EUTC_ECOLI
ID EUTC_ECOLI Reviewed; 295 AA.
AC P19636; P78273;
DT 01-FEB-1991, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1997, sequence version 2.
DT 03-AUG-2022, entry version 150.
DE RecName: Full=Ethanolamine ammonia-lyase small subunit {ECO:0000255|HAMAP-Rule:MF_00601, ECO:0000303|PubMed:2197274};
DE Short=EAL small subunit {ECO:0000255|HAMAP-Rule:MF_00601, ECO:0000303|PubMed:15466038};
DE EC=4.3.1.7 {ECO:0000255|HAMAP-Rule:MF_00601, ECO:0000269|PubMed:15466038, ECO:0000269|PubMed:19762342};
DE AltName: Full=Ethanolamine ammonia-lyase beta subunit {ECO:0000303|PubMed:19762342};
DE AltName: Full=Ethanolamine ammonia-lyase light chain;
DE AltName: Full=Ethanolamine deaminase small subunit {ECO:0000303|PubMed:19762342};
GN Name=eutC {ECO:0000255|HAMAP-Rule:MF_00601};
GN OrderedLocusNames=b2440, JW2433;
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 1-15, 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 AND 29-34, FUNCTION, CATALYTIC ACTIVITY, COFACTOR,
RP ACTIVITY REGULATION, BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT, AND DOMAIN.
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) OF 44-295 IN COMPLEX WITH COFACTORS,
RP 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) OF 44-295 IN COMPLEX WITH COFACTOR,
RP 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) OF 44-295 IN COMPLEX WITH
RP ADENOSYLCOBALAMIN, 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). Ethanolamine ammonia-lyase (EAL)
CC allows bacteria to utilize ethanolamine as the sole source of nitrogen
CC and carbon in the presence of external vitamin B12. It is spontaneously
CC inactivated by its substrate and reactivated by EutA (PubMed:15466038).
CC Directly targeted to the BMC. May play a role in bacterial
CC microcompartment (BMC) assembly or maintenance (By similarity).
CC {ECO:0000250|UniProtKB:P19265, ECO:0000269|PubMed:15466038,
CC ECO:0000269|PubMed:19762342, 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_00601,
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_00601,
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_00601,
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_00601}.
CC -!- SUBUNIT: The basic unit is a heterodimer, which further associates into
CC a trimer of heterotetramers (PubMed:20519496, PubMed:21142024,
CC PubMed:29797764, PubMed:19762342). 6 large subunits form a core ring
CC 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_00601}.
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 -!- DOMAIN: Partial trypsin digestion of this subunit (removing the first
CC 28 residues) yields an active protein less susceptible to aggregation.
CC {ECO:0000269|PubMed:19762342}.
CC -!- SIMILARITY: Belongs to the EutC family. {ECO:0000255|HAMAP-
CC Rule:MF_00601, 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; AAC75493.1; -; Genomic_DNA.
DR EMBL; AP009048; BAA16322.1; -; Genomic_DNA.
DR PIR; G65018; G65018.
DR RefSeq; NP_416935.1; NC_000913.3.
DR RefSeq; WP_000372316.1; NZ_LN832404.1.
DR PDB; 3ABO; X-ray; 2.10 A; B/D=44-295.
DR PDB; 3ABQ; X-ray; 2.05 A; B/D=44-295.
DR PDB; 3ABR; X-ray; 2.10 A; B/D=44-295.
DR PDB; 3ABS; X-ray; 2.25 A; B/D=44-295.
DR PDB; 3ANY; X-ray; 2.10 A; B/D=44-295.
DR PDB; 3AO0; X-ray; 2.25 A; B/D=44-295.
DR PDB; 5YSN; X-ray; 2.00 A; B/D=44-295.
DR PDB; 5YSR; X-ray; 2.05 A; B/D=44-295.
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; P19636; -.
DR SMR; P19636; -.
DR BioGRID; 4260577; 15.
DR BioGRID; 851264; 23.
DR ComplexPortal; CPX-2313; Ethanolamine ammonia-lyase complex.
DR IntAct; P19636; 30.
DR STRING; 511145.b2440; -.
DR jPOST; P19636; -.
DR PaxDb; P19636; -.
DR PRIDE; P19636; -.
DR EnsemblBacteria; AAC75493; AAC75493; b2440.
DR EnsemblBacteria; BAA16322; BAA16322; BAA16322.
DR GeneID; 946925; -.
DR KEGG; ecj:JW2433; -.
DR KEGG; eco:b2440; -.
DR PATRIC; fig|1411691.4.peg.4291; -.
DR EchoBASE; EB4300; -.
DR eggNOG; COG4302; Bacteria.
DR HOGENOM; CLU_068224_0_0_6; -.
DR InParanoid; P19636; -.
DR OMA; ADRNCVS; -.
DR PhylomeDB; P19636; -.
DR BioCyc; EcoCyc:EUTC-MON; -.
DR BioCyc; MetaCyc:EUTC-MON; -.
