EUTB_ECOLI
ID EUTB_ECOLI Reviewed; 453 AA.
AC P0AEJ6; 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 111.
DE RecName: Full=Ethanolamine ammonia-lyase large subunit {ECO:0000255|HAMAP-Rule:MF_00861, ECO:0000303|PubMed:2197274};
DE Short=EAL large subunit {ECO:0000255|HAMAP-Rule:MF_00861, ECO:0000303|PubMed:15466038};
DE EC=4.3.1.7 {ECO:0000255|HAMAP-Rule:MF_00861, ECO:0000269|PubMed:15466038, ECO:0000269|PubMed:19762342};
DE AltName: Full=Ethanolamine ammonia-lyase alpha subunit {ECO:0000303|PubMed:19762342};
DE AltName: Full=Ethanolamine ammonia-lyase heavy chain;
DE AltName: Full=Ethanolamine deaminase large subunit {ECO:0000303|PubMed:19762342};
GN Name=eutB {ECO:0000255|HAMAP-Rule:MF_00861};
GN OrderedLocusNames=b2441, JW2434;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=9205837; DOI=10.1093/dnares/4.2.91;
RA Yamamoto Y., Aiba H., Baba T., Hayashi K., Inada T., Isono K., Itoh T.,
RA Kimura S., Kitagawa M., Makino K., Miki T., Mitsuhashi N., Mizobuchi K.,
RA Mori H., Nakade S., Nakamura Y., Nashimoto H., Oshima T., Oyama S.,
RA Saito N., Sampei G., Satoh Y., Sivasundaram S., Tagami H., Takahashi H.,
RA Takeda J., Takemoto K., Uehara K., Wada C., Yamagata S., Horiuchi T.;
RT "Construction of a contiguous 874-kb sequence of the Escherichia coli-K12
RT genome corresponding to 50.0-68.8 min on the linkage map and analysis of
RT its sequence features.";
RL DNA Res. 4:91-113(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B.,
RA Shao Y.;
RT "The complete genome sequence of Escherichia coli K-12.";
RL Science 277:1453-1462(1997).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=16738553; DOI=10.1038/msb4100049;
RA Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655
RT and W3110.";
RL Mol. Syst. Biol. 2:E1-E5(2006).
RN [4]
RP PROTEIN SEQUENCE OF 1-30, AND FUNCTION.
RC STRAIN=ATCC 9723;
RX PubMed=2197274; DOI=10.1016/s0021-9258(19)38368-1;
RA Faust L.R.P., Connor J.A., Roof D.M., Hoch J.A., Babior B.M.;
RT "Cloning, sequencing, and expression of the genes encoding the
RT adenosylcobalamin-dependent ethanolamine ammonia-lyase of Salmonella
RT typhimurium.";
RL J. Biol. Chem. 265:12462-12466(1990).
RN [5]
RP PROTEIN SEQUENCE OF 1-6, FUNCTION, CATALYTIC ACTIVITY, COFACTOR, ACTIVITY
RP REGULATION, BIOPHYSICOCHEMICAL PROPERTIES, AND SUBUNIT.
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=19762342; DOI=10.1093/jb/mvp145;
RA Akita K., Hieda N., Baba N., Kawaguchi S., Sakamoto H., Nakanishi Y.,
RA Yamanishi M., Mori K., Toraya T.;
RT "Purification and some properties of wild-type and N-terminal-truncated
RT ethanolamine ammonia-lyase of Escherichia coli.";
RL J. Biochem. 147:83-93(2010).
RN [6]
RP FUNCTION, CATALYTIC ACTIVITY, ACTIVITY REGULATION, AND INDUCTION.
RC STRAIN=K12 / JM109 / ATCC 53323, and K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=15466038; DOI=10.1128/jb.186.20.6845-6854.2004;
RA Mori K., Bando R., Hieda N., Toraya T.;
RT "Identification of a reactivating factor for adenosylcobalamin-dependent
RT ethanolamine ammonia lyase.";
RL J. Bacteriol. 186:6845-6854(2004).
