EUTC_ECOL5
ID EUTC_ECOL5 Reviewed; 295 AA.
AC Q0TF29;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 05-SEP-2006, sequence version 1.
DT 03-AUG-2022, entry version 81.
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=ECP_2461;
OS Escherichia coli O6:K15:H31 (strain 536 / UPEC).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=362663;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=536 / UPEC;
RX PubMed=16879640; DOI=10.1111/j.1365-2958.2006.05255.x;
RA Hochhut B., Wilde C., Balling G., Middendorf B., Dobrindt U.,
RA Brzuszkiewicz E., Gottschalk G., Carniel E., Hacker J.;
RT "Role of pathogenicity island-associated integrases in the genome
RT plasticity of uropathogenic Escherichia coli strain 536.";
RL Mol. Microbiol. 61:584-595(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; CP000247; ABG70450.1; -; Genomic_DNA.
DR RefSeq; WP_000372316.1; NC_008253.1.
DR AlphaFoldDB; Q0TF29; -.
DR SMR; Q0TF29; -.
DR STRING; 362663.ECP_2461; -.
DR EnsemblBacteria; ABG70450; ABG70450; ECP_2461.
DR KEGG; ecp:ECP_2461; -.
DR HOGENOM; CLU_068224_0_0_6; -.
DR OMA; ADRNCVS; -.
DR UniPathway; UPA00560; -.
DR Proteomes; UP000009182; 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_1000025854"
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; 31782 MW; C7E87143B8E050E5 CRC64;
MDQKQIEEIV RSVMASMGQA APAPSEAKCA TTNCAAPVTS ESCALDLGSA EAKAWIGVEN
PHRADVLTEL RRSTVARVCT GRAGPRPRTQ ALLRFLADHS RSKDTVLKEV PEEWVKAQGL
LEVRSEISDK NLYLTRPDMG RRLCAEAVEA LKAQCVANPD VQVVISDGLS TDAITVNYEE
ILPPLMAGLK QAGLKVGTPF FVRYGRVKIE DQIGEILGAK VVILLVGERP GLGQSESLSC
YAVYSPRMAT TVEADRTCIS NIHQGGTPPV EAAAVIVDLA KRMLEQKASG INMTR