ID Q8TWE9_METKA Unreviewed; 390 AA.
AC Q8TWE9;
DT 01-JUN-2002, integrated into UniProtKB/TrEMBL.
DT 01-JUN-2002, sequence version 1.
DT 24-JAN-2024, entry version 113.
DE SubName: Full=Ferredoxin domain fused to pyruvate-formate lyase-activating enzyme {ECO:0000313|EMBL:AAM02299.1};
GN OrderedLocusNames=MK1086 {ECO:0000313|EMBL:AAM02299.1};
OS Methanopyrus kandleri (strain AV19 / DSM 6324 / JCM 9639 / NBRC 100938).
OC Archaea; Euryarchaeota; Methanomada group; Methanopyri; Methanopyrales;
OC Methanopyraceae; Methanopyrus.
OX NCBI_TaxID=190192 {ECO:0000313|EMBL:AAM02299.1, ECO:0000313|Proteomes:UP000001826};
RN [1] {ECO:0000313|EMBL:AAM02299.1, ECO:0000313|Proteomes:UP000001826}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AV19 / DSM 6324 / JCM 9639 / NBRC 100938
RC {ECO:0000313|Proteomes:UP000001826};
RX PubMed=11930014; DOI=10.1073/pnas.032671499;
RA Slesarev A.I., Mezhevaya K.V., Makarova K.S., Polushin N.N.,
RA Shcherbinina O.V., Shakhova V.V., Belova G.I., Aravind L., Natale D.A.,
RA Rogozin I.B., Tatusov R.L., Wolf Y.I., Stetter K.O., Malykh A.G.,
RA Koonin E.V., Kozyavkin S.A.;
RT "The complete genome of hyperthermophile Methanopyrus kandleri AV19 and
RT monophyly of archaeal methanogens.";
RL Proc. Natl. Acad. Sci. U.S.A. 99:4644-4649(2002).
CC -!- COFACTOR:
CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC Evidence={ECO:0000256|ARBA:ARBA00001966};
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DR EMBL; AE009439; AAM02299.1; -; Genomic_DNA.
DR AlphaFoldDB; Q8TWE9; -.
DR STRING; 190192.MK1086; -.
DR PaxDb; 190192-MK1086; -.
DR EnsemblBacteria; AAM02299; AAM02299; MK1086.
DR KEGG; mka:MK1086; -.
DR PATRIC; fig|190192.8.peg.1141; -.
DR HOGENOM; CLU_690041_0_0_2; -.
DR InParanoid; Q8TWE9; -.
DR OMA; CNLRCPQ; -.
DR OrthoDB; 371936at2157; -.
DR Proteomes; UP000001826; Chromosome.
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 CDD; cd01335; Radical_SAM; 1.
DR Gene3D; 3.30.70.20; -; 1.
DR Gene3D; 3.20.20.70; Aldolase class I; 1.
DR InterPro; IPR001041; 2Fe-2S_ferredoxin-type.
DR InterPro; IPR017896; 4Fe4S_Fe-S-bd.
DR InterPro; IPR017900; 4Fe4S_Fe_S_CS.
DR InterPro; IPR013785; Aldolase_TIM.
DR InterPro; IPR006638; Elp3/MiaA/NifB-like_rSAM.
DR InterPro; IPR034457; Organic_radical-activating.
DR InterPro; IPR007197; rSAM.
DR PANTHER; PTHR30352:SF5; PYRUVATE FORMATE-LYASE 1-ACTIVATING ENZYME; 1.
DR PANTHER; PTHR30352; PYRUVATE FORMATE-LYASE-ACTIVATING ENZYME; 1.
DR Pfam; PF00111; Fer2; 1.
DR Pfam; PF00037; Fer4; 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 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; 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:AAM02299.1};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Pyruvate {ECO:0000313|EMBL:AAM02299.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000001826};
KW S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691}.
FT DOMAIN 25..54
FT /note="4Fe-4S ferredoxin-type"
FT /evidence="ECO:0000259|PROSITE:PS51379"
FT DOMAIN 151..379
FT /note="Radical SAM core"
FT /evidence="ECO:0000259|PROSITE:PS51918"
SQ SEQUENCE 390 AA; 43064 MW; 64297CE8BDEDAC7F CRC64;
MVRKVRLVGC RHCGYCSQVV DCPVGDPLWN REDCVGCGAC VPACPYGARR LVEVEEGPIT
VRVDGEEVEV ESRWVEGALR EIGHDVDAPC GVGGCYACAV RLNGEVVPAC NSKLTEGDEV
ETEDVDGKIR VVSGFQPHPV GGVGTPVELK DKPGYVEAAC FAHGCNLRCP QCQNHSIAFG
AAMGARMRPE EAARLLVGTA REYGVNRVAI SGGEPTLNRE FLVEFVRKCR EYGGPDLRVH
VDTNGTVLSP DYVDELVEAG MTDIGIDVKG FRPETFAEVA GIDVKGAAEY VDGVLRILEY
LADEYLEEVF VGVGIPYNPE LVDKEEVFAL TDWLYEHLGE DVQVCYLDYR PEFRRRDLPL
PKYEDMVELE EYARSLGFRR VHAQKVSVRR
//