YFCD_ECOLI
ID YFCD_ECOLI Reviewed; 180 AA.
AC P65556; P76494; Q2MAM0;
DT 11-OCT-2004, integrated into UniProtKB/Swiss-Prot.
DT 11-OCT-2004, sequence version 1.
DT 03-AUG-2022, entry version 126.
DE RecName: Full=Uncharacterized Nudix hydrolase YfcD;
DE EC=3.6.-.-;
GN Name=yfcD; OrderedLocusNames=b2299, JW2296;
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 X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) IN COMPLEX WITH MAGNESIUM IONS.
RG Midwest center for structural genomics (MCSG);
RT "Crystal structure of a putative enzyme (possible nudix hydrolase) from
RT Escherichia coli K12.";
RL Submitted (FEB-2009) to the PDB data bank.
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
CC -!- INTERACTION:
CC P65556; P31663: panC; NbExp=6; IntAct=EBI-545346, EBI-545354;
CC -!- SIMILARITY: Belongs to the Nudix hydrolase family. {ECO:0000305}.
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DR EMBL; U00096; AAC75359.1; -; Genomic_DNA.
DR EMBL; AP009048; BAE76686.1; -; Genomic_DNA.
DR PIR; A65002; A65002.
DR RefSeq; NP_416802.1; NC_000913.3.
DR RefSeq; WP_000437935.1; NZ_STEB01000008.1.
DR PDB; 2FKB; X-ray; 2.00 A; A/B/C=1-180.
DR PDBsum; 2FKB; -.
DR AlphaFoldDB; P65556; -.
DR SMR; P65556; -.
DR BioGRID; 4260514; 14.
DR BioGRID; 851124; 1.
DR DIP; DIP-28086N; -.
DR IntAct; P65556; 5.
DR STRING; 511145.b2299; -.
DR jPOST; P65556; -.
DR PaxDb; P65556; -.
DR PRIDE; P65556; -.
DR EnsemblBacteria; AAC75359; AAC75359; b2299.
DR EnsemblBacteria; BAE76686; BAE76686; BAE76686.
DR GeneID; 67416729; -.
DR GeneID; 946783; -.
DR KEGG; ecj:JW2296; -.
DR KEGG; eco:b2299; -.
DR PATRIC; fig|511145.12.peg.2394; -.
DR EchoBASE; EB3860; -.
DR eggNOG; COG1443; Bacteria.
DR HOGENOM; CLU_060552_3_0_6; -.
DR InParanoid; P65556; -.
DR OMA; PGYWDVA; -.
DR PhylomeDB; P65556; -.
DR BioCyc; EcoCyc:G7191-MON; -.
DR EvolutionaryTrace; P65556; -.
DR PRO; PR:P65556; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; IDA:EcoCyc.
DR GO; GO:0016818; F:hydrolase activity, acting on acid anhydrides, in phosphorus-containing anhydrides; IDA:EcoCyc.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR InterPro; IPR015797; NUDIX_hydrolase-like_dom_sf.
DR InterPro; IPR000086; NUDIX_hydrolase_dom.
DR InterPro; IPR024195; NUDIX_hydrolase_YfcD_pred.
DR Pfam; PF00293; NUDIX; 1.
DR PIRSF; PIRSF017340; Nudix_hydro; 1.
DR SUPFAM; SSF55811; SSF55811; 1.
DR PROSITE; PS51462; NUDIX; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Hydrolase; Magnesium; Metal-binding; Reference proteome.
FT CHAIN 1..180
FT /note="Uncharacterized Nudix hydrolase YfcD"
FT /id="PRO_0000057077"
FT DOMAIN 35..163
FT /note="Nudix hydrolase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00794"
FT MOTIF 72..94
FT /note="Nudix box"
FT BINDING 88
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000269|Ref.3, ECO:0007744|PDB:2FKB"
FT BINDING 92
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000269|Ref.3, ECO:0007744|PDB:2FKB"
FT HELIX 4..6
FT /evidence="ECO:0007829|PDB:2FKB"
FT STRAND 11..15
FT /evidence="ECO:0007829|PDB:2FKB"
FT STRAND 21..26
FT /evidence="ECO:0007829|PDB:2FKB"
FT HELIX 27..33
FT /evidence="ECO:0007829|PDB:2FKB"
FT STRAND 37..45
FT /evidence="ECO:0007829|PDB:2FKB"
FT STRAND 47..49
FT /evidence="ECO:0007829|PDB:2FKB"
FT STRAND 51..56
FT /evidence="ECO:0007829|PDB:2FKB"
FT STRAND 61..63
FT /evidence="ECO:0007829|PDB:2FKB"
FT STRAND 67..71
FT /evidence="ECO:0007829|PDB:2FKB"
FT HELIX 81..93
FT /evidence="ECO:0007829|PDB:2FKB"
FT STRAND 101..110
FT /evidence="ECO:0007829|PDB:2FKB"
FT STRAND 113..123
FT /evidence="ECO:0007829|PDB:2FKB"
FT TURN 132..134
FT /evidence="ECO:0007829|PDB:2FKB"
FT STRAND 135..141
FT /evidence="ECO:0007829|PDB:2FKB"
FT HELIX 143..147
FT /evidence="ECO:0007829|PDB:2FKB"
FT HELIX 148..152
FT /evidence="ECO:0007829|PDB:2FKB"
FT HELIX 155..167
FT /evidence="ECO:0007829|PDB:2FKB"
SQ SEQUENCE 180 AA; 20376 MW; 83FC88B71EF9D58B CRC64;
MEQRRLASTE WVDIVNEENE VIAQASREQM RAQCLRHRAT YIVVHDGMGK ILVQRRTETK
DFLPGMLDAT AGGVVQADEQ LLESARREAE EELGIAGVPF AEHGQFYFED KNCRVWGALF
SCVSHGPFAL QEDEVSEVCW LTPEEITARC DEFTPDSLKA LALWMKRNAK NEAVETETAE
