EUTC_SALTY
ID EUTC_SALTY Reviewed; 298 AA.
AC P19265; Q9ZFV0;
DT 01-NOV-1990, integrated into UniProtKB/Swiss-Prot.
DT 30-MAY-2000, sequence version 3.
DT 03-AUG-2022, entry version 121.
DE RecName: Full=Ethanolamine ammonia-lyase small subunit {ECO:0000255|HAMAP-Rule:MF_00601, ECO:0000303|PubMed:2197274};
DE Short=EAL small subunit {ECO:0000255|HAMAP-Rule:MF_00601};
DE EC=4.3.1.7 {ECO:0000255|HAMAP-Rule:MF_00601, ECO:0000269|PubMed:1550360};
DE AltName: Full=Ethanolamine ammonia-lyase beta subunit {ECO:0000303|PubMed:1550360};
GN Name=eutC {ECO:0000255|HAMAP-Rule:MF_00601, ECO:0000303|PubMed:2197274};
GN OrderedLocusNames=STM2457;
OS Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Salmonella.
OX NCBI_TaxID=99287;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND FUNCTION.
RC STRAIN=LT2;
RX PubMed=2197274; DOI=10.1016/s0021-9258(19)38368-1;
RA Faust L.R.P., Connor J.A., Roof D.M., Hoch J.A., Babior B.M.;
RT "Cloning, sequencing, and expression of the genes encoding the
RT adenosylcobalamin-dependent ethanolamine ammonia-lyase of Salmonella
RT typhimurium.";
RL J. Biol. Chem. 265:12462-12466(1990).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], DISRUPTION PHENOTYPE, AND SEQUENCE
RP REVISION.
RC STRAIN=LT2;
RX PubMed=10464203; DOI=10.1128/jb.181.17.5317-5329.1999;
RA Kofoid E.C., Rappleye C.A., Stojiljkovic I., Roth J.R.;
RT "The 17-gene ethanolamine (eut) operon of Salmonella typhimurium encodes
RT five homologues of carboxysome shell proteins.";
RL J. Bacteriol. 181:5317-5329(1999).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LT2 / SGSC1412 / ATCC 700720;
RX PubMed=11677609; DOI=10.1038/35101614;
RA McClelland M., Sanderson K.E., Spieth J., Clifton S.W., Latreille P.,
RA Courtney L., Porwollik S., Ali J., Dante M., Du F., Hou S., Layman D.,
RA Leonard S., Nguyen C., Scott K., Holmes A., Grewal N., Mulvaney E.,
RA Ryan E., Sun H., Florea L., Miller W., Stoneking T., Nhan M., Waterston R.,
RA Wilson R.K.;
RT "Complete genome sequence of Salmonella enterica serovar Typhimurium LT2.";
RL Nature 413:852-856(2001).
RN [4]
RP FUNCTION, PATHWAY, OPERON, AND INDUCTION BY ETHANOLAMINE AND COBALAMIN.
RC STRAIN=LT2;
RX PubMed=3045078; DOI=10.1128/jb.170.9.3855-3863.1988;
RA Roof D.M., Roth J.R.;
RT "Ethanolamine utilization in Salmonella typhimurium.";
RL J. Bacteriol. 170:3855-3863(1988).
RN [5]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RC STRAIN=LT2;
RX PubMed=2656649; DOI=10.1128/jb.171.6.3316-3323.1989;
RA Roof D.M., Roth J.R.;
RT "Functions required for vitamin B12-dependent ethanolamine utilization in
RT Salmonella typhimurium.";
RL J. Bacteriol. 171:3316-3323(1989).
RN [6]
RP FUNCTION, CATALYTIC ACTIVITY, COFACTOR, BIOPHYSICOCHEMICAL PROPERTIES, AND
RP SUBUNIT.
RC STRAIN=LT2;
RX PubMed=1550360; DOI=10.1016/0003-9861(92)90135-j;
RA Faust L.P., Babior B.M.;
RT "Overexpression, purification, and some properties of the AdoCbl-dependent
RT ethanolamine ammonia-lyase from Salmonella typhimurium.";
RL Arch. Biochem. Biophys. 294:50-54(1992).
RN [7]
RP DISRUPTION PHENOTYPE.
