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P48445 (BPL1_YEAST) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 115. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | 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
Synonyms:ACC2
Ordered Locus Names:YDL141W
ORF Names:D2140
OrganismSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) [Reference proteome]
Taxonomic identifier559292 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces

Protein attributes

Sequence length690 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

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.

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 Ref.5.

Miscellaneous

Present with 1970 molecules/cell in log phase SD medium.

Sequence similarities

Belongs to the biotin--protein ligase family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 690690Biotin--protein ligase
PRO_0000064981

Sequences

Sequence LengthMass (Da)Tools
P48445 [UniParc].

Last modified February 1, 1996. Version 1.
Checksum: ADA6BFE411C656AB

FASTA69076,363
        10         20         30         40         50         60 
MNVLVYNGPG TTPGSVKHAV ESLRDFLEPY YAVSTVNVKV LQTEPWMSKT SAVVFPGGAD 

        70         80         90        100        110        120 
LPYVQACQPI ISRLKHFVSK QGGVFIGFCA GGYFGTSRVE FAQGDPTMEV SGSRDLRFFP 

       130        140        150        160        170        180 
GTSRGPAYNG FQYNSEAGAR AVKLNLPDGS QFSTYFNGGA VFVDADKFDN VEILATYAEH 

       190        200        210        220        230        240 
PDVPSSDSGK GQSENPAAVV LCTVGRGKVL LTGPHPEFNV RFMRKSTDKH FLETVVENLK 

       250        260        270        280        290        300 
AQEIMRLKFM RTVLTKTGLN CNNDFNYVRA PNLTPLFMAS APNKRNYLQE MENNLAHHGM 

       310        320        330        340        350        360 
HANNVELCSE LNAETDSFQF YRGYRASYDA ASSSLLHKEP DEVPKTVIFP GVDEDIPPFQ 

       370        380        390        400        410        420 
YTPNFDMKEY FKYLNVQNTI GSLLLYGEVV TSTSTILNNN KSLLSSIPES TLLHVGTIQV 

       430        440        450        460        470        480 
SGRGRGGNTW INPKGVCAST AVVTMPLQSP VTNRNISVVF VQYLSMLAYC KAILSYAPGF 

       490        500        510        520        530        540 
SDIPVRIKWP NDLYALSPTY YKRKNLKLVN TGFEHTKLPL GDIEPAYLKI SGLLVNTHFI 

       550        560        570        580        590        600 
NNKYCLLLGC GINLTSDGPT TSLQTWIDIL NEERQQLHLD LLPAIKAEKL QALYMNNLEV 

       610        620        630        640        650        660 
ILKQFINYGA AEILPSYYEL WLHSNQIVTL PDHGNTQAMI TGITEDYGLL IAKELVSGSS 

