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Database: UniProt
Entry: Q6LNK2_PHOPR
LinkDB: Q6LNK2_PHOPR
Original site: Q6LNK2_PHOPR 
ID   Q6LNK2_PHOPR            Unreviewed;       246 AA.
AC   Q6LNK2;
DT   05-JUL-2004, integrated into UniProtKB/TrEMBL.
DT   05-JUL-2004, sequence version 1.
DT   24-JAN-2024, entry version 106.
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:CAG21124.1};
GN   OrderedLocusNames=PBPRA2752 {ECO:0000313|EMBL:CAG21124.1};
OS   Photobacterium profundum (strain SS9).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC   Photobacterium.
OX   NCBI_TaxID=298386 {ECO:0000313|EMBL:CAG21124.1, ECO:0000313|Proteomes:UP000000593};
RN   [1] {ECO:0000313|Proteomes:UP000000593}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-1253 / SS9 {ECO:0000313|Proteomes:UP000000593};
RX   PubMed=15746425; DOI=10.1126/science.1103341;
RA   Vezzi A., Campanaro S., D'Angelo M., Simonato F., Vitulo N., Lauro F.M.,
RA   Cestaro A., Malacrida G., Simionati B., Cannata N., Romualdi C.,
RA   Bartlett D.H., Valle G.;
RT   "Life at depth: Photobacterium profundum genome sequence and expression
RT   analysis.";
RL   Science 307:1459-1461(2005).
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:0000256|ARBA:ARBA00002918}.
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|ARBA:ARBA00001872,
CC         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|ARBA:ARBA00004496,
CC       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; CR378672; CAG21124.1; -; Genomic_DNA.
DR   RefSeq; WP_011219399.1; NC_006370.1.
DR   AlphaFoldDB; Q6LNK2; -.
DR   STRING; 298386.PBPRA2752; -.
DR   KEGG; ppr:PBPRA2752; -.
DR   eggNOG; COG1180; Bacteria.
DR   HOGENOM; CLU_058969_1_0_6; -.
DR   OMA; IGVPNKR; -.
DR   Proteomes; UP000000593; Chromosome 1.
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: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; 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   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   PIRSF; PIRSF000371; PFL_act_enz; 2.
DR   SFLD; SFLDG01066; organic_radical-activating_enz; 1.
DR   SFLD; SFLDF00278; pyruvate_formate-lyase_activas; 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   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:CAG21124.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000593};
KW   S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691,
KW   ECO:0000256|RuleBase:RU362053}.
FT   DOMAIN          16..243
FT                   /note="Radical SAM core"
FT                   /evidence="ECO:0000259|PROSITE:PS51918"
SQ   SEQUENCE   246 AA;  28199 MW;  04EF9C80E594A18B CRC64;
     MSVKGRIHSF ESCGTVDGPG IRFIIFMQGC LMRCQYCHNR DTWDLHDGRE ISVEEIMKEA
     VSYRHFMKAS GGGVTASGGE AMLQPEFIRD FFRAAQAENI HTCLDTNGYI RKHTDVVDEV
     LDATDLVMLD LKQMDDTIHQ ELVGVSNKRV LDFARYLHKR GQKTWIRYVI VPGYTDDEQS
     AHNLGAFIKD MDNIEKIELL PYHQLGEHKW DAMGYDYPLS GVQPPSKETM EKMKEIISSY
     GHKVIY
//
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