EUTB_SALTY
ID EUTB_SALTY Reviewed; 453 AA.
AC P19264; Q9ZFV1;
DT 01-NOV-1990, integrated into UniProtKB/Swiss-Prot.
DT 30-MAY-2000, sequence version 2.
DT 03-AUG-2022, entry version 121.
DE RecName: Full=Ethanolamine ammonia-lyase large subunit {ECO:0000255|HAMAP-Rule:MF_00861, ECO:0000303|PubMed:2197274};
DE Short=EAL large subunit {ECO:0000255|HAMAP-Rule:MF_00861};
DE EC=4.3.1.7 {ECO:0000255|HAMAP-Rule:MF_00861, ECO:0000269|PubMed:1550360};
DE AltName: Full=Ethanolamine ammonia-lyase alpha subunit {ECO:0000303|PubMed:1550360};
DE AltName: Full=Ethanolamine ammonia-lyase heavy chain;
GN Name=eutB {ECO:0000255|HAMAP-Rule:MF_00861, ECO:0000303|PubMed:2656649};
GN OrderedLocusNames=STM2458;
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 DISRUPTION PHENOTYPE.
RC STRAIN=SL1344;
RX PubMed=26565973; DOI=10.1371/journal.ppat.1005278;
RA Anderson C.J., Clark D.E., Adli M., Kendall M.M.;
RT "Ethanolamine Signaling Promotes Salmonella Niche Recognition and
RT Adaptation during Infection.";
RL PLoS Pathog. 11:e1005278-e1005278(2015).
RN [9]
RP ERRATUM OF PUBMED:26565973.
RX PubMed=26684793; DOI=10.1371/journal.ppat.1005365;
RA Anderson C.J., Clark D.E., Adli M., Kendall M.M.;
RT "Correction: Ethanolamine Signaling Promotes Salmonella Niche Recognition
RT and Adaptation during Infection.";
RL PLoS Pathog. 11:e1005365-e1005365(2015).
RN [10]
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 [11]
RP SUBCELLULAR LOCATION.
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 [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 BMC assembly or maintenance (Probable). {ECO:0000250|UniProtKB:P0AEJ6,
CC ECO:0000305|PubMed:1550360, ECO:0000305|PubMed:2197274,
CC 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_00861,
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_00861,
CC ECO:0000269|PubMed:1550360};
CC Note=Binds between the large and small subunits. {ECO:0000255|HAMAP-
CC Rule:MF_00861};
CC -!- PATHWAY: Amine and polyamine degradation; ethanolamine degradation.
CC {ECO:0000255|HAMAP-Rule:MF_00861, ECO:0000269|PubMed:3045078}.
CC -!- SUBUNIT: The basic unit is a heterodimer which dimerizes to form
CC tetramers. The heterotetramers trimerize; 6 large subunits form a core
CC ring with 6 small subunits projecting outwards. {ECO:0000255|HAMAP-
CC Rule:MF_00861, ECO:0000305|PubMed:1550360}.
CC -!- SUBCELLULAR LOCATION: Bacterial microcompartment {ECO:0000255|HAMAP-
CC Rule:MF_00861, ECO:0000305|PubMed:22428024}. Note=Probably located in
CC the BMC; as EutC is targeted to the BMC interior this subunit should be
CC in the same location (Probable). Has been suggested to be on the
CC exterior of the BMC (PubMed:23585538). {ECO:0000269|PubMed:23585538,
CC ECO:0000305|PubMed:22428024}.
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 -!- DISRUPTION PHENOTYPE: No aerobic growth on ethanolamine (EA)
CC supplemented with cobalamin (vitamin B12) (PubMed:10464203,
CC PubMed:2656649). No phenotype during growth in vitro. Decreased
CC expression of eutR during bacterial growth in vitro. About 10-fold
CC outcompeted by wild-type in mouse intestine at 2 and 4 days following
CC oral infection, but no effect seen during growth in peritoneal exudate
CC macrophages (PubMed:26565973). A non-polar deletion mutant does not
CC grow on EA between pH 5.5 and pH 8.5, stops acetaldehyde release on EA
CC plus vitamin B12 (PubMed:16585748). A deletion allows growth on
CC 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:26565973, ECO:0000269|PubMed:2656649}.
CC -!- SIMILARITY: Belongs to the EutB family. {ECO:0000255|HAMAP-
CC Rule:MF_00861}.
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DR EMBL; J05518; AAA27061.1; -; Genomic_DNA.
DR EMBL; AF093749; AAC78123.1; -; Genomic_DNA.
DR EMBL; AE006468; AAL21352.1; -; Genomic_DNA.
DR PIR; A36570; A36570.
DR RefSeq; NP_461393.1; NC_003197.2.
