EUTT_ECOLI
ID EUTT_ECOLI Reviewed; 267 AA.
AC P65643; P76554; Q2MAI9;
DT 11-OCT-2004, integrated into UniProtKB/Swiss-Prot.
DT 11-OCT-2004, sequence version 1.
DT 03-AUG-2022, entry version 100.
DE RecName: Full=Corrinoid adenosyltransferase EutT {ECO:0000305};
DE AltName: Full=ATP:co(I)rrinoid adenosyltransferase;
DE Short=ACAT;
DE AltName: Full=Cob(II)alamin adenosyltransferase EutT;
DE AltName: Full=Ethanolamine utilization cobalamin adenosyltransferase;
DE AltName: Full=Ethanolamine utilization corrinoid adenosyltransferase;
DE AltName: Full=EutT adenosyltransferase {ECO:0000250|UniProtKB:Q9ZFV4};
GN Name=eutT; Synonyms=ypfB; OrderedLocusNames=b2459, JW2443;
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).
CC -!- FUNCTION: Converts cyanocobalamin (CN-B12) to adenosylcobalamin
CC (AdoCbl), the inducer of the eut operon. Is not active on cobinamide
CC nor other intermediates in the adenosylcobalamin synthetic pathway.
CC Allows full induction of the eut operon.
CC {ECO:0000250|UniProtKB:Q9ZFV4}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2 ATP + 2 cob(II)inamide + 2 H2O + reduced [electron-transfer
CC flavoprotein] = 2 adenosylcob(III)inamide + 2 diphosphate + 3 H(+) +
CC oxidized [electron-transfer flavoprotein] + 2 phosphate;
CC Xref=Rhea:RHEA:66824, Rhea:RHEA-COMP:10685, Rhea:RHEA-COMP:10686,
CC ChEBI:CHEBI:2480, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:43474,
CC ChEBI:CHEBI:57692, ChEBI:CHEBI:58307, ChEBI:CHEBI:141013;
CC Evidence={ECO:0000250|UniProtKB:Q9ZFV4};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + cob(I)alamin-[corrinoid adenosyltransferase] =
CC adenosylcob(III)alamin + apo-[corrinoid adenosyltransferase] +
CC triphosphate; Xref=Rhea:RHEA:56796, Rhea:RHEA-COMP:14743, Rhea:RHEA-
CC COMP:14744, ChEBI:CHEBI:18036, ChEBI:CHEBI:18408, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:60488, ChEBI:CHEBI:83228;
CC Evidence={ECO:0000250|UniProtKB:Q9ZFV4};
CC -!- COFACTOR:
CC Name=a divalent metal cation; Xref=ChEBI:CHEBI:60240;
CC Evidence={ECO:0000250|UniProtKB:Q9ZFV4};
CC Note=Binds 1 divalent metal cation ion per homodimer with both subunits
CC providing Cys ligands; Fe(2+) gives most activity and is possibly the
CC physiological cofactor. {ECO:0000250|UniProtKB:Q9ZFV4};
CC -!- PATHWAY: Amine and polyamine degradation; ethanolamine degradation.
CC -!- SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:Q9ZFV4}.
CC -!- SUBCELLULAR LOCATION: Bacterial microcompartment {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the Cob(I)alamin adenosyltransferase family.
CC EutT subfamily. {ECO:0000305}.
CC -!- CAUTION: In strain MG1655 the eut operon is interrupted by the CPZ-55
CC prophage, encoding 9 genes situated between eutA and eutB, which are
CC translated in the other direction. CPZ-55 may prevent expression of the
CC eut operon in strain MG1655. Strain W3110 does not have this prophage
CC element and should be able to express the operon.
CC {ECO:0000305|PubMed:9278503}.
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DR EMBL; U00096; AAC75512.1; -; Genomic_DNA.
DR EMBL; AP009048; BAE76717.1; -; Genomic_DNA.
DR PIR; B65021; B65021.
DR RefSeq; NP_416954.1; NC_000913.3.
DR RefSeq; WP_000651298.1; NZ_STEB01000051.1.
DR AlphaFoldDB; P65643; -.
DR SMR; P65643; -.
DR BioGRID; 4260919; 3.
DR DIP; DIP-9543N; -.
DR IntAct; P65643; 7.
DR STRING; 511145.b2459; -.
DR PaxDb; P65643; -.
DR PRIDE; P65643; -.
DR EnsemblBacteria; AAC75512; AAC75512; b2459.
DR EnsemblBacteria; BAE76717; BAE76717; BAE76717.
DR GeneID; 66673680; -.
DR GeneID; 946939; -.
DR KEGG; ecj:JW2443; -.
DR KEGG; eco:b2459; -.
DR PATRIC; fig|1411691.4.peg.4281; -.
DR EchoBASE; EB3941; -.
DR eggNOG; COG4812; Bacteria.
DR HOGENOM; CLU_093470_1_0_6; -.
DR InParanoid; P65643; -.
DR OMA; ACCELCH; -.
DR PhylomeDB; P65643; -.
DR BioCyc; EcoCyc:G7289-MON; -.
DR UniPathway; UPA00560; -.
DR PRO; PR:P65643; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0031469; C:bacterial microcompartment; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0008817; F:cob(I)yrinic acid a,c-diamide adenosyltransferase activity; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0009236; P:cobalamin biosynthetic process; IEA:InterPro.
DR GO; GO:0046336; P:ethanolamine catabolic process; IEA:UniProtKB-UniPathway.
DR Gene3D; 1.20.1200.10; -; 1.
DR InterPro; IPR009194; AdoTrfase_EutT.
DR InterPro; IPR016030; CblAdoTrfase-like.
DR InterPro; IPR036451; CblAdoTrfase-like_sf.
DR Pfam; PF01923; Cob_adeno_trans; 1.
DR PIRSF; PIRSF012294; ATR_EutT; 1.
DR SUPFAM; SSF89028; SSF89028; 1.
PE 3: Inferred from homology;
KW ATP-binding; Bacterial microcompartment; Metal-binding; Nucleotide-binding;
KW Reference proteome; Transferase.
FT CHAIN 1..267
FT /note="Corrinoid adenosyltransferase EutT"
FT /id="PRO_0000087100"
FT BINDING 80
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /ligand_note="ligand shared between homodimeric partners"
FT /evidence="ECO:0000250|UniProtKB:Q9ZFV4"
FT BINDING 83
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /ligand_note="ligand shared between homodimeric partners"
FT /evidence="ECO:0000250|UniProtKB:Q9ZFV4"
SQ SEQUENCE 267 AA; 30172 MW; E51EDAB528B4FA76 CRC64;
MKDFITEAWL RANHTLSEGA EIHLPADSRL TPSARELLES RHLRIKFIDE QGRLFVDDEQ
QQPQPVHGLT SSDEHPQACC ELCRQPVAKK PDTLTHLSAE KMVAKSDPRL GFRAVLDSTI
ALAVWLQIEL AEPWQPWLAD IRSRLGNIMR ADALGEPLGC QAIVGLSDED LHRLSHQPLR
YLDHDHLVPE ASHGRDAALL NLLRTKVRET ETVAAQVFIT RSFEVLRPDI LQALNRLSST
VYVMMILSVT KQPLTVKQIQ QRLGETQ
