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Database: UniProt
Entry: A1ASV3_PELPD
LinkDB: A1ASV3_PELPD
Original site: A1ASV3_PELPD 
ID   A1ASV3_PELPD            Unreviewed;       476 AA.
AC   A1ASV3;
DT   23-JAN-2007, integrated into UniProtKB/TrEMBL.
DT   23-JAN-2007, sequence version 1.
DT   27-MAR-2024, entry version 89.
DE   SubName: Full=Radical SAM domain protein {ECO:0000313|EMBL:ABL00424.1};
GN   OrderedLocusNames=Ppro_2825 {ECO:0000313|EMBL:ABL00424.1};
OS   Pelobacter propionicus (strain DSM 2379 / NBRC 103807 / OttBd1).
OC   Bacteria; Thermodesulfobacteriota; Desulfuromonadia; Desulfuromonadales;
OC   Desulfuromonadaceae; Pelobacter.
OX   NCBI_TaxID=338966 {ECO:0000313|EMBL:ABL00424.1, ECO:0000313|Proteomes:UP000006732};
RN   [1] {ECO:0000313|EMBL:ABL00424.1, ECO:0000313|Proteomes:UP000006732}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 2379 / NBRC 103807 / OttBd1
RC   {ECO:0000313|Proteomes:UP000006732};
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA   Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA   Saunders E., Brettin T., Bruce D., Han C., Tapia R., Schmutz J.,
RA   Larimer F., Land M., Hauser L., Kyrpides N., Kim E., Lovley D.,
RA   Richardson P.;
RT   "Complete sequence of chromosome of Pelobacter propionicus DSM 2379.";
RL   Submitted (OCT-2006) to the EMBL/GenBank/DDBJ databases.
CC   -!- COFACTOR:
CC       Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC         Evidence={ECO:0000256|ARBA:ARBA00001966};
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DR   EMBL; CP000482; ABL00424.1; -; Genomic_DNA.
DR   RefSeq; WP_011736665.1; NC_008609.1.
DR   AlphaFoldDB; A1ASV3; -.
DR   STRING; 338966.Ppro_2825; -.
DR   KEGG; ppd:Ppro_2825; -.
DR   eggNOG; COG1032; Bacteria.
DR   HOGENOM; CLU_021572_4_2_7; -.
DR   OrthoDB; 9762608at2; -.
DR   Proteomes; UP000006732; Chromosome.
DR   GO; GO:0003824; F:catalytic activity; IEA:InterPro.
DR   GO; GO:0031419; F:cobalamin binding; IEA:InterPro.
DR   GO; GO:0051536; F:iron-sulfur cluster binding; IEA:InterPro.
DR   GO; GO:0046872; F:metal ion binding; IEA:InterPro.
DR   CDD; cd01335; Radical_SAM; 1.
DR   Gene3D; 3.40.50.280; Cobalamin-binding domain; 1.
DR   Gene3D; 3.80.30.20; tm_1862 like domain; 1.
DR   InterPro; IPR006158; Cobalamin-bd.
DR   InterPro; IPR006638; Elp3/MiaA/NifB-like_rSAM.
DR   InterPro; IPR017834; Hopanoid_synth-assoc_rSAM_HpnJ.
DR   InterPro; IPR034466; Methyltransferase_Class_B.
DR   InterPro; IPR007197; rSAM.
DR   InterPro; IPR023404; rSAM_horseshoe.
DR   NCBIfam; TIGR03471; HpnJ; 1.
DR   PANTHER; PTHR43409; ANAEROBIC MAGNESIUM-PROTOPORPHYRIN IX MONOMETHYL ESTER CYCLASE-RELATED; 1.
DR   PANTHER; PTHR43409:SF16; RADICAL SAM DOMAIN PROTEIN; 1.
DR   Pfam; PF02310; B12-binding; 1.
DR   Pfam; PF04055; Radical_SAM; 1.
DR   SFLD; SFLDF00404; hopanetetrol_cyclitol_ether_sy; 1.
DR   SFLD; SFLDG01123; methyltransferase_(Class_B); 1.
DR   SFLD; SFLDS00029; Radical_SAM; 1.
DR   SMART; SM00729; Elp3; 1.
DR   SUPFAM; SSF102114; Radical SAM enzymes; 1.
DR   PROSITE; PS51918; RADICAL_SAM; 1.
PE   4: Predicted;
KW   4Fe-4S {ECO:0000256|ARBA:ARBA00022485};
KW   Iron {ECO:0000256|ARBA:ARBA00022485};
KW   Iron-sulfur {ECO:0000256|ARBA:ARBA00022485};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022485};
KW   Reference proteome {ECO:0000313|Proteomes:UP000006732}.
FT   DOMAIN          192..412
FT                   /note="Radical SAM core"
FT                   /evidence="ECO:0000259|PROSITE:PS51918"
SQ   SEQUENCE   476 AA;  54620 MW;  324F35CC97B7F01E CRC64;
     MKPLFLNPPT FDDFDGGAGA RYQASREVTS FWYPTWLCFP AAMIEGSRVV DAPVQKFDLE
     KCLEIARDFD MVVMYTSTPT LMIDIATARR IKEVKPDVIT VLTGPHVTIL PEESLRAGKG
     AIDIVCRGEF DYSTKELCEG RPWDRVDGIS FLRDGKAVHT PDRPMIEDLD ALPFVAPVYR
     RDLPISEYVI PHFKNPYVSI YSSRGCPSKC IYCLWPQTFS GQRMRTRSAR NVYEEIKWIT
     ENIPEMRELS FDDDTFTANR EHAREVARLI KPLGISWTIN ARANTDYETL RVMRECGLRH
     VVVGFESGNA QILKNIKKGV SKEQAIQFVK DCKKLGLSIH GAFIMGLPGE TRETIAETIN
     YAKQLDLNSI QASLASPYPG TEFYTMCKEQ GWIASDNFLD DSGHQKCVIN YPHLSNAEIF
     NSVEEFYDKF YFRPKYILRS IGKMIVDGEE RRKLLKEGKQ YLQYMRKRKE SRCDCK
//
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