EUTB_ECO57
ID EUTB_ECO57 Reviewed; 453 AA.
AC P0AEJ7; P19635; P78094; P78300;
DT 20-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT 20-DEC-2005, sequence version 1.
DT 03-AUG-2022, entry version 90.
DE RecName: Full=Ethanolamine ammonia-lyase large subunit {ECO:0000255|HAMAP-Rule:MF_00861};
DE Short=EAL large subunit {ECO:0000255|HAMAP-Rule:MF_00861};
DE EC=4.3.1.7 {ECO:0000255|HAMAP-Rule:MF_00861};
GN Name=eutB {ECO:0000255|HAMAP-Rule:MF_00861};
GN OrderedLocusNames=Z3706, ECs3312;
OS Escherichia coli O157:H7.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83334;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=O157:H7 / EDL933 / ATCC 700927 / EHEC;
RX PubMed=11206551; DOI=10.1038/35054089;
RA Perna N.T., Plunkett G. III, Burland V., Mau B., Glasner J.D., Rose D.J.,
RA Mayhew G.F., Evans P.S., Gregor J., Kirkpatrick H.A., Posfai G.,
RA Hackett J., Klink S., Boutin A., Shao Y., Miller L., Grotbeck E.J.,
RA Davis N.W., Lim A., Dimalanta E.T., Potamousis K., Apodaca J.,
RA Anantharaman T.S., Lin J., Yen G., Schwartz D.C., Welch R.A.,
RA Blattner F.R.;
RT "Genome sequence of enterohaemorrhagic Escherichia coli O157:H7.";
RL Nature 409:529-533(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=O157:H7 / Sakai / RIMD 0509952 / EHEC;
RX PubMed=11258796; DOI=10.1093/dnares/8.1.11;
RA Hayashi T., Makino K., Ohnishi M., Kurokawa K., Ishii K., Yokoyama K.,
RA Han C.-G., Ohtsubo E., Nakayama K., Murata T., Tanaka M., Tobe T., Iida T.,
RA Takami H., Honda T., Sasakawa C., Ogasawara N., Yasunaga T., Kuhara S.,
RA Shiba T., Hattori M., Shinagawa H.;
RT "Complete genome sequence of enterohemorrhagic Escherichia coli O157:H7 and
RT genomic comparison with a laboratory strain K-12.";
RL DNA Res. 8:11-22(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 vitamin B12.
CC {ECO:0000255|HAMAP-Rule:MF_00861}.
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_00861};
CC -!- COFACTOR:
CC Name=adenosylcob(III)alamin; Xref=ChEBI:CHEBI:18408;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_00861};
CC Note=Binds between the large and small subunits. {ECO:0000255|HAMAP-
CC Rule:MF_00861};
CC -!- PATHWAY: Amine and polyamine degradation; ethanolamine degradation.
CC {ECO:0000255|HAMAP-Rule:MF_00861}.
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_00861}.
CC -!- SUBCELLULAR LOCATION: Bacterial microcompartment {ECO:0000255|HAMAP-
CC Rule:MF_00861}.
CC -!- SIMILARITY: Belongs to the EutB family. {ECO:0000255|HAMAP-
CC Rule:MF_00861}.
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DR EMBL; AE005174; AAG57559.1; -; Genomic_DNA.
DR EMBL; BA000007; BAB36735.1; -; Genomic_DNA.
DR PIR; C85887; C85887.
DR PIR; H91042; H91042.
DR RefSeq; NP_311339.1; NC_002695.1.
DR RefSeq; WP_000769961.1; NZ_SWKA01000005.1.
DR AlphaFoldDB; P0AEJ7; -.
DR SMR; P0AEJ7; -.
DR STRING; 155864.EDL933_3604; -.
DR EnsemblBacteria; AAG57559; AAG57559; Z3706.
DR EnsemblBacteria; BAB36735; BAB36735; ECs_3312.
