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Protein

Biotin synthase

Gene

bio2

Organism
Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at protein leveli

Functioni

Catalytic activityi

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.

Cofactori

Protein has several cofactor binding sites:
  • [4Fe-4S] clusterBy similarityNote: Binds 1 [4Fe-4S] cluster. The cluster is coordinated with 3 cysteines and an exchangeable S-adenosyl-L-methionine.By similarity
  • [2Fe-2S] clusterBy similarityNote: Binds 1 [2Fe-2S] cluster. The cluster is coordinated with 3 cysteines and 1 arginine.By similarity

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi69 – 691Iron-sulfur 1 (4Fe-4S-S-AdoMet)By similarity
Metal bindingi73 – 731Iron-sulfur 1 (4Fe-4S-S-AdoMet)By similarity
Metal bindingi76 – 761Iron-sulfur 1 (4Fe-4S-S-AdoMet)By similarity
Metal bindingi113 – 1131Iron-sulfur 2 (2Fe-2S)By similarity
Metal bindingi146 – 1461Iron-sulfur 2 (2Fe-2S)By similarity
Metal bindingi206 – 2061Iron-sulfur 2 (2Fe-2S)By similarity
Metal bindingi280 – 2801Iron-sulfur 2 (2Fe-2S)By similarity

GO - Molecular functioni

  • 2 iron, 2 sulfur cluster binding Source: UniProtKB-KW
  • 4 iron, 4 sulfur cluster binding Source: UniProtKB-KW
  • biotin synthase activity Source: PomBase
  • metal ion binding Source: UniProtKB-KW

GO - Biological processi

  • biotin biosynthetic process Source: PomBase
Complete GO annotation...

Keywords - Molecular functioni

Transferase

Keywords - Biological processi

Biotin biosynthesis

Keywords - Ligandi

2Fe-2S, 4Fe-4S, Iron, Iron-sulfur, Metal-binding, S-adenosyl-L-methionine

Enzyme and pathway databases

UniPathwayiUPA00078; UER00162.

Names & Taxonomyi

Protein namesi
Recommended name:
Biotin synthase (EC:2.8.1.6)
Gene namesi
Name:bio2
ORF Names:SPCC1235.02, SPCC320.01c
OrganismiSchizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Taxonomic identifieri284812 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaTaphrinomycotinaSchizosaccharomycetesSchizosaccharomycetalesSchizosaccharomycetaceaeSchizosaccharomyces
ProteomesiUP000002485 Componenti: Chromosome III

Organism-specific databases

EuPathDBiFungiDB:SPCC1235.02.
PomBaseiSPCC1235.02.

Subcellular locationi

GO - Cellular componenti

  • mitochondrion Source: PomBase
Complete GO annotation...

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 363363Biotin synthasePRO_0000185566Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei13 – 131Phosphoserine1 Publication
Modified residuei14 – 141Phosphoserine1 Publication
Modified residuei17 – 171Phosphoserine1 Publication

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiO59778.
PaxDbiO59778.

Interactioni

Protein-protein interaction databases

BioGridi275301. 33 interactions.
MINTiMINT-4676108.
STRINGi4896.SPCC1235.02-1.

Structurei

3D structure databases

ProteinModelPortaliO59778.
SMRiO59778. Positions 20-332.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

eggNOGiCOG0502.
HOGENOMiHOG000239957.
InParanoidiO59778.
KOiK01012.
OMAiCGYCPQS.
OrthoDBiEOG7V76GZ.
PhylomeDBiO59778.

Family and domain databases

Gene3Di3.20.20.70. 1 hit.
HAMAPiMF_01694. BioB.
InterProiIPR013785. Aldolase_TIM.
IPR010722. BATS_dom.
IPR002684. Biotin_synth/BioAB.
IPR024177. Biotin_synthase.
IPR006638. Elp3/MiaB/NifB.
IPR007197. rSAM.
[Graphical view]
PfamiPF06968. BATS. 1 hit.
PF04055. Radical_SAM. 1 hit.
[Graphical view]
PIRSFiPIRSF001619. Biotin_synth. 1 hit.
SMARTiSM00876. BATS. 1 hit.
SM00729. Elp3. 1 hit.
[Graphical view]
TIGRFAMsiTIGR00433. bioB. 1 hit.

Sequencei

Sequence statusi: Complete.

