ID A5D3M6_PELTS Unreviewed; 359 AA.
AC A5D3M6;
DT 12-JUN-2007, integrated into UniProtKB/TrEMBL.
DT 12-JUN-2007, sequence version 1.
DT 27-MAR-2024, entry version 92.
DE SubName: Full=Biotin synthase and related enzymes {ECO:0000313|EMBL:BAF59164.1};
GN Name=BioB {ECO:0000313|EMBL:BAF59164.1};
GN OrderedLocusNames=PTH_0983 {ECO:0000313|EMBL:BAF59164.1};
OS Pelotomaculum thermopropionicum (strain DSM 13744 / JCM 10971 / SI).
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Desulfotomaculaceae;
OC Pelotomaculum.
OX NCBI_TaxID=370438 {ECO:0000313|EMBL:BAF59164.1, ECO:0000313|Proteomes:UP000006556};
RN [1] {ECO:0000313|Proteomes:UP000006556}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 13744 / JCM 10971 / SI {ECO:0000313|Proteomes:UP000006556};
RX PubMed=18218977; DOI=10.1101/gr.7136508;
RA Kosaka T., Kato S., Shimoyama T., Ishii S., Abe T., Watanabe K.;
RT "The genome of Pelotomaculum thermopropionicum reveals niche-associated
RT evolution in anaerobic microbiota.";
RL Genome Res. 18:442-448(2008).
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; AP009389; BAF59164.1; -; Genomic_DNA.
DR AlphaFoldDB; A5D3M6; -.
DR STRING; 370438.PTH_0983; -.
DR KEGG; pth:PTH_0983; -.
DR eggNOG; COG0502; Bacteria.
DR HOGENOM; CLU_033172_0_1_9; -.
DR Proteomes; UP000006556; 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; SFLDF00348; FeFe_hydrogenase_maturase_(Hyd; 1.
DR SFLD; SFLDG01280; HydE/PylB-like; 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:UP000006556};
KW S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691}.
FT DOMAIN 51..278
FT /note="Radical SAM core"
FT /evidence="ECO:0000259|PROSITE:PS51918"
SQ SEQUENCE 359 AA; 39361 MW; 884D5EB15716BD97 CRC64;
MRTDFVRALE RAANLEELSR DELAVLISAD EEESAALFDC ADMMRSRFMG DEVHLRGIIE
FSNICSSNCY YCGLRKGNTA LKRYRMSKAE ILESARKAAV LGCRTIVLQS GEDRSYPAGL
LAEIVAEIKS ELDVAITLSV GERPREDYAL WREAGADRYL LKHETCDGKL FSELRPGTVL
EERLQRLAWL RELGYQVGSG NMVGLPGQTV ETLAGDIVLM REMEVEMAGI GPFVPNRQTP
LGSCPGGTLE LTLKTLAAAR LALPRTHLPA TTATATIDAL GRVKALRCGA NVIMPNMTPL
KYRASYSIYP GKTGLEDTPE ESYAKAVRMV ESAGRKVGTG YGHSLRHLEK KAEAQAQAV
//
