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Database: UniProt
Entry: A0PY52_CLONN
LinkDB: A0PY52_CLONN
Original site: A0PY52_CLONN 
ID   A0PY52_CLONN            Unreviewed;       304 AA.
AC   A0PY52;
DT   09-JAN-2007, integrated into UniProtKB/TrEMBL.
DT   09-JAN-2007, sequence version 1.
DT   27-MAR-2024, entry version 97.
DE   SubName: Full=Glycerol dehydratase activator {ECO:0000313|EMBL:ABK61835.1};
DE            EC=1.97.1.4 {ECO:0000313|EMBL:ABK61835.1};
GN   Name=pflC {ECO:0000313|EMBL:ABK61835.1};
GN   OrderedLocusNames=NT01CX_1221 {ECO:0000313|EMBL:ABK61835.1};
OS   Clostridium novyi (strain NT).
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC   Clostridium.
OX   NCBI_TaxID=386415 {ECO:0000313|EMBL:ABK61835.1, ECO:0000313|Proteomes:UP000008220};
RN   [1] {ECO:0000313|EMBL:ABK61835.1, ECO:0000313|Proteomes:UP000008220}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NT {ECO:0000313|EMBL:ABK61835.1,
RC   ECO:0000313|Proteomes:UP000008220};
RX   PubMed=17115055; DOI=10.1038/nbt1256;
RA   Bettegowda C., Huang X., Lin J., Cheong I., Kohli M., Szabo S.A., Zhang X.,
RA   Diaz L.A. Jr., Velculescu V.E., Parmigiani G., Kinzler K.W., Vogelstein B.,
RA   Zhou S.;
RT   "The genome and transcriptomes of the anti-tumor agent Clostridium novyi-
RT   NT.";
RL   Nat. Biotechnol. 24:1573-1580(2006).
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|ARBA:ARBA00000544};
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}.
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DR   EMBL; CP000382; ABK61835.1; -; Genomic_DNA.
DR   RefSeq; WP_011721312.1; NC_008593.1.
DR   AlphaFoldDB; A0PY52; -.
DR   STRING; 386415.NT01CX_1221; -.
DR   KEGG; cno:NT01CX_1221; -.
DR   PATRIC; fig|386415.7.peg.332; -.
DR   eggNOG; COG1180; Bacteria.
DR   HOGENOM; CLU_058969_0_0_9; -.
DR   Proteomes; UP000008220; Chromosome.
DR   GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW.
DR   GO; GO:0043365; F:[formate-C-acetyltransferase]-activating enzyme activity; IEA:UniProtKB-EC.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   CDD; cd01335; Radical_SAM; 1.
DR   Gene3D; 3.30.70.20; -; 1.
DR   Gene3D; 3.20.20.70; Aldolase class I; 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; IPR034457; Organic_radical-activating.
DR   InterPro; IPR012839; Organic_radical_activase.
DR   InterPro; IPR001989; Radical_activat_CS.
DR   InterPro; IPR007197; rSAM.
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; PF00037; Fer4; 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};
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:ABK61835.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000008220};
KW   S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691}.
FT   DOMAIN          19..295
FT                   /note="Radical SAM core"
FT                   /evidence="ECO:0000259|PROSITE:PS51918"
FT   DOMAIN          50..77
FT                   /note="4Fe-4S ferredoxin-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51379"
FT   DOMAIN          78..107
FT                   /note="4Fe-4S ferredoxin-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51379"
SQ   SEQUENCE   304 AA;  34098 MW;  1D54A3ACCB5984F7 CRC64;
     MSKDSIKGCL FNIQKFSLND GPGIRSIVFF KGCPMSCLWC SNPESQCVTP QIMYNKSLCL
     ECGTCNEVCK SSAINLNSLN RIDRERCIAC GKCVEHCPTE ALVMSGESVS VDETIEKLKK
     DSIYYRRSGG GVTLSGGEAL LQPEFAVELL KRCKALGWHT AIETAMYVKS ETVKKVVPYL
     DLILVDVKSM NTSRHKEFTG VDNNLILNNI RLSDEIAKEI IIRVPVIEGF NSDEKSIRDI
     AEFAKTLNKV NRIDLLPYHS YGENKYETIG RNYFLKDLKP PSDDKMNYFK KIVEDMGLIC
     TIGA
//
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