ID Q8R8V5_CALS4 Unreviewed; 353 AA.
AC Q8R8V5;
DT 01-JUN-2002, integrated into UniProtKB/TrEMBL.
DT 01-JUN-2002, sequence version 1.
DT 27-MAR-2024, entry version 112.
DE SubName: Full=Biotin synthase and related enzymes {ECO:0000313|EMBL:AAM25069.1};
GN Name=BioB2 {ECO:0000313|EMBL:AAM25069.1};
GN OrderedLocusNames=TTE1885 {ECO:0000313|EMBL:AAM25069.1};
OS Caldanaerobacter subterraneus subsp. tengcongensis (strain DSM 15242 / JCM
OS 11007 / NBRC 100824 / MB4) (Thermoanaerobacter tengcongensis).
OC Bacteria; Bacillota; Clostridia; Thermoanaerobacterales;
OC Thermoanaerobacteraceae; Caldanaerobacter.
OX NCBI_TaxID=273068 {ECO:0000313|EMBL:AAM25069.1, ECO:0000313|Proteomes:UP000000555};
RN [1] {ECO:0000313|EMBL:AAM25069.1, ECO:0000313|Proteomes:UP000000555}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 15242 / JCM 11007 / NBRC 100824 / MB4
RC {ECO:0000313|Proteomes:UP000000555};
RX PubMed=11997336; DOI=10.1101/gr.219302;
RA Bao Q., Tian Y., Li W., Xu Z., Xuan Z., Hu S., Dong W., Yang J., Chen Y.,
RA Xue Y., Xu Y., Lai X., Huang L., Dong X., Ma Y., Ling L., Tan H., Chen R.,
RA Wang J., Yu J., Yang H.;
RT "A complete sequence of the T. tengcongensis genome.";
RL Genome Res. 12:689-700(2002).
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; AE008691; AAM25069.1; -; Genomic_DNA.
DR RefSeq; WP_011026045.1; NZ_JANUCV010000001.1.
DR AlphaFoldDB; Q8R8V5; -.
DR STRING; 273068.TTE1885; -.
DR KEGG; tte:TTE1885; -.
DR eggNOG; COG0502; Bacteria.
DR HOGENOM; CLU_033172_0_1_9; -.
DR OrthoDB; 9775764at2; -.
DR Proteomes; UP000000555; 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; SFLDS00029; Radical_SAM; 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:UP000000555};
KW S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691}.
FT DOMAIN 55..274
FT /note="Radical SAM core"
FT /evidence="ECO:0000259|PROSITE:PS51918"
SQ SEQUENCE 353 AA; 40112 MW; CA9D7DD0A8C03811 CRC64;
MIKELTAEKN ISSLIEKLEK QHSLDKKGLI MLLSMENPSE LYKAADRVRK KYVGDEVHLR
GLIEFSNYCH NTCFYCGLRG PNKAIKRYRM EPEEIIECAK RGVEMELKTI VLQSGEDRYY
KITTLCNIVE KIKEMDVAVT LIIGELSKKE YAELKKAGAD RYLLRIETTN RELYRKLHPG
MSYENRLRCL MDLRELGYEV GTGSLIGLPG QTLEMLADDL LFFKKINADM LGIGPFIPCE
NTPLEKEKGG DVNLVLKMIA LSRLLLPDIN IPATTALAVK DKDGYAKGLQ CGANVIMPNI
GIEEYKRLYK LYPGKVPDDP NEAVNSIENI KKVILSQNRS IGKDKGYRKK VFH
//