ID R7GH75_9CLOT Unreviewed; 243 AA.
AC R7GH75;
DT 24-JUL-2013, integrated into UniProtKB/TrEMBL.
DT 24-JUL-2013, sequence version 1.
DT 27-MAR-2024, entry version 32.
DE RecName: Full=Pyruvate formate-lyase-activating enzyme {ECO:0000256|ARBA:ARBA00021356, ECO:0000256|RuleBase:RU362053};
DE EC=1.97.1.4 {ECO:0000256|RuleBase:RU362053};
GN ORFNames=BN598_00626 {ECO:0000313|EMBL:CDE26505.1};
OS Clostridium sp. CAG:307.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC Clostridium.
OX NCBI_TaxID=1262795 {ECO:0000313|EMBL:CDE26505.1, ECO:0000313|Proteomes:UP000018128};
RN [1] {ECO:0000313|EMBL:CDE26505.1, ECO:0000313|Proteomes:UP000018128}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MGS:307 {ECO:0000313|Proteomes:UP000018128};
RA Nielsen H.B., Almeida M., Juncker A.S., Rasmussen S., Li J., Sunagawa S.,
RA Plichta D., Gautier L., Le Chatelier E., Peletier E., Bonde I., Nielsen T.,
RA Manichanh C., Arumugam M., Batto J., Santos M.B.Q.D., Blom N., Borruel N.,
RA Burgdorf K.S., Boumezbeur F., Casellas F., Dore J., Guarner F., Hansen T.,
RA Hildebrand F., Kaas R.S., Kennedy S., Kristiansen K., Kultima J.R.,
RA Leonard P., Levenez F., Lund O., Moumen B., Le Paslier D., Pons N.,
RA Pedersen O., Prifti E., Qin J., Raes J., Tap J., Tims S., Ussery D.W.,
RA Yamada T., MetaHit consortium, Renault P., Sicheritz-Ponten T., Bork P.,
RA Wang J., Brunak S., Ehrlich S.D.;
RT "Dependencies among metagenomic species, viruses, plasmids and units of
RT genetic variation.";
RL Submitted (NOV-2012) 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|ARBA:ARBA00003141,
CC 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}.
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:CDE26505.1}.
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DR EMBL; CBIO010000107; CDE26505.1; -; Genomic_DNA.
DR AlphaFoldDB; R7GH75; -.
DR Proteomes; UP000018128; Unassembled WGS sequence.
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:CDE26505.1};
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:CDE26505.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000018128};
KW S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691,
KW ECO:0000256|RuleBase:RU362053}.
FT DOMAIN 14..243
FT /note="Radical SAM core"
FT /evidence="ECO:0000259|PROSITE:PS51918"
SQ SEQUENCE 243 AA; 27944 MW; B8E1CDFA010E2322 CRC64;
MKGKIHSFES FGTVDGPGIR YVIFFKGCPL RCKYCHNPDT WSQDGAEEWE AQDIVNQAMK
YKGYWGDKGG VTITGGEPLL QLDFAIELLR LFHEQGVRTA VDTSGYIFDP EDPQSVKKHE
ELIKYADLFL LDIKHINRDA HKELTGVYND HTLAFAKWLS EHDKHMWIRH VLVPGITTDD
EELHELKAFL DTLKTVDKVE VLPYHTMGIV KYEKLGIPYR LKGVEPPTKE QVLHAREILK
VVK
//