O59778-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MFTRTIRQQI RRSSALSLVR NNWTREEIQK IYDTPLIDLI FRAASIHRKF
60 70 80 90 100
HDPKKVQQCT LLSIKTGGCT EDCKYCAQSS RYNTGVKATK LMKIDEVLEK
110 120 130 140 150
AKIAKAKGST RFCMGSAWRD LNGRNRTFKN ILEIIKEVRS MDMEVCVTLG
160 170 180 190 200
MLNEQQAKEL KDAGLTAYNH NLDTSREYYS KIISTRTYDE RLNTIDNLRK
210 220 230 240 250
AGLKVCSGGI LGLGEKKHDR VGLIHSLATM PTHPESVPFN LLVPIPGTPV
260 270 280 290 300
GDAVKERLPI HPFLRSIATA RICMPKTIIR FAAGRNTCSE SEQALAFMAG
310 320 330 340 350
ANAVFTGEKM LTTPAVSWDS DSQLFYNWGL EGMQSFEYGT STEGEDGTFT
360
LPPKERLAPS PSL
Length:363
Mass (Da):40,651
Last modified:August 1, 1998 - v1
Checksum:i008E2EDF9901AEB1
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti13 – 142SS → FF in CAA12229 (PubMed:10525840).Curated
Sequence conflicti17 – 171S → F in CAA12229 (PubMed:10525840).Curated
Sequence conflicti312 – 3187TTPAVSW → LLLLFL in CAA12229 (PubMed:10525840).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AJ224930 mRNA. Translation: CAA12229.1.
CU329672 Genomic DNA. Translation: CAA18303.1.
PIRiT40876.
RefSeqiNP_587728.1. NM_001022723.2.

Genome annotation databases

EnsemblFungiiSPCC1235.02.1; SPCC1235.02.1:pep; SPCC1235.02.
GeneIDi2538717.
KEGGispo:SPCC1235.02.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AJ224930 mRNA. Translation: CAA12229.1.
CU329672 Genomic DNA. Translation: CAA18303.1.
PIRiT40876.
RefSeqiNP_587728.1. NM_001022723.2.

3D structure databases

ProteinModelPortaliO59778.
SMRiO59778. Positions 20-332.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi275301. 33 interactions.
MINTiMINT-4676108.
STRINGi4896.SPCC1235.02-1.

Proteomic databases

MaxQBiO59778.
PaxDbiO59778.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiSPCC1235.02.1; SPCC1235.02.1:pep; SPCC1235.02.
GeneIDi2538717.
KEGGispo:SPCC1235.02.

Organism-specific databases

EuPathDBiFungiDB:SPCC1235.02.
PomBaseiSPCC1235.02.

Phylogenomic databases

eggNOGiCOG0502.
HOGENOMiHOG000239957.
InParanoidiO59778.
KOiK01012.
OMAiCGYCPQS.
OrthoDBiEOG7V76GZ.
PhylomeDBiO59778.

Enzyme and pathway databases

UniPathwayiUPA00078; UER00162.

Miscellaneous databases

NextBioi20799902.
PROiO59778.

Family and domain databases

Gene3Di3.20.20.70. 1 hit.
HAMAPiMF_01694. BioB.
InterProiIPR013785. Aldolase_TIM.
IPR010722. BATS_dom.
IPR002684. Biotin_synth/BioAB.
IPR024177. Biotin_synthase.
IPR006638. Elp3/MiaB/NifB.
IPR007197. rSAM.
[Graphical view]
PfamiPF06968. BATS. 1 hit.
PF04055. Radical_SAM. 1 hit.
[Graphical view]
PIRSFiPIRSF001619. Biotin_synth. 1 hit.
SMARTiSM00876. BATS. 1 hit.
SM00729. Elp3. 1 hit.
[Graphical view]
TIGRFAMsiTIGR00433. bioB. 1 hit.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Cloning of Schizosaccharomyces pombe bio2 by heterologous complementation of a Saccharomyces cerevisiae mutant."
    Phalip V., Jeltsch J.-M., Lemoine Y.
    Curr. Microbiol. 39:348-350(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], CHARACTERIZATION.
    Strain: D18.
  2. "The genome sequence of Schizosaccharomyces pombe."
    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.
    Nature 415:871-880(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: 972 / ATCC 24843.
  3. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-13; SER-14 AND SER-17, IDENTIFICATION BY MASS SPECTROMETRY.

Entry informationi

Entry nameiBIOB_SCHPO
AccessioniPrimary (citable) accession number: O59778
Secondary accession number(s): O60050
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 11, 2001
Last sequence update: August 1, 1998
Last modified: May 27, 2015
This is version 120 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. Schizosaccharomyces pombe
    Schizosaccharomyces pombe: entries and gene names
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.