ID   EUTC_CLOP1              Reviewed;         295 AA.
AC   Q0TSP9;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   05-SEP-2006, sequence version 1.
DT   28-JAN-2026, entry version 89.
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};
GN   OrderedLocusNames=CPF_0892;
OS   Clostridium perfringens (strain ATCC 13124 / DSM 756 / JCM 1290 / NCIMB
OS   6125 / NCTC 8237 / Type A).
OC   Bacteria; Bacillati; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC   Clostridium.
OX   NCBI_TaxID=195103;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 13124 / DSM 756 / JCM 1290 / NCIMB 6125 / NCTC 8237 / S
RC   107 / Type A;
RX   PubMed=16825665; DOI=10.1101/gr.5238106;
RA   Myers G.S.A., Rasko D.A., Cheung J.K., Ravel J., Seshadri R., DeBoy R.T.,
RA   Ren Q., Varga J., Awad M.M., Brinkac L.M., Daugherty S.C., Haft D.H.,
RA   Dodson R.J., Madupu R., Nelson W.C., Rosovitz M.J., Sullivan S.A.,
RA   Khouri H., Dimitrov G.I., Watkins K.L., Mulligan S., Benton J., Radune D.,
RA   Fisher D.J., Atkins H.S., Hiscox T., Jost B.H., Billington S.J.,
RA   Songer J.G., McClane B.A., Titball R.W., Rood J.I., Melville S.B.,
RA   Paulsen I.T.;
RT   "Skewed genomic variability in strains of the toxigenic bacterial pathogen,
RT   Clostridium perfringens.";
RL   Genome Res. 16:1031-1040(2006).
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; CP000246; ABG82727.1; -; Genomic_DNA.
DR   RefSeq; WP_003454028.1; NC_008261.1.
DR   AlphaFoldDB; Q0TSP9; -.
DR   SMR; Q0TSP9; -.
DR   STRING; 195103.CPF_0892; -.
DR   PaxDb; 195103-CPF_0892; -.
DR   GeneID; 93002776; -.
DR   KEGG; cpf:CPF_0892; -.
DR   eggNOG; COG4302; Bacteria.
DR   HOGENOM; CLU_068224_0_0_9; -.
DR   UniPathway; UPA00560; -.
DR   Proteomes; UP000001823; 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:amino acid metabolic process; IEA:InterPro.
DR   GO; GO:0046336; P:ethanolamine catabolic process; IEA:UniProtKB-UniRule.
DR   FunFam; 1.10.30.40:FF:000001; Ethanolamine ammonia-lyase light chain; 1.
DR   FunFam; 3.40.50.11240:FF:000001; Ethanolamine ammonia-lyase light chain; 1.
DR   Gene3D; 3.40.50.11240; Ethanolamine ammonia-lyase light chain (EutC); 1.
DR   Gene3D; 1.10.30.40; Ethanolamine ammonia-lyase light chain (EutC), N-terminal domain; 1.
DR   HAMAP; MF_00601; EutC; 1.
DR   InterPro; IPR009246; EutC.
DR   InterPro; IPR042251; EutC_C.
DR   InterPro; IPR042255; EutC_N.
DR   NCBIfam; NF003971; PRK05465.1; 1.
DR   PANTHER; PTHR39330; ETHANOLAMINE AMMONIA-LYASE LIGHT CHAIN; 1.
DR   PANTHER; PTHR39330:SF1; ETHANOLAMINE AMMONIA-LYASE SMALL SUBUNIT; 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_1000025852"
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
//