EUTC_PHOLL
ID EUTC_PHOLL Reviewed; 284 AA.
AC Q7N2V3;
DT 15-DEC-2003, integrated into UniProtKB/Swiss-Prot.
DT 15-DEC-2003, sequence version 1.
DT 03-AUG-2022, entry version 100.
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=plu2971;
OS Photorhabdus laumondii subsp. laumondii (strain DSM 15139 / CIP 105565 /
OS TT01).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Morganellaceae; Photorhabdus.
OX NCBI_TaxID=243265;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 15139 / CIP 105565 / TT01;
RX PubMed=14528314; DOI=10.1038/nbt886;
RA Duchaud E., Rusniok C., Frangeul L., Buchrieser C., Givaudan A.,
RA Taourit S., Bocs S., Boursaux-Eude C., Chandler M., Charles J.-F.,
RA Dassa E., Derose R., Derzelle S., Freyssinet G., Gaudriault S., Medigue C.,
RA Lanois A., Powell K., Siguier P., Vincent R., Wingate V., Zouine M.,
RA Glaser P., Boemare N., Danchin A., Kunst F.;
RT "The genome sequence of the entomopathogenic bacterium Photorhabdus
RT luminescens.";
RL Nat. Biotechnol. 21:1307-1313(2003).
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; BX571869; CAE15345.1; -; Genomic_DNA.
DR RefSeq; WP_011147190.1; NC_005126.1.
DR AlphaFoldDB; Q7N2V3; -.
DR SMR; Q7N2V3; -.
DR STRING; 243265.plu2971; -.
DR EnsemblBacteria; CAE15345; CAE15345; plu2971.
DR GeneID; 24170212; -.
DR KEGG; plu:plu2971; -.
DR eggNOG; COG4302; Bacteria.
DR HOGENOM; CLU_068224_1_0_6; -.
DR OMA; ADRNCVS; -.
DR OrthoDB; 1115166at2; -.
DR BioCyc; PLUM243265:PLU_RS14780-MON; -.
DR UniPathway; UPA00560; -.
DR Proteomes; UP000002514; 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; Reference proteome.
FT CHAIN 1..284
FT /note="Ethanolamine ammonia-lyase small subunit"
FT /id="PRO_0000205996"
FT BINDING 196
FT /ligand="adenosylcob(III)alamin"
FT /ligand_id="ChEBI:CHEBI:18408"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00601"
FT BINDING 217
FT /ligand="adenosylcob(III)alamin"
FT /ligand_id="ChEBI:CHEBI:18408"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00601"
FT BINDING 247
FT /ligand="adenosylcob(III)alamin"
FT /ligand_id="ChEBI:CHEBI:18408"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00601"
SQ SEQUENCE 284 AA; 31208 MW; 9928B46D4491ACA9 CRC64;
MNQKTIEKNV SERVSNLKPH ASPEITNEIE SCMPDLGSLE AKQWIGVQNP NRIEVLQELR
RSTVARVGTG RSGPRPRTQA LLRFQADHSR SKDTVLKEVP TEWIEKQGLL EVQSQVSDKN
LYLTRPDLGR KLSANAVETL LTQCKTAPDV QVVISDGLST DAITTNYEDL VPPLLKGLEQ
AGMCIGTPFF VRYGRVKIED QIGELLKAKV VVLLIGERPG LGQSESLSCY AVYQPTVEKT
VEADRTCISN IHRGGTPPIE AAAIIVDLAK NMLEQQASGI ALSR
