ID K4LLH0_THEPS Unreviewed; 381 AA.
AC K4LLH0;
DT 09-JAN-2013, integrated into UniProtKB/TrEMBL.
DT 09-JAN-2013, sequence version 1.
DT 27-MAR-2024, entry version 49.
DE SubName: Full=Biotin synthase {ECO:0000313|EMBL:AFV12942.1};
DE EC=2.8.1.6 {ECO:0000313|EMBL:AFV12942.1};
GN OrderedLocusNames=Tph_c27770 {ECO:0000313|EMBL:AFV12942.1};
OS Thermacetogenium phaeum (strain ATCC BAA-254 / DSM 26808 / PB).
OC Bacteria; Bacillota; Clostridia; Thermoanaerobacterales;
OC Thermoanaerobacteraceae; Thermacetogenium.
OX NCBI_TaxID=1089553 {ECO:0000313|EMBL:AFV12942.1, ECO:0000313|Proteomes:UP000000467};
RN [1] {ECO:0000313|EMBL:AFV12942.1, ECO:0000313|Proteomes:UP000000467}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-254 / DSM 26808 / PB
RC {ECO:0000313|Proteomes:UP000000467};
RX PubMed=23259483; DOI=10.1186/1471-2164-13-723;
RA Oehler D., Poehlein A., Leimbach A., Muller N., Daniel R., Gottschalk G.,
RA Schink B.;
RT "Genome-guided analysis of physiological and morphological traits of the
RT fermentative acetate oxidizer Thermacetogenium phaeum.";
RL BMC Genomics 13:723-723(2012).
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CP003732; AFV12942.1; -; Genomic_DNA.
DR AlphaFoldDB; K4LLH0; -.
DR STRING; 1089553.Tph_c27770; -.
DR KEGG; tpz:Tph_c27770; -.
DR eggNOG; COG0502; Bacteria.
DR HOGENOM; CLU_033172_0_0_9; -.
DR Proteomes; UP000000467; Chromosome.
DR GO; GO:0004076; F:biotin synthase activity; IEA:UniProtKB-EC.
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:0071524; P:pyrrolysine biosynthetic process; 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; IPR006638; Elp3/MiaA/NifB-like_rSAM.
DR InterPro; IPR034422; HydE/PylB-like.
DR InterPro; IPR023891; Pyrrolys_PylB.
DR InterPro; IPR007197; rSAM.
DR NCBIfam; TIGR03910; pyrrolys_PylB; 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; SFLDF00349; 3-methylornithine_synthase_(Py; 1.
DR SFLD; SFLDG01060; BATS_domain_containing; 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:UP000000467};
KW S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691};
KW Transferase {ECO:0000313|EMBL:AFV12942.1}.
FT DOMAIN 59..285
FT /note="Radical SAM core"
FT /evidence="ECO:0000259|PROSITE:PS51918"
SQ SEQUENCE 381 AA; 42698 MW; C589772B9AF44C81 CRC64;
MAALRNQSEH RLEGILEKAG LLQELTDREA AFLLGLQSRD DLDKLFRTAR SLRERFFGNK
IFLYGFIYLS TWCRNNCTFC YYRKSNSKSV RYRKTAEEVL DAAARLAASG VHLIDLTLGE
DPYFHNRKEG FQPLIALVHQ VKKRTGLPVM ISPGVVPGRI LQDFATAGAD WYACYQETHN
ERLFAELRLE QSYQQRLASK EEALRCGLLV EEGILTGIGD TESDIMLSLQ GMRQLQAQQV
RVMSFVPQQG TPLADRETPA RIRELKIIAV MRILFPDRLI PASLDVDGVA GLRDRINAGA
NVVTSIIPPL MGLAGVAQCR RDIDEGNRTV AGVLPFLEEM GLTAATAEEY LSWVEKEKAK
LIRLHGTCLS GSNPFSEISH Q
//
