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Biotin synthase (EC 2.8.1.6)

 F8L018_PARAV            Unreviewed;       333 AA.
F8L018;
21-SEP-2011, integrated into UniProtKB/TrEMBL.
21-SEP-2011, sequence version 1.
28-FEB-2018, entry version 53.
RecName: Full=Biotin synthase {ECO:0000256|HAMAP-Rule:MF_01694, ECO:0000256|SAAS:SAAS00833216};
EC=2.8.1.6 {ECO:0000256|HAMAP-Rule:MF_01694, ECO:0000256|SAAS:SAAS00391055};
Name=biO2 {ECO:0000313|EMBL:CCB86533.1};
Synonyms=bioB {ECO:0000256|HAMAP-Rule:MF_01694};
OrderedLocusNames=PUV_15830 {ECO:0000313|EMBL:CCB86533.1};
Parachlamydia acanthamoebae (strain UV7).
Bacteria; Chlamydiae; Parachlamydiales; Parachlamydiaceae;
Parachlamydia.
NCBI_TaxID=765952 {ECO:0000313|EMBL:CCB86533.1, ECO:0000313|Proteomes:UP000000495};
[1] {ECO:0000313|EMBL:CCB86533.1, ECO:0000313|Proteomes:UP000000495}
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=UV7 {ECO:0000313|Proteomes:UP000000495};
PubMed=21690563; DOI=10.1093/molbev/msr161;
Collingro A., Tischler P., Weinmaier T., Penz T., Heinz E.,
Brunham R.C., Read T.D., Bavoil P.M., Sachse K., Kahane S.,
Friedman M.G., Rattei T., Myers G.S., Horn M.;
"Unity in variety--the pan-genome of the chlamydiae.";
Mol. Biol. Evol. 28:3253-3270(2011).
-!- FUNCTION: Catalyzes the conversion of dethiobiotin (DTB) to biotin
by the insertion of a sulfur atom into dethiobiotin via a radical-
based mechanism. {ECO:0000256|HAMAP-Rule:MF_01694,
ECO:0000256|SAAS:SAAS00833214}.
-!- CATALYTIC ACTIVITY: Dethiobiotin + sulfur-(sulfur carrier) + 2 S-
adenosyl-L-methionine + 2 reduced [2Fe-2S] ferredoxin = biotin +
(sulfur carrier) + 2 L-methionine + 2 5'-deoxyadenosine + 2
oxidized [2Fe-2S] ferredoxin. {ECO:0000256|HAMAP-Rule:MF_01694,
ECO:0000256|SAAS:SAAS00190209}.
-!- PATHWAY: Cofactor biosynthesis; biotin biosynthesis; biotin from
7,8-diaminononanoate: step 2/2. {ECO:0000256|HAMAP-Rule:MF_01694,
ECO:0000256|SAAS:SAAS00370166}.
-!- SUBUNIT: Homodimer. {ECO:0000256|HAMAP-Rule:MF_01694,
ECO:0000256|SAAS:SAAS00063319}.
-!- SIMILARITY: Belongs to the radical SAM superfamily. Biotin
synthase family. {ECO:0000256|HAMAP-Rule:MF_01694,
ECO:0000256|SAAS:SAAS00577385}.
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EMBL; FR872580; CCB86533.1; -; Genomic_DNA.
RefSeq; WP_013925054.1; NC_015702.1.
ProteinModelPortal; F8L018; -.
STRING; 765952.PUV_15830; -.
EnsemblBacteria; CCB86533; CCB86533; PUV_15830.
KEGG; puv:PUV_15830; -.
eggNOG; ENOG4107QSQ; Bacteria.
eggNOG; COG0502; LUCA.
KO; K01012; -.
OMA; ADRFCMG; -.
OrthoDB; POG091H01DF; -.
BioCyc; PACA765952:G1H3Q-1548-MONOMER; -.
UniPathway; UPA00078; UER00162.
Proteomes; UP000000495; Chromosome.
GO; GO:0051537; F:2 iron, 2 sulfur cluster binding; IEA:UniProtKB-KW.
GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW.
GO; GO:0004076; F:biotin synthase activity; IEA:UniProtKB-UniRule.
GO; GO:0005506; F:iron ion binding; IEA:UniProtKB-UniRule.
GO; GO:0009102; P:biotin biosynthetic process; IEA:UniProtKB-UniRule.
Gene3D; 3.20.20.70; -; 1.
HAMAP; MF_01694; BioB; 1.
InterPro; IPR013785; Aldolase_TIM.
InterPro; IPR010722; BATS_dom.
InterPro; IPR034416; BATS_domain_containing.
InterPro; IPR002684; Biotin_synth/BioAB.
InterPro; IPR024177; Biotin_synthase.
InterPro; IPR006638; Elp3/MiaB/NifB.
InterPro; IPR007197; rSAM.
PANTHER; PTHR22976; PTHR22976; 1.
Pfam; PF06968; BATS; 1.
Pfam; PF04055; Radical_SAM; 1.
