ID A0A014M200_9GAMM Unreviewed; 793 AA.
AC A0A014M200;
DT 11-JUN-2014, integrated into UniProtKB/TrEMBL.
DT 11-JUN-2014, sequence version 1.
DT 24-JAN-2024, entry version 38.
DE RecName: Full=Choline trimethylamine-lyase {ECO:0000256|HAMAP-Rule:MF_02058};
DE Short=Choline TMA-lyase {ECO:0000256|HAMAP-Rule:MF_02058};
DE EC=4.3.99.4 {ECO:0000256|HAMAP-Rule:MF_02058};
DE AltName: Full=Choline utilization protein C {ECO:0000256|HAMAP-Rule:MF_02058};
GN Name=cutC {ECO:0000256|HAMAP-Rule:MF_02058};
GN ORFNames=BG55_08790 {ECO:0000313|EMBL:EXU75861.1};
OS Erwinia mallotivora.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Erwiniaceae; Erwinia.
OX NCBI_TaxID=69222 {ECO:0000313|EMBL:EXU75861.1, ECO:0000313|Proteomes:UP000019918};
RN [1] {ECO:0000313|EMBL:EXU75861.1, ECO:0000313|Proteomes:UP000019918}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BT-MARDI {ECO:0000313|EMBL:EXU75861.1,
RC ECO:0000313|Proteomes:UP000019918};
RA Redzuan R., Abu Bakar N., Badrun R., Mohd Raih M.F., Rozano L.,
RA Mat Amin N.;
RT "Draft genome of Erwinia mallotivora strain BT-MARDI, a papaya dieback
RT pathogen.";
RL Submitted (FEB-2014) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Glycine radical enzyme that catalyzes the cleavage of a C-N
CC bond in choline, producing trimethylamine (TMA) and acetaldehyde.
CC {ECO:0000256|HAMAP-Rule:MF_02058}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=choline = acetaldehyde + trimethylamine; Xref=Rhea:RHEA:35095,
CC ChEBI:CHEBI:15343, ChEBI:CHEBI:15354, ChEBI:CHEBI:58389; EC=4.3.99.4;
CC Evidence={ECO:0000256|HAMAP-Rule:MF_02058};
CC -!- PATHWAY: Amine and polyamine metabolism; choline degradation.
CC {ECO:0000256|HAMAP-Rule:MF_02058}.
CC -!- PTM: Requires the activating protein CutD to generate the key active
CC site glycyl radical on Gly-768 that is involved in catalysis.
CC {ECO:0000256|HAMAP-Rule:MF_02058}.
CC -!- SIMILARITY: Belongs to the glycyl radical enzyme (GRE) family. CutC
CC subfamily. {ECO:0000256|HAMAP-Rule:MF_02058}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:EXU75861.1}.
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DR EMBL; JFHN01000043; EXU75861.1; -; Genomic_DNA.
DR RefSeq; WP_034936401.1; NZ_JFHN01000043.1.
DR AlphaFoldDB; A0A014M200; -.
DR STRING; 69222.BG55_08790; -.
DR PATRIC; fig|69222.5.peg.1812; -.
DR OrthoDB; 9803969at2; -.
DR UniPathway; UPA01069; -.
DR Proteomes; UP000019918; Unassembled WGS sequence.
DR GO; GO:0016840; F:carbon-nitrogen lyase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0016740; F:transferase activity; IEA:UniProtKB-KW.
DR GO; GO:0042426; P:choline catabolic process; IEA:UniProtKB-UniRule.
DR CDD; cd01677; PFL2_DhaB_BssA; 1.
DR Gene3D; 3.20.70.20; -; 1.
DR HAMAP; MF_02058; Choline_CutC; 1.
DR InterPro; IPR030897; Choline_CutC.
DR InterPro; IPR001150; Gly_radical.
DR InterPro; IPR004184; PFL_dom.
DR NCBIfam; TIGR04394; choline_CutC; 1.
DR PANTHER; PTHR43641:SF2; DEHYDRATASE YBIW-RELATED; 1.
DR PANTHER; PTHR43641; FORMATE ACETYLTRANSFERASE 3-RELATED; 1.
DR Pfam; PF01228; Gly_radical; 1.
DR Pfam; PF02901; PFL-like; 1.
DR SUPFAM; SSF51998; PFL-like glycyl radical enzymes; 1.
DR PROSITE; PS51149; GLY_RADICAL_2; 1.
DR PROSITE; PS51554; PFL; 1.
PE 3: Inferred from homology;
KW Lyase {ECO:0000256|ARBA:ARBA00023239, ECO:0000256|HAMAP-Rule:MF_02058};
KW Organic radical {ECO:0000256|ARBA:ARBA00022818, ECO:0000256|HAMAP-
KW Rule:MF_02058}; Reference proteome {ECO:0000313|Proteomes:UP000019918};
KW Transferase {ECO:0000313|EMBL:EXU75861.1}.
FT DOMAIN 8..665
FT /note="PFL"
FT /evidence="ECO:0000259|PROSITE:PS51554"
FT DOMAIN 672..793
FT /note="Glycine radical"
FT /evidence="ECO:0000259|PROSITE:PS51149"
FT ACT_SITE 437
FT /note="Cysteine radical intermediate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02058"
FT ACT_SITE 439
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02058"
FT MOD_RES 768
FT /note="Glycine radical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02058,
FT ECO:0000256|PROSITE-ProRule:PRU00493"
SQ SEQUENCE 793 AA; 88986 MW; CDA021D4FE2B05C7 CRC64;
MTNETLLPRI SALRERYLQA KPFISASRAR AVTEIYRRYP GMPVLLLRAM AFRRACQIAP
LVIGEQELII SHPAGAARGG EISPEIAWRW VADELETMST RTQDPYQISE EVKRELREEI
FPFWQGRSLD EMAETQLRHA GLWEWSTHDG ICDLSIKTQN GGGDTCPGYD IILLQKGLGG
VRKEAEEALC QLSATCAEDQ EKQYFYQAII ETCQGVTDYA HRYADYADQL AQQETSAQRK
AELENLAVIC RRVPEQPPQS FHEALQAIWF AQSLFILEEN QTGISLGRVD QYLWPLLEAD
LASGVLTLEQ AEELLCCWMI KMSECMWICS AASAMYFAGY QPFVNLVVGG QKREGGDATN
PLSLLIMDCS RKLKIYQPSL AVRIHNQSPQ PFMRKIVEVV RAGIGFPACH FDDAHIKMML
RKGFDYDDAR DYCLMGCVEP QRAGRIYQWT SVGYTTFTCA IELALNNGKT VTGSQAGPQT
GELHQLTSYE AFESAVKQQL SHIVQQAARA TLLVQKLHKS LAPKPFISCL LEGCMAQGKE
VMQGGAMINN GPGLIWTGMA DYANSMMVMH ELVWRRQQVT LEQMAQALRD NFDGHQQLHL
ACLNVVKFGN DVEEVDVIAR DLIRFTENEH RQYQMLYGPF THGTLSISNN TPFGLVTGAL
PSGRLAGMPL ADGISPSQQT DFAGPTAIIN SVGRINVEEM EIGMVHNFKL LHGILDTPEG
EQGLITLLRS ASMLGNAQMQ FSYVDDETLR KAQQDPQQYR NLMIRVAGYS AFFVELSREV
QDEIISRTQL ERF
//
