AC   MF_00861;
DC   Protein; auto
TR   HAMAP; MF_00861; -; 1; level=0
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Names: EutB
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ID   EUTB
case <OC:Bacteria>
DE   RecName: Full=Ethanolamine ammonia-lyase large subunit;
DE            Short=EAL large subunit;
DE            EC=4.3.1.7;
else case <OC:Archaea>
DE   RecName: Full=Putative ethanolamine ammonia-lyase large subunit;
DE            Short=EAL large subunit;
DE            EC=4.3.1.7;
end case
GN   Name=eutB;
XX
case <OC:Bacteria>
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 vitamin B12.
else case <OC:Archaea>
CC   -!- FUNCTION: May catalyze the deamination of various vicinal amino-
CC       alcohols to oxo compounds. Would allow this organism to utilize
CC       ethanolamine as the sole source of nitrogen and carbon in the presence
CC       of vitamin B12.
end case
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   -!- COFACTOR: adenosylcob(III)alamin; Xref=CHEBI:18408;
CC       Note=Binds between the large and small subunits.
CC   -!- PATHWAY: Amine and polyamine degradation; ethanolamine degradation.
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.
case <OC:Bacteria>
CC   -!- SUBCELLULAR LOCATION: Bacterial microcompartment.
end case
CC   -!- SIMILARITY: Belongs to the EutB family.
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DR   Pfam; PF06751; EutB; 1; trigger=no
DR   PIRSF; PIRSF018788; EutB; 0-1; trigger=no
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KW   Cobalt
KW   Cobalamin
KW   Lyase
case <OC:Bacteria>
KW   Bacterial microcompartment
end case
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GO   GO:0008851; F:ethanolamine ammonia-lyase activity
GO   GO:0009350; C:ethanolamine ammonia-lyase complex
GO   GO:0046336; P:ethanolamine catabolic process
GO   GO:0031419; F:cobalamin binding
case <OC:Bacteria>
GO   GO:0031471; C:ethanolamine degradation polyhedral organelle
end case
XX
FT   From: EUTB_ECOLI (P0AEJ6)
FT   BINDING         160..162
FT                   /ligand="substrate"
FT   Condition: R-x-Q
FT   BINDING         193
FT                   /ligand="substrate"
FT   Condition: N
FT   BINDING         194
FT                   /ligand="adenosylcob(III)alamin"
FT                   /ligand_id="ChEBI:CHEBI:18408"
FT   Condition: P
FT   BINDING         246
FT                   /ligand="adenosylcob(III)alamin"
FT                   /ligand_id="ChEBI:CHEBI:18408"
FT   Condition: Q
FT   BINDING         287
FT                   /ligand="substrate"
FT   Condition: E
FT   BINDING         295
FT                   /ligand="adenosylcob(III)alamin"
FT                   /ligand_id="ChEBI:CHEBI:18408"
FT   Condition: S
FT   BINDING         362
FT                   /ligand="substrate"
FT   Condition: D
FT   BINDING         401
FT                   /ligand="adenosylcob(III)alamin"
FT                   /ligand_id="ChEBI:CHEBI:18408"
FT   Condition: M
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Size: 409-527;
Related: None;
Template: P0AEJ7; P19264;
Scope:
 Bacteria
 Archaea; Halobacteria
Fusion:
 Nter: None
 Cter: None
Duplicate: None
Plasmid: None
Comments: Both large and small subunits are found in Archaeal Halobacteria.
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# Revision 1.6 2022/11/19
//