EUTC_SHISS
ID EUTC_SHISS Reviewed; 295 AA.
AC Q3YZA3;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 27-SEP-2005, sequence version 1.
DT 03-AUG-2022, entry version 79.
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=SSON_2529;
OS Shigella sonnei (strain Ss046).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Shigella.
OX NCBI_TaxID=300269;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Ss046;
RX PubMed=16275786; DOI=10.1093/nar/gki954;
RA Yang F., Yang J., Zhang X., Chen L., Jiang Y., Yan Y., Tang X., Wang J.,
RA Xiong Z., Dong J., Xue Y., Zhu Y., Xu X., Sun L., Chen S., Nie H., Peng J.,
RA Xu J., Wang Y., Yuan Z., Wen Y., Yao Z., Shen Y., Qiang B., Hou Y., Yu J.,
RA Jin Q.;
RT "Genome dynamics and diversity of Shigella species, the etiologic agents of
RT bacillary dysentery.";
RL Nucleic Acids Res. 33:6445-6458(2005).
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; CP000038; AAZ89159.1; -; Genomic_DNA.
DR AlphaFoldDB; Q3YZA3; -.
DR SMR; Q3YZA3; -.
DR EnsemblBacteria; AAZ89159; AAZ89159; SSON_2529.
DR KEGG; ssn:SSON_2529; -.
DR HOGENOM; CLU_068224_0_0_6; -.
DR OMA; ADRNCVS; -.
DR UniPathway; UPA00560; -.
DR Proteomes; UP000002529; 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_1000025866"
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; 31812 MW; 26B0CE62E6EEAB11 CRC64;
MDQKQIEEIV RSVMASMGQA APAPSEAKCA TTNCAAPVTS ESCALDLGSA EAKAWIGVEN
PHRADVLTEL RRSTVARVCT GRTGPRPRTQ ALLRFLADHS RSKDTVLKEV PEEWVKAQGL
LEVRSEISDK NLYLTRPDMG RRLCAEAVEA LKAQCVANPD VQVVISDGLS TDAITVNYEE
ILPPLMAGLK QAGLKVGTPF FVRYGRVKIE DQIGEILGAK VVILLVGERP GLGQSESLSC
YAVYSPRMAT TVEADRTCIS NIHQGGTPPV EAAAVIVDLA KRMLEQKASG INMTR
