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Database: UniProt
Entry: U5VNR8_9ACTN
LinkDB: U5VNR8_9ACTN
Original site: U5VNR8_9ACTN 
ID   U5VNR8_9ACTN            Unreviewed;       367 AA.
AC   U5VNR8;
DT   22-JAN-2014, integrated into UniProtKB/TrEMBL.
DT   22-JAN-2014, sequence version 1.
DT   27-MAR-2024, entry version 46.
DE   RecName: Full=Radical SAM core domain-containing protein {ECO:0000259|PROSITE:PS51918};
GN   ORFNames=AFR_00750 {ECO:0000313|EMBL:AGZ38439.1};
OS   Actinoplanes friuliensis DSM 7358.
OC   Bacteria; Actinomycetota; Actinomycetes; Micromonosporales;
OC   Micromonosporaceae; Actinoplanes.
OX   NCBI_TaxID=1246995 {ECO:0000313|EMBL:AGZ38439.1, ECO:0000313|Proteomes:UP000017746};
RN   [1] {ECO:0000313|EMBL:AGZ38439.1, ECO:0000313|Proteomes:UP000017746}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 7358 {ECO:0000313|EMBL:AGZ38439.1,
RC   ECO:0000313|Proteomes:UP000017746};
RX   PubMed=24637369; DOI=10.1016/j.jbiotec.2014.03.011;
RA   Ruckert C., Szczepanowski R., Albersmeier A., Goesmann A., Fischer N.,
RA   Steinkamper A., Puhler A., Biener R., Schwartz D., Kalinowski J.;
RT   "Complete genome sequence of the actinobacterium Actinoplanes friuliensis
RT   HAG 010964, producer of the lipopeptide antibiotic friulimycin.";
RL   J. Biotechnol. 178:41-42(2014).
CC   -!- SIMILARITY: Belongs to the radical SAM superfamily. Anaerobic
CC       sulfatase-maturating enzyme family. {ECO:0000256|ARBA:ARBA00023601}.
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DR   EMBL; CP006272; AGZ38439.1; -; Genomic_DNA.
DR   RefSeq; WP_023357383.1; NC_022657.1.
DR   AlphaFoldDB; U5VNR8; -.
DR   STRING; 1246995.AFR_00750; -.
DR   KEGG; afs:AFR_00750; -.
DR   PATRIC; fig|1246995.3.peg.151; -.
DR   eggNOG; COG0641; Bacteria.
DR   HOGENOM; CLU_009273_10_0_11; -.
DR   OrthoDB; 9782387at2; -.
DR   Proteomes; UP000017746; Chromosome.
DR   GO; GO:0051536; F:iron-sulfur cluster binding; IEA:UniProtKB-KW.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0016491; F:oxidoreductase activity; IEA:InterPro.
DR   CDD; cd01335; Radical_SAM; 1.
DR   Gene3D; 3.20.20.70; Aldolase class I; 1.
DR   InterPro; IPR013785; Aldolase_TIM.
DR   InterPro; IPR007197; rSAM.
DR   InterPro; IPR023867; Sulphatase_maturase_rSAM.
DR   NCBIfam; NF041718; rSAM_phane_AMC; 1.
DR   PANTHER; PTHR43273; ANAEROBIC SULFATASE-MATURATING ENZYME HOMOLOG ASLB-RELATED; 1.
DR   PANTHER; PTHR43273:SF8; RADICAL SAM PROTEIN-RELATED; 1.
DR   Pfam; PF04055; Radical_SAM; 1.
DR   SFLD; SFLDG01072; dehydrogenase_like; 1.
DR   SFLD; SFLDS00029; Radical_SAM; 1.
DR   SUPFAM; SSF102114; Radical SAM enzymes; 1.
DR   PROSITE; PS51918; RADICAL_SAM; 1.
PE   3: Inferred from homology;
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:UP000017746};
KW   S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691}.
FT   DOMAIN          5..230
FT                   /note="Radical SAM core"
FT                   /evidence="ECO:0000259|PROSITE:PS51918"
SQ   SEQUENCE   367 AA;  40888 MW;  3BBBE39085B06C88 CRC64;
     MRGISTTPTY VVMQPTTLCN LDCSYCYLPF RQVDRKMSVE VARAVAASVN PWSRTGRFSV
     VWHGGEPLAA GRDHFAALLE PFADDVEHHV QTNATLIDDA WCKFFTERQI RVSVSVDGPE
     ARNGDRVTRG DKPAYARIMR GVEALHRHGI PFSALCVVGN PEPGLATELY AYFLELGCDV
     LGINVEELEG VNKRDNRHPA AEVTAFWAEL VGAWRQDPRI HLREVEWSLR YAAAVLDGTA
     DQVLPRRLDP IPTVAEDGSV VLLSPELAGF HDPRYGDFSS GNVLTTPLGE ILERATETPW
     IREFLDGVEA CRARCPYFGF CGGAHAANRY FEQGRFDVTE TDHCRNSKIR LLEGVLDHAR
     DHEPTAV
//
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