ID   EUTC_ECOSE              Reviewed;         295 AA.
AC   B6I516;
DT   14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT   16-DEC-2008, sequence version 1.
DT   03-AUG-2022, entry version 61.
DE   RecName: Full=Ethanolamine ammonia-lyase small subunit {ECO:0000255|HAMAP-Rule:MF_00601};
DE            Short=EAL small subunit {ECO:0000255|HAMAP-Rule:MF_00601};
DE            EC=4.3.1.7 {ECO:0000255|HAMAP-Rule:MF_00601};
GN   Name=eutC {ECO:0000255|HAMAP-Rule:MF_00601}; OrderedLocusNames=ECSE_2730;
OS   Escherichia coli (strain SE11).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=409438;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SE11;
RX   PubMed=18931093; DOI=10.1093/dnares/dsn026;
RA   Oshima K., Toh H., Ogura Y., Sasamoto H., Morita H., Park S.-H., Ooka T.,
RA   Iyoda S., Taylor T.D., Hayashi T., Itoh K., Hattori M.;
RT   "Complete genome sequence and comparative analysis of the wild-type
RT   commensal Escherichia coli strain SE11 isolated from a healthy adult.";
RL   DNA Res. 15:375-386(2008).
CC   -!- FUNCTION: Catalyzes the deamination of various vicinal amino-alcohols
CC       to oxo compounds. Allows this organism to utilize ethanolamine as the
CC       sole source of nitrogen and carbon in the presence of external vitamin
CC       B12. {ECO:0000255|HAMAP-Rule:MF_00601}.
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   -!- COFACTOR:
CC       Name=adenosylcob(III)alamin; Xref=ChEBI:CHEBI:18408;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_00601};
CC       Note=Binds between the large and small subunits. {ECO:0000255|HAMAP-
CC       Rule:MF_00601};
CC   -!- PATHWAY: Amine and polyamine degradation; ethanolamine degradation.
CC       {ECO:0000255|HAMAP-Rule:MF_00601}.
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_00601}.
CC   -!- SUBCELLULAR LOCATION: Bacterial microcompartment {ECO:0000255|HAMAP-
CC       Rule:MF_00601}.
CC   -!- SIMILARITY: Belongs to the EutC family. {ECO:0000255|HAMAP-
CC       Rule:MF_00601}.
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DR   EMBL; AP009240; BAG78254.1; -; Genomic_DNA.
DR   RefSeq; WP_000372307.1; NC_011415.1.
DR   AlphaFoldDB; B6I516; -.
DR   SMR; B6I516; -.
DR   EnsemblBacteria; BAG78254; BAG78254; ECSE_2730.
DR   KEGG; ecy:ECSE_2730; -.
DR   HOGENOM; CLU_068224_0_0_6; -.
DR   OMA; ADRNCVS; -.
DR   UniPathway; UPA00560; -.
DR   Proteomes; UP000008199; Chromosome.
DR   GO; GO:0009350; C:ethanolamine ammonia-lyase complex; IEA:UniProtKB-UniRule.
DR   GO; GO:0031471; C:ethanolamine degradation polyhedral organelle; IEA:UniProtKB-UniRule.
DR   GO; GO:0031419; F:cobalamin binding; IEA:UniProtKB-UniRule.
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   3: Inferred from homology;
KW   Bacterial microcompartment; Cobalamin; Cobalt; Lyase.
FT   CHAIN           1..295
FT                   /note="Ethanolamine ammonia-lyase small subunit"
FT                   /id="PRO_1000130091"
FT   BINDING         207
FT                   /ligand="adenosylcob(III)alamin"
FT                   /ligand_id="ChEBI:CHEBI:18408"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00601"
FT   BINDING         228
FT                   /ligand="adenosylcob(III)alamin"
FT                   /ligand_id="ChEBI:CHEBI:18408"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00601"
FT   BINDING         258
FT                   /ligand="adenosylcob(III)alamin"
FT                   /ligand_id="ChEBI:CHEBI:18408"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00601"
SQ   SEQUENCE   295 AA;  31738 MW;  FEA9FAE9DBC8417B CRC64;
     MDQKQIEEIV RSVMASMGQA APAPSEAKCA ATTCAAPVTS ESCALDLGSA EAKAWIGVEN
     PHRADVLTEL RRSTVARVCT GRAGPRPRTQ ALLRFLADHS RSKDTVLKEV PEEWVKAQGL
     LEVRSEISNK NLYLTRPDMG RRLCAEAVEA LKAQCVANPD VQVVISDGLS TDAITVNYEE
     ILPPLMAGLK QAGLKVGTPF FVRYGRVKIE DQIGEILGAK VVILLVGERP GLGQSESLSC
     YAVYSPRMAT TVEADRTCIS NIHQGGTPPV EAAAVIVDLA KRMLEQKASG INMTR