RN [7] {ECO:0007744|PDB:3ABO, ECO:0007744|PDB:3ABQ, ECO:0007744|PDB:3ABR, ECO:0007744|PDB:3ABS}
RP X-RAY CRYSTALLOGRAPHY (2.05 ANGSTROMS) IN COMPLEX WITH COFACTORS AND
RP ETHANOLAMINE, COFACTOR, AND SUBUNIT.
RX PubMed=20519496; DOI=10.1074/jbc.m110.125112;
RA Shibata N., Tamagaki H., Hieda N., Akita K., Komori H., Shomura Y.,
RA Terawaki S., Mori K., Yasuoka N., Higuchi Y., Toraya T.;
RT "Crystal structures of ethanolamine ammonia-lyase complexed with coenzyme
RT B12 analogs and substrates.";
RL J. Biol. Chem. 285:26484-26493(2010).
RN [8] {ECO:0007744|PDB:3ANY, ECO:0007744|PDB:3AO0}
RP X-RAY CRYSTALLOGRAPHY (2.10 ANGSTROMS) IN COMPLEX WITH COFACTOR AND
RP ETHANOLAMINE, COFACTOR, AND SUBUNIT.
RX PubMed=21142024; DOI=10.1021/bi101696h;
RA Shibata N., Higuchi Y., Toraya T.;
RT "How coenzyme B12-dependent ethanolamine ammonia-lyase deals with both
RT enantiomers of 2-amino-1-propanol as substrates: structure-based
RT rationalization.";
RL Biochemistry 50:591-598(2011).
RN [9] {ECO:0007744|PDB:5YSN, ECO:0007744|PDB:5YSR}
RP X-RAY CRYSTALLOGRAPHY (2.00 ANGSTROMS) IN COMPLEX WITH ADENOSYLCOBALAMIN,
RP REACTION MECHANISM, COFACTOR, AND SUBUNIT.
RX PubMed=29797764; DOI=10.1002/anie.201803591;
RA Shibata N., Sueyoshi Y., Higuchi Y., Toraya T.;
RT "Direct Participation of a Peripheral Side Chain of a Corrin Ring in
RT CoenzymeB12 Catalysis.";
RL Angew. Chem. Int. Ed. Engl. 57:7830-7835(2018).
CC -!- FUNCTION: Catalyzes the deamination of various vicinal amino-alcohols
CC to oxo compounds (PubMed:19762342). Allows this organism to utilize
CC ethanolamine as the sole source of nitrogen and carbon in the presence
CC of external vitamin B12. It is spontaneously inactivated by its
CC substrate and reactivated by EutA (PubMed:15466038).
CC {ECO:0000269|PubMed:15466038, ECO:0000269|PubMed:19762342,
CC ECO:0000305|PubMed:2197274}.
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 ECO:0000269|PubMed:15466038, ECO:0000269|PubMed:19762342};
CC -!- COFACTOR:
CC Name=adenosylcob(III)alamin; Xref=ChEBI:CHEBI:18408;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_00861,
CC ECO:0000269|PubMed:19762342, ECO:0000269|PubMed:20519496,
CC ECO:0000269|PubMed:21142024, ECO:0000269|PubMed:29797764};
CC Note=Binds 1 AdoCbl between the large and small subunits, with 6
CC cofactors per holoenzyme. {ECO:0000255|HAMAP-Rule:MF_00861,
CC ECO:0000269|PubMed:20519496, ECO:0000269|PubMed:21142024,
CC ECO:0000269|PubMed:29797764, ECO:0000305|PubMed:19762342};
CC -!- ACTIVITY REGULATION: Inhibited by 5-adeninylpentylcobalamin (AdePeCbl),
CC a cofactor analog (PubMed:19762342). Irreversibly inhibited during
CC catalysis by cleavage of the Co-C bond of the cobalamin coenzyme
CC (Probable) (PubMed:19762342). Reactivated by EutA, which probably
CC involves an ATP-dependent cobalamin exchange (PubMed:15466038).
