ID   EUTC_CLOAB              Reviewed;         242 AA.
AC   Q97FL9;
DT   25-NOV-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2001, sequence version 1.
DT   03-AUG-2022, entry version 97.
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=CA_C2717;
OS   Clostridium acetobutylicum (strain ATCC 824 / DSM 792 / JCM 1419 / LMG 5710
OS   / VKM B-1787).
OC   Bacteria; Firmicutes; Clostridia; Eubacteriales; Clostridiaceae;
OC   Clostridium.
OX   NCBI_TaxID=272562;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 824 / DSM 792 / JCM 1419 / LMG 5710 / VKM B-1787;
RX   PubMed=11466286; DOI=10.1128/jb.183.16.4823-4838.2001;
RA   Noelling J., Breton G., Omelchenko M.V., Makarova K.S., Zeng Q., Gibson R.,
RA   Lee H.M., Dubois J., Qiu D., Hitti J., Wolf Y.I., Tatusov R.L., Sabathe F.,
RA   Doucette-Stamm L.A., Soucaille P., Daly M.J., Bennett G.N., Koonin E.V.,
RA   Smith D.R.;
RT   "Genome sequence and comparative analysis of the solvent-producing
RT   bacterium Clostridium acetobutylicum.";
RL   J. Bacteriol. 183:4823-4838(2001).
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; AE001437; AAK80663.1; -; Genomic_DNA.
DR   PIR; D97234; D97234.
DR   RefSeq; NP_349323.1; NC_003030.1.
DR   RefSeq; WP_010966004.1; NC_003030.1.
DR   AlphaFoldDB; Q97FL9; -.
DR   SMR; Q97FL9; -.
DR   STRING; 272562.CA_C2717; -.
DR   EnsemblBacteria; AAK80663; AAK80663; CA_C2717.
DR   GeneID; 44999205; -.
DR   KEGG; cac:CA_C2717; -.
DR   PATRIC; fig|272562.8.peg.2906; -.
DR   eggNOG; COG4302; Bacteria.
DR   HOGENOM; CLU_068224_1_0_9; -.
DR   OMA; ADRNCVS; -.
DR   OrthoDB; 1115166at2; -.
DR   UniPathway; UPA00560; -.
DR   Proteomes; UP000000814; 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..242
FT                   /note="Ethanolamine ammonia-lyase small subunit"
FT                   /id="PRO_0000205985"
FT   BINDING         155
FT                   /ligand="adenosylcob(III)alamin"
FT                   /ligand_id="ChEBI:CHEBI:18408"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00601"
FT   BINDING         176
FT                   /ligand="adenosylcob(III)alamin"
FT                   /ligand_id="ChEBI:CHEBI:18408"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00601"
SQ   SEQUENCE   242 AA;  27149 MW;  672216BAA9B4178F CRC64;
     MENLLKIYDI KEEELSELKA LTPARICVGR AGTRLKTNTF LKFRADHAVA MDAVWSSVDE
     KLIDTLNFLK VQTLAKDKEE YITRPDLGRK FSEETLDYIK NNCINEPDVQ IIAGDGLSAT
     AINANLRKIY FVIVEKLKSR GYKVGTPIFV KYARVATMDK ISEELNAKVT IILIGERPGL
     ATGESMSSYM AYESSTKKPE SQRTVVSNIH NKGIPSVDAG KEIVRIIDIM MKEKKSGVEL
     RI