ID   PFLA_HAEIN              Reviewed;         246 AA.
AC   P43751;
DT   01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 2.
DT   02-SEP-2026, entry version 144.
DE   RecName: Full=Pyruvate formate-lyase 1-activating enzyme;
DE            EC=1.97.1.4;
DE   AltName: Full=Formate-C-acetyltransferase-activating enzyme 1;
DE   AltName: Full=PFL-activating enzyme 1;
GN   Name=pflA; Synonyms=act; OrderedLocusNames=HI_0179;
OS   Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd).
OC   Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
OC   Pasteurellales; Pasteurellaceae; Haemophilus.
OX   NCBI_TaxID=71421;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd;
RX   PubMed=7542800; DOI=10.1126/science.7542800;
RA   Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F.,
RA   Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M.,
RA   McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D.,
RA   Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., Weidman J.F.,
RA   Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., Utterback T.R.,
RA   Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., Fine L.D.,
RA   Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., Gnehm C.L., McDonald L.A.,
RA   Small K.V., Fraser C.M., Smith H.O., Venter J.C.;
RT   "Whole-genome random sequencing and assembly of Haemophilus influenzae
RT   Rd.";
RL   Science 269:496-512(1995).
CC   -!- FUNCTION: Activation of pyruvate formate-lyase 1 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:0000250}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=glycyl-[formate C-acetyltransferase] + reduced [flavodoxin] +
CC         S-adenosyl-L-methionine = glycin-2-yl radical-[formate C-
CC         acetyltransferase] + semiquinone [flavodoxin] + 5'-deoxyadenosine +
CC         L-methionine + H(+); Xref=Rhea:RHEA:19225, Rhea:RHEA-COMP:10622,
CC         Rhea:RHEA-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   -!- COFACTOR:
CC       Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883; Evidence={ECO:0000250};
CC       Note=Binds 1 [4Fe-4S] cluster. The cluster is coordinated with 3
CC       cysteines and an exchangeable S-adenosyl-L-methionine. {ECO:0000250};
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the organic radical-activating enzymes family.
CC       {ECO:0000305}.
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DR   EMBL; L42023; AAC21848.1; -; Genomic_DNA.
DR   PIR; E64052; E64052.
DR   AlphaFoldDB; P43751; -.
DR   SMR; P43751; -.
DR   STRING; 71421.HI_0179; -.
DR   EnsemblBacteria; AAC21848; AAC21848; HI_0179.
DR   KEGG; hin:HI_0179; -.
DR   PATRIC; fig|71421.8.peg.183; -.
DR   eggNOG; COG1180; Bacteria.
DR   HOGENOM; CLU_058969_1_0_6; -.
DR   OrthoDB; 9782387at2; -.
DR   PhylomeDB; P43751; -.
DR   BioCyc; HINF71421:G1GJ1-189-MONOMER; -.
DR   Proteomes; UP000000579; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:InterPro.
DR   GO; GO:0043365; F:[formate-C-acetyltransferase]-activating enzyme activity; IEA:UniProtKB-EC.
DR   CDD; cd01335; Radical_SAM; 1.
DR   Gene3D; 3.20.20.70; Aldolase class I; 1.
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; IPR012838; PFL1_activating.
DR   InterPro; IPR034465; Pyruvate_for-lyase_activase.
DR   InterPro; IPR001989; Radical_activat_CS.
DR   InterPro; IPR007197; rSAM.
DR   InterPro; IPR058240; rSAM_sf.
DR   NCBIfam; TIGR02493; PFLA; 1.
DR   NCBIfam; NF008356; PRK11145.1; 1.
DR   PANTHER; PTHR30352:SF5; PYRUVATE FORMATE-LYASE 1-ACTIVATING ENZYME; 1.
DR   PANTHER; PTHR30352; PYRUVATE FORMATE-LYASE-ACTIVATING ENZYME; 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   SFLD; SFLDF00278; pyruvate_formate-lyase_activas; 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; Carbohydrate metabolism; Cytoplasm; Glucose metabolism; Iron;
KW   Iron-sulfur; Metal-binding; Oxidoreductase; Reference proteome;
KW   S-adenosyl-L-methionine.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000250"
FT   CHAIN           2..246
FT                   /note="Pyruvate formate-lyase 1-activating enzyme"
FT                   /id="PRO_0000200525"
FT   DOMAIN          16..241
FT                   /note="Radical SAM core"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01266"
FT   BINDING         30
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /ligand_note="4Fe-4S-S-AdoMet"
FT                   /evidence="ECO:0000250|UniProtKB:P0A9N4"
FT   BINDING         34
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /ligand_note="4Fe-4S-S-AdoMet"
FT                   /evidence="ECO:0000250|UniProtKB:P0A9N4"
FT   BINDING         36..38
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000250|UniProtKB:P0A9N4"
FT   BINDING         37
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /ligand_note="4Fe-4S-S-AdoMet"
FT                   /evidence="ECO:0000250|UniProtKB:P0A9N4"
FT   BINDING         79
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000250|UniProtKB:P0A9N4"
FT   BINDING         130..132
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000250|UniProtKB:P0A9N4"
FT   BINDING         203
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000250|UniProtKB:P0A9N4"
SQ   SEQUENCE   246 AA;  28235 MW;  884313BD5B84376F CRC64;
     MSVLGRIHSF ESCGTVDGPG IRFILFMQGC LMRCKYCHNR DTWDLEGGKE ISVEDLMKEV
     VTYRHFMNAT GGGVTASGGE AVLQAEFVRD WFRACKEEGI NTCLDTNGFV RHYDHIIDEL
     LDVTDLVLLD LKELNDQVHQ NLIGVPNKRT LEFAKYLQKR NQHTWIRYVV VPGYTDSDHD
     VHLLGQFIEG MTNIEKVELL PYHRLGVHKW KTLGLDYELE NVLPPTKESL EHIKTILEGY
     GHTVKF
//