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O14353 (BPL1_SCHPO) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 81. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Biotin--protein ligase

EC=6.3.4.-
Alternative name(s):
Biotin apo-protein ligase

Including the following 4 domains:

  1. Biotin--[methylmalonyl-CoA-carboxytransferase] ligase
    EC=6.3.4.9
  2. Biotin--[propionyl-CoA-carboxylase [ATP-hydrolyzing]] ligase
    EC=6.3.4.10
    Alternative name(s):
    Holocarboxylase synthetase
    Short name=HCS
  3. Biotin--[methylcrotonoyl-CoA-carboxylase] ligase
    EC=6.3.4.11
  4. Biotin--[acetyl-CoA-carboxylase] ligase
    EC=6.3.4.15
Gene names
Name:bpl1
ORF Names:SPBC30D10.07c
OrganismSchizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast) [Reference proteome]
Taxonomic identifier284812 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaTaphrinomycotinaSchizosaccharomycetesSchizosaccharomycetalesSchizosaccharomycetaceaeSchizosaccharomyces

Protein attributes

Sequence length631 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Function

Post-translational modification of specific protein by attachment of biotin. Acts on various carboxylases such as acetyl-CoA-carboxylase, pyruvate carboxylase, propionyl CoA carboxylase, and 3-methylcrotonyl CoA carboxylase By similarity.

Catalytic activity

ATP + biotin + apo-[methylmalonyl-CoA:pyruvate carboxytransferase] = AMP + diphosphate + [methylmalonyl-CoA:pyruvate carboxytransferase].

ATP + biotin + apo-[propionyl-CoA:carbon-dioxide ligase (ADP-forming)] = AMP + diphosphate + [propionyl-CoA:carbon-dioxide ligase (ADP-forming)].

ATP + biotin + apo-[3-methylcrotonoyl-CoA:carbon-dioxide ligase (ADP-forming)] = AMP + diphosphate + [3-methylcrotonoyl-CoA:carbon-dioxide ligase (ADP-forming)].

ATP + biotin + apo-[acetyl-CoA:carbon-dioxide ligase (ADP-forming)] = AMP + diphosphate + [acetyl-CoA:carbon-dioxide ligase (ADP-forming)].

Subunit structure

Monomer By similarity.

Subcellular location

Cytoplasm By similarity.

Sequence similarities

Belongs to the biotin--protein ligase family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 631631Biotin--protein ligase
PRO_0000315970

Sequences

Sequence LengthMass (Da)Tools
O14353 [UniParc].

Last modified January 1, 1998. Version 1.
Checksum: 37E08571359F5112

FASTA63170,632
        10         20         30         40         50         60 
MNVLIYNGNG ASKICLLRTF QSLLPFVVPL YAMRFVDAST LEKEPWPAST ALLVMPGGRD 

        70         80         90        100        110        120 
MGYCSSFNET IYRKITDFVK RGGAYLGLCA GGYFGSAVVD FRMPDSDLNV VGKRKLQFFP 

       130        140        150        160        170        180 
GTCAGPTFPG FTYDSEDGAR RASIIVDGMQ SSPVHTHIYF NGGGSFLETE NYSNVKVVAR 

       190        200        210        220        230        240 
YQETDFEKSA AIIYVKVGKG NVVLTGIHPE FSAEGSPILD KRDEKTRLEL LSYILKLLGL 

       250        260        270        280        290        300 
KVPKDTSKCG QPTLTDQYLF PNNVETKRFI EKALTNKVKN QDEDTLYTFQ FSDISSEIPE 

       310        320        330        340        350        360 
HQLANLDISA DLSDSDNEIV KIWYGDEEKI CKKAKPSFDL ELYAKLINGC RFGLPIIVAP 

       370        380        390        400        410        420 
VIRSTQTLLD KNYRFLDSTN TGFTVLGNYQ TAGRGRGQNM WVSPYGTLAF SFIINVDAKN 

       430        440        450        460        470        480 
FSTTPIALFQ YLMALAVVRG IREYAPGYEN IPAFIKWPND VYVRVDKGGI NFQGKQYMKL 

       490        500        510        520        530        540 
SGIIVTSNYR KNVLHLVVGC GINVSNLGPT VSLNTLVDEW NKNSDNPRLE KFSFEKLLAS 

       550        560        570        580        590        600 
VLNQFDRYHR LLLEEGFSLI LPEYYQYWLH SNQTVNLASG GKAIIQGITS DFGFLLAQLL 

       610        620        630 
NENNEPTTKV VHLQPDGNSF DLMRNLITRK T 

« Hide

References

[1]"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. expand/collapse author list , 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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CU329671 Genomic DNA. Translation: CAB10802.1.
PIRT40189.
RefSeqNP_596278.1. NM_001022199.2.

3D structure databases

ProteinModelPortalO14353.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING4896.SPBC30D10.07c-1.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiSPBC30D10.07c.1; SPBC30D10.07c.1:pep; SPBC30D10.07c.
GeneID2540476.
KEGGspo:SPBC30D10.07c.

Organism-specific databases

PomBaseSPBC30D10.07c.

Phylogenomic databases

eggNOGCOG0340.
HOGENOMHOG000214585.
KOK01942.
OMAAVVYCKV.
OrthoDBEOG7KQ2BG.
PhylomeDBO14353.

Family and domain databases

InterProIPR019197. Biotin-prot_ligase_N.
IPR004408. Biotin_CoA_COase_ligase.
IPR003142. BPL_C.
IPR004143. BPL_LipA_LipB.
[Graphical view]
PANTHERPTHR12835. PTHR12835. 1 hit.
PfamPF02237. BPL_C. 1 hit.
PF03099. BPL_LplA_LipB. 1 hit.
PF09825. BPL_N. 1 hit.
[Graphical view]
TIGRFAMsTIGR00121. birA_ligase. 1 hit.
ProtoNetSearch...

Other

NextBio20801603.
PROO14353.

Entry information

Entry nameBPL1_SCHPO
AccessionPrimary (citable) accession number: O14353
Entry history
Integrated into UniProtKB/Swiss-Prot: January 15, 2008
Last sequence update: January 1, 1998
Last modified: April 16, 2014
This is version 81 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

Schizosaccharomyces pombe

Schizosaccharomyces pombe: entries and gene names