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Database: UniProt
Entry: A0A062UVG7_9EURY
LinkDB: A0A062UVG7_9EURY
Original site: A0A062UVG7_9EURY 
ID   A0A062UVG7_9EURY        Unreviewed;       356 AA.
AC   A0A062UVG7;
DT   03-SEP-2014, integrated into UniProtKB/TrEMBL.
DT   03-SEP-2014, sequence version 1.
DT   27-MAR-2024, entry version 28.
DE   SubName: Full=Pyruvate-formate lyase-activating enzyme {ECO:0000313|EMBL:KCZ71011.1};
DE            EC=1.97.1.4 {ECO:0000313|EMBL:KCZ71011.1};
GN   ORFNames=ANME2D_03040 {ECO:0000313|EMBL:KCZ71011.1};
OS   Candidatus Methanoperedens nitroreducens.
OC   Archaea; Euryarchaeota; Stenosarchaea group; Methanomicrobia;
OC   Methanosarcinales; Candidatus Methanoperedenaceae; Methanoperedens.
OX   NCBI_TaxID=1392998 {ECO:0000313|EMBL:KCZ71011.1, ECO:0000313|Proteomes:UP000027153};
RN   [1] {ECO:0000313|EMBL:KCZ71011.1, ECO:0000313|Proteomes:UP000027153}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ANME-2d {ECO:0000313|EMBL:KCZ71011.1,
RC   ECO:0000313|Proteomes:UP000027153};
RX   PubMed=23892779; DOI=10.1038/nature12375;
RA   Haroon M.F., Hu S., Shi Y., Imelfort M., Keller J., Hugenholtz P., Yuan Z.,
RA   Tyson G.W.;
RT   "Anaerobic oxidation of methane coupled to nitrate reduction in a novel
RT   archaeal lineage.";
RL   Nature 500:567-570(2013).
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:KCZ71011.1}.
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DR   EMBL; JMIY01000007; KCZ71011.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A062UVG7; -.
DR   Proteomes; UP000027153; 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; cd00207; fer2; 1.
DR   CDD; cd01335; Radical_SAM; 1.
DR   Gene3D; 3.10.20.740; -; 1.
DR   Gene3D; 3.20.20.70; Aldolase class I; 1.
DR   InterPro; IPR036010; 2Fe-2S_ferredoxin-like_sf.
DR   InterPro; IPR001041; 2Fe-2S_ferredoxin-type.
DR   InterPro; IPR013785; Aldolase_TIM.
DR   InterPro; IPR034457; Organic_radical-activating.
DR   InterPro; IPR007197; rSAM.
DR   PANTHER; PTHR30352; PYRUVATE FORMATE-LYASE-ACTIVATING ENZYME; 1.
DR   Pfam; PF13510; Fer2_4; 1.
DR   Pfam; PF13353; Fer4_12; 1.
DR   Pfam; PF04055; Radical_SAM; 1.
DR   SFLD; SFLDS00029; Radical_SAM; 1.
DR   SFLD; SFLDG01067; SPASM/twitch_domain_containing; 1.
DR   SUPFAM; SSF54292; 2Fe-2S ferredoxin-like; 1.
DR   SUPFAM; SSF102114; Radical SAM enzymes; 1.
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:KCZ71011.1};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Oxidoreductase {ECO:0000313|EMBL:KCZ71011.1};
KW   Pyruvate {ECO:0000313|EMBL:KCZ71011.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000027153};
KW   S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691}.
FT   DOMAIN          116..353
FT                   /note="Radical SAM core"
FT                   /evidence="ECO:0000259|PROSITE:PS51918"
SQ   SEQUENCE   356 AA;  39660 MW;  9C0307433B3070D6 CRC64;
     MLACSGEAIE MVEDKRQRNT IKFEFNNRVL EAPERITIKK ALEYAGIRFS ELPDGLYSPC
     NAGGCYCCAV SADGEVVPSC ITEIKDGMKL SPASKPLRVV TGFVPHMVGG VGTPYYLKSY
     SSYIEVACFT HGCNFRCPQC QNNVMAFTGG MAISPETAAE VLTSVRSMYK VNRMAFSGGE
     CTLNRQWLTG AIRHLKELNK DKKARIHVDT NASIFTKDYL EELVLAGMTD IGIDIKSLHL
     DTFEKITGTD GKTAKTYLEN EWFSARYMIE NHPEVFTGIG IPYNKALISK EEIYDMGLRI
     ADISKDVQVC VLDYRRAFRR EMAAPDIQEM KEVKEILNST GLKTVIAQTM KGNIVP
//
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