PIRSF; PIRSF001619; Biotin_synth; 1.
SFLD; SFLDF00272; biotin_synthase; 1.
SFLD; SFLDG01060; BATS_domain_containing; 1.
SFLD; SFLDG01278; biotin_synthase_like; 1.
SFLD; SFLDS00029; Radical_SAM; 1.
SMART; SM00876; BATS; 1.
SMART; SM00729; Elp3; 1.
TIGRFAMs; TIGR00433; bioB; 1.
3: Inferred from homology;
2Fe-2S {ECO:0000256|HAMAP-Rule:MF_01694,
ECO:0000256|PIRSR:PIRSR001619-1, ECO:0000256|SAAS:SAAS00063334};
4Fe-4S {ECO:0000256|HAMAP-Rule:MF_01694,
ECO:0000256|PIRSR:PIRSR001619-1, ECO:0000256|SAAS:SAAS00911672};
Biotin biosynthesis {ECO:0000256|HAMAP-Rule:MF_01694,
ECO:0000256|SAAS:SAAS00063242}; Coiled coil {ECO:0000256|SAM:Coils};
Complete proteome {ECO:0000313|Proteomes:UP000000495};
Iron {ECO:0000256|HAMAP-Rule:MF_01694, ECO:0000256|PIRSR:PIRSR001619-
1, ECO:0000256|SAAS:SAAS00063334, ECO:0000256|SAAS:SAAS00911672};
Iron-sulfur {ECO:0000256|HAMAP-Rule:MF_01694,
ECO:0000256|PIRSR:PIRSR001619-1, ECO:0000256|SAAS:SAAS00063334,
ECO:0000256|SAAS:SAAS00911672};
Metal-binding {ECO:0000256|HAMAP-Rule:MF_01694,
ECO:0000256|PIRSR:PIRSR001619-1, ECO:0000256|SAAS:SAAS00063334,
ECO:0000256|SAAS:SAAS00911672};
Reference proteome {ECO:0000313|Proteomes:UP000000495};
S-adenosyl-L-methionine {ECO:0000256|HAMAP-Rule:MF_01694,
ECO:0000256|PIRSR:PIRSR001619-1, ECO:0000256|SAAS:SAAS00911682};
Transferase {ECO:0000256|HAMAP-Rule:MF_01694,
ECO:0000256|SAAS:SAAS00063301, ECO:0000313|EMBL:CCB86533.1}.
DOMAIN 45 252 Elp3. {ECO:0000259|SMART:SM00729}.
DOMAIN 223 315 BATS. {ECO:0000259|SMART:SM00876}.
COILED 73 93 {ECO:0000256|SAM:Coils}.
METAL 55 55 Iron-sulfur 1 (4Fe-4S-S-AdoMet).
{ECO:0000256|HAMAP-Rule:MF_01694,
ECO:0000256|PIRSR:PIRSR001619-1}.
METAL 59 59 Iron-sulfur 1 (4Fe-4S-S-AdoMet).
{ECO:0000256|HAMAP-Rule:MF_01694,
ECO:0000256|PIRSR:PIRSR001619-1}.
METAL 62 62 Iron-sulfur 1 (4Fe-4S-S-AdoMet).
{ECO:0000256|HAMAP-Rule:MF_01694,
ECO:0000256|PIRSR:PIRSR001619-1}.
METAL 99 99 Iron-sulfur 2 (2Fe-2S).
{ECO:0000256|HAMAP-Rule:MF_01694,
ECO:0000256|PIRSR:PIRSR001619-1}.
METAL 131 131 Iron-sulfur 2 (2Fe-2S).
{ECO:0000256|HAMAP-Rule:MF_01694,
ECO:0000256|PIRSR:PIRSR001619-1}.
METAL 191 191 Iron-sulfur 2 (2Fe-2S).
{ECO:0000256|HAMAP-Rule:MF_01694,
ECO:0000256|PIRSR:PIRSR001619-1}.
METAL 263 263 Iron-sulfur 2 (2Fe-2S).
{ECO:0000256|HAMAP-Rule:MF_01694,
ECO:0000256|PIRSR:PIRSR001619-1}.
SEQUENCE 333 AA; 36996 MW; 258CADAC0267C9E8 CRC64;
MPYPIRHNWS REEISSIYHS PLLDLIFEAA SVHRKFHASR EIQLCTLLSI KTGGCPENCS
YCPQSARYNT DVKAEALMQL EEVLDAAKNA KNAGSTRFCM GAAWRQVRNS PDFERVLVMV
REVSQLGLEV CCCLGMLTEE QAKKLKEAGL HSYNHNVDSG EEFYPSIITS RTYQDRLNTL
ENVRKADLSV CCGGIIGLGE KSEDRISMLH TLATLPTHPD SVPINMLVSV KGTPLQNQAP
IPVWEMLRMV ATARLIMPQS MVRLSAGRLS LSDAEQALCF MAGANSIFTG DKLLTTPNPD
FDRDQIMLKT LGLVSKPAEK SEEEETCECT THA


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