ID   CMO_PYRFU               Reviewed;         356 AA.
AC   Q51741;
DT   15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT   03-APR-2002, sequence version 2.
DT   03-AUG-2022, entry version 114.
DE   RecName: Full=Tungsten-containing aldehyde ferredoxin oxidoreductase cofactor-modifying protein;
GN   Name=cmo; OrderedLocusNames=PF0344;
OS   Pyrococcus furiosus (strain ATCC 43587 / DSM 3638 / JCM 8422 / Vc1).
OC   Archaea; Euryarchaeota; Thermococci; Thermococcales; Thermococcaceae;
OC   Pyrococcus.
OX   NCBI_TaxID=186497;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 43587 / DSM 3638 / JCM 8422 / Vc1;
RX   PubMed=7642512; DOI=10.1128/jb.177.16.4817-4819.1995;
RA   Kletzin A., Mukund S., Kelley-Crouse T.L., Chan M.K.S., Rees D.C.,
RA   Adams M.W.W.;
RT   "Molecular characterization of the genes encoding the tungsten-containing
RT   aldehyde ferredoxin oxidoreductase from Pyrococcus furiosus and
RT   formaldehyde ferredoxin oxidoreductase from Thermococcus litoralis.";
RL   J. Bacteriol. 177:4817-4819(1995).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 43587 / DSM 3638 / JCM 8422 / Vc1;
RX   PubMed=10430560; DOI=10.1093/genetics/152.4.1299;
RA   Maeder D.L., Weiss R.B., Dunn D.M., Cherry J.L., Gonzalez J.M.,
RA   DiRuggiero J., Robb F.T.;
RT   "Divergence of the hyperthermophilic archaea Pyrococcus furiosus and P.
RT   horikoshii inferred from complete genomic sequences.";
RL   Genetics 152:1299-1305(1999).
CC   -!- FUNCTION: Involved in the biosynthesis of a molybdopterin-based
CC       tungsten cofactor.
CC   -!- COFACTOR:
CC       Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883; Evidence={ECO:0000250};
CC       Note=Binds 1 [4Fe-4S] cluster. The cluster is coordinated with 3
CC       cysteines and an exchangeable S-adenosyl-L-methionine. {ECO:0000250};
CC   -!- SIMILARITY: Belongs to the radical SAM superfamily. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAL80468.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; X79777; CAA56172.1; -; Genomic_DNA.
DR   EMBL; AE009950; AAL80468.1; ALT_INIT; Genomic_DNA.
DR   AlphaFoldDB; Q51741; -.
DR   SMR; Q51741; -.
DR   STRING; 186497.PF0344; -.
DR   EnsemblBacteria; AAL80468; AAL80468; PF0344.
DR   KEGG; pfu:PF0344; -.
DR   PATRIC; fig|186497.12.peg.358; -.
DR   eggNOG; arCOG00938; Archaea.
DR   HOGENOM; CLU_009273_1_1_2; -.
DR   OMA; MCFKQYW; -.
DR   PhylomeDB; Q51741; -.
DR   Proteomes; UP000001013; Chromosome.
DR   GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW.
DR   GO; GO:0003824; F:catalytic activity; IEA:InterPro.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   Gene3D; 3.20.20.70; -; 1.
DR   InterPro; IPR023885; 4Fe4S-binding_SPASM_dom.
DR   InterPro; IPR013785; Aldolase_TIM.
DR   InterPro; IPR034391; Cmo-like_SPASM_containing.
DR   InterPro; IPR006638; Elp3/MiaB/NifB.
DR   InterPro; IPR000385; MoaA_NifB_PqqE_Fe-S-bd_CS.
DR   InterPro; IPR017200; PqqE-like.
DR   InterPro; IPR007197; rSAM.
DR   InterPro; IPR027604; W_rSAM_matur.
DR   Pfam; PF04055; Radical_SAM; 1.
DR   Pfam; PF13186; SPASM; 1.
DR   PIRSF; PIRSF037420; PQQ_syn_pqqE; 1.
DR   SFLD; SFLDG01387; BtrN-like_SPASM_domain_contain; 1.
DR   SFLD; SFLDF00570; tungsten_cofactor_oxidoreducas; 1.
DR   SMART; SM00729; Elp3; 1.
DR   TIGRFAMs; TIGR04317; W_rSAM_matur; 1.
DR   PROSITE; PS01305; MOAA_NIFB_PQQE; 1.
DR   PROSITE; PS51918; RADICAL_SAM; 1.
PE   3: Inferred from homology;
KW   4Fe-4S; Iron; Iron-sulfur; Metal-binding; Reference proteome;
KW   S-adenosyl-L-methionine; Tungsten.
FT   CHAIN           1..356
FT                   /note="Tungsten-containing aldehyde ferredoxin
FT                   oxidoreductase cofactor-modifying protein"
FT                   /id="PRO_0000153048"
FT   DOMAIN          1..214
FT                   /note="Radical SAM core"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01266"
FT   BINDING         12
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /ligand_note="4Fe-4S-S-AdoMet"
FT                   /evidence="ECO:0000250"
FT   BINDING         16
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /ligand_note="4Fe-4S-S-AdoMet"
FT                   /evidence="ECO:0000250"
FT   BINDING         19
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /ligand_note="4Fe-4S-S-AdoMet"
FT                   /evidence="ECO:0000250"
FT   CONFLICT        41..56
FT                   /note="DDAEKFPELKMIYFGG -> RRCREVSRAKDDILRRS (in Ref. 1;
FT                   CAA56172)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   356 AA;  41381 MW;  3E863DC559FC6F62 CRC64;
     MKYLYLEITS RCNLRCEMCF KQHWEDEEGD MDYDLFLKIL DDAEKFPELK MIYFGGIGEP
     TVHPRFMDMV REVKKRGFAL GISTNGTLLT DEMLKELAEL GVDLVYFSMD VLPTAQNVVT
     LGHILAGVTA EKIKKLVKYR EEVGTHKPSI GVEVVVTKEN YKQLPELARY LLNLGVDAML
     VSNLLPLTPE QVNDIVYDGS IDMTPIVNEL YKIAHNGLYI KLPYFELKTE RVCDFDENKV
     AVIRWDGEVV PCYRFLHTYR EYIFGREKKV NTYSFGNVRE KSLADIWTSE RYTWFRFITK
     NYLYPSCTDC SLRDACDFVK TTDIDCWGNE PSCADCLWSR RIVMCPIPQY NFGKFL