O59778 (BIOB_SCHPO) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Biotin synthase
EC=2.8.1.6

Gene names

Name:	bio2
ORF Names:	SPCC1235.02, SPCC320.01c

Organism

Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast) [Reference proteome]

Taxonomic identifier

284812 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Fungi › Dikarya › Ascomycota › Taphrinomycotina › Schizosaccharomycetes › Schizosaccharomycetales › Schizosaccharomycetaceae › Schizosaccharomyces › Schizosaccharomyces pombe

Protein attributes

Sequence length	363 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Catalytic activity	Dethiobiotin + sulfur + 2 S-adenosyl-L-methionine = biotin + 2 L-methionine + 2 5'-deoxyadenosine.
Cofactor	Binds 1 4Fe-4S cluster. The cluster is coordinated with 3 cysteines and an exchangeable S-adenosyl-L-methionine By similarity. Binds 1 2Fe-2S cluster. The cluster is coordinated with 3 cysteines and 1 arginine By similarity.
Pathway	Cofactor biosynthesis; biotin biosynthesis; biotin from 7,8-diaminononanoate: step 2/2.
Sequence similarities	Belongs to the radical SAM superfamily. Biotin synthase family.

Ontologies

Keywords
Biological process	Biotin biosynthesis
Ligand	2Fe-2S 4Fe-4S Iron Iron-sulfur Metal-binding S-adenosyl-L-methionine
Molecular function	Transferase
PTM	Phosphoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	biotin biosynthetic process Inferred by curator. Source: PomBase
Cellular_component	mitochondrion Inferred from direct assay PubMed 16823372. Source: PomBase
Molecular_function	2 iron, 2 sulfur cluster binding Inferred from electronic annotation. Source: UniProtKB-KW 4 iron, 4 sulfur cluster binding Inferred from electronic annotation. Source: UniProtKB-KW biotin synthase activity Inferred from sequence orthology. Source: PomBase metal ion binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 363	363	Biotin synthase		PRO_0000185566
Sites
	Metal binding	69	1	Iron-sulfur 1 (4Fe-4S-S-AdoMet) By similarity
	Metal binding	73	1	Iron-sulfur 1 (4Fe-4S-S-AdoMet) By similarity
	Metal binding	76	1	Iron-sulfur 1 (4Fe-4S-S-AdoMet) By similarity
	Metal binding	113	1	Iron-sulfur 2 (2Fe-2S) By similarity
	Metal binding	146	1	Iron-sulfur 2 (2Fe-2S) By similarity
	Metal binding	206	1	Iron-sulfur 2 (2Fe-2S) By similarity
	Metal binding	280	1	Iron-sulfur 2 (2Fe-2S) By similarity
Amino acid modifications
	Modified residue	13	1	Phosphoserine Ref.3
	Modified residue	14	1	Phosphoserine Ref.3
	Modified residue	17	1	Phosphoserine Ref.3
Experimental info
	Sequence conflict	13 – 14	2	SS → FF in CAA12229. Ref.1
	Sequence conflict	17	1	S → F in CAA12229. Ref.1
	Sequence conflict	312 – 318	7	TTPAVSW → LLLLFL in CAA12229. Ref.1

Sequences

	Sequence		Length	Mass (Da)
	O59778 [UniParc]. Last modified August 1, 1998. Version 1. Checksum: 008E2EDF9901AEB1	FASTA	363	40,651
	10 20 30 40 50 60 MFTRTIRQQI RRSSALSLVR NNWTREEIQK IYDTPLIDLI FRAASIHRKF HDPKKVQQCT 70 80 90 100 110 120 LLSIKTGGCT EDCKYCAQSS RYNTGVKATK LMKIDEVLEK AKIAKAKGST RFCMGSAWRD 130 140 150 160 170 180 LNGRNRTFKN ILEIIKEVRS MDMEVCVTLG MLNEQQAKEL KDAGLTAYNH NLDTSREYYS 190 200 210 220 230 240 KIISTRTYDE RLNTIDNLRK AGLKVCSGGI LGLGEKKHDR VGLIHSLATM PTHPESVPFN 250 260 270 280 290 300 LLVPIPGTPV GDAVKERLPI HPFLRSIATA RICMPKTIIR FAAGRNTCSE SEQALAFMAG 310 320 330 340 350 360 ANAVFTGEKM LTTPAVSWDS DSQLFYNWGL EGMQSFEYGT STEGEDGTFT LPPKERLAPS PSL

References

	« Hide 'large scale' referencesShow 'large scale' references »
[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]	"Phosphoproteome analysis of fission yeast." Wilson-Grady J.T., Villen J., Gygi S.P. J. Proteome Res. 7:1088-1097(2008) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-13; SER-14 AND SER-17, MASS SPECTROMETRY.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AJ224930 mRNA. Translation: CAA12229.1. CU329672 Genomic DNA. Translation: CAA18303.1.
PIR	T40876.
RefSeq	NP_587728.1. NM_001022723.2.
3D structure databases
ProteinModelPortal	O59778.
SMR	O59778. Positions 20-332.
ModBase	Search...
Protein-protein interaction databases
STRING	4896.SPCC1235.02-1.
Proteomic databases
PaxDb	O59778.
PRIDE	O59778.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblFungi	SPCC1235.02.1; SPCC1235.02.1:pep; SPCC1235.02.
GeneID	2538717.
KEGG	spo:SPCC1235.02.
Organism-specific databases
PomBase	SPCC1235.02.
Phylogenomic databases
eggNOG	COG0502.
HOGENOM	HOG000239957.
KO	K01012.
OMA	RIMMPAS.
OrthoDB	EOG4BS0VB.
Enzyme and pathway databases
UniPathway	UPA00078; UER00162.
Family and domain databases
Gene3D	3.20.20.70. 1 hit.
InterPro	IPR013785. Aldolase_TIM. IPR010722. Biotin/thiamin_synth-assoc. IPR002684. Biotin_synth/BioAB. IPR024177. Biotin_synthase. IPR006638. Elp3/MiaB/NifB. IPR007197. rSAM. [Graphical view]
Pfam	PF06968. BATS. 1 hit. PF04055. Radical_SAM. 1 hit. [Graphical view]
PIRSF	PIRSF001619. Biotin_synth. 1 hit.
SMART	SM00876. BATS. 1 hit. SM00729. Elp3. 1 hit. [Graphical view]
TIGRFAMs	TIGR00433. bioB. 1 hit.
ProtoNet	Search...
Other
NextBio	20799902.

Entry information

Entry name

BIOB_SCHPO

Accession

Primary (citable) accession number: O59778
Secondary accession number(s): O60050

Entry history

Integrated into UniProtKB/Swiss-Prot:	January 11, 2001
Last sequence update:	August 1, 1998
Last modified:	May 1, 2013
This is version 104 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Fungal Protein Annotation Program