ID A0A1Q8QN98_9FIRM Unreviewed; 315 AA.
AC A0A1Q8QN98;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 24-JAN-2024, entry version 21.
DE SubName: Full=Pyruvate formate-lyase activating enzyme {ECO:0000313|EMBL:OLN28817.1};
GN ORFNames=DSOL_3894 {ECO:0000313|EMBL:OLN28817.1};
OS Desulfosporosinus metallidurans.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Desulfitobacteriaceae;
OC Desulfosporosinus.
OX NCBI_TaxID=1888891 {ECO:0000313|EMBL:OLN28817.1, ECO:0000313|Proteomes:UP000186102};
RN [1] {ECO:0000313|EMBL:OLN28817.1, ECO:0000313|Proteomes:UP000186102}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=OL {ECO:0000313|EMBL:OLN28817.1,
RC ECO:0000313|Proteomes:UP000186102};
RA Mardanov A., Beletsky A., Panova A., Karnachuk O., Ravin N.;
RT "Complete genome of Desulfosporosinus sp. OL.";
RL Submitted (SEP-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=glycyl-[protein] + reduced [flavodoxin] + S-adenosyl-L-
CC methionine = 5'-deoxyadenosine + glycin-2-yl radical-[protein] + H(+)
CC + L-methionine + semiquinone [flavodoxin]; Xref=Rhea:RHEA:61976,
CC Rhea:RHEA-COMP:10622, Rhea:RHEA-COMP:14480, Rhea:RHEA-COMP:15993,
CC Rhea:RHEA-COMP:15994, ChEBI:CHEBI:15378, ChEBI:CHEBI:17319,
CC ChEBI:CHEBI:29947, ChEBI:CHEBI:32722, ChEBI:CHEBI:57618,
CC ChEBI:CHEBI:57844, ChEBI:CHEBI:59789, ChEBI:CHEBI:140311;
CC Evidence={ECO:0000256|ARBA:ARBA00000544};
CC -!- COFACTOR:
CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC Evidence={ECO:0000256|ARBA:ARBA00001966};
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:OLN28817.1}.
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DR EMBL; MLBF01000039; OLN28817.1; -; Genomic_DNA.
DR RefSeq; WP_075366311.1; NZ_MLBF01000039.1.
DR AlphaFoldDB; A0A1Q8QN98; -.
DR STRING; 1888891.DSOL_3894; -.
DR OrthoDB; 9782387at2; -.
DR Proteomes; UP000186102; Unassembled WGS sequence.
DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW.
DR GO; GO:0016829; F:lyase activity; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:InterPro.
DR Gene3D; 3.30.70.20; -; 1.
DR Gene3D; 3.20.20.70; Aldolase class I; 1.
DR InterPro; IPR017896; 4Fe4S_Fe-S-bd.
DR InterPro; IPR017900; 4Fe4S_Fe_S_CS.
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; IPR007197; rSAM.
DR NCBIfam; TIGR02494; PFLE_PFLC; 1.
DR PANTHER; PTHR30352:SF4; PYRUVATE FORMATE-LYASE 2-ACTIVATING ENZYME; 1.
DR PANTHER; PTHR30352; PYRUVATE FORMATE-LYASE-ACTIVATING ENZYME; 1.
DR Pfam; PF13237; Fer4_10; 1.
DR Pfam; PF13353; Fer4_12; 1.
DR Pfam; PF04055; Radical_SAM; 1.
DR PIRSF; PIRSF000371; PFL_act_enz; 1.
DR SFLD; SFLDG01118; activating_enzymes__group_2; 1.
DR SFLD; SFLDS00029; Radical_SAM; 1.
DR SUPFAM; SSF54862; 4Fe-4S ferredoxins; 1.
DR SUPFAM; SSF102114; Radical SAM enzymes; 1.
DR PROSITE; PS00198; 4FE4S_FER_1; 1.
DR PROSITE; PS51379; 4FE4S_FER_2; 2.
DR PROSITE; PS51918; RADICAL_SAM; 1.
PE 4: Predicted;
KW 4Fe-4S {ECO:0000256|ARBA:ARBA00022485};
KW Iron {ECO:0000256|ARBA:ARBA00023004};
KW Iron-sulfur {ECO:0000256|ARBA:ARBA00023014};
KW Lyase {ECO:0000313|EMBL:OLN28817.1};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Pyruvate {ECO:0000313|EMBL:OLN28817.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000186102};
KW S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691}.
FT DOMAIN 19..301
FT /note="Radical SAM core"
FT /evidence="ECO:0000259|PROSITE:PS51918"
FT DOMAIN 50..79
FT /note="4Fe-4S ferredoxin-type"
FT /evidence="ECO:0000259|PROSITE:PS51379"
FT DOMAIN 81..110
FT /note="4Fe-4S ferredoxin-type"
FT /evidence="ECO:0000259|PROSITE:PS51379"
SQ SEQUENCE 315 AA; 35248 MW; C7C3DA57AA37EDEB CRC64;
MNHSKLMGSV LRIERTSIHD GQGLRTVLFL KGCPLKCRWC STPESQRTDP EKGYVLDRCV
KCGICVRSCL EGALAMSEDG LKILINAAKC KNCFVCVAKC PQNAFKKYGS IMSVREAIRE
ISKDEIFFFH SGGGVTISGG EPLNQPDFVS EVLKECRELG IHTAIETSLH APYENIETIL
PWLNVLYVDL KQMDQEFHKQ WVGPDNSLIL ANIRRIDQAN YPLEIIVRIP LIPGVNDSNS
NLSATAEFCK SLKIIKGIEL LAYHRLGMET YRNLGMDYPL QDLVPPSRER ILERADFLSR
QNPGVPIRVG GGLIS
//
