ID D3GMP6_9ENTR Unreviewed; 522 AA.
AC D3GMP6;
DT 23-MAR-2010, integrated into UniProtKB/TrEMBL.
DT 23-MAR-2010, sequence version 1.
DT 27-MAR-2024, entry version 41.
DE RecName: Full=Bifunctional metallophosphatase/5'-nucleotidase {ECO:0008006|Google:ProtNLM};
OS Enterobacter hormaechei.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Enterobacter; Enterobacter cloacae complex.
OX NCBI_TaxID=158836 {ECO:0000313|EMBL:CAX65533.1};
RN [1] {ECO:0000313|EMBL:CAX65533.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=05-545 {ECO:0000313|EMBL:CAX65533.1};
RX PubMed=20084283; DOI=10.1371/journal.pone.0008662;
RA Paauw A., Leverstein-van Hall M.A., Verhoef J., Fluit A.C.;
RT "Evolution in quantum leaps: multiple combinatorial transfers of HPI and
RT other genetic modules in Enterobacteriaceae.";
RL PLoS ONE 5:e8662-e8662(2010).
CC -!- SIMILARITY: Belongs to the 5'-nucleotidase family.
CC {ECO:0000256|ARBA:ARBA00006654, ECO:0000256|RuleBase:RU362119}.
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DR EMBL; FN297818; CAX65533.1; -; Genomic_DNA.
DR AlphaFoldDB; D3GMP6; -.
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: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; 5'-NUCLEOTIDASE-RELATED; 1.
DR PANTHER; PTHR11575:SF46; PROTEIN USHA; 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 Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|RuleBase:RU362119}; Signal {ECO:0000256|RuleBase:RU362119}.
FT SIGNAL 1..26
FT /evidence="ECO:0000256|RuleBase:RU362119"
FT CHAIN 27..522
FT /note="Bifunctional metallophosphatase/5'-nucleotidase"
FT /evidence="ECO:0000256|RuleBase:RU362119"
FT /id="PRO_5005126302"
FT DOMAIN 30..257
FT /note="Calcineurin-like phosphoesterase"
FT /evidence="ECO:0000259|Pfam:PF00149"
FT DOMAIN 333..479
FT /note="5'-Nucleotidase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02872"
SQ SEQUENCE 522 AA; 57358 MW; 7AD48E33AE84060A CRC64;
MIMKKNIKLS LITLCWFATL TASVHAKDVT IYYTNDLHAH VSPGKPPTVD KERLVGGFAN
IATIVNDAKK ISKDVFFFDA GDYFTGPYIS TLTKGEAIID IMNTMPFDAV SVGNHEFDYG
VDNMVKQLSR AHFPILLGNV FYTNSEKPVW NTPWTVVEKD GIKIGVLGVH QKFAFYDTIA
AKAYAGSEAR DEEPYIQKGL DALKGKVDII VLLIHEGTPA RQSSYGNKDV ARMLQADIDT
AKKFKDIDVL ITGHAHVGTP EPIKVNDTLI VSTDAYGTDI GKLVLDFNPQ TKKIERYKGE
LITVFSDEYK PDPKVQLKID EWNASLKKIT GQVIGSTTAH FTRSYGESSP VGNLIIDAMM
AKVPDAVVGL QNSGGIRADF PQGNLTYGDV ITTFPFNNDL VEMDLSGKDL TDLMIHATNL
TNGILQVSKS VHVVYDSTKP LGKRLIKFTV NNQPIDPTRI YRVATHSFCA TGGDGFEAFL
KGKNIKTINS TTSADSIIDY VKAHSPVKPD HEMRVTDVSA AK
//
