Q9ZFV4EUTT_SALTYCorrinoid adenosyltransferase EutT2.5.1.154ATP:co(I)rrinoid adenosyltransferaseACATCob(II)alamin adenosyltransferase EutTEthanolamine utilization cobalamin adenosyltransferaseEthanolamine utilization corrinoid adenosyltransferaseEutT adenosyltransferaseeutTSTM2467Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)BacteriaPseudomonadotaGammaproteobacteriaEnterobacteralesEnterobacteriaceaeSalmonellaThe 17-gene ethanolamine (eut) operon of Salmonella typhimurium encodes five homologues of carboxysome shell proteins.NUCLEOTIDE SEQUENCE [GENOMIC DNA]DISRUPTION PHENOTYPEComplete genome sequence of Salmonella enterica serovar Typhimurium LT2.NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]Ethanolamine utilization in Salmonella typhimurium.FUNCTIONPATHWAYOPERONINDUCTION BY ETHANOLAMINE AND COBALAMINEvidence that a B12-adenosyl transferase is encoded within the ethanolamine operon of Salmonella enterica.FUNCTIONDISRUPTION PHENOTYPEConserving a volatile metabolite: a role for carboxysome-like organelles in Salmonella enterica.DISRUPTION PHENOTYPEPurification and initial biochemical characterization of ATP:Cob(I)alamin adenosyltransferase (EutT) enzyme of Salmonella enterica.FUNCTIONCATALYTIC ACTIVITYSUBSTRATE SPECIFICITYCOFACTORBIOPHYSICOCHEMICAL PROPERTIESMUTAGENESIS OF CYS-79; CYS-80 AND CYS-83The EutT enzyme of Salmonella enterica is a unique ATP:Cob(I)alamin adenosyltransferase metalloprotein that requires ferrous ions for maximal activity.FUNCTIONCOFACTORSUBUNITMUTAGENESIS OF HIS-67; HIS-75; CYS-79; CYS-80 AND CYS-83Spectroscopic Studies of the EutT Adenosyltransferase from Salmonella enterica: Evidence of a Tetrahedrally Coordinated Divalent Transition Metal Cofactor with Cysteine Ligation.COFACTORMUTAGENESIS OF HIS-67; HIS-75; CYS-79; CYS-80 AND CYS-83The Ethanolamine Permease EutH Promotes Vacuole Adaptation of Salmonella enterica and Listeria monocytogenes during Macrophage Infection.FUNCTIONConverts cyanocobalamin (CN-B12) to adenosylcobalamin (AdoCbl), the inducer of the eut operon (PubMed:15516577, PubMed:16636051, PubMed:24336938). Is not active on cobinamide nor other intermediates in the adenosylcobalamin synthetic pathway. Allows full induction of the eut operon (PubMed:15516577). Can use ADP, CTP and dATP in place of ATP, and cobinamide in place of cobalamin, none are as efficiently used as ATP and cobalamin (PubMed:16636051).Expression of the eut operon allows this bacteria to use ethanolamine (EA) as a carbon, nitrogen and energy source. It relies on cobalamin (vitamin B12) both as a cofactor for the ethanolamine ammonia-lyase (EAL) activity and to induce the operon (PubMed:3045078). EA enhances bacterial survival in macrophages in a concentration-dependent manner, suggesting it is an important nutrient during infection (PubMed:29531136).2 ATP + 2 cob(II)alamin + 2 H2O + reduced [electron-transfer flavoprotein] = 2 adenosylcob(III)alamin + 2 diphosphate + 3 H(+) + oxidized [electron-transfer flavoprotein] + 2 phosphate2 ATP + 2 cob(II)inamide + 2 H2O + reduced [electron-transfer flavoprotein] = 2 adenosylcob(III)inamide + 2 diphosphate + 3 H(+) + oxidized [electron-transfer flavoprotein] + 2 phosphatea divalent metal cationBinds 1 divalent metal cation ion per homodimer with both subunits providing Cys ligands; Fe(2+) gives most activity and is possibly the physiological cofactor, followed by Zn(2+) and Co(2+) (PubMed:24336938, PubMed:28045498). Activity stimulated by Mn(2+) (PubMed:16636051).10 uM for ATP4.1 uM for cob(I)alaminkcat is 0.03 sec(-1).Optimum pH is 7.0.Amine and polyamine degradation; ethanolamine degradation.Homodimer.Bacterial microcompartmentPart of the 17-gene eut operon transcribed from a single promoter, induced by ethanolamine and adenosylcobalamin (AdoCbl, vitamin B12).A quadruple eutP-eutQ-eutT-eutD deletion is not impaired for aerobic growth on ethanolamine (EA) supplemented with cobalamin (vitamin B12) (PubMed:10464203). Can grow on EA as sole carbon source when AdoB12 is supplied; double cobA-eutT mutants do not grow with CN-B12 as a nitrogen source (PubMed:15516577). A non-polar deletion mutant grows on EA from pH 5.5 to pH 8.0, but does not grow at pH 8.5, no change in acetaldehyde release on EA plus vitamin B12 (PubMed:16585748).Belongs to the Cob(I)alamin adenosyltransferase family. EutT subfamily.ATP-bindingBacterial microcompartmentIronMetal-bindingNucleotide-bindingReference proteomeTransferasea divalent metal cationligand shared between homodimeric partnersa divalent metal cationligand shared between homodimeric partnersHAHACACACAMNDFITETWLRANHTLSEGSEIHLPADARLTPSARELLESRRLRIKFLDPQGRLFVDDDEQQPQPVHGLTSSDTHPQACCELCRQPVVKKPDTLTHLTADKMVAKSDPRLGFRAALDSAIALTVWLQIELAEPWQPWLFDIRSRLGNIMRADAIDEPLAAQSIVGLNEDELHRLSHQPLRYLDHDHLVPEASHGRDAALLNLLRTKVRETETLAAQVFITRSFEVLRPDILQALNRLSSTVYVMMILSVAKHPLTVAQIQQRLGEKP
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