       670        680        690 
TQFTGNVYNL QPDGNTFDIF KSLIAKKVQS 

« Hide

References

« Hide 'large scale' references
[1]"The gene encoding the biotin-apoprotein ligase of Saccharomyces cerevisiae."
Cronan J.E. Jr., Wallace J.C.
FEMS Microbiol. Lett. 130:221-230(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: ATCC 204508 / S288c.
[2]"Analysis of a 26,756 bp segment from the left arm of yeast chromosome IV."
Woelfl S., Haneman V., Saluz H.P.
Yeast 12:1549-1554(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: ATCC 96604 / S288c / FY1679.
[3]"The nucleotide sequence of Saccharomyces cerevisiae chromosome IV."
Jacq C., Alt-Moerbe J., Andre B., Arnold W., Bahr A., Ballesta J.P.G., Bargues M., Baron L., Becker A., Biteau N., Bloecker H., Blugeon C., Boskovic J., Brandt P., Brueckner M., Buitrago M.J., Coster F., Delaveau T. expand/collapse author list , del Rey F., Dujon B., Eide L.G., Garcia-Cantalejo J.M., Goffeau A., Gomez-Peris A., Granotier C., Hanemann V., Hankeln T., Hoheisel J.D., Jaeger W., Jimenez A., Jonniaux J.-L., Kraemer C., Kuester H., Laamanen P., Legros Y., Louis E.J., Moeller-Rieker S., Monnet A., Moro M., Mueller-Auer S., Nussbaumer B., Paricio N., Paulin L., Perea J., Perez-Alonso M., Perez-Ortin J.E., Pohl T.M., Prydz H., Purnelle B., Rasmussen S.W., Remacha M.A., Revuelta J.L., Rieger M., Salom D., Saluz H.P., Saiz J.E., Saren A.-M., Schaefer M., Scharfe M., Schmidt E.R., Schneider C., Scholler P., Schwarz S., Soler-Mira A., Urrestarazu L.A., Verhasselt P., Vissers S., Voet M., Volckaert G., Wagner G., Wambutt R., Wedler E., Wedler H., Woelfl S., Harris D.E., Bowman S., Brown D., Churcher C.M., Connor R., Dedman K., Gentles S., Hamlin N., Hunt S., Jones L., McDonald S., Murphy L.D., Niblett D., Odell C., Oliver K., Rajandream M.A., Richards C., Shore L., Walsh S.V., Barrell B.G., Dietrich F.S., Mulligan J.T., Allen E., Araujo R., Aviles E., Berno A., Carpenter J., Chen E., Cherry J.M., Chung E., Duncan M., Hunicke-Smith S., Hyman R.W., Komp C., Lashkari D., Lew H., Lin D., Mosedale D., Nakahara K., Namath A., Oefner P., Oh C., Petel F.X., Roberts D., Schramm S., Schroeder M., Shogren T., Shroff N., Winant A., Yelton M.A., Botstein D., Davis R.W., Johnston M., Andrews S., Brinkman R., Cooper J., Ding H., Du Z., Favello A., Fulton L., Gattung S., Greco T., Hallsworth K., Hawkins J., Hillier L.W., Jier M., Johnson D., Johnston L., Kirsten J., Kucaba T., Langston Y., Latreille P., Le T., Mardis E., Menezes S., Miller N., Nhan M., Pauley A., Peluso D., Rifkin L., Riles L., Taich A., Trevaskis E., Vignati D., Wilcox L., Wohldman P., Vaudin M., Wilson R., Waterston R., Albermann K., Hani J., Heumann K., Kleine K., Mewes H.-W., Zollner A., Zaccaria P.
Nature 387:75-78(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 204508 / S288c.
[4]"The reference genome sequence of Saccharomyces cerevisiae: Then and now."
Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R., Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S., Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.
G3 (Bethesda) 4:389-398(2014) [PubMed] [Europe PMC] [Abstract]
Cited for: GENOME REANNOTATION.
Strain: ATCC 204508 / S288c.
[5]"Global analysis of protein localization in budding yeast."
Huh W.-K., Falvo J.V., Gerke L.C., Carroll A.S., Howson R.W., Weissman J.S., O'Shea E.K.
Nature 425:686-691(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
[6]"Global analysis of protein expression in yeast."
Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N., O'Shea E.K., Weissman J.S.
Nature 425:737-741(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
U27182 Genomic DNA. Translation: AAC49057.1.
X96876 Genomic DNA. Translation: CAA65617.1.
Z74189 Genomic DNA. Translation: CAA98714.1.
BK006938 Genomic DNA. Translation: DAA11717.1.
PIRS64646.
RefSeqNP_010140.1. NM_001180201.1.

3D structure databases

ProteinModelPortalP48445.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid31920. 21 interactions.
IntActP48445. 1 interaction.
MINTMINT-2780539.
STRING4932.YDL141W.

Proteomic databases

MaxQBP48445.
PaxDbP48445.
PeptideAtlasP48445.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiYDL141W; YDL141W; YDL141W.
GeneID851414.
KEGGsce:YDL141W.

Organism-specific databases

CYGDYDL141w.
SGDS000002300. BPL1.

Phylogenomic databases

eggNOGCOG0340.
GeneTreeENSGT00390000002960.
HOGENOMHOG000214585.
KOK01942.
OMAAVVYCKV.
OrthoDBEOG7KQ2BG.

Enzyme and pathway databases

BioCycYEAST:YDL141W-MONOMER.

Gene expression databases

GenevestigatorP48445.

Family and domain databases

Gene3D3.40.50.880. 1 hit.
InterProIPR019197. Biotin-prot_ligase_N.
IPR004408. Biotin_CoA_COase_ligase.
IPR003142. BPL_C.
IPR004143. BPL_LipA_LipB.
IPR029062. Class_I_gatase-like.
[Graphical view]
PANTHERPTHR12835. PTHR12835. 1 hit.
PfamPF02237. BPL_C. 1 hit.
PF03099. BPL_LplA_LipB. 1 hit.
PF09825. BPL_N. 1 hit.
[Graphical view]
SUPFAMSSF52317. SSF52317. 1 hit.
ProtoNetSearch...

Other

NextBio968603.
PROP48445.

Entry information

Entry nameBPL1_YEAST
AccessionPrimary (citable) accession number: P48445
Secondary accession number(s): D6VRK7
Entry history
Integrated into UniProtKB/Swiss-Prot: February 1, 1996
Last sequence update: February 1, 1996
Last modified: June 11, 2014
This is version 115 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Relevant documents

Yeast chromosome IV

Yeast (Saccharomyces cerevisiae) chromosome IV: entries and gene names

Yeast

Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD

SIMILARITY comments

Index of protein domains and families