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Biotin synthase (EC 2.8.1.6)

 BIOB_SCHPO              Reviewed;         363 AA.
O59778; O60050;
11-JAN-2001, integrated into UniProtKB/Swiss-Prot.
01-AUG-1998, sequence version 1.
22-NOV-2017, entry version 136.
RecName: Full=Biotin synthase;
EC=2.8.1.6;
Name=bio2; ORFNames=SPCC1235.02, SPCC320.01c;
Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
Schizosaccharomycetes; Schizosaccharomycetales;
Schizosaccharomycetaceae; Schizosaccharomyces.
NCBI_TaxID=284812;
[1]
NUCLEOTIDE SEQUENCE [MRNA], AND CHARACTERIZATION.
STRAIN=D18;
PubMed=10525840; DOI=10.1007/s002849900470;
Phalip V., Jeltsch J.-M., Lemoine Y.;
"Cloning of Schizosaccharomyces pombe bio2 by heterologous
complementation of a Saccharomyces cerevisiae mutant.";
Curr. Microbiol. 39:348-350(1999).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=972 / ATCC 24843;
PubMed=11859360; DOI=10.1038/nature724;
Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A.,
Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S.,
Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M.,
Collins M., Connor R., Cronin A., Davis P., Feltwell T., Fraser A.,
Gentles S., Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G.,
Holroyd S., Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K.,
James K.D., Jones L., Jones M., Leather S., McDonald S., McLean J.,
Mooney P., Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C.,
Oliver K., O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E.,
Rutherford K.M., Rutter S., Saunders D., Seeger K., Sharp S.,
Skelton J., Simmonds M.N., Squares R., Squares S., Stevens K.,
Taylor K., Taylor R.G., Tivey A., Walsh S.V., Warren T., Whitehead S.,
Woodward J.R., Volckaert G., Aert R., Robben J., Grymonprez B.,
Weltjens I., Vanstreels E., Rieger M., Schaefer M., Mueller-Auer S.,
Gabel C., Fuchs M., Duesterhoeft A., Fritzc C., Holzer E., Moestl D.,
Hilbert H., Borzym K., Langer I., Beck A., Lehrach H., Reinhardt R.,
Pohl T.M., Eger P., Zimmermann W., Wedler H., Wambutt R., Purnelle B.,
Goffeau A., Cadieu E., Dreano S., Gloux S., Lelaure V., Mottier S.,
Galibert F., Aves S.J., Xiang Z., Hunt C., Moore K., Hurst S.M.,
Lucas M., Rochet M., Gaillardin C., Tallada V.A., Garzon A., Thode G.,
Daga R.R., Cruzado L., Jimenez J., Sanchez M., del Rey F., Benito J.,
Dominguez A., Revuelta J.L., Moreno S., Armstrong J., Forsburg S.L.,
Cerutti L., Lowe T., McCombie W.R., Paulsen I., Potashkin J.,
Shpakovski G.V., Ussery D., Barrell B.G., Nurse P.;
"The genome sequence of Schizosaccharomyces pombe.";
Nature 415:871-880(2002).
[3]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-13; SER-14 AND SER-17,
AND IDENTIFICATION BY MASS SPECTROMETRY.
PubMed=18257517; DOI=10.1021/pr7006335;
Wilson-Grady J.T., Villen J., Gygi S.P.;
"Phosphoproteome analysis of fission yeast.";
J. Proteome Res. 7:1088-1097(2008).
-!- 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.
-!- COFACTOR:
Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
Evidence={ECO:0000250};
Note=Binds 1 [4Fe-4S] cluster. The cluster is coordinated with 3
cysteines and an exchangeable S-adenosyl-L-methionine.
{ECO:0000250};
-!- COFACTOR:
Name=[2Fe-2S] cluster; Xref=ChEBI:CHEBI:49601;
Evidence={ECO:0000250};
Note=Binds 1 [2Fe-2S] cluster. The cluster is coordinated with 3
cysteines and 1 arginine. {ECO:0000250};
-!- PATHWAY: Cofactor biosynthesis; biotin biosynthesis; biotin from
7,8-diaminononanoate: step 2/2.
-!- SIMILARITY: Belongs to the radical SAM superfamily. Biotin
synthase family. {ECO:0000305}.
