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Database: UniProt
Entry: D0GMM9_9FUSO
LinkDB: D0GMM9_9FUSO
Original site: D0GMM9_9FUSO 
ID   D0GMM9_9FUSO            Unreviewed;       243 AA.
AC   D0GMM9;
DT   15-DEC-2009, integrated into UniProtKB/TrEMBL.
DT   15-DEC-2009, sequence version 1.
DT   24-JAN-2024, entry version 46.
DE   SubName: Full=Glycine radical enzyme activase, YjjW family {ECO:0000313|EMBL:EEY34653.1};
DE            EC=1.97.1.- {ECO:0000313|EMBL:EEY34653.1};
GN   Name=yjjW {ECO:0000313|EMBL:EEY34653.1};
GN   ORFNames=HMPREF0554_1513 {ECO:0000313|EMBL:EEY34653.1};
OS   Pseudoleptotrichia goodfellowii F0264.
OC   Bacteria; Fusobacteriota; Fusobacteriia; Fusobacteriales; Leptotrichiaceae;
OC   Pseudoleptotrichia.
OX   NCBI_TaxID=596323 {ECO:0000313|EMBL:EEY34653.1, ECO:0000313|Proteomes:UP000004226};
RN   [1] {ECO:0000313|EMBL:EEY34653.1, ECO:0000313|Proteomes:UP000004226}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=F0264 {ECO:0000313|EMBL:EEY34653.1,
RC   ECO:0000313|Proteomes:UP000004226};
RA   Harkins D.M., Madupu R., Durkin A.S., Torralba M., Methe B., Sutton G.G.,
RA   Strausberg R.L., Nelson K.E.;
RL   Submitted (OCT-2009) to the EMBL/GenBank/DDBJ databases.
CC   -!- COFACTOR:
CC       Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC         Evidence={ECO:0000256|ARBA:ARBA00001966};
CC   -!- SIMILARITY: Belongs to the organic radical-activating enzymes family.
CC       {ECO:0000256|ARBA:ARBA00009777}.
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:EEY34653.1}.
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DR   EMBL; ADAD01000145; EEY34653.1; -; Genomic_DNA.
DR   RefSeq; WP_006807752.1; NZ_ADAD01000145.1.
DR   AlphaFoldDB; D0GMM9; -.
DR   eggNOG; COG1180; Bacteria.
DR   Proteomes; UP000004226; Unassembled WGS sequence.
DR   GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR   CDD; cd01335; Radical_SAM; 1.
DR   Gene3D; 3.20.20.70; Aldolase class I; 1.
DR   InterPro; IPR013785; Aldolase_TIM.
DR   InterPro; IPR034457; Organic_radical-activating.
DR   InterPro; IPR001989; Radical_activat_CS.
DR   InterPro; IPR007197; rSAM.
DR   PANTHER; PTHR30352:SF13; GLYCYL-RADICAL ENZYME ACTIVATING ENZYME YJJW-RELATED; 1.
DR   PANTHER; PTHR30352; PYRUVATE FORMATE-LYASE-ACTIVATING ENZYME; 1.
DR   Pfam; PF13353; Fer4_12; 1.
DR   Pfam; PF04055; Radical_SAM; 1.
DR   SFLD; SFLDG01066; organic_radical-activating_enz; 1.
DR   SFLD; SFLDS00029; Radical_SAM; 1.
DR   SUPFAM; SSF102114; Radical SAM enzymes; 1.
DR   PROSITE; PS01087; RADICAL_ACTIVATING; 1.
DR   PROSITE; PS51918; RADICAL_SAM; 1.
PE   3: Inferred from homology;
KW   4Fe-4S {ECO:0000256|ARBA:ARBA00022485};
KW   Iron {ECO:0000256|ARBA:ARBA00023004};
KW   Iron-sulfur {ECO:0000256|ARBA:ARBA00023014};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW   ECO:0000313|EMBL:EEY34653.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000004226};
KW   S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691}.
FT   DOMAIN          14..243
FT                   /note="Radical SAM core"
FT                   /evidence="ECO:0000259|PROSITE:PS51918"
SQ   SEQUENCE   243 AA;  27885 MW;  F949359907ACAA2D CRC64;
     MKGIVNKIIP FSNVDGPGNR LSIFFQGCNF DCLYCHNPET IEVFGENKVP EEISVMEIDD
     ILKEIEEVAP FISGITVSGG ECSLQWKFLT ELFKAVKKRW ERMTCFVDSN GSIPLWTEDK
     KEFLSVTDKI MLDIKAFDEK DHILMVGVSN ENVIKNFKFL VEIGKIYEVR TVIVPEIIDN
     EKTVDNISKL IAEYDKNLKY KLLRFRQNGV RRDVLVAYTP NDDYMNNLKN IATKNGLTDV
     VII
//
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