YDEM_ECOLI
ID YDEM_ECOLI Reviewed; 385 AA.
AC P76134; P77755;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 15-JUL-1998, sequence version 2.
DT 03-AUG-2022, entry version 136.
DE RecName: Full=Anaerobic sulfatase-maturating enzyme homolog YdeM;
DE Short=AnSME homolog;
GN Name=ydeM; OrderedLocusNames=b1497, JW1492;
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 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=9097039; DOI=10.1093/dnares/3.6.363;
RA Aiba H., Baba T., Fujita K., Hayashi K., Inada T., Isono K., Itoh T.,
RA Kasai H., Kashimoto K., Kimura S., Kitakawa M., Kitagawa M., Makino K.,
RA Miki T., Mizobuchi K., Mori H., Mori T., Motomura K., Nakade S.,
RA Nakamura Y., Nashimoto H., Nishio Y., Oshima T., Saito N., Sampei G.,
RA Seki Y., Sivasundaram S., Tagami H., Takeda J., Takemoto K., Takeuchi Y.,
RA Wada C., Yamamoto Y., Horiuchi T.;
RT "A 570-kb DNA sequence of the Escherichia coli K-12 genome corresponding to
RT the 28.0-40.1 min region on the linkage map.";
RL DNA Res. 3:363-377(1996).
RN [2]
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 [3]
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 [4]
RP NON-INVOLVEMENT IN SULFATASE MATURATION.
RC STRAIN=K12 / BW25113;
RX PubMed=17303125; DOI=10.1016/j.febslet.2007.01.076;
RA Benjdia A., Deho G., Rabot S., Berteau O.;
RT "First evidences for a third sulfatase maturation system in prokaryotes
RT from E. coli aslB and ydeM deletion mutants.";
RL FEBS Lett. 581:1009-1014(2007).
CC -!- COFACTOR:
CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC Evidence={ECO:0000250|UniProtKB:Q0TTH1};
CC Note=Binds 3 [4Fe-4S] clusters (By similarity). The first cluster is
CC coordinated with 3 cysteines and an exchangeable S-adenosyl-L-
CC methionine (By similarity). {ECO:0000250|UniProtKB:Q0TTH1};
CC -!- SIMILARITY: Belongs to the radical SAM superfamily. Anaerobic
CC sulfatase-maturating enzyme family. {ECO:0000305}.
CC -!- CAUTION: Despite its homology to the anaerobic sulfatase-maturating
CC enzymes, it is not involved in Cys-type sulfatase maturation in vivo.
CC {ECO:0000305}.
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DR EMBL; U00096; AAC74570.2; -; Genomic_DNA.
DR EMBL; AP009048; BAA15168.1; -; Genomic_DNA.
DR PIR; D64903; D64903.
DR RefSeq; NP_416014.4; NC_000913.3.
DR RefSeq; WP_001301030.1; NZ_SSZK01000001.1.
DR AlphaFoldDB; P76134; -.
DR SMR; P76134; -.
DR BioGRID; 4260790; 10.
DR IntAct; P76134; 1.
DR STRING; 511145.b1497; -.
DR PaxDb; P76134; -.
DR PRIDE; P76134; -.
DR EnsemblBacteria; AAC74570; AAC74570; b1497.
DR EnsemblBacteria; BAA15168; BAA15168; BAA15168.
DR GeneID; 945981; -.
DR KEGG; ecj:JW1492; -.
DR KEGG; eco:b1497; -.
DR PATRIC; fig|511145.12.peg.1564; -.
DR EchoBASE; EB3556; -.
DR eggNOG; COG0641; Bacteria.
DR HOGENOM; CLU_009273_10_0_6; -.
DR InParanoid; P76134; -.
DR OMA; YPCYRFV; -.
DR PhylomeDB; P76134; -.
DR BioCyc; EcoCyc:G6787-MON; -.
DR PRO; PR:P76134; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:InterPro.