DR GeneID; 66673689; -.
DR GeneID; 915295; -.
DR KEGG; ece:Z3706; -.
DR KEGG; ecs:ECs_3312; -.
DR PATRIC; fig|386585.9.peg.3459; -.
DR eggNOG; COG4303; Bacteria.
DR HOGENOM; CLU_048555_0_0_6; -.
DR OMA; FGKTYQF; -.
DR UniPathway; UPA00560; -.
DR Proteomes; UP000000558; Chromosome.
DR Proteomes; UP000002519; Chromosome.
DR GO; GO:0031469; C:bacterial microcompartment; IEA:UniProtKB-SubCell.
DR GO; GO:0031419; F:cobalamin binding; IEA:UniProtKB-KW.
DR GO; GO:0008851; F:ethanolamine ammonia-lyase activity; IEA:UniProtKB-EC.
DR GO; GO:0006520; P:cellular amino acid metabolic process; IEA:InterPro.
DR GO; GO:0046336; P:ethanolamine catabolic process; IEA:UniProtKB-UniPathway.
DR Gene3D; 1.10.220.70; -; 1.
DR Gene3D; 2.30.170.30; -; 1.
DR Gene3D; 3.20.20.70; -; 1.
DR HAMAP; MF_00861; EutB; 1.
DR InterPro; IPR013785; Aldolase_TIM.
DR InterPro; IPR010628; EutB.
DR InterPro; IPR044939; EutB_dom_2_sf.
DR InterPro; IPR044941; EutB_N_sf.
DR PANTHER; PTHR39329; PTHR39329; 1.
DR Pfam; PF06751; EutB; 1.
DR PIRSF; PIRSF018788; EutB; 1.
PE 3: Inferred from homology;
KW Bacterial microcompartment; Cobalamin; Cobalt; Lyase; Reference proteome.
FT CHAIN 1..453
FT /note="Ethanolamine ammonia-lyase large subunit"
FT /id="PRO_0000087082"
FT BINDING 160..162
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00861"
FT BINDING 193
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00861"
FT BINDING 194
FT /ligand="adenosylcob(III)alamin"
FT /ligand_id="ChEBI:CHEBI:18408"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00861"
FT BINDING 246
FT /ligand="adenosylcob(III)alamin"
FT /ligand_id="ChEBI:CHEBI:18408"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00861"
FT BINDING 287
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00861"
FT BINDING 295
FT /ligand="adenosylcob(III)alamin"
FT /ligand_id="ChEBI:CHEBI:18408"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00861"
FT BINDING 362
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00861"
FT BINDING 401
FT /ligand="adenosylcob(III)alamin"
FT /ligand_id="ChEBI:CHEBI:18408"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00861"
SQ SEQUENCE 453 AA; 49403 MW; 21C14FC469716060 CRC64;
MKLKTTLFGN VYQFKDVKEV LAKANELRSG DVLAGVAAAS SQERVAAKQV LSEMTVADIR
NNPVIAYEDD CVTRLIQDDV NETAYNQIKN WSISELREYV LSDETSVDDI AFTRKGLTSE
VVAAVAKICS NADLIYGAKK MPVIKKANTT IGIPGTFSAR LQPNDTRDDV QSIAAQIYEG
LSFGVGDAVI GVNPVTDDVE NLSRVLDTIY GVIDKFNIPT QGCVLAHVTT QIEAIRRGAP
GGLIFQSICG SEKGLKEFGV ELAMLDEARA VGAEFNRIAG ENCLYFETGQ GSALSAGANF
GADQVTMEAR NYGLARHYDP FIVNTVVGFI GPEYLYNDRQ IIRAGLEDHF MGKLSGISMG
CDCCYTNHAD ADQNLNENLM ILLATAGCNY IMGMPLGDDI MLNYQTTAFH DTATVRQLLN
LRPSPEFERW LESMGIMANG RLTKRAGDPS LFF