CC {ECO:0000269|PubMed:15466038, ECO:0000269|PubMed:19762342,
CC ECO:0000305|PubMed:15466038}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=8.2 uM for ethanolamine {ECO:0000269|PubMed:19762342};
CC KM=0.055 uM for adenosylcob(III)alamin {ECO:0000269|PubMed:19762342};
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 (PubMed:20519496, PubMed:21142024, PubMed:29797764,
CC PubMed:19762342). The heterotetramers trimerize; 6 large subunits form
CC a core ring with 6 small subunits projecting outwards (Probable).
CC {ECO:0000269|PubMed:19762342, ECO:0000269|PubMed:20519496,
CC ECO:0000269|PubMed:21142024, ECO:0000269|PubMed:29797764,
CC ECO:0000305|PubMed:20519496}.
CC -!- SUBCELLULAR LOCATION: Bacterial microcompartment {ECO:0000255|HAMAP-
CC Rule:MF_00861}.
CC -!- INDUCTION: When grown in ethanolamine and adenosylcobalamin (AdoCbl)
CC (at protein level). Note this experiment was done in strain JM109,
CC which expresses the eut operon. {ECO:0000269|PubMed:15466038}.
CC -!- SIMILARITY: Belongs to the EutB family. {ECO:0000255|HAMAP-
CC Rule:MF_00861, ECO:0000305}.
CC -!- CAUTION: In strain MG1655 the eut operon is interrupted by the CPZ-55
CC prophage, encoding 9 genes situated between eutA and eutB, which are
CC translated in the other direction. CPZ-55 may prevent expression of the
CC eut operon in strain MG1655. Strain W3110 does not have this prophage
CC element and should be able to express the operon.
CC {ECO:0000305|PubMed:9278503}.
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DR EMBL; U00096; AAC75494.2; -; Genomic_DNA.
DR EMBL; AP009048; BAA16323.1; -; Genomic_DNA.
DR PIR; H65018; H65018.
DR RefSeq; NP_416936.4; NC_000913.3.
DR RefSeq; WP_000769961.1; NZ_SSUR01000044.1.
DR PDB; 3ABO; X-ray; 2.10 A; A/C=1-453.
DR PDB; 3ABQ; X-ray; 2.05 A; A/C=1-453.
DR PDB; 3ABR; X-ray; 2.10 A; A/C=1-453.
DR PDB; 3ABS; X-ray; 2.25 A; A/C=1-453.
DR PDB; 3ANY; X-ray; 2.10 A; A/C=1-453.
DR PDB; 3AO0; X-ray; 2.25 A; A/C=1-453.
DR PDB; 5YSN; X-ray; 2.00 A; A/C=1-453.
DR PDB; 5YSR; X-ray; 2.05 A; A/C=1-453.
DR PDBsum; 3ABO; -.
DR PDBsum; 3ABQ; -.
DR PDBsum; 3ABR; -.
DR PDBsum; 3ABS; -.
DR PDBsum; 3ANY; -.
DR PDBsum; 3AO0; -.
DR PDBsum; 5YSN; -.
DR PDBsum; 5YSR; -.
DR AlphaFoldDB; P0AEJ6; -.
DR SMR; P0AEJ6; -.
DR BioGRID; 4260578; 10.
DR ComplexPortal; CPX-2313; Ethanolamine ammonia-lyase complex.
DR IntAct; P0AEJ6; 1.
DR STRING; 511145.b2441; -.
DR jPOST; P0AEJ6; -.
DR PaxDb; P0AEJ6; -.
DR PRIDE; P0AEJ6; -.
DR DNASU; 946924; -.
DR EnsemblBacteria; AAC75494; AAC75494; b2441.
DR EnsemblBacteria; BAA16323; BAA16323; BAA16323.
DR GeneID; 66673689; -.
