YFCE_ECOLI
ID YFCE_ECOLI Reviewed; 184 AA.
AC P67095; P76495; Q2MAL9;
DT 11-OCT-2004, integrated into UniProtKB/Swiss-Prot.
DT 11-OCT-2004, sequence version 1.
DT 03-AUG-2022, entry version 121.
DE RecName: Full=Phosphodiesterase YfcE;
DE EC=3.1.4.-;
GN Name=yfcE; OrderedLocusNames=b2300, JW5377;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B.,
RA Shao Y.;
RT "The complete genome sequence of Escherichia coli K-12.";
RL Science 277:1453-1462(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=16738553; DOI=10.1038/msb4100049;
RA Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655
RT and W3110.";
RL Mol. Syst. Biol. 2:E1-E5(2006).
RN [3]
RP FUNCTION, AND COFACTOR.
RX PubMed=15808744; DOI=10.1016/j.fmrre.2004.12.006;
RA Kuznetsova E., Proudfoot M., Sanders S.A., Reinking J., Savchenko A.,
RA Arrowsmith C.H., Edwards A.M., Yakunin A.F.;
RT "Enzyme genomics: application of general enzymatic screens to discover new
RT enzymes.";
RL FEMS Microbiol. Rev. 29:263-279(2005).
RN [4]
RP X-RAY CRYSTALLOGRAPHY (2.25 ANGSTROMS).
RA Miller D.J., Shuvalova L., Evdokimova E., Savchenko A., Yakunin A.F.,
RA Anderson W.F.;
RT "Structural and biochemical characterization of YfcE, a phosphoesterase
RT from E. coli.";
RL Submitted (AUG-2004) to the PDB data bank.
CC -!- FUNCTION: Shows phosphodiesterase activity, hydrolyzing phosphodiesters
CC bonds in the artificial chromogenic substrates bis-p-nitrophenyl
CC phosphate (bis-pNPP), and less efficiently thymidine 5'-monophosphate
CC p-nitrophenyl ester (pNP-TMP) and p-nitrophenylphosphorylcholine
CC (pNPPC). The physiological substrate is unknown.
CC {ECO:0000269|PubMed:15808744}.
CC -!- COFACTOR:
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000269|PubMed:15808744};
CC Note=Binds 2 manganese ions per subunit. {ECO:0000269|PubMed:15808744};
CC -!- SIMILARITY: Belongs to the metallophosphoesterase superfamily. YfcE
CC family. {ECO:0000305}.
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DR EMBL; U00096; AAC75360.1; -; Genomic_DNA.
DR EMBL; AP009048; BAE76687.1; -; Genomic_DNA.
DR PIR; B65002; B65002.
DR RefSeq; NP_416803.3; NC_000913.3.
DR PDB; 1SU1; X-ray; 2.25 A; A/B/C/D=1-184.
DR PDBsum; 1SU1; -.
DR AlphaFoldDB; P67095; -.
DR SMR; P67095; -.
DR BioGRID; 4260515; 361.
DR STRING; 511145.b2300; -.
DR jPOST; P67095; -.
DR PaxDb; P67095; -.
DR PRIDE; P67095; -.
DR EnsemblBacteria; AAC75360; AAC75360; b2300.
DR EnsemblBacteria; BAE76687; BAE76687; BAE76687.
DR GeneID; 946755; -.
DR KEGG; ecj:JW5377; -.
DR KEGG; eco:b2300; -.
DR PATRIC; fig|511145.12.peg.2395; -.
DR EchoBASE; EB3861; -.
DR eggNOG; COG0622; Bacteria.
DR HOGENOM; CLU_063749_1_1_6; -.
DR InParanoid; P67095; -.
DR OMA; DILYHGP; -.
DR PhylomeDB; P67095; -.
DR BioCyc; EcoCyc:G7192-MON; -.
DR BRENDA; 3.1.4.1; 2026.