DR GO; GO:0006974; P:cellular response to DNA damage stimulus; IEP:EcoliWiki.
DR GO; GO:0051604; P:protein maturation; ISS:EcoCyc.
DR Gene3D; 3.20.20.70; -; 1.
DR InterPro; IPR023885; 4Fe4S-binding_SPASM_dom.
DR InterPro; IPR013785; Aldolase_TIM.
DR InterPro; IPR034491; Anaerob_Ser_sulfatase-maturase.
DR InterPro; IPR007197; rSAM.
DR InterPro; IPR023867; Sulphatase_maturase_rSAM.
DR PANTHER; PTHR43273; PTHR43273; 1.
DR Pfam; PF04055; Radical_SAM; 1.
DR Pfam; PF13186; SPASM; 1.
DR SFLD; SFLDF00285; anaerobic_Ser-type_sulfatase-m; 1.
DR SFLD; SFLDG01384; thioether_bond_formation_requi; 1.
DR TIGRFAMs; TIGR04085; rSAM_more_4Fe4S; 1.
DR PROSITE; PS51918; RADICAL_SAM; 1.
PE 3: Inferred from homology;
KW 4Fe-4S; Iron; Iron-sulfur; Metal-binding; Reference proteome;
KW S-adenosyl-L-methionine.
FT CHAIN 1..385
FT /note="Anaerobic sulfatase-maturating enzyme homolog YdeM"
FT /id="PRO_0000134463"
FT DOMAIN 1..231
FT /note="Radical SAM core"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01266"
FT ACT_SITE 279
FT /note="Proton acceptor"
FT /evidence="ECO:0000250|UniProtKB:Q0TTH1"
FT BINDING 12
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="1"
FT /ligand_note="4Fe-4S-S-AdoMet"
FT /evidence="ECO:0000250|UniProtKB:Q0TTH1"
FT BINDING 16
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="1"
FT /ligand_note="4Fe-4S-S-AdoMet"
FT /evidence="ECO:0000250|UniProtKB:Q0TTH1"
FT BINDING 18
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:Q0TTH1"
FT BINDING 19
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="1"
FT /ligand_note="4Fe-4S-S-AdoMet"
FT /evidence="ECO:0000250|UniProtKB:Q0TTH1"
FT BINDING 61
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:Q0TTH1"
FT BINDING 116
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:Q0TTH1"
FT BINDING 128
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:Q0TTH1"
FT BINDING 189
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:Q0TTH1"
FT BINDING 257
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q0TTH1"
FT BINDING 263
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q0TTH1"
FT BINDING 278
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q0TTH1"
FT BINDING 315
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:Q0TTH1"
FT BINDING 318
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:Q0TTH1"
FT BINDING 324
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:Q0TTH1"
FT BINDING 328
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q0TTH1"
FT BINDING 345
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:Q0TTH1"
SQ SEQUENCE 385 AA; 44518 MW; 964E34F73E680329 CRC64;
MHVTAKPSSF QCNLKCDYCF YLEKESQFTH EKWMDDSTLK EFIKQYIAAS GNQVYFTWQG
GEPTLAGLDF FRKVIHYQQR YAGQKRIFNA LQTNGILLNN EWCAFLKEHE FLVGISIDGP
QELHDRYRRS NSGNGTFAKV IAAIERLKSY QVEFNTLTVI NNVNVHYPLE VYHFLKSIGS
KHMQFIELLE TGTPNIDFSG HSENTFRIID FSVPPTAYGK FMSTIFMQWV KNDVGEIFIR
QFESFVSRFL GNGHTSCIFQ ESCKDNLVVE SNGDIYECDH FVYPQYKIGN INKSELKTMN
SVQLTAQKKR IPAKCQQCAY KPICNGGCPK HRITKVNNET VSYFCEGYKI LFSTMVPYMN
AMVELAKNRV PLYHIMDVAK QMENN
