ID Q8TWY6_METKA Unreviewed; 457 AA.
AC Q8TWY6;
DT 01-JUN-2002, integrated into UniProtKB/TrEMBL.
DT 01-JUN-2002, sequence version 1.
DT 27-MAR-2024, entry version 95.
DE SubName: Full=Fe-S oxidoreductase {ECO:0000313|EMBL:AAM02108.1};
GN OrderedLocusNames=MK0895 {ECO:0000313|EMBL:AAM02108.1};
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:AAM02108.1, ECO:0000313|Proteomes:UP000001826};
RN [1] {ECO:0000313|EMBL:AAM02108.1, 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; AAM02108.1; -; Genomic_DNA.
DR AlphaFoldDB; Q8TWY6; -.
DR STRING; 190192.MK0895; -.
DR PaxDb; 190192-MK0895; -.
DR EnsemblBacteria; AAM02108; AAM02108; MK0895.
DR KEGG; mka:MK0895; -.
DR HOGENOM; CLU_021572_4_3_2; -.
DR InParanoid; Q8TWY6; -.
DR OrthoDB; 2305at2157; -.
DR Proteomes; UP000001826; Chromosome.
DR GO; GO:0003824; F:catalytic activity; IEA:InterPro.
DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro.
DR GO; GO:0051536; F:iron-sulfur cluster binding; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:InterPro.
DR CDD; cd01335; Radical_SAM; 1.
DR CDD; cd02068; radical_SAM_B12_BD; 1.
DR Gene3D; 3.40.50.280; Cobalamin-binding domain; 1.
DR Gene3D; 3.80.30.20; tm_1862 like domain; 1.
DR InterPro; IPR006158; Cobalamin-bd.
DR InterPro; IPR006638; Elp3/MiaA/NifB-like_rSAM.
DR InterPro; IPR034466; Methyltransferase_Class_B.
DR InterPro; IPR007197; rSAM.
DR InterPro; IPR023404; rSAM_horseshoe.
DR PANTHER; PTHR43409:SF7; ANAEROBIC MAGNESIUM-PROTOPORPHYRIN IX MONOMETHYL ESTER CYCLASE; 1.
DR PANTHER; PTHR43409; ANAEROBIC MAGNESIUM-PROTOPORPHYRIN IX MONOMETHYL ESTER CYCLASE-RELATED; 1.
DR Pfam; PF02310; B12-binding; 1.
DR Pfam; PF04055; Radical_SAM; 1.
DR SFLD; SFLDG01123; methyltransferase_(Class_B); 1.
DR SFLD; SFLDS00029; Radical_SAM; 1.
DR SMART; SM00729; Elp3; 1.
DR SUPFAM; SSF102114; Radical SAM enzymes; 1.
DR PROSITE; PS51332; B12_BINDING; 1.
DR PROSITE; PS51918; RADICAL_SAM; 1.
PE 4: Predicted;
KW 4Fe-4S {ECO:0000256|ARBA:ARBA00022485};
KW Iron {ECO:0000256|ARBA:ARBA00022485};
KW Iron-sulfur {ECO:0000256|ARBA:ARBA00022485};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022485};
KW Reference proteome {ECO:0000313|Proteomes:UP000001826}.
FT DOMAIN 9..138
FT /note="B12-binding"
FT /evidence="ECO:0000259|PROSITE:PS51332"
FT DOMAIN 183..409
FT /note="Radical SAM core"
FT /evidence="ECO:0000259|PROSITE:PS51918"
SQ SEQUENCE 457 AA; 51855 MW; E6C2A6E662B60355 CRC64;
MKVLLVQPPF EDDIARVLGV RGFPIGLVYL AAKLEKEGFS VDILDCPAEG VEMEDLRGRI
RGYDAVGITA TTPVAPSAYK VAKLAKDEGA FVFLGGPHPT FMDREALRES PADVVIRGEG
ESTTVEVLEA VDRWEESDLS NIPGITYREG SKIVRNPDRQ EPEDLDSLPL PAYDKVDLDQ
YSADSVRFVP VITSRGCPFR CLFCASSRIF GPKWRGKSPD RVVEEISYLV EELGVERLEF
VDDVFTAHKR RVREICEKMR EEGIDVPWDC GARADTLTPE LARTIREHGC RTVYVGAESA
SNETLKRINK GITVQDVIAC RKVAKRHGLR ILLSFILGFP WEDREDVFRT IKFARRLEPD
YVQFTVCTPY PGTPLYDLAK ERGLIEVHDW SKYTTVDPVM RTEHLSTREL GRLLQRAYLS
FYLNPRYLLN ALREGKLFLF KRIVKSGIRA VLSYLSR
//