DR BRENDA; 3.1.4.16; 2026.
DR EvolutionaryTrace; P67095; -.
DR PRO; PR:P67095; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0005829; C:cytosol; IDA:EcoCyc.
DR GO; GO:0032991; C:protein-containing complex; IDA:EcoCyc.
DR GO; GO:0042802; F:identical protein binding; IDA:EcoCyc.
DR GO; GO:0030145; F:manganese ion binding; IDA:EcoCyc.
DR GO; GO:0008081; F:phosphoric diester hydrolase activity; IDA:EcoCyc.
DR CDD; cd00841; MPP_YfcE; 1.
DR Gene3D; 3.60.21.10; -; 1.
DR InterPro; IPR024654; Calcineurin-like_PHP_lpxH.
DR InterPro; IPR029052; Metallo-depent_PP-like.
DR InterPro; IPR041802; MPP_YfcE.
DR InterPro; IPR020935; PdiEstase_YfcE_CS.
DR InterPro; IPR000979; Phosphodiesterase_MJ0936/Vps29.
DR PANTHER; PTHR11124; PTHR11124; 1.
DR Pfam; PF12850; Metallophos_2; 1.
DR SUPFAM; SSF56300; SSF56300; 1.
DR TIGRFAMs; TIGR00040; yfcE; 1.
DR PROSITE; PS01269; UPF0025; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Hydrolase; Manganese; Metal-binding; Reference proteome.
FT CHAIN 1..184
FT /note="Phosphodiesterase YfcE"
FT /id="PRO_0000155605"
FT BINDING 9
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT BINDING 11
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT BINDING 37
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT BINDING 37
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT BINDING 73
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT BINDING 105
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT BINDING 127
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT BINDING 129
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT STRAND 3..7
FT /evidence="ECO:0007829|PDB:1SU1"
FT HELIX 14..27
FT /evidence="ECO:0007829|PDB:1SU1"
FT STRAND 30..34
FT /evidence="ECO:0007829|PDB:1SU1"
FT HELIX 53..61
FT /evidence="ECO:0007829|PDB:1SU1"
FT HELIX 62..66
FT /evidence="ECO:0007829|PDB:1SU1"
FT STRAND 67..69
FT /evidence="ECO:0007829|PDB:1SU1"
FT HELIX 77..82
FT /evidence="ECO:0007829|PDB:1SU1"
FT STRAND 83..85
FT /evidence="ECO:0007829|PDB:1SU1"
FT STRAND 90..95
FT /evidence="ECO:0007829|PDB:1SU1"
FT STRAND 100..104
FT /evidence="ECO:0007829|PDB:1SU1"
FT STRAND 106..110
FT /evidence="ECO:0007829|PDB:1SU1"
FT STRAND 122..124
FT /evidence="ECO:0007829|PDB:1SU1"
FT STRAND 132..136
FT /evidence="ECO:0007829|PDB:1SU1"
FT STRAND 139..143
FT /evidence="ECO:0007829|PDB:1SU1"
FT STRAND 157..162
FT /evidence="ECO:0007829|PDB:1SU1"
FT STRAND 165..170
FT /evidence="ECO:0007829|PDB:1SU1"
FT TURN 171..173
FT /evidence="ECO:0007829|PDB:1SU1"
FT STRAND 176..181
FT /evidence="ECO:0007829|PDB:1SU1"
SQ SEQUENCE 184 AA; 20122 MW; 15C5AA0BE6541AB6 CRC64;
MMKLMFASDI HGSLPATERV LELFAQSGAQ WLVILGDVLN HGPRNALPEG YAPAKVAERL
NEVAHKVIAV RGNCDSEVDQ MLLHFPITAP WQQVLLEKQR LFLTHGHLFG PENLPALNQN
DVLVYGHTHL PVAEQRGEIF HFNPGSVSIP KGGNPASYGM LDNDVLSVIA LNDQSIIAQV
AINP
