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
//