DR RefSeq; WP_000769990.1; NC_003197.2.
DR AlphaFoldDB; P19264; -.
DR SMR; P19264; -.
DR STRING; 99287.STM2458; -.
DR PaxDb; P19264; -.
DR EnsemblBacteria; AAL21352; AAL21352; STM2458.
DR GeneID; 1253980; -.
DR KEGG; stm:STM2458; -.
DR PATRIC; fig|99287.12.peg.2596; -.
DR HOGENOM; CLU_048555_0_0_6; -.
DR OMA; FGKTYQF; -.
DR PhylomeDB; P19264; -.
DR BioCyc; SENT99287:STM2458-MON; -.
DR BRENDA; 4.3.1.7; 5542.
DR UniPathway; UPA00560; -.
DR Proteomes; UP000001014; Chromosome.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0009350; C:ethanolamine ammonia-lyase complex; IDA:UniProtKB.
DR GO; GO:0031471; C:ethanolamine degradation polyhedral organelle; IPI:UniProtKB.
DR GO; GO:0031419; F:cobalamin binding; IEA:UniProtKB-KW.
DR GO; GO:0008851; F:ethanolamine ammonia-lyase activity; IEA:UniProtKB-EC.
DR GO; GO:0006520; P:cellular amino acid metabolic process; IEA:InterPro.
DR GO; GO:0046336; P:ethanolamine catabolic process; IBA:GO_Central.
DR Gene3D; 1.10.220.70; -; 1.
DR Gene3D; 2.30.170.30; -; 1.
DR Gene3D; 3.20.20.70; -; 1.
DR HAMAP; MF_00861; EutB; 1.
DR InterPro; IPR013785; Aldolase_TIM.
DR InterPro; IPR010628; EutB.
DR InterPro; IPR044939; EutB_dom_2_sf.
DR InterPro; IPR044941; EutB_N_sf.
DR PANTHER; PTHR39329; PTHR39329; 1.
DR Pfam; PF06751; EutB; 1.
DR PIRSF; PIRSF018788; EutB; 1.
PE 1: Evidence at protein level;
KW Bacterial microcompartment; Cobalamin; Cobalt; Lyase; Reference proteome;
KW Virulence.
FT CHAIN 1..453
FT /note="Ethanolamine ammonia-lyase large subunit"
FT /id="PRO_0000087083"
FT BINDING 160..162
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00861"
FT BINDING 193
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00861"
FT BINDING 194
FT /ligand="adenosylcob(III)alamin"
FT /ligand_id="ChEBI:CHEBI:18408"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00861"
FT BINDING 246
FT /ligand="adenosylcob(III)alamin"
FT /ligand_id="ChEBI:CHEBI:18408"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00861"
FT BINDING 287
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00861"
FT BINDING 295
FT /ligand="adenosylcob(III)alamin"
FT /ligand_id="ChEBI:CHEBI:18408"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00861"
FT BINDING 362
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00861"
FT BINDING 401
FT /ligand="adenosylcob(III)alamin"
FT /ligand_id="ChEBI:CHEBI:18408"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00861"
FT CONFLICT 211..238
FT /note="GVIDKFNIPTQGCVLAHVTTQIEAIRRG -> ALSINSIFRPRAACWRTSPP
FT RSKRFVA (in Ref. 1; AAA27061)"
FT /evidence="ECO:0000305"
FT CONFLICT 242..251
FT /note="GLIFQSICGS -> RTDFPEHLRH (in Ref. 1; AAA27061)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 453 AA; 49449 MW; 0B4025D42F283BF8 CRC64;
MKLKTTLFGN VYQFKDVKEV LAKANELRSG DVLAGVAAAS SQERVAAKQV LSEMTVADIR
NNPVIAYEED CVTRLIQDDV NETAYNRIKN WSISELREYV LSDETSVDDI AFTRKGLTSE
VVAAVAKICS NADLIYGGKK MPVIKKANTT IGIPGTFSCR LQPNDTRDDV QSIAAQIYEG
LSFGAGDAVI GVNPVTDDVE NLTRVLDTVY GVIDKFNIPT QGCVLAHVTT QIEAIRRGAP
GGLIFQSICG SEKGLKEFGV ELAMLDEARA VGAEFNRIAG ENCLYFETGQ GSALSAGANF
GADQVTMEAR NYGLARHYDP FLVNTVVGFI GPEYLYNDRQ IIRAGLEDHF MGKLSGISMG
CDCCYTNHAD ADQNLNENLM ILLATAGCNY IMGMPLGDDI MLNYQTTAFH DTATVRQLLN
LRPSPEFERW LETMGIMANG RLTKRAGDPS LFF
