ID C9R7S6_AMMDK Unreviewed; 360 AA.
AC C9R7S6;
DT 24-NOV-2009, integrated into UniProtKB/TrEMBL.
DT 24-NOV-2009, sequence version 1.
DT 27-MAR-2024, entry version 73.
DE SubName: Full=Radical SAM domain protein {ECO:0000313|EMBL:ACX52355.1};
GN OrderedLocusNames=Adeg_1244 {ECO:0000313|EMBL:ACX52355.1};
OS Ammonifex degensii (strain DSM 10501 / KC4).
OC Bacteria; Bacillota; Clostridia; Thermoanaerobacterales;
OC Thermoanaerobacteraceae; Ammonifex.
OX NCBI_TaxID=429009 {ECO:0000313|EMBL:ACX52355.1, ECO:0000313|Proteomes:UP000002620};
RN [1] {ECO:0000313|EMBL:ACX52355.1, ECO:0000313|Proteomes:UP000002620}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 10501 / KC4 {ECO:0000313|Proteomes:UP000002620};
RG US DOE Joint Genome Institute;
RA Kerfeld C., Goodner B., Huber H., Stetter K., Lucas S., Copeland A.,
RA Lapidus A., Glavina del Rio T., Dalin E., Tice H., Bruce D., Goodwin L.,
RA Pitluck S., Saunders E., Brettin T., Detter J.C., Han C., Larimer F.,
RA Land M., Hauser L., Kyrpides N., Ovchinnikova G., Richardson P.;
RT "Complete sequence of chromosome of Ammonifex degensii KC4.";
RL Submitted (OCT-2009) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=[2Fe-2S] cluster; Xref=ChEBI:CHEBI:190135;
CC Evidence={ECO:0000256|ARBA:ARBA00034078};
CC -!- COFACTOR:
CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC Evidence={ECO:0000256|ARBA:ARBA00001966};
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DR EMBL; CP001785; ACX52355.1; -; Genomic_DNA.
DR RefSeq; WP_015739232.1; NC_013385.1.
DR AlphaFoldDB; C9R7S6; -.
DR STRING; 429009.Adeg_1244; -.
DR KEGG; adg:Adeg_1244; -.
DR eggNOG; COG0502; Bacteria.
DR HOGENOM; CLU_033172_0_1_9; -.
DR OrthoDB; 9775764at2; -.
DR Proteomes; UP000002620; 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 GO; GO:0044271; P:cellular nitrogen compound biosynthetic process; IEA:UniProt.
DR GO; GO:0018130; P:heterocycle biosynthetic process; IEA:UniProt.
DR GO; GO:1901362; P:organic cyclic compound biosynthetic process; IEA:UniProt.
DR GO; GO:1901566; P:organonitrogen compound biosynthetic process; IEA:UniProt.
DR GO; GO:0044272; P:sulfur compound biosynthetic process; IEA:UniProt.
DR GO; GO:0042364; P:water-soluble vitamin biosynthetic process; IEA:UniProt.
DR CDD; cd01335; Radical_SAM; 1.
DR Gene3D; 3.20.20.70; Aldolase class I; 1.
DR InterPro; IPR013785; Aldolase_TIM.
DR InterPro; IPR010722; BATS_dom.
DR InterPro; IPR006638; Elp3/MiaA/NifB-like_rSAM.
DR InterPro; IPR024021; FeFe-hyd_HydE_rSAM.
DR InterPro; IPR034422; HydE/PylB-like.
DR InterPro; IPR007197; rSAM.
DR NCBIfam; TIGR03956; rSAM_HydE; 1.
DR PANTHER; PTHR43726; 3-METHYLORNITHINE SYNTHASE; 1.
DR PANTHER; PTHR43726:SF1; BIOTIN SYNTHASE; 1.
DR Pfam; PF04055; Radical_SAM; 1.
DR PIRSF; PIRSF004762; CHP00423; 1.
DR SFLD; SFLDG01082; B12-binding_domain_containing; 1.
DR SFLD; SFLDG01060; BATS_domain_containing; 1.
DR SFLD; SFLDF00348; FeFe_hydrogenase_maturase_(Hyd; 1.
DR SMART; SM00876; BATS; 1.
DR SMART; SM00729; Elp3; 1.
DR SUPFAM; SSF102114; Radical SAM enzymes; 1.
DR PROSITE; PS51918; RADICAL_SAM; 1.
PE 4: Predicted;
KW Iron {ECO:0000256|ARBA:ARBA00023004};
KW Iron-sulfur {ECO:0000256|ARBA:ARBA00023014};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000002620};
KW S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691}.
FT DOMAIN 53..272
FT /note="Radical SAM core"
FT /evidence="ECO:0000259|PROSITE:PS51918"
FT REGION 337..360
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 360 AA; 39814 MW; 8D024F1769EB0AC2 CRC64;
MEFCFTAEEL VKRSFSGPPF TREEILCLLR AGEEEAEVLF TAADRVRAKV FGPVVHLRAV
IEFSNFCRNN CLYCGLRREN RRLPRYRMAA REVVQAAEEA AAQGFKTVVL QSGEDPYWTP
ERLAEVVKEI KKLGVAVTLS VGELDYEDYA LLKEAGADRY LLRHETADPS LFAQLKPDSS
LARRRQCLEW LKELGYETGA GCMVGLPGQS LESLAEDVLF MRELQVEMAG IGPFIPHPDT
PLGKASSGSP FLTLKVLALT RLCLPYANLP ATTATGVAQK GGREAALLCG ANVVMPDVTP
YHYRLFYQLY PGKAQADPHP NAFAYWQERL RALGRTVGQD PGFSPRPQDA SAVADPDLLA
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