ID A0A200JBK8_9ENTE Unreviewed; 316 AA.
AC A0A200JBK8;
DT 25-OCT-2017, integrated into UniProtKB/TrEMBL.
DT 25-OCT-2017, sequence version 1.
DT 24-JAN-2024, entry version 23.
DE RecName: Full=Choline trimethylamine-lyase activating enzyme {ECO:0000256|HAMAP-Rule:MF_02059};
DE EC=1.97.1.- {ECO:0000256|HAMAP-Rule:MF_02059};
DE AltName: Full=Choline utilization protein D {ECO:0000256|HAMAP-Rule:MF_02059};
DE AltName: Full=GRE activase CutD {ECO:0000256|HAMAP-Rule:MF_02059};
DE AltName: Full=Glycyl-radical enzyme activating enzyme CutD {ECO:0000256|HAMAP-Rule:MF_02059};
DE Short=GRE activating enzyme CutD {ECO:0000256|HAMAP-Rule:MF_02059};
GN Name=cutD {ECO:0000256|HAMAP-Rule:MF_02059};
GN ORFNames=A5889_000059 {ECO:0000313|EMBL:OUZ34584.1};
OS Enterococcus sp. 9D6_DIV0238.
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Enterococcaceae;
OC Enterococcus.
OX NCBI_TaxID=1834192 {ECO:0000313|EMBL:OUZ34584.1, ECO:0000313|Proteomes:UP000196151};
RN [1] {ECO:0000313|EMBL:OUZ34584.1, ECO:0000313|Proteomes:UP000196151}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=9D6_DIV0238 {ECO:0000313|EMBL:OUZ34584.1,
RC ECO:0000313|Proteomes:UP000196151};
RG The Broad Institute Genomics Platform;
RG The Broad Institute Genomic Center for Infectious Diseases;
RA Earl A., Manson A., Schwartman J., Gilmore M., Abouelleil A., Cao P.,
RA Chapman S., Cusick C., Shea T., Young S., Neafsey D., Nusbaum C.,
RA Birren B.;
RT "The Genome Sequence of Enterococcus sp. 9D6_DIV0238.";
RL Submitted (MAY-2017) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Catalyzes activation of the choline trimethylamine-lyase CutC
CC under anaerobic conditions by generation of an organic free radical on
CC a glycine residue, via an homolytic cleavage of S-adenosyl-L-methionine
CC (SAM). {ECO:0000256|HAMAP-Rule:MF_02059}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=glycyl-[protein] + reduced [flavodoxin] + S-adenosyl-L-
CC methionine = 5'-deoxyadenosine + glycin-2-yl radical-[protein] + H(+)
CC + L-methionine + semiquinone [flavodoxin]; Xref=Rhea:RHEA:61976,
CC Rhea:RHEA-COMP:10622, Rhea:RHEA-COMP:14480, Rhea:RHEA-COMP:15993,
CC Rhea:RHEA-COMP:15994, ChEBI:CHEBI:15378, ChEBI:CHEBI:17319,
CC ChEBI:CHEBI:29947, ChEBI:CHEBI:32722, ChEBI:CHEBI:57618,
CC ChEBI:CHEBI:57844, ChEBI:CHEBI:59789, ChEBI:CHEBI:140311;
CC Evidence={ECO:0000256|HAMAP-Rule:MF_02059};
CC -!- COFACTOR:
CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC Evidence={ECO:0000256|HAMAP-Rule:MF_02059};
CC Note=Binds 2 [4Fe-4S] clusters. One cluster is coordinated with 3
CC cysteines and an exchangeable S-adenosyl-L-methionine.
CC {ECO:0000256|HAMAP-Rule:MF_02059};
CC -!- PATHWAY: Amine and polyamine metabolism; choline degradation.
CC {ECO:0000256|HAMAP-Rule:MF_02059}.
CC -!- SIMILARITY: Belongs to the organic radical-activating enzymes family.
CC {ECO:0000256|ARBA:ARBA00009777, ECO:0000256|HAMAP-Rule:MF_02059}.
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:OUZ34584.1}.
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DR EMBL; NIBQ01000001; OUZ34584.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A200JBK8; -.
DR OrthoDB; 9782387at2; -.
DR UniPathway; UPA01069; -.
DR Proteomes; UP000196151; Unassembled WGS sequence.
DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-UniRule.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0042426; P:choline catabolic process; IEA:UniProtKB-UniRule.
DR CDD; cd01335; Radical_SAM; 1.
DR Gene3D; 3.30.70.20; -; 1.
DR Gene3D; 3.20.20.70; Aldolase class I; 1.
DR HAMAP; MF_02059; Activ_enz_CutD; 1.