DR BRENDA; 4.3.1.7; 2026.
DR UniPathway; UPA00560; -.
DR EvolutionaryTrace; P19636; -.
DR PRO; PR:P19636; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0009350; C:ethanolamine ammonia-lyase complex; IDA:EcoCyc.
DR GO; GO:0031471; C:ethanolamine degradation polyhedral organelle; IEA:UniProtKB-UniRule.
DR GO; GO:0031419; F:cobalamin binding; IBA:GO_Central.
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; IDA:ComplexPortal.
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 1: Evidence at protein level;
KW 3D-structure; Bacterial microcompartment; Cobalamin; Cobalt;
KW Direct protein sequencing; Lyase; Reference proteome.
FT CHAIN 1..295
FT /note="Ethanolamine ammonia-lyase small subunit"
FT /id="PRO_0000205988"
FT BINDING 207
FT /ligand="adenosylcob(III)alamin"
FT /ligand_id="ChEBI:CHEBI:18408"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00601,
FT ECO:0000269|PubMed:20519496, ECO:0000269|PubMed:21142024,
FT ECO:0007744|PDB:3ABO, ECO:0007744|PDB:3ABQ,
FT ECO:0007744|PDB:3ABR, ECO:0007744|PDB:5YSN,
FT ECO:0007744|PDB:5YSR"
FT BINDING 228
FT /ligand="adenosylcob(III)alamin"
FT /ligand_id="ChEBI:CHEBI:18408"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00601,
FT ECO:0000269|PubMed:20519496, ECO:0000269|PubMed:21142024,
FT ECO:0007744|PDB:3ABO, ECO:0007744|PDB:3ABQ,
FT ECO:0007744|PDB:3ABR, ECO:0007744|PDB:3ANY,
FT ECO:0007744|PDB:3AO0"
FT BINDING 258
FT /ligand="adenosylcob(III)alamin"
FT /ligand_id="ChEBI:CHEBI:18408"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00601,
FT ECO:0000269|PubMed:20519496, ECO:0000269|PubMed:21142024,
FT ECO:0007744|PDB:3ABO, ECO:0007744|PDB:3ABR,
FT ECO:0007744|PDB:3AO0, ECO:0007744|PDB:5YSN"
FT HELIX 50..54
FT /evidence="ECO:0007829|PDB:5YSN"
FT HELIX 64..73
FT /evidence="ECO:0007829|PDB:5YSN"
FT HELIX 89..107
FT /evidence="ECO:0007829|PDB:5YSN"
FT HELIX 112..117
FT /evidence="ECO:0007829|PDB:5YSN"
FT STRAND 121..126
FT /evidence="ECO:0007829|PDB:5YSN"
FT HELIX 130..135
FT /evidence="ECO:0007829|PDB:5YSN"
FT HELIX 137..140
FT /evidence="ECO:0007829|PDB:5YSN"
FT STRAND 141..143
FT /evidence="ECO:0007829|PDB:5YSR"
FT HELIX 145..154
FT /evidence="ECO:0007829|PDB:5YSN"
FT STRAND 160..168
FT /evidence="ECO:0007829|PDB:5YSN"
FT HELIX 171..190
FT /evidence="ECO:0007829|PDB:5YSN"
FT TURN 191..193
FT /evidence="ECO:0007829|PDB:5YSN"
FT STRAND 200..203
FT /evidence="ECO:0007829|PDB:5YSN"
FT HELIX 209..217
FT /evidence="ECO:0007829|PDB:5YSN"
FT STRAND 220..227
FT /evidence="ECO:0007829|PDB:5YSN"
FT STRAND 238..245
FT /evidence="ECO:0007829|PDB:5YSN"
FT TURN 248..250
FT /evidence="ECO:0007829|PDB:5YSN"
FT HELIX 253..255
FT /evidence="ECO:0007829|PDB:5YSN"
FT STRAND 256..263
FT /evidence="ECO:0007829|PDB:5YSN"
FT HELIX 269..286
FT /evidence="ECO:0007829|PDB:5YSN"
FT HELIX 290..292
FT /evidence="ECO:0007829|PDB:5YSN"
SQ SEQUENCE 295 AA; 31782 MW; C7E87143B8E050E5 CRC64;
MDQKQIEEIV RSVMASMGQA APAPSEAKCA TTNCAAPVTS ESCALDLGSA EAKAWIGVEN
PHRADVLTEL RRSTVARVCT GRAGPRPRTQ ALLRFLADHS RSKDTVLKEV PEEWVKAQGL
LEVRSEISDK NLYLTRPDMG RRLCAEAVEA LKAQCVANPD VQVVISDGLS TDAITVNYEE
ILPPLMAGLK QAGLKVGTPF FVRYGRVKIE DQIGEILGAK VVILLVGERP GLGQSESLSC
YAVYSPRMAT TVEADRTCIS NIHQGGTPPV EAAAVIVDLA KRMLEQKASG INMTR
