BIOB_SCHPO
ID BIOB_SCHPO Reviewed; 363 AA.
AC O59778; O60050;
DT 11-JAN-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1998, sequence version 1.
DT 03-AUG-2022, entry version 154.
DE RecName: Full=Biotin synthase;
DE EC=2.8.1.6 {ECO:0000305|PubMed:10525840};
GN Name=bio2; ORFNames=SPCC1235.02, SPCC320.01c;
OS Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC Schizosaccharomycetes; Schizosaccharomycetales; Schizosaccharomycetaceae;
OC Schizosaccharomyces.
OX NCBI_TaxID=284812;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, CATALYTIC ACTIVITY, AND PATHWAY.
RC STRAIN=D18;
RX PubMed=10525840; DOI=10.1007/s002849900470;
RA Phalip V., Jeltsch J.-M., Lemoine Y.;
RT "Cloning of Schizosaccharomyces pombe bio2 by heterologous complementation
RT of a Saccharomyces cerevisiae mutant.";
RL Curr. Microbiol. 39:348-350(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=972 / ATCC 24843;
RX PubMed=11859360; DOI=10.1038/nature724;
RA Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A.,
RA Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S.,
RA Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M.,
RA Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S.,
RA Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S.,
RA Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D.,
RA Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P.,
RA Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K.,
RA O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M.,
RA Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N.,
RA Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A.,
RA Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R.,
RA Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M.,
RA Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A.,
RA Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A.,
RA Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H.,
RA Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S.,
RA Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C.,
RA Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A.,
RA Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M.,
RA del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S.,
RA Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R.,
RA Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G.,
RA Nurse P.;
RT "The genome sequence of Schizosaccharomyces pombe.";
RL Nature 415:871-880(2002).
RN [3]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-13; SER-14 AND SER-17, AND
RP IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=18257517; DOI=10.1021/pr7006335;
RA Wilson-Grady J.T., Villen J., Gygi S.P.;
RT "Phosphoproteome analysis of fission yeast.";
RL J. Proteome Res. 7:1088-1097(2008).
CC -!- FUNCTION: Catalyzes the last step of biotin biosynthesis, the
CC conversion of dethiobiotin to biotin. {ECO:0000305|PubMed:10525840}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(4R,5S)-dethiobiotin + [sulfur carrier]-SH + 2 reduced [2Fe-
CC 2S]-[ferredoxin] + 2 S-adenosyl-L-methionine = 2 5'-deoxyadenosine +
CC [sulfur carrier]-H + biotin + 2 L-methionine + 2 oxidized [2Fe-2S]-
CC [ferredoxin]; Xref=Rhea:RHEA:22060, Rhea:RHEA-COMP:10000, Rhea:RHEA-
CC COMP:10001, Rhea:RHEA-COMP:14737, Rhea:RHEA-COMP:14739,
CC ChEBI:CHEBI:17319, ChEBI:CHEBI:29917, ChEBI:CHEBI:33737,
CC ChEBI:CHEBI:33738, ChEBI:CHEBI:57586, ChEBI:CHEBI:57844,
CC ChEBI:CHEBI:59789, ChEBI:CHEBI:64428, ChEBI:CHEBI:149473; EC=2.8.1.6;
CC Evidence={ECO:0000305|PubMed:10525840};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:22061;
CC Evidence={ECO:0000305|PubMed:10525840};
CC -!- COFACTOR:
CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883; Evidence={ECO:0000250};
CC Note=Binds 1 [4Fe-4S] cluster. The cluster is coordinated with 3
CC cysteines and an exchangeable S-adenosyl-L-methionine. {ECO:0000250};
CC -!- COFACTOR:
CC Name=[2Fe-2S] cluster; Xref=ChEBI:CHEBI:190135; Evidence={ECO:0000250};
CC Note=Binds 1 [2Fe-2S] cluster. The cluster is coordinated with 3
CC cysteines and 1 arginine. {ECO:0000250};
CC -!- PATHWAY: Cofactor biosynthesis; biotin biosynthesis; biotin from 7,8-
CC diaminononanoate: step 2/2. {ECO:0000305|PubMed:10525840}.
CC -!- SIMILARITY: Belongs to the radical SAM superfamily. Biotin synthase
CC family. {ECO:0000305}.