DR InterPro; IPR017896; 4Fe4S_Fe-S-bd.
DR InterPro; IPR017900; 4Fe4S_Fe_S_CS.
DR InterPro; IPR013785; Aldolase_TIM.
DR InterPro; IPR040074; BssD/PflA/YjjW.
DR InterPro; IPR030905; CutC_activ_rSAM.
DR InterPro; IPR034457; Organic_radical-activating.
DR InterPro; IPR012839; Organic_radical_activase.
DR InterPro; IPR001989; Radical_activat_CS.
DR InterPro; IPR007197; rSAM.
DR NCBIfam; TIGR04395; cutC_activ_rSAM; 1.
DR NCBIfam; TIGR02494; PFLE_PFLC; 1.
DR PANTHER; PTHR30352:SF4; PYRUVATE FORMATE-LYASE 2-ACTIVATING ENZYME; 1.
DR PANTHER; PTHR30352; PYRUVATE FORMATE-LYASE-ACTIVATING ENZYME; 1.
DR Pfam; PF13353; Fer4_12; 1.
DR Pfam; PF13187; Fer4_9; 1.
DR Pfam; PF04055; Radical_SAM; 1.
DR PIRSF; PIRSF000371; PFL_act_enz; 1.
DR SFLD; SFLDG01118; activating_enzymes__group_2; 1.
DR SFLD; SFLDG01066; organic_radical-activating_enz; 1.
DR SUPFAM; SSF54862; 4Fe-4S ferredoxins; 1.
DR SUPFAM; SSF102114; Radical SAM enzymes; 1.
DR PROSITE; PS00198; 4FE4S_FER_1; 1.
DR PROSITE; PS51379; 4FE4S_FER_2; 2.
DR PROSITE; PS01087; RADICAL_ACTIVATING; 1.
DR PROSITE; PS51918; RADICAL_SAM; 1.
PE 3: Inferred from homology;
KW 4Fe-4S {ECO:0000256|ARBA:ARBA00022485, ECO:0000256|HAMAP-Rule:MF_02059};
KW Iron {ECO:0000256|ARBA:ARBA00023004, ECO:0000256|HAMAP-Rule:MF_02059};
KW Iron-sulfur {ECO:0000256|ARBA:ARBA00023014, ECO:0000256|HAMAP-
KW Rule:MF_02059};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|HAMAP-
KW Rule:MF_02059};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002, ECO:0000256|HAMAP-
KW Rule:MF_02059}; Reference proteome {ECO:0000313|Proteomes:UP000196151};
KW Repeat {ECO:0000256|HAMAP-Rule:MF_02059};
KW S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691, ECO:0000256|HAMAP-
KW Rule:MF_02059}.
FT DOMAIN 24..310
FT /note="Radical SAM core"
FT /evidence="ECO:0000259|PROSITE:PS51918"
FT DOMAIN 55..84
FT /note="4Fe-4S ferredoxin-type"
FT /evidence="ECO:0000259|PROSITE:PS51379"
FT DOMAIN 85..115
FT /note="4Fe-4S ferredoxin-type"
FT /evidence="ECO:0000259|PROSITE:PS51379"
FT BINDING 38
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="1"
FT /ligand_note="4Fe-4S-S-AdoMet"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02059"
FT BINDING 42
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="1"
FT /ligand_note="4Fe-4S-S-AdoMet"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02059"
FT BINDING 44..46
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02059"
FT BINDING 45
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="1"
FT /ligand_note="4Fe-4S-S-AdoMet"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02059"
FT BINDING 64
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="2"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02059"
FT BINDING 67
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="2"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02059"
FT BINDING 70
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="2"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02059"
FT BINDING 105
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="2"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02059"
FT BINDING 145
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02059"
FT BINDING 194..196
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02059"
FT BINDING 270
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02059"
SQ SEQUENCE 316 AA; 35673 MW; B0FB5C1A5ED164DC CRC64;
MNNPSTETIE RQVMIFNVQK YSLYDGPGIR TIVFFKGCPL RCQWCANPEG LERKFEVMYK
ESVCSDCRAC VDVCPVGIHY MDENGDHQVN RDIACTGCRA CSDVCPMAAL NITGEIKSIS
EVMEIVHEDD EFYEQSGGGV TLSGGECTAQ PEAALALLQA CKADGINTAI ETCGHSRMER
LLKIAEYVDL FLFDLKHMDP VRHNELTGIS NEKILANLKE VLELGHDVQI RMPMLKMIND
SQQEIQAIIE FLLPYKDYPN FHGIDLLPYH KLGVNKYGQL GMEYPVAGDP SLTDPELDQI
ERWIKDYDFP VKVVRH
//
