ID A0A1V0AE03_9ACTN Unreviewed; 584 AA.
AC A0A1V0AE03;
DT 07-JUN-2017, integrated into UniProtKB/TrEMBL.
DT 07-JUN-2017, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE SubName: Full=Bifunctional metallophosphatase/5'-nucleotidase {ECO:0000313|EMBL:AQZ68416.1};
GN ORFNames=BKM31_49335 {ECO:0000313|EMBL:AQZ68416.1};
OS Nonomuraea sp. ATCC 55076.
OC Bacteria; Actinomycetota; Actinomycetes; Streptosporangiales;
OC Streptosporangiaceae; Nonomuraea.
OX NCBI_TaxID=1909395 {ECO:0000313|EMBL:AQZ68416.1, ECO:0000313|Proteomes:UP000190797};
RN [1] {ECO:0000313|Proteomes:UP000190797}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 55076 {ECO:0000313|Proteomes:UP000190797};
RX PubMed=28626548; DOI=10.1039/c6md00637j;
RA Nazari B., Forneris C.C., Gibson M.I., Moon K., Schramma K.R.,
RA Seyedsayamdost M.R.;
RT "Nonomuraea sp. ATCC 55076 harbours the largest actinomycete chromosome to
RT date and the kistamicin biosynthetic gene cluster.";
RL Med. Chem. Commun. 8:780-788(2017).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a nucleoside 2',3'-cyclic phosphate + H2O = a nucleoside 3'-
CC phosphate + H(+); Xref=Rhea:RHEA:19621, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:66949, ChEBI:CHEBI:66954; EC=3.1.4.16;
CC Evidence={ECO:0000256|ARBA:ARBA00001730};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a ribonucleoside 3'-phosphate + H2O = a ribonucleoside +
CC phosphate; Xref=Rhea:RHEA:10144, ChEBI:CHEBI:13197,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:18254, ChEBI:CHEBI:43474; EC=3.1.3.6;
CC Evidence={ECO:0000256|ARBA:ARBA00000527};
CC -!- COFACTOR:
CC Name=a divalent metal cation; Xref=ChEBI:CHEBI:60240;
CC Evidence={ECO:0000256|ARBA:ARBA00001968};
CC -!- SIMILARITY: Belongs to the 5'-nucleotidase family.
CC {ECO:0000256|RuleBase:RU362119}.
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DR EMBL; CP017717; AQZ68416.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1V0AE03; -.
DR STRING; 1909395.BKM31_49335; -.
DR KEGG; noa:BKM31_49335; -.
DR OrthoDB; 1016457at2; -.
DR Proteomes; UP000190797; Chromosome.
DR GO; GO:0008663; F:2',3'-cyclic-nucleotide 2'-phosphodiesterase activity; IEA:UniProtKB-EC.
DR GO; GO:0008254; F:3'-nucleotidase activity; IEA:UniProtKB-EC.
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 CDD; cd07410; MPP_CpdB_N; 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; IPR041827; CpdB_N.
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; PS00786; 5_NUCLEOTIDASE_2; 1.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000256|RuleBase:RU362119};
KW Multifunctional enzyme {ECO:0000256|ARBA:ARBA00023268};
KW Nucleotide-binding {ECO:0000256|RuleBase:RU362119};
KW Reference proteome {ECO:0000313|Proteomes:UP000190797};
KW Signal {ECO:0000256|RuleBase:RU362119}.
FT SIGNAL 1..26
FT /evidence="ECO:0000256|RuleBase:RU362119"
FT CHAIN 27..584
FT /evidence="ECO:0000256|RuleBase:RU362119"
FT /id="PRO_5011817575"
FT DOMAIN 36..280
FT /note="Calcineurin-like phosphoesterase"
FT /evidence="ECO:0000259|Pfam:PF00149"
FT DOMAIN 362..537
FT /note="5'-Nucleotidase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02872"
SQ SEQUENCE 584 AA; 62574 MW; 7E880F2B1B3F4D5F CRC64;
MQTMKLALAG AAATSVLALA ALPAQAAAPA KTVTVTVMGT SDLHSNALNW DYFKDAAYAD
SQGNHVGLAK VSSLVNRIRA ERGADHTLLF DSGDTIQGTP LAYYYAKVEP ITETGETHPM
AKAMNAIGYD AVTLGNHEFN YGLPLLATWI DQMKAPVLAA NAVRDRSGLP AYKPFVIKTM
KVKGEQPIKV GVLGLTNPGV AIWDKANVEG KLRFTDLVES AKKWVPVIRG LGADVVVVTA
HAGDNGMSSY GGDLPVENAS AMVAEQVPGI DAVLFGHAHN EVAQRFVTNK ATGKQVLLTE
PGKWGQRLSR LDFQLTKQRG RWVVTSKSST TLNTNTVPED PKIVTLLKPQ HDTTVGYVNK
VVAKSAQELS AAESPYKDTP ILDYIQHVQI ETVKQALPDN TLPVLSIAAP FSRSAVFPAG
DVRVRDVAGL YVYDNTLLAV KLTGAQIKDY LEYSAKYFNQ LAPGDPVDVA KLTNAGNTPD
YNYDQLAGVS YDIDVAKPVG QRIANLTYDG APIPADKEFV VAINNYRQSG GGGFPHVTTA
PVLYNAQVEI RQALIEYATA QGTIDPAGFA AANWKLTRDG APLF
//
