EUTC_PSEAE
ID EUTC_PSEAE Reviewed; 273 AA.
AC Q9HX02;
DT 25-NOV-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 99.
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=PA4025;
OS Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM
OS 14847 / LMG 12228 / 1C / PRS 101 / PAO1).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=208964;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C /
RC PRS 101 / PAO1;
RX PubMed=10984043; DOI=10.1038/35023079;
RA Stover C.K., Pham X.-Q.T., Erwin A.L., Mizoguchi S.D., Warrener P.,
RA Hickey M.J., Brinkman F.S.L., Hufnagle W.O., Kowalik D.J., Lagrou M.,
RA Garber R.L., Goltry L., Tolentino E., Westbrock-Wadman S., Yuan Y.,
RA Brody L.L., Coulter S.N., Folger K.R., Kas A., Larbig K., Lim R.M.,
RA Smith K.A., Spencer D.H., Wong G.K.-S., Wu Z., Paulsen I.T., Reizer J.,
RA Saier M.H. Jr., Hancock R.E.W., Lory S., Olson M.V.;
RT "Complete genome sequence of Pseudomonas aeruginosa PAO1, an opportunistic
RT pathogen.";
RL Nature 406:959-964(2000).
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; AE004091; AAG07412.1; -; Genomic_DNA.
DR PIR; A83143; A83143.
DR RefSeq; NP_252714.1; NC_002516.2.
DR RefSeq; WP_003114907.1; NZ_QZGE01000013.1.
DR AlphaFoldDB; Q9HX02; -.
DR SMR; Q9HX02; -.
DR STRING; 287.DR97_3842; -.
DR PaxDb; Q9HX02; -.
DR PRIDE; Q9HX02; -.
DR DNASU; 879003; -.
DR EnsemblBacteria; AAG07412; AAG07412; PA4025.
DR GeneID; 879003; -.
DR KEGG; pae:PA4025; -.
DR PATRIC; fig|208964.12.peg.4217; -.
DR PseudoCAP; PA4025; -.
DR HOGENOM; CLU_068224_1_0_6; -.
DR InParanoid; Q9HX02; -.
DR OMA; FQFAHAQ; -.
DR PhylomeDB; Q9HX02; -.
DR BioCyc; PAER208964:G1FZ6-4098-MON; -.
DR UniPathway; UPA00560; -.
DR Proteomes; UP000002438; Chromosome.
DR GO; GO:0009350; C:ethanolamine ammonia-lyase complex; IBA:GO_Central.
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; IEA:UniProtKB-UniRule.
DR Gene3D; 1.10.30.40; -; 1.
DR Gene3D; 3.40.50.11240; -; 1.
DR HAMAP; MF_00601; EutC; 1.
DR InterPro; IPR009246; EutC.
DR InterPro; IPR042251; EutC_C.
DR InterPro; IPR042255; EutC_N.
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..273
FT /note="Ethanolamine ammonia-lyase small subunit"
FT /id="PRO_0000205997"
FT BINDING 164
FT /ligand="adenosylcob(III)alamin"
FT /ligand_id="ChEBI:CHEBI:18408"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00601"
FT BINDING 185
FT /ligand="adenosylcob(III)alamin"
FT /ligand_id="ChEBI:CHEBI:18408"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00601"
FT BINDING 214
FT /ligand="adenosylcob(III)alamin"
FT /ligand_id="ChEBI:CHEBI:18408"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00601"
SQ SEQUENCE 273 AA; 30144 MW; 0247EE5E719D788A CRC64;
MNDKHLPDAS AENPWLPLRQ LTPARIALGR TGTSLPTRPQ LDFQYAHAQA RDAVHLPFDH
AAISDGLRQR GRDSLLLHSA AADRHVYLQR PDLGRRLDEA SVQRLREHAA GYDGQIDLAI
VVADGLSALA VQRHTLPFLE RLEEQALAEG WSLSPVVLVE QGRVAVADEI GELLRAKMSV
ILIGERPGLS SPDSLGLYFT WAPRVGLTDA YRNCISNVRL EGLSYGMAAH RLLYLMREAC
RRQLSGVNLK DEAEVQALDG EAPRTGNFLL ARD
