EKPDLIIAVT HMGHYQNGEH GVNAPGDVAL
ARYLPAGELD MIVGGHSQEP VCMEGPNLVK KNFKPGDECK PDIQNGTYIV QAYEWGKYVG
RADYEFRNGE LNMVSYNLIP VNLKKKVEVN GETQRVFATS EIKEDSAMLE FLRPFQEKGQ
EQLSIKIAHS NGKLEGDRNV VRFEQTNLGR MIAMAHMQRA KADFAVMNSG GVRDSIQAGD
ITYKDVLKVQ PFGNIVSYVD MNGQEVLDYL NVVATKPVDS GAYAQFAGIS MTVADGKVSN
VVIGGKQLRL DATYRFTVPS FNAAGGDGYP KITDHPGYVN TGFVDAEVLK DYLEANSPID
VNRFAPAGEI VYR