RC STRAIN=LT2;
RX PubMed=16585748; DOI=10.1128/jb.188.8.2865-2874.2006;
RA Penrod J.T., Roth J.R.;
RT "Conserving a volatile metabolite: a role for carboxysome-like organelles
RT in Salmonella enterica.";
RL J. Bacteriol. 188:2865-2874(2006).
RN [8]
RP FUNCTION, INTERACTION WITH EUTS, SUBUNIT, SUBCELLULAR LOCATION, DOMAIN, AND
RP BIOTECHNOLOGY.
RC STRAIN=LT2;
RX PubMed=22428024; DOI=10.1371/journal.pone.0033342;
RA Choudhary S., Quin M.B., Sanders M.A., Johnson E.T., Schmidt-Dannert C.;
RT "Engineered protein nano-compartments for targeted enzyme localization.";
RL PLoS ONE 7:e33342-e33342(2012).
RN [9]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RC STRAIN=LT2;
RX PubMed=23585538; DOI=10.1128/jb.02179-12;
RA Huseby D.L., Roth J.R.;
RT "Evidence that a metabolic microcompartment contains and recycles private
RT cofactor pools.";
RL J. Bacteriol. 195:2864-2879(2013).
RN [10]
RP FUNCTION, SUBUNIT, SUBCELLULAR LOCATION, AND BIOTECHNOLOGY.
RC STRAIN=LT2;
RX PubMed=27063436; DOI=10.1038/srep24359;
RA Held M., Kolb A., Perdue S., Hsu S.Y., Bloch S.E., Quin M.B.,
RA Schmidt-Dannert C.;
RT "Engineering formation of multiple recombinant Eut protein nanocompartments
RT in E. coli.";
RL Sci. Rep. 6:24359-24359(2016).
RN [11]
RP FUNCTION, SUBUNIT, SUBCELLULAR LOCATION, DOMAIN, AND BIOTECHNOLOGY.
RC STRAIN=LT2;
RX PubMed=27450681; DOI=10.1007/s00253-016-7737-8;
RA Quin M.B., Perdue S.A., Hsu S.Y., Schmidt-Dannert C.;
RT "Encapsulation of multiple cargo proteins within recombinant Eut
RT nanocompartments.";
RL Appl. Microbiol. Biotechnol. 100:9187-9200(2016).
RN [12]
RP FUNCTION.
RC STRAIN=SL1344;
RX PubMed=29531136; DOI=10.1128/iai.00172-18;
RA Anderson C.J., Satkovich J., Koeseoglu V.K., Agaisse H., Kendall M.M.;
RT "The Ethanolamine Permease EutH Promotes Vacuole Adaptation of Salmonella
RT enterica and Listeria monocytogenes during Macrophage Infection.";
RL Infect. Immun. 86:0-0(2018).
CC -!- FUNCTION: Catalyzes the deamination of various vicinal amino-alcohols
CC to oxo compounds (Probable). It is spontaneously inactivated by its
CC substrate and reactivated by EutA (By similarity). May play a role in
CC bacterial microcompartment (BMC) assembly or maintenance (Probable).
CC Directly targeted to the BMC (PubMed:22428024, PubMed:27063436,
CC PubMed:27450681). {ECO:0000250|UniProtKB:P19636,
CC ECO:0000269|PubMed:22428024, ECO:0000269|PubMed:27063436,
CC ECO:0000269|PubMed:27450681, ECO:0000305|PubMed:1550360,
CC ECO:0000305|PubMed:2197274, ECO:0000305|PubMed:23585538}.
CC -!- FUNCTION: Expression of the eut operon allows this bacteria to use
CC ethanolamine (EA) as a carbon, nitrogen and energy source. It relies on
CC cobalamin (vitamin B12) both as a cofactor for the ethanolamine
CC ammonia-lyase activity and to induce the operon. EA enhances bacterial
CC survival in macrophages in a concentration-dependent manner, suggesting
CC it is an important nutrient during infection (PubMed:29531136).