DR GeneID; 946924; -.
DR KEGG; ecj:JW2434; -.
DR KEGG; eco:b2441; -.
DR PATRIC; fig|1411691.4.peg.4290; -.
DR EchoBASE; EB4299; -.
DR eggNOG; COG4303; Bacteria.
DR HOGENOM; CLU_048555_0_0_6; -.
DR InParanoid; P0AEJ6; -.
DR OMA; FGKTYQF; -.
DR PhylomeDB; P0AEJ6; -.
DR BioCyc; EcoCyc:EUTB-MON; -.
DR BioCyc; MetaCyc:EUTB-MON; -.
DR UniPathway; UPA00560; -.
DR EvolutionaryTrace; P0AEJ6; -.
DR PRO; PR:P0AEJ6; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0031469; C:bacterial microcompartment; IEA:UniProtKB-SubCell.
DR GO; GO:0005829; C:cytosol; IDA:EcoCyc.
DR GO; GO:0009350; C:ethanolamine ammonia-lyase complex; IDA:EcoCyc.
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; IDA:ComplexPortal.
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 1: Evidence at protein level;
KW 3D-structure; Bacterial microcompartment; Cobalamin; Cobalt;
KW Direct protein sequencing; Lyase; Reference proteome.
FT CHAIN 1..453
FT /note="Ethanolamine ammonia-lyase large subunit"
FT /id="PRO_0000087081"
FT BINDING 160..162
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00861,
FT ECO:0000269|PubMed:20519496, ECO:0000269|PubMed:21142024,
FT ECO:0007744|PDB:3ABO, ECO:0007744|PDB:3ABS,
FT ECO:0007744|PDB:3ANY, ECO:0007744|PDB:3AO0"
FT BINDING 193
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00861,
FT ECO:0000269|PubMed:20519496, ECO:0000269|PubMed:21142024,
FT ECO:0007744|PDB:3ABO, ECO:0007744|PDB:3ABS,
FT ECO:0007744|PDB:3AO0"
FT BINDING 194
FT /ligand="adenosylcob(III)alamin"
FT /ligand_id="ChEBI:CHEBI:18408"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00861,
FT ECO:0000269|PubMed:29797764, ECO:0007744|PDB:3ABR,
FT ECO:0007744|PDB:5YSN, ECO:0007744|PDB:5YSR"
FT BINDING 246
FT /ligand="adenosylcob(III)alamin"
FT /ligand_id="ChEBI:CHEBI:18408"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00861,
FT ECO:0000269|PubMed:20519496, ECO:0000269|PubMed:21142024,
FT ECO:0007744|PDB:3ABO, ECO:0007744|PDB:3ABQ,
FT ECO:0007744|PDB:3ANY, ECO:0007744|PDB:3AO0,
FT ECO:0007744|PDB:5YSN"
FT BINDING 287
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00861,
FT ECO:0000269|PubMed:20519496, ECO:0000269|PubMed:21142024,
FT ECO:0007744|PDB:3ABO, ECO:0007744|PDB:3ABS,
FT ECO:0007744|PDB:3ANY, ECO:0007744|PDB:3AO0"
FT BINDING 295
FT /ligand="adenosylcob(III)alamin"
FT /ligand_id="ChEBI:CHEBI:18408"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00861, ECO:0000305,
FT ECO:0007744|PDB:3ABR, ECO:0007744|PDB:3ANY,
FT ECO:0007744|PDB:3AO0"
FT BINDING 362
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00861,
FT ECO:0000269|PubMed:20519496, ECO:0000269|PubMed:21142024,
