ID   EUTC_CLOPE              Reviewed;         295 AA.
AC   Q8XLZ1;
DT   25-NOV-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2002, sequence version 1.
DT   03-AUG-2022, entry version 95.
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=CPE0899;
OS   Clostridium perfringens (strain 13 / Type A).
OC   Bacteria; Firmicutes; Clostridia; Eubacteriales; Clostridiaceae;
OC   Clostridium.
OX   NCBI_TaxID=195102;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=13 / Type A;
RX   PubMed=11792842; DOI=10.1073/pnas.022493799;
RA   Shimizu T., Ohtani K., Hirakawa H., Ohshima K., Yamashita A., Shiba T.,
RA   Ogasawara N., Hattori M., Kuhara S., Hayashi H.;
RT   "Complete genome sequence of Clostridium perfringens, an anaerobic flesh-
RT   eater.";
RL   Proc. Natl. Acad. Sci. U.S.A. 99:996-1001(2002).
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; BA000016; BAB80605.1; -; Genomic_DNA.
DR   RefSeq; WP_003454028.1; NC_003366.1.
DR   AlphaFoldDB; Q8XLZ1; -.
DR   SMR; Q8XLZ1; -.
DR   STRING; 195102.gene:10490162; -.
DR   EnsemblBacteria; BAB80605; BAB80605; BAB80605.
DR   GeneID; 29571989; -.
DR   KEGG; cpe:CPE0899; -.
DR   HOGENOM; CLU_068224_0_0_9; -.
DR   OMA; ADRNCVS; -.
DR   UniPathway; UPA00560; -.
DR   Proteomes; UP000000818; 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; 1.10.30.40; -; 1.
DR   Gene3D; 3.40.50.11240; -; 1.
DR   HAMAP; MF_00601; EutC; 1.
DR   InterPro; IPR009246; EutC.
DR   InterPro; IPR042251; EutC_C.
DR   InterPro; IPR042255; EutC_N.
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; Reference proteome.
FT   CHAIN           1..295
FT                   /note="Ethanolamine ammonia-lyase small subunit"
FT                   /id="PRO_0000205986"
FT   BINDING         209
FT                   /ligand="adenosylcob(III)alamin"
FT                   /ligand_id="ChEBI:CHEBI:18408"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00601"
FT   BINDING         230
FT                   /ligand="adenosylcob(III)alamin"
FT                   /ligand_id="ChEBI:CHEBI:18408"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00601"
SQ   SEQUENCE   295 AA;  32309 MW;  155C2C662D362E69 CRC64;
     MNEKDLKLMV EQLVSQMVGQ VDMQSVEKVV KEVSKNQSQV ESDEFIPDIT EIDIKKQLLV
     DNPADREAYL EMKAKTPARL GSGRAGARYK TITALRMRAD HAAAQDSVFS DVSEEFIKKN
     NFIPVKTMCT DKDEYVTRPD LGRRFSPETT EIIKEKCDKN PKVQIMVGDG LSSAAIEANV
     EDILPSIEQG LKMYGLNVGP ILFVKYCRVP AMDAVGEATG ADVVCLLVGE RPGLVTAESM
     SAYIAYKPKV GMPEAKRTVI SNIHKGGTTA VEAGAHIAEL IKTMLDKKAS GIDLK