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Entry: A0A1Q5PJC5_9ACTO
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ID   A0A1Q5PJC5_9ACTO        Unreviewed;       298 AA.
AC   A0A1Q5PJC5;
DT   12-APR-2017, integrated into UniProtKB/TrEMBL.
DT   12-APR-2017, sequence version 1.
DT   24-JAN-2024, entry version 25.
DE   RecName: Full=Pyruvate formate-lyase-activating enzyme {ECO:0000256|RuleBase:RU362053};
DE            EC=1.97.1.4 {ECO:0000256|RuleBase:RU362053};
GN   ORFNames=BSR29_08415 {ECO:0000313|EMBL:OKL45993.1};
OS   Boudabousia liubingyangii.
OC   Bacteria; Actinomycetota; Actinomycetes; Actinomycetales; Actinomycetaceae;
OC   Boudabousia.
OX   NCBI_TaxID=1921764 {ECO:0000313|EMBL:OKL45993.1, ECO:0000313|Proteomes:UP000186785};
RN   [1] {ECO:0000313|EMBL:OKL45993.1, ECO:0000313|Proteomes:UP000186785}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=VUL4_2 {ECO:0000313|EMBL:OKL45993.1,
RC   ECO:0000313|Proteomes:UP000186785};
RA   Meng X.;
RT   "Actinomyces gypaetusis sp. nov. isolated from the vulture Gypaetus
RT   barbatus in Qinghai Tibet Plateau China.";
RL   Submitted (NOV-2016) 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}.
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:OKL45993.1}.
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DR   EMBL; MQSV01000007; OKL45993.1; -; Genomic_DNA.
DR   RefSeq; WP_073709860.1; NZ_MQSV01000007.1.
DR   AlphaFoldDB; A0A1Q5PJC5; -.
DR   STRING; 1921764.BSR28_04410; -.
DR   OrthoDB; 9782387at2; -.
DR   Proteomes; UP000186785; 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:SF5; 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|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:OKL45993.1};
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:OKL45993.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000186785};
KW   S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691,
KW   ECO:0000256|RuleBase:RU362053}.
FT   DOMAIN          71..296
FT                   /note="Radical SAM core"
FT                   /evidence="ECO:0000259|PROSITE:PS51918"
FT   REGION          1..23
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   298 AA;  33447 MW;  E60AAD1AEF84F57B CRC64;
     MEEVRFDATR YSDGSTGEYR PQPLDYEVPR LKGAGTAGIA GAPLMDRREH LEAVRRGELG
     SIHSWELVTA VDGPGTRMTI FLAGCPLRCL YCHNPDTFKM KDGEPVRAED LLSRISRYVP
     IFRSSGGGIT ISGGEPLMQP QFVAWLLRGA KDMGVHTCID TSGFLGRNLT DEMMADLDLV
     LLDVKSGIPE TYRRTTGRDL QPTIDFGDRL NAAGKKIWIR FVVVPGLTDA PENVEAVANI
     VSRWENVQRV EVLPFHQMGR DKWRELGYEY QLEDVQPPSK ESVESIRQVF RSRGIETY
//
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