-----------------------------------------------------------------------
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EMBL; AJ224930; CAA12229.1; -; mRNA.
EMBL; CU329672; CAA18303.1; -; Genomic_DNA.
PIR; T40876; T40876.
RefSeq; NP_587728.1; NM_001022723.2.
ProteinModelPortal; O59778; -.
SMR; O59778; -.
BioGrid; 275301; 33.
MINT; MINT-4676108; -.
STRING; 4896.SPCC1235.02.1; -.
iPTMnet; O59778; -.
MaxQB; O59778; -.
PRIDE; O59778; -.
EnsemblFungi; SPCC1235.02.1; SPCC1235.02.1:pep; SPCC1235.02.
GeneID; 2538717; -.
KEGG; spo:SPCC1235.02; -.
EuPathDB; FungiDB:SPCC1235.02; -.
PomBase; SPCC1235.02; bio2.
HOGENOM; HOG000239957; -.
InParanoid; O59778; -.
KO; K01012; -.
OMA; ADRFCMG; -.
OrthoDB; EOG092C24WQ; -.
PhylomeDB; O59778; -.
UniPathway; UPA00078; UER00162.
PRO; PR:O59778; -.
Proteomes; UP000002485; Chromosome III.
GO; GO:0005739; C:mitochondrion; IDA:PomBase.
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; IGI:PomBase.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0009102; P:biotin biosynthetic process; IGI:PomBase.
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.
1: Evidence at protein level;
2Fe-2S; 4Fe-4S; Biotin biosynthesis; Complete proteome; Iron;
Iron-sulfur; Metal-binding; Phosphoprotein; Reference proteome;
S-adenosyl-L-methionine; Transferase.
CHAIN 1 363 Biotin synthase.
/FTId=PRO_0000185566.
METAL 69 69 Iron-sulfur 1 (4Fe-4S-S-AdoMet).
{ECO:0000250}.
METAL 73 73 Iron-sulfur 1 (4Fe-4S-S-AdoMet).
{ECO:0000250}.
METAL 76 76 Iron-sulfur 1 (4Fe-4S-S-AdoMet).
{ECO:0000250}.
METAL 113 113 Iron-sulfur 2 (2Fe-2S). {ECO:0000250}.
METAL 146 146 Iron-sulfur 2 (2Fe-2S). {ECO:0000250}.
METAL 206 206 Iron-sulfur 2 (2Fe-2S). {ECO:0000250}.
METAL 280 280 Iron-sulfur 2 (2Fe-2S). {ECO:0000250}.
MOD_RES 13 13 Phosphoserine.
{ECO:0000269|PubMed:18257517}.
MOD_RES 14 14 Phosphoserine.
{ECO:0000269|PubMed:18257517}.
MOD_RES 17 17 Phosphoserine.
{ECO:0000269|PubMed:18257517}.
CONFLICT 13 14 SS -> FF (in Ref. 1; CAA12229).
{ECO:0000305}.
CONFLICT 17 17 S -> F (in Ref. 1; CAA12229).
{ECO:0000305}.
CONFLICT 312 318 TTPAVSW -> LLLLFL (in Ref. 1; CAA12229).
{ECO:0000305}.
SEQUENCE 363 AA; 40651 MW; 008E2EDF9901AEB1 CRC64;
MFTRTIRQQI RRSSALSLVR NNWTREEIQK IYDTPLIDLI FRAASIHRKF HDPKKVQQCT
LLSIKTGGCT EDCKYCAQSS RYNTGVKATK LMKIDEVLEK AKIAKAKGST RFCMGSAWRD
LNGRNRTFKN ILEIIKEVRS MDMEVCVTLG MLNEQQAKEL KDAGLTAYNH NLDTSREYYS
KIISTRTYDE RLNTIDNLRK AGLKVCSGGI LGLGEKKHDR VGLIHSLATM PTHPESVPFN
LLVPIPGTPV GDAVKERLPI HPFLRSIATA RICMPKTIIR FAAGRNTCSE SEQALAFMAG
ANAVFTGEKM LTTPAVSWDS DSQLFYNWGL EGMQSFEYGT STEGEDGTFT LPPKERLAPS
PSL


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