P48445 (BPL1_YEAST) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended 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

Organism

Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) [Reference proteome]

Taxonomic identifier

559292 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Fungi › Dikarya › Ascomycota › saccharomyceta › Saccharomycotina › Saccharomycetes › Saccharomycetales › Saccharomycetaceae › Saccharomyces › Saccharomyces cerevisiae

Protein attributes

Sequence length	690 AA.
Sequence status	Complete.
Protein existence	Evidence 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.

Ontologies

Keywords
Cellular component	Cytoplasm
Ligand	ATP-binding Nucleotide-binding
Molecular function	Ligase
Technical term	Complete proteome Multifunctional enzyme Reference proteome
Gene Ontology (GO)
Biological_process	protein biotinylation Inferred from direct assay PubMed 10551847. Source: SGD
Cellular_component	cytoplasm Inferred from direct assay PubMed 11914276Ref.5. Source: SGD nucleus Inferred from direct assay Ref.5. Source: SGD
Molecular_function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW biotin-[acetyl-CoA-carboