ID A0A1Y3XBA8_9FIRM Unreviewed; 645 AA.
AC A0A1Y3XBA8;
DT 30-AUG-2017, integrated into UniProtKB/TrEMBL.
DT 30-AUG-2017, sequence version 1.
DT 27-MAR-2024, entry version 23.
DE SubName: Full=Bifunctional metallophosphatase/5'-nucleotidase {ECO:0000313|EMBL:OUN82824.1};
GN ORFNames=B5G06_09300 {ECO:0000313|EMBL:OUN82824.1};
OS Flavonifractor sp. An52.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Oscillospiraceae;
OC Flavonifractor.
OX NCBI_TaxID=1965642 {ECO:0000313|EMBL:OUN82824.1, ECO:0000313|Proteomes:UP000195424};
RN [1] {ECO:0000313|Proteomes:UP000195424}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=An52 {ECO:0000313|Proteomes:UP000195424};
RA Medvecky M., Cejkova D., Polansky O., Karasova D., Kubasova T., Cizek A.,
RA Rychlik I.;
RT "Function of individual gut microbiota members based on whole genome
RT sequencing of pure cultures obtained from chicken caecum.";
RL Submitted (APR-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:OUN82824.1}.
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DR EMBL; NFIB01000021; OUN82824.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1Y3XBA8; -.
DR Proteomes; UP000195424; 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 Coiled coil {ECO:0000256|SAM:Coils};
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:UP000195424};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 600..621
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 37..266
FT /note="Calcineurin-like phosphoesterase"
FT /evidence="ECO:0000259|Pfam:PF00149"
FT DOMAIN 362..513
FT /note="5'-Nucleotidase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02872"
FT COILED 201..228
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 645 AA; 70122 MW; 30A7988A1E06D394 CRC64;
MVHHGLKRLF LTVLTLILLI FICPAWGAAE NSHDAVILFT HDTHDHFYPA PSEDGGEYGG
YTRLATLLAL ERVKYPDAIT VDGGDFSMGT LFQTIYATQA PELKALGAMG YDVTTLGNHE
FDYRASGLAQ MLETAAASGS QVPAIVQSNG TVLDGEGAEE LRAAMEAYGV QNHMILTRGG
INYGIFGLMG EDADACAPMS GMEFEAVADA ARREVAALEE ELAQLEGPSV IVCLSHTGTD
GGKGEDYELA KAVDGIDVII SGHTHSTLEE PIQVNDTLIV SCGEYTTNLG VLVLELDDAG
TVTDYDYRLV PVDETVTANT EMERLAQSFQ PIIEEEYLSQ FGLTFDQVLA RSEFDFTPIS
QFGKEHKEDT LGNLIADSYI YAVQQAEGED YVPVDFAVVA AGVIRESFSA GEITTSDVFN
VASLGSGADG TPGYPLISVW ITGRELRDAF EVDASVTGLM PAAQIYGSGM TWTWNPYRII
LNRVNDYAQV LPDGTTVPLE DDKLYRVVTG LYTGQMLGTV NDQSFGILTI TPKDAQGNPV
TNFEDQIIYT PNGSELKEWY ALATYLQSMG TVDQRYAAPE GRKVEEASLN PVSLLKGLNL
VGWIALVVCL VVLALIVFIV YRIATRGRRR RYGGQKGRGY HRYRG
//