ID   A0A1G6EN51_9FIRM        Unreviewed;       626 AA.
AC   A0A1G6EN51;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   27-MAR-2024, entry version 20.
DE   SubName: Full=2',3'-cyclic-nucleotide 2'-phosphodiesterase/5'-or 3'-nucleotidase, 5'-nucleotidase family {ECO:0000313|EMBL:SDB58726.1};
GN   ORFNames=SAMN02910317_03091 {ECO:0000313|EMBL:SDB58726.1};
OS   Ruminococcaceae bacterium FB2012.
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Oscillospiraceae.
OX   NCBI_TaxID=1520817 {ECO:0000313|EMBL:SDB58726.1, ECO:0000313|Proteomes:UP000199364};
RN   [1] {ECO:0000313|EMBL:SDB58726.1, ECO:0000313|Proteomes:UP000199364}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=FB2012 {ECO:0000313|EMBL:SDB58726.1,
RC   ECO:0000313|Proteomes:UP000199364};
RA   de Groot N.N.;
RL   Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the 5'-nucleotidase family.
CC       {ECO:0000256|RuleBase:RU362119}.
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DR   EMBL; FMXS01000027; SDB58726.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1G6EN51; -.
DR   STRING; 1520817.SAMN02910317_03091; -.
DR   OrthoDB; 9800780at2; -.
DR   Proteomes; UP000199364; Unassembled WGS sequence.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR   GO; GO:0046872; F:metal ion binding; IEA:InterPro.
DR   GO; GO:0008252; F:nucleotidase activity; IEA:UniProt.
DR   GO; GO:0000166; F:nucleotide binding; IEA:UniProtKB-KW.
DR   GO; GO:0005975; P:carbohydrate metabolic process; IEA:UniProtKB-KW.
DR   GO; GO:0009166; P:nucleotide catabolic process; IEA:InterPro.
DR   CDD; cd00845; MPP_UshA_N_like; 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_ApaH.
DR   InterPro; IPR029052; Metallo-depent_PP-like.
DR   PANTHER; PTHR11575:SF48; 5' NUCLEOTIDASE, ECTO-LIKE; 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; PS00786; 5_NUCLEOTIDASE_2; 1.
PE   3: Inferred from homology;
KW   Carbohydrate metabolism {ECO:0000256|ARBA:ARBA00023277};
KW   Hydrolase {ECO:0000256|RuleBase:RU362119};
KW   Membrane {ECO:0000256|SAM:Phobius};
KW   Nucleotide-binding {ECO:0000256|RuleBase:RU362119};
KW   Reference proteome {ECO:0000313|Proteomes:UP000199364};
KW   Signal {ECO:0000256|RuleBase:RU362119};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   SIGNAL          1..24
FT                   /evidence="ECO:0000256|RuleBase:RU362119"
FT   CHAIN           25..626
FT                   /evidence="ECO:0000256|RuleBase:RU362119"
FT                   /id="PRO_5011328382"
FT   TRANSMEM        604..622
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          33..247
FT                   /note="Calcineurin-like phosphoesterase"
FT                   /evidence="ECO:0000259|Pfam:PF00149"
FT   DOMAIN          356..508
FT                   /note="5'-Nucleotidase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02872"
FT   REGION          558..602
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        571..598
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   626 AA;  67457 MW;  9377914A9B9C3225 CRC64;
     MKKLLAFLTA VTVAAGGLCL PAAAETADDE TVILFTNDVH CGVDDVIGYD GLALYKREMQ
     AKHKNVLLVD AGDFIQGANL GSLSKGEYIT ELMNEVGYDA VALGNHEFDY GIPTLSERTS
     ELDCGVICCN LTNTETGEKL CEPYKIFDLG DEQIAFVGVT TPDTFGQTTP AFFQNDEGEY
     IYDFGQKDTQ LYDIVQENVD KARAEGADRV ILLAHLGENN VVEKWSSEAV AANTVGVDAV
     ISGHSHEVTL GLTVNNKEGK PVQIAQTGTK LNNIGKMTLS GDSIDIEMVD TVPEPSEDMG
     LDNESWKKTE DRGGRYIDTA VSGKIAELKG KLEELIGQKI GHSNFKLWDS DPETGERRVR
     NGETNLGNFA ADIFRAVYGT DIAFLNGGGL RASIEAGDIS FGDVYNVMPF GNNTCSAKIT
     GRQLLDYLEY SVKSYPEEEG CFSSVSGIEF SIDPTVKSSV ITDEYGDFKG VDGEYRVKEV
     FVNGEPLDLE KTYTAASISY LLQGGGDAHI LSGHCEILEE RPGTDAELVA EYIKKLENGE
     IPEKYRDPYG EGRIKLYEEK SGEDGSSSDE DSSVPDSSSE SETSGEDSSG QAKNDDTNPA
     TGHAAAAGIT VLLLLTGAAA AGRRRQ
//