FT ECO:0007744|PDB:3ABO, ECO:0007744|PDB:3ABS,
FT ECO:0007744|PDB:3ANY, ECO:0007744|PDB:3AO0"
FT BINDING 401
FT /ligand="adenosylcob(III)alamin"
FT /ligand_id="ChEBI:CHEBI:18408"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00861,
FT ECO:0000269|PubMed:20519496, ECO:0000269|PubMed:21142024,
FT ECO:0007744|PDB:3ABO, ECO:0007744|PDB:3ABQ,
FT ECO:0007744|PDB:3ANY, ECO:0007744|PDB:3AO0,
FT ECO:0007744|PDB:5YSN, ECO:0007744|PDB:5YSR"
FT STRAND 4..7
FT /evidence="ECO:0007829|PDB:5YSN"
FT STRAND 10..13
FT /evidence="ECO:0007829|PDB:5YSN"
FT HELIX 17..23
FT /evidence="ECO:0007829|PDB:5YSN"
FT HELIX 29..33
FT /evidence="ECO:0007829|PDB:5YSN"
FT HELIX 41..53
FT /evidence="ECO:0007829|PDB:5YSN"
FT HELIX 56..60
FT /evidence="ECO:0007829|PDB:5YSN"
FT HELIX 67..69
FT /evidence="ECO:0007829|PDB:5YSN"
FT HELIX 71..78
FT /evidence="ECO:0007829|PDB:5YSN"
FT HELIX 82..88
FT /evidence="ECO:0007829|PDB:5YSN"
FT HELIX 93..101
FT /evidence="ECO:0007829|PDB:5YSN"
FT HELIX 107..113
FT /evidence="ECO:0007829|PDB:5YSN"
FT HELIX 114..116
FT /evidence="ECO:0007829|PDB:5YSN"
FT HELIX 119..127
FT /evidence="ECO:0007829|PDB:5YSN"
FT HELIX 131..139
FT /evidence="ECO:0007829|PDB:5YSN"
FT STRAND 145..151
FT /evidence="ECO:0007829|PDB:5YSN"
FT STRAND 158..161
FT /evidence="ECO:0007829|PDB:5YSN"
FT HELIX 170..182
FT /evidence="ECO:0007829|PDB:5YSN"
FT STRAND 190..192
FT /evidence="ECO:0007829|PDB:5YSN"
FT HELIX 199..215
FT /evidence="ECO:0007829|PDB:5YSN"
FT STRAND 222..224
FT /evidence="ECO:0007829|PDB:5YSN"
FT HELIX 228..236
FT /evidence="ECO:0007829|PDB:5YSN"
FT STRAND 244..247
FT /evidence="ECO:0007829|PDB:5YSN"
FT HELIX 252..257
FT /evidence="ECO:0007829|PDB:5YSN"
FT HELIX 262..275
FT /evidence="ECO:0007829|PDB:5YSN"
FT STRAND 279..281
FT /evidence="ECO:0007829|PDB:5YSN"
FT STRAND 284..288
FT /evidence="ECO:0007829|PDB:5YSN"
FT HELIX 292..295
FT /evidence="ECO:0007829|PDB:5YSN"
FT HELIX 304..316
FT /evidence="ECO:0007829|PDB:5YSN"
FT STRAND 321..326
FT /evidence="ECO:0007829|PDB:5YSN"
FT TURN 332..334
FT /evidence="ECO:0007829|PDB:5YSN"
FT HELIX 338..354
FT /evidence="ECO:0007829|PDB:5YSN"
FT STRAND 359..362
FT /evidence="ECO:0007829|PDB:5YSN"
FT HELIX 373..385
FT /evidence="ECO:0007829|PDB:5YSN"
FT STRAND 390..394
FT /evidence="ECO:0007829|PDB:5YSN"
FT HELIX 395..397
FT /evidence="ECO:0007829|PDB:5YSN"
FT TURN 400..403
FT /evidence="ECO:0007829|PDB:5YSN"
FT HELIX 409..419
FT /evidence="ECO:0007829|PDB:5YSN"
FT HELIX 425..433
FT /evidence="ECO:0007829|PDB:5YSN"
FT STRAND 436..438
FT /evidence="ECO:0007829|PDB:5YSN"
FT HELIX 449..452
FT /evidence="ECO:0007829|PDB:5YSN"
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
