ID   EUTT_ECOL6              Reviewed;         267 AA.
AC   P65644; P76554;
DT   11-OCT-2004, integrated into UniProtKB/Swiss-Prot.
DT   11-OCT-2004, sequence version 1.
DT   27-MAR-2024, entry version 86.
DE   RecName: Full=Corrinoid adenosyltransferase EutT {ECO:0000305};
DE            EC=2.5.1.154 {ECO:0000250|UniProtKB:Q9ZFV4};
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; OrderedLocusNames=c2984;
OS   Escherichia coli O6:H1 (strain CFT073 / ATCC 700928 / UPEC).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=199310;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CFT073 / ATCC 700928 / UPEC;
RX   PubMed=12471157; DOI=10.1073/pnas.252529799;
RA   Welch R.A., Burland V., Plunkett G. III, Redford P., Roesch P., Rasko D.,
RA   Buckles E.L., Liou S.-R., Boutin A., Hackett J., Stroud D., Mayhew G.F.,
RA   Rose D.J., Zhou S., Schwartz D.C., Perna N.T., Mobley H.L.T.,
RA   Donnenberg M.S., Blattner F.R.;
RT   "Extensive mosaic structure revealed by the complete genome sequence of
RT   uropathogenic Escherichia coli.";
RL   Proc. Natl. Acad. Sci. U.S.A. 99:17020-17024(2002).
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)alamin + 2 H2O + reduced [electron-transfer
CC         flavoprotein] = 2 adenosylcob(III)alamin + 2 diphosphate + 3 H(+) +
CC         oxidized [electron-transfer flavoprotein] + 2 phosphate;
CC         Xref=Rhea:RHEA:66828, Rhea:RHEA-COMP:10685, Rhea:RHEA-COMP:10686,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:16304,
CC         ChEBI:CHEBI:18408, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019,
CC         ChEBI:CHEBI:43474, ChEBI:CHEBI:57692, ChEBI:CHEBI:58307;
CC         EC=2.5.1.154; Evidence={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         EC=2.5.1.154; 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}.
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DR   EMBL; AE014075; AAN81434.1; -; Genomic_DNA.
DR   RefSeq; WP_000651298.1; NZ_CP051263.1.
DR   AlphaFoldDB; P65644; -.
DR   SMR; P65644; -.
DR   STRING; 199310.c2984; -.
DR   GeneID; 75204269; -.
DR   KEGG; ecc:c2984; -.
DR   eggNOG; COG4812; Bacteria.
DR   HOGENOM; CLU_093470_1_0_6; -.
DR   BioCyc; ECOL199310:C2984-MONOMER; -.
DR   UniPathway; UPA00560; -.
DR   Proteomes; UP000001410; 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:corrinoid 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; Cobalamin adenosyltransferase-like; 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; Cobalamin adenosyltransferase-like; 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_0000087099"
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
//