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DR EMBL; AJ224930; CAA12229.1; -; mRNA.
DR EMBL; CU329672; CAA18303.1; -; Genomic_DNA.
DR PIR; T40876; T40876.
DR RefSeq; NP_587728.1; NM_001022723.2.
DR AlphaFoldDB; O59778; -.
DR SMR; O59778; -.
DR BioGRID; 275301; 35.
DR STRING; 4896.SPCC1235.02.1; -.
DR iPTMnet; O59778; -.
DR MaxQB; O59778; -.
DR PaxDb; O59778; -.
DR PRIDE; O59778; -.
DR EnsemblFungi; SPCC1235.02.1; SPCC1235.02.1:pep; SPCC1235.02.
DR GeneID; 2538717; -.
DR KEGG; spo:SPCC1235.02; -.
DR PomBase; SPCC1235.02; bio2.
DR VEuPathDB; FungiDB:SPCC1235.02; -.
DR eggNOG; KOG2900; Eukaryota.
DR HOGENOM; CLU_033172_1_2_1; -.
DR InParanoid; O59778; -.
DR OMA; ADRFCMG; -.
DR PhylomeDB; O59778; -.
DR UniPathway; UPA00078; UER00162.
DR PRO; PR:O59778; -.
DR Proteomes; UP000002485; Chromosome III.
DR GO; GO:0005739; C:mitochondrion; HDA:PomBase.
DR GO; GO:0051537; F:2 iron, 2 sulfur cluster binding; IBA:GO_Central.
DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW.
DR GO; GO:0004076; F:biotin synthase activity; IGI:PomBase.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0009102; P:biotin biosynthetic process; IGI:PomBase.
DR Gene3D; 3.20.20.70; -; 1.
DR HAMAP; MF_01694; BioB; 1.
DR InterPro; IPR013785; Aldolase_TIM.
DR InterPro; IPR010722; BATS_dom.
DR InterPro; IPR002684; Biotin_synth/BioAB.
DR InterPro; IPR024177; Biotin_synthase.
DR InterPro; IPR006638; Elp3/MiaB/NifB.
DR InterPro; IPR007197; rSAM.
DR PANTHER; PTHR22976; PTHR22976; 1.
DR Pfam; PF06968; BATS; 1.
DR Pfam; PF04055; Radical_SAM; 1.
DR PIRSF; PIRSF001619; Biotin_synth; 1.
DR SFLD; SFLDF00272; biotin_synthase; 1.
DR SMART; SM00876; BATS; 1.
DR SMART; SM00729; Elp3; 1.
DR TIGRFAMs; TIGR00433; bioB; 1.
DR PROSITE; PS51918; RADICAL_SAM; 1.
PE 1: Evidence at protein level;
KW 2Fe-2S; 4Fe-4S; Biotin biosynthesis; Iron; Iron-sulfur; Metal-binding;
KW Phosphoprotein; Reference proteome; S-adenosyl-L-methionine; Transferase.
FT CHAIN 1..363
FT /note="Biotin synthase"
FT /id="PRO_0000185566"
FT DOMAIN 54..276
FT /note="Radical SAM core"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01266"
FT REGION 337..363
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 69
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_note="4Fe-4S-S-AdoMet"
FT /evidence="ECO:0000250"
FT BINDING 73
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_note="4Fe-4S-S-AdoMet"
FT /evidence="ECO:0000250"
FT BINDING 76
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_note="4Fe-4S-S-AdoMet"
FT /evidence="ECO:0000250"
FT BINDING 113
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000250"
FT BINDING 146
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000250"
FT BINDING 206
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000250"
FT BINDING 280
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000250"
FT MOD_RES 13
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18257517"
FT MOD_RES 14
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18257517"
FT MOD_RES 17
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18257517"
FT CONFLICT 13..14
FT /note="SS -> FF (in Ref. 1; CAA12229)"
FT /evidence="ECO:0000305"
FT CONFLICT 17
FT /note="S -> F (in Ref. 1; CAA12229)"
FT /evidence="ECO:0000305"
FT CONFLICT 312..318
FT /note="TTPAVSW -> LLLLFL (in Ref. 1; CAA12229)"
FT /evidence="ECO:0000305"
SQ 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