CC {ECO:0000269|PubMed:29531136, ECO:0000269|PubMed:3045078}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ethanolamine = acetaldehyde + NH4(+); Xref=Rhea:RHEA:15313,
CC ChEBI:CHEBI:15343, ChEBI:CHEBI:28938, ChEBI:CHEBI:57603; EC=4.3.1.7;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_00601,
CC ECO:0000269|PubMed:1550360, ECO:0000305|PubMed:2656649,
CC ECO:0000305|PubMed:3045078};
CC -!- COFACTOR:
CC Name=adenosylcob(III)alamin; Xref=ChEBI:CHEBI:18408;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_00601,
CC ECO:0000269|PubMed:1550360};
CC Note=Binds between the large and small subunits. {ECO:0000255|HAMAP-
CC Rule:MF_00601};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.51 uM for adenosylcob(III)alamin {ECO:0000269|PubMed:1550360};
CC -!- PATHWAY: Amine and polyamine degradation; ethanolamine degradation.
CC {ECO:0000255|HAMAP-Rule:MF_00601, ECO:0000269|PubMed:3045078}.
CC -!- SUBUNIT: The basic unit is a heterodimer which dimerizes to form
CC tetramers (PubMed:1550360). The heterotetramers trimerize; 6 large
CC subunits form a core ring with 6 small subunits projecting outwards
CC (Probable). Interacts with EutS, which targets it to the interior of
CC the BMC (PubMed:22428024, PubMed:27063436, PubMed:27450681).
CC {ECO:0000269|PubMed:1550360, ECO:0000269|PubMed:22428024,
CC ECO:0000269|PubMed:27063436, ECO:0000269|PubMed:27450681,
CC ECO:0000305|PubMed:1550360}.
CC -!- SUBCELLULAR LOCATION: Bacterial microcompartment {ECO:0000255|HAMAP-
CC Rule:MF_00601, ECO:0000269|PubMed:22428024,
CC ECO:0000269|PubMed:27063436, ECO:0000269|PubMed:27450681}.
CC Note=Probably located inside the BMC (Probable). Has been suggested to
CC be on the BMC exterior. {ECO:0000269|PubMed:23585538,
CC ECO:0000305|PubMed:22428024, ECO:0000305|PubMed:23585538,
CC ECO:0000305|PubMed:27063436, ECO:0000305|PubMed:27450681}.
CC -!- INDUCTION: Part of the 17-gene eut operon transcribed from a single
CC promoter, induced by ethanolamine and adenosylcobalamin (AdoCbl,
CC vitamin B12). {ECO:0000269|PubMed:3045078}.
CC -!- DOMAIN: The first 19 residues target foreign proteins (tested with
CC eGFP, mCherry and lacZ) to the BMC both in situ and in E.coli. The
CC cargo is only detected by Western blot in broken shells, strongly
CC suggesting this protein is normally found inside the BMC and not on its
CC exterior. {ECO:0000269|PubMed:22428024, ECO:0000269|PubMed:27063436,
CC ECO:0000269|PubMed:27450681}.
CC -!- DISRUPTION PHENOTYPE: No aerobic growth on ethanolamine (EA)
CC supplemented with cobalamin (vitamin B12) (PubMed:10464203,
CC PubMed:2656649). A non-polar deletion mutant does not grow on EA
CC between pH 5.5 and pH 8.5 (PubMed:16585748). A deletion allows growth
CC on acetate, suggesting BMC assembly or maintenance is impaired
CC (PubMed:23585538). {ECO:0000269|PubMed:10464203,
CC ECO:0000269|PubMed:16585748, ECO:0000269|PubMed:23585538,
CC ECO:0000269|PubMed:2656649}.
CC -!- BIOTECHNOLOGY: Artificial BMCs can be made in E.coli by expressing
CC eutK, eutL, eutM, eutN, eutS (eutSMNLK) or eutS alone. Cargo proteins
CC can be targeted to them using the first 19 residues of this protein.
CC Beta-galactosidase (lacZ) was active within the BMC, showing the BMC
CC allows passage of substrate into the interior. This can lead to the
CC development of tailored BMCs for specific metabolic reactions.
CC {ECO:0000269|PubMed:22428024, ECO:0000269|PubMed:27063436}.
CC -!- SIMILARITY: Belongs to the EutC family. {ECO:0000255|HAMAP-
CC Rule:MF_00601}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; J05518; AAA27062.1; -; Genomic_DNA.
DR EMBL; AF093749; AAC78124.1; -; Genomic_DNA.
DR EMBL; AE006468; AAL21351.1; -; Genomic_DNA.
DR PIR; B36570; B36570.
DR RefSeq; NP_461392.1; NC_003197.2.
