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Database: UniProt
Entry: Q1D120_MYXXD
LinkDB: Q1D120_MYXXD
Original site: Q1D120_MYXXD 
ID   Q1D120_MYXXD            Unreviewed;       671 AA.
AC   Q1D120;
DT   11-JUL-2006, integrated into UniProtKB/TrEMBL.
DT   11-JUL-2006, sequence version 1.
DT   27-MAR-2024, entry version 111.
DE   SubName: Full=Radical SAM domain protein {ECO:0000313|EMBL:ABF91812.1};
GN   OrderedLocusNames=MXAN_5510 {ECO:0000313|EMBL:ABF91812.1};
OS   Myxococcus xanthus (strain DK1622).
OC   Bacteria; Myxococcota; Myxococcia; Myxococcales; Cystobacterineae;
OC   Myxococcaceae; Myxococcus.
OX   NCBI_TaxID=246197 {ECO:0000313|EMBL:ABF91812.1, ECO:0000313|Proteomes:UP000002402};
RN   [1] {ECO:0000313|EMBL:ABF91812.1, ECO:0000313|Proteomes:UP000002402}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DK1622 {ECO:0000313|Proteomes:UP000002402};
RX   PubMed=17015832; DOI=10.1073/pnas.0607335103;
RA   Goldman B.S., Nierman W.C., Kaiser D., Slater S.C., Durkin A.S.,
RA   Eisen J.A., Ronning C.M., Barbazuk W.B., Blanchard M., Field C.,
RA   Halling C., Hinkle G., Iartchuk O., Kim H.S., Mackenzie C., Madupu R.,
RA   Miller N., Shvartsbeyn A., Sullivan S.A., Vaudin M., Wiegand R.,
RA   Kaplan H.B.;
RT   "Evolution of sensory complexity recorded in a myxobacterial genome.";
RL   Proc. Natl. Acad. Sci. U.S.A. 103:15200-15205(2006).
CC   -!- COFACTOR:
CC       Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC         Evidence={ECO:0000256|HAMAP-Rule:MF_01251};
CC       Note=Binds 1 [4Fe-4S] cluster. The cluster is coordinated with 3
CC       cysteines and an exchangeable S-adenosyl-L-methionine.
CC       {ECO:0000256|HAMAP-Rule:MF_01251};
CC   -!- SIMILARITY: Belongs to the UPF0313 family. {ECO:0000256|HAMAP-
CC       Rule:MF_01251}.
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DR   EMBL; CP000113; ABF91812.1; -; Genomic_DNA.
DR   RefSeq; WP_011555468.1; NC_008095.1.
DR   AlphaFoldDB; Q1D120; -.
DR   STRING; 246197.MXAN_5510; -.
DR   EnsemblBacteria; ABF91812; ABF91812; MXAN_5510.
DR   GeneID; 41362764; -.
DR   KEGG; mxa:MXAN_5510; -.
DR   eggNOG; COG1032; Bacteria.
DR   HOGENOM; CLU_018288_2_0_7; -.
DR   OrthoDB; 9803479at2; -.
DR   Proteomes; UP000002402; 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:0005506; F:iron ion binding; IEA:UniProtKB-UniRule.
DR   Gene3D; 3.80.30.20; tm_1862 like domain; 1.
DR   HAMAP; MF_01251; UPF0313; 1.
DR   InterPro; IPR006638; Elp3/MiaA/NifB-like_rSAM.
DR   InterPro; IPR020612; Methylthiotransferase_CS.
DR   InterPro; IPR007197; rSAM.
DR   InterPro; IPR023404; rSAM_horseshoe.
DR   InterPro; IPR022946; UPF0313.
DR   InterPro; IPR024560; UPF0313_C.
DR   InterPro; IPR013704; UPF0313_N.
DR   NCBIfam; TIGR03904; SAM_YgiQ; 1.
DR   PANTHER; PTHR32331; UPF0313 PROTEIN YGIQ; 1.
DR   PANTHER; PTHR32331:SF0; UPF0313 PROTEIN YGIQ; 1.
DR   Pfam; PF11842; DUF3362; 1.
DR   Pfam; PF04055; Radical_SAM; 1.
DR   Pfam; PF08497; Radical_SAM_N; 1.
DR   SFLD; SFLDG01082; B12-binding_domain_containing; 1.
DR   SFLD; SFLDS00029; Radical_SAM; 1.
DR   SFLD; SFLDG01069; UPF0313; 1.
DR   SMART; SM00729; Elp3; 1.
DR   SUPFAM; SSF102114; Radical SAM enzymes; 1.
DR   PROSITE; PS01278; MTTASE_RADICAL; 1.
DR   PROSITE; PS51918; RADICAL_SAM; 1.
PE   3: Inferred from homology;
KW   4Fe-4S {ECO:0000256|ARBA:ARBA00022485, ECO:0000256|HAMAP-Rule:MF_01251};
KW   Iron {ECO:0000256|ARBA:ARBA00023004, ECO:0000256|HAMAP-Rule:MF_01251};
KW   Iron-sulfur {ECO:0000256|ARBA:ARBA00023014, ECO:0000256|HAMAP-
KW   Rule:MF_01251};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|HAMAP-
KW   Rule:MF_01251}; Reference proteome {ECO:0000313|Proteomes:UP000002402};
KW   S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691, ECO:0000256|HAMAP-
KW   Rule:MF_01251}.
FT   DOMAIN          321..592
FT                   /note="Radical SAM core"
FT                   /evidence="ECO:0000259|PROSITE:PS51918"
FT   REGION          613..671
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        627..641
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         335
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /ligand_note="4Fe-4S-S-AdoMet"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01251"
FT   BINDING         339
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /ligand_note="4Fe-4S-S-AdoMet"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01251"
FT   BINDING         342
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /ligand_note="4Fe-4S-S-AdoMet"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01251"
SQ   SEQUENCE   671 AA;  75234 MW;  260B62C8541B9827 CRC64;
     MAHSTRYAHP FLPTTRADMQ ARGWEQCDII IVTGDAYVDH PAFGPVLIAR FLEGRGFKVG
     LLPQPDWHSA EPFKALGPPR LFFGVAAGNL DSMLNRLTAQ KKNRSEDQYS PGGQTNCRPD
     RATIVYAQRC REAYPDVPII LGGIEASLRR IAHFDYWSEK VRRSILFDAK ADLLVFGMGE
     RPIMEVADRM RQGERIQDIR DVRGTAYTIN DEEMRALEAD PARRAADRKT VVLPSYEQVI
     EDKHAFAVMS RDFQMETNPG NARPLAQRHG NRAIYMNSPA LPLEDGVGTA GAEGKSVAMD
     ELYDLPFNRV PHPMYRERIP AYETVKHSIV LMRGCFGGCT FCSITEHEGR VIQSRSAESV
     LREVRALRRM GDFRGTITDL GGPTANMYKL KCKSEDIEKR CRKLSCVHPG VCENLQTDHG
     PLISLMQDVR KEDGVKHVFI ASGVRYDLAE RSPEYVKELA AHHVGGQLSV APEHVSPRVL
     EKMKKPGIES FERFQQMFAC ASEEAGKEQY DIPYFISGHP GSTLEDMVEL ALWLKQNGKR
     PRQVQDFIPT PMAMATAMYF TGLDPLKMEP VYTAQGLREK RLQKALLLYW NPEQWPLARE
     ALKLAGREDL IGRGPHALVP PESPGEAARR QRTERDTGAG ASAPRHEAAP RLGPHGTARP
     RARRPGGPRA R
//
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