ID A0A0G3HA13_9CORY Unreviewed; 292 AA.
AC A0A0G3HA13;
DT 16-SEP-2015, integrated into UniProtKB/TrEMBL.
DT 16-SEP-2015, sequence version 1.
DT 27-MAR-2024, entry version 31.
DE RecName: Full=Pyruvate formate-lyase-activating enzyme {ECO:0000256|RuleBase:RU362053};
DE EC=1.97.1.4 {ECO:0000256|RuleBase:RU362053};
GN Name=pflA {ECO:0000313|EMBL:AKK08733.1};
GN ORFNames=CTEST_06475 {ECO:0000313|EMBL:AKK08733.1};
OS Corynebacterium testudinoris.
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales;
OC Corynebacteriaceae; Corynebacterium.
OX NCBI_TaxID=136857 {ECO:0000313|EMBL:AKK08733.1, ECO:0000313|Proteomes:UP000035540};
RN [1] {ECO:0000313|EMBL:AKK08733.1, ECO:0000313|Proteomes:UP000035540}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 44614 {ECO:0000313|EMBL:AKK08733.1,
RC ECO:0000313|Proteomes:UP000035540};
RX PubMed=26227591;
RA Ruckert C., Kriete M., Jaenicke S., Winkler A., Tauch A.;
RT "Complete Genome Sequence of the Type Strain Corynebacterium testudinoris
RT DSM 44614, Recovered from Necrotic Lesions in the Mouth of a Tortoise.";
RL Genome Announc. 3:e00784-15(2015).
RN [2] {ECO:0000313|Proteomes:UP000035540}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 44614 {ECO:0000313|Proteomes:UP000035540};
RA Ruckert C., Albersmeier A., Winkler A., Tauch A.;
RT "Complete genome sequence of Corynebacterium testudinoris DSM 44614,
RT recovered from necrotic lesions in the mouth of a tortoise.";
RL Submitted (MAY-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Activation of pyruvate formate-lyase under anaerobic
CC conditions by generation of an organic free radical, using S-
CC adenosylmethionine and reduced flavodoxin as cosubstrates to produce
CC 5'-deoxy-adenosine. {ECO:0000256|RuleBase:RU362053}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=glycyl-[formate C-acetyltransferase] + reduced [flavodoxin] +
CC S-adenosyl-L-methionine = 5'-deoxyadenosine + glycin-2-yl radical-
CC [formate C-acetyltransferase] + H(+) + L-methionine + semiquinone
CC [flavodoxin]; Xref=Rhea:RHEA:19225, Rhea:RHEA-COMP:10622, Rhea:RHEA-
CC COMP:12190, Rhea:RHEA-COMP:12191, Rhea:RHEA-COMP:14480,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:17319, ChEBI:CHEBI:29947,
CC ChEBI:CHEBI:32722, ChEBI:CHEBI:57618, ChEBI:CHEBI:57844,
CC ChEBI:CHEBI:59789, ChEBI:CHEBI:140311; EC=1.97.1.4;
CC Evidence={ECO:0000256|RuleBase:RU362053};
CC -!- COFACTOR:
CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC Evidence={ECO:0000256|RuleBase:RU362053};
CC Note=Binds 1 [4Fe-4S] cluster. The cluster is coordinated with 3
CC cysteines and an exchangeable S-adenosyl-L-methionine.
CC {ECO:0000256|RuleBase:RU362053};
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|RuleBase:RU362053}.
CC -!- SIMILARITY: Belongs to the organic radical-activating enzymes family.
CC {ECO:0000256|ARBA:ARBA00009777, ECO:0000256|RuleBase:RU362053}.
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DR EMBL; CP011545; AKK08733.1; -; Genomic_DNA.
DR RefSeq; WP_047253044.1; NZ_JAASJB010000002.1.
DR AlphaFoldDB; A0A0G3HA13; -.
DR STRING; 136857.CTEST_06475; -.
DR KEGG; cted:CTEST_06475; -.
DR PATRIC; fig|136857.5.peg.1286; -.
DR OrthoDB; 9782387at2; -.
DR Proteomes; UP000035540; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-UniRule.
DR GO; GO:0043365; F:[formate-C-acetyltransferase]-activating enzyme activity; IEA:UniProtKB-UniRule.
DR GO; GO:0016829; F:lyase activity; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-UniRule.
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; IPR012838; PFL1_activating.
DR InterPro; IPR001989; Radical_activat_CS.
DR InterPro; IPR007197; rSAM.
DR NCBIfam; TIGR02493; PFLA; 1.
DR PANTHER; PTHR30352:SF23; PYRUVATE FORMATE-LYASE 1-ACTIVATING ENZYME; 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, ECO:0000256|RuleBase:RU362053};
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490, ECO:0000256|RuleBase:RU362053};
KW Iron {ECO:0000256|ARBA:ARBA00023004, ECO:0000256|RuleBase:RU362053};
KW Iron-sulfur {ECO:0000256|ARBA:ARBA00023014, ECO:0000256|RuleBase:RU362053};
KW Lyase {ECO:0000313|EMBL:AKK08733.1};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|RuleBase:RU362053};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000256|RuleBase:RU362053}; Pyruvate {ECO:0000313|EMBL:AKK08733.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000035540};
KW S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691,
KW ECO:0000256|RuleBase:RU362053}.
FT DOMAIN 65..290
FT /note="Radical SAM core"
FT /evidence="ECO:0000259|PROSITE:PS51918"
SQ SEQUENCE 292 AA; 32230 MW; 12A7435866FB9311 CRC64;
MAHSSDGVTG VVHLEPEVGE RVRGVAGGLG GTEDLAEDLT RPELMAARQT GDVALVHSWE
MVTAVDGPGT RMTLFLSGCP LRCLYCHNPD TMEMRTGTLE KVEDVVKRIT RYKRVFQASQ
GGLTISGGEP LFQIAFTRRV LAEVHAAGIH TAIDTSGFLG SRLRDEDLDN IDLVLLDVKS
GDPDTYKRVT SRELQPTIDF GDRLAAANKP VWVRFVLVPG LTDDPANVAS VADIVSRWPN
VERVEVLPFH NMGADKWREL DMTYQLSDVR PPTPESVNEV REVFRSRGML TY
//
