ID A0A0M2NGW8_9FIRM Unreviewed; 295 AA.
AC A0A0M2NGW8;
DT 11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT 11-NOV-2015, sequence version 1.
DT 24-JAN-2024, entry version 24.
DE SubName: Full=Pyruvate formate-lyase activating enzyme {ECO:0000313|EMBL:KKI50196.1};
DE EC=1.97.1.4 {ECO:0000313|EMBL:KKI50196.1};
GN ORFNames=CHK_2259 {ECO:0000313|EMBL:KKI50196.1};
OS Christensenella hongkongensis.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Christensenellaceae;
OC Christensenella.
OX NCBI_TaxID=270498 {ECO:0000313|EMBL:KKI50196.1, ECO:0000313|Proteomes:UP000034076};
RN [1] {ECO:0000313|EMBL:KKI50196.1, ECO:0000313|Proteomes:UP000034076}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HKU16 {ECO:0000313|EMBL:KKI50196.1,
RC ECO:0000313|Proteomes:UP000034076};
RA Lau S.K., Teng J.L., Huang Y., Curreem S.O., Tsui S.K., Woo P.C.;
RT "Draft genome sequence of bacteremic isolate Catabacter hongkongensis type
RT strain HKU16T.";
RL Submitted (APR-2015) 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 -!- SIMILARITY: Belongs to the organic radical-activating enzymes family.
CC {ECO:0000256|ARBA:ARBA00009777}.
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:KKI50196.1}.
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DR EMBL; LAYJ01000112; KKI50196.1; -; Genomic_DNA.
DR RefSeq; WP_052740535.1; NZ_SMCZ01000001.1.
DR AlphaFoldDB; A0A0M2NGW8; -.
DR STRING; 270498.CHK_2259; -.
DR PATRIC; fig|270498.16.peg.2010; -.
DR Proteomes; UP000034076; Unassembled WGS sequence.
DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW.
DR GO; GO:0043365; F:[formate-C-acetyltransferase]-activating enzyme activity; IEA:UniProtKB-EC.
DR GO; GO:0016829; F:lyase activity; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR CDD; cd01335; Radical_SAM; 1.
DR Gene3D; 3.30.70.20; -; 2.
DR Gene3D; 3.80.30.10; pyruvate-formate lyase- activating enzyme; 1.
DR InterPro; IPR017896; 4Fe4S_Fe-S-bd.
DR InterPro; IPR017900; 4Fe4S_Fe_S_CS.
DR InterPro; IPR040074; BssD/PflA/YjjW.
DR InterPro; IPR006638; Elp3/MiaA/NifB-like_rSAM.
DR InterPro; IPR034457; Organic_radical-activating.
DR InterPro; IPR012839; Organic_radical_activase.
DR InterPro; IPR001989; Radical_activat_CS.
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; PF13353; Fer4_12; 1.
DR Pfam; PF12837; Fer4_6; 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 SMART; SM00729; Elp3; 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; PS01087; RADICAL_ACTIVATING; 1.
DR PROSITE; PS51918; RADICAL_SAM; 1.
PE 3: Inferred from homology;
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:KKI50196.1};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000313|EMBL:KKI50196.1}; Pyruvate {ECO:0000313|EMBL:KKI50196.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000034076};
KW S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691}.
FT DOMAIN 15..290
FT /note="Radical SAM core"
FT /evidence="ECO:0000259|PROSITE:PS51918"
FT DOMAIN 46..75
FT /note="4Fe-4S ferredoxin-type"
FT /evidence="ECO:0000259|PROSITE:PS51379"
FT DOMAIN 78..99
FT /note="4Fe-4S ferredoxin-type"
FT /evidence="ECO:0000259|PROSITE:PS51379"
SQ SEQUENCE 295 AA; 33049 MW; 095592FDDE96FFCC CRC64;
MKQGTIFNIQ RYSLHDGPGI RTIIFLKGCP LKCAWCSNPE SQPLRKQVVF KPDLCIGCGK
CFSSCPTGER GREPFTICDI ACGKCVNICP TEALEMIGEK VSVEQVMREV EKDRSFYRKS
GGGMTLSGGE PLMQGEFALE LIRAAKKSGI DTAIETTGYA KWEAAEEIFG EVDHILYDLK
HMDDGLHKKY TGVSNRLILE NLKKVAAKRS DALITRIPII GMVNADEQNM KRSAEFLQEA
GVREVHLLPY HKYGEGKYHK LYRDYELQAI TPEDAQIDSI IELMREYGIS AKKSG
//