DR RefSeq; WP_000372335.1; NC_003197.2.
DR AlphaFoldDB; P19265; -.
DR SMR; P19265; -.
DR STRING; 99287.STM2457; -.
DR PaxDb; P19265; -.
DR DNASU; 1253979; -.
DR EnsemblBacteria; AAL21351; AAL21351; STM2457.
DR GeneID; 1253979; -.
DR KEGG; stm:STM2457; -.
DR PATRIC; fig|99287.12.peg.2595; -.
DR HOGENOM; CLU_068224_2_0_6; -.
DR OMA; ADRNCVS; -.
DR PhylomeDB; P19265; -.
DR BioCyc; SENT99287:STM2457-MON; -.
DR BRENDA; 4.3.1.7; 5542.
DR UniPathway; UPA00560; -.
DR Proteomes; UP000001014; Chromosome.
DR GO; GO:0009350; C:ethanolamine ammonia-lyase complex; IDA:UniProtKB.
DR GO; GO:0031471; C:ethanolamine degradation polyhedral organelle; IMP:UniProtKB.
DR GO; GO:0031419; F:cobalamin binding; IBA:GO_Central.
DR GO; GO:0008851; F:ethanolamine ammonia-lyase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0006520; P:cellular amino acid metabolic process; IEA:InterPro.
DR GO; GO:0046336; P:ethanolamine catabolic process; IEA:UniProtKB-UniRule.
DR Gene3D; 3.40.50.11240; -; 1.
DR HAMAP; MF_00601; EutC; 1.
DR InterPro; IPR009246; EutC.
DR InterPro; IPR042251; EutC_C.
DR PANTHER; PTHR39330; PTHR39330; 1.
DR Pfam; PF05985; EutC; 1.
DR PIRSF; PIRSF018982; EutC; 1.
PE 1: Evidence at protein level;
KW Bacterial microcompartment; Cobalamin; Cobalt; Lyase; Reference proteome;
KW Virulence.
FT CHAIN 1..298
FT /note="Ethanolamine ammonia-lyase small subunit"
FT /id="PRO_0000206003"
FT REGION 1..19
FT /note="Targets protein to the BMC"
FT /evidence="ECO:0000269|PubMed:22428024,
FT ECO:0000269|PubMed:23585538, ECO:0000269|PubMed:27450681"
FT BINDING 210
FT /ligand="adenosylcob(III)alamin"
FT /ligand_id="ChEBI:CHEBI:18408"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00601"
FT BINDING 231
FT /ligand="adenosylcob(III)alamin"
FT /ligand_id="ChEBI:CHEBI:18408"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00601"
FT BINDING 261
FT /ligand="adenosylcob(III)alamin"
FT /ligand_id="ChEBI:CHEBI:18408"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00601"
FT CONFLICT 45
FT /note="S -> T (in Ref. 1; AAA27062)"
FT /evidence="ECO:0000305"
FT CONFLICT 82..97
FT /note="CTGRAGPRPRTQALLR -> LYGACRAASAHPGAVA (in Ref. 1;
FT AAA27062)"
FT /evidence="ECO:0000305"
FT CONFLICT 122
FT /note="G -> GLLEVRSEEWVKAQG (in Ref. 1; AAA27062)"
FT /evidence="ECO:0000305"
FT CONFLICT 253..298
FT /note="TTVEADRTCISNIHQGGTPPVEAAAVIVDLAKRMLEQKASGINMTR -> PP
FT SRPTEPVFQTFIRGGRRQ (in Ref. 1; AAA27062)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 298 AA; 32137 MW; C681A995C6A1671A CRC64;
MDQKQIEEIV RSVMASMGQD VPQPAAPSTQ EGAKPQCAAP TVTESCALDL GSAEAKAWIG
VENPHRADVL TELRRSTAAR VCTGRAGPRP RTQALLRFLA DHSRSKDTVL KEVPEEWVKA
QGLLEVRSEI SDKNLYLTRP DMGRRLSPEA IDALKSQCVM NPDVQVVVSD GLSTDAITAN
YEEILPPLLA GLKQAGLNVG TPFFVRYGRV KIEDQIGEIL GAKVVILLVG ERPGLGQSES
LSCYAVYSPR VATTVEADRT CISNIHQGGT PPVEAAAVIV DLAKRMLEQK ASGINMTR
