ID   A0A1W9T543_9BACT        Unreviewed;       584 AA.
AC   A0A1W9T543;
DT   05-JUL-2017, integrated into UniProtKB/TrEMBL.
DT   05-JUL-2017, sequence version 1.
DT   27-MAR-2024, entry version 19.
DE   SubName: Full=Bifunctional metallophosphatase/5'-nucleotidase {ECO:0000313|EMBL:OQY03701.1};
GN   ORFNames=B6I20_04515 {ECO:0000313|EMBL:OQY03701.1};
OS   Bacteroidetes bacterium 4572_117.
OC   Bacteria; Bacteroidota.
OX   NCBI_TaxID=1971632 {ECO:0000313|EMBL:OQY03701.1, ECO:0000313|Proteomes:UP000192701};
RN   [1] {ECO:0000313|Proteomes:UP000192701}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Dombrowski N., Seitz K., Teske A., Baker B.;
RT   "Novel pathways for hydrocarbon cycling and metabolic interdependencies in
RT   hydrothermal sediment communities.";
RL   Submitted (MAR-2017) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the 5'-nucleotidase family.
CC       {ECO:0000256|RuleBase:RU362119}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:OQY03701.1}.
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DR   EMBL; NBLH01000052; OQY03701.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1W9T543; -.
DR   Proteomes; UP000192701; Unassembled WGS sequence.
DR   GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0000166; F:nucleotide binding; IEA:UniProtKB-KW.
DR   GO; GO:0009166; P:nucleotide catabolic process; IEA:InterPro.
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; IPR006179; 5_nucleotidase/apyrase.
DR   InterPro; IPR004843; Calcineurin-like_PHP_ApaH.
DR   InterPro; IPR029052; Metallo-depent_PP-like.
DR   PANTHER; PTHR11575:SF6; 2',3'-CYCLIC-NUCLEOTIDE 2'-PHOSPHODIESTERASE_3'-NUCLEOTIDASE; 1.
DR   PANTHER; PTHR11575; 5'-NUCLEOTIDASE-RELATED; 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; PS51257; PROKAR_LIPOPROTEIN; 1.
PE   3: Inferred from homology;
KW   Hydrolase {ECO:0000256|RuleBase:RU362119};
KW   Nucleotide-binding {ECO:0000256|RuleBase:RU362119}.
FT   DOMAIN          33..264
FT                   /note="Calcineurin-like phosphoesterase"
FT                   /evidence="ECO:0000259|Pfam:PF00149"
FT   DOMAIN          346..515
FT                   /note="5'-Nucleotidase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02872"
SQ   SEQUENCE   584 AA;  66903 MW;  F7FEE0896B614E83 CRC64;
     MTLKKFLFTI IVVTGLLFSC NTKPKRAKNV KLRMIQTTDV HGSIFPYDFI RNKETNNSLA
     SVYTYVQKQR ANKDIETILL DNGDILQGQP VVYYSNFESA DNEHICASVM NFMGYDAATI
     GNHDIEAGHE VYDKINKEFK FPWLAANAID KKTREPYFKA YTIINRKGLK IAVLGLITPA
     IPNWLPENIW EGIKFEDMVV SAKKWIKIIK KNEKPDLIVG MFHSGVDFTY GNQTDTTFKN
     ENATRLVAEQ VPGFDIVFAG HDHQEYNLWF KSSDSSDVLL LDPRSYAKYV AVADIEFTWN
     KNQDKYDKII KGDIVKTENI EADSTFLAKF EEYVEEVKNY VNHEIGFISK SISSRKALFG
     NSEFVDLIHK IQLEISGADI SFTAPLNYDA EIKSGPVYVR DMFNLYRFEN LLYTMNLNGN
     EIKDYLEFST DLWFNEMTSE NDNLIKMKKT HDGKQRLASA YYNFSSAAGI DYSINLKGEK
     GNRVNITGLS NGDKFELAKK YTVAINSYRG NGGGGHLIEG AGILKSQLAA RIITSTDKDL
     RYYMIKWIEK NKTITPEKYD NWQLTPKKWW EKAKAKDIKI LFPD
//