EUTT_ECOL6
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 03-AUG-2022, entry version 79.
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; OrderedLocusNames=c2984;
OS Escherichia coli O6:H1 (strain CFT073 / ATCC 700928 / UPEC).
OC Bacteria; Proteobacteria; 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)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}.
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DR EMBL; AE014075; AAN81434.1; -; Genomic_DNA.
DR RefSeq; WP_000651298.1; NC_004431.1.
DR AlphaFoldDB; P65644; -.
DR SMR; P65644; -.
DR STRING; 199310.c2984; -.
DR EnsemblBacteria; AAN81434; AAN81434; c2984.
DR GeneID; 66673680; -.
DR KEGG; ecc:c2984; -.
DR eggNOG; COG4812; Bacteria.
DR HOGENOM; CLU_093470_1_0_6; -.
DR OMA; ACCELCH; -.
DR BioCyc; ECOL199310:C2984-MON; -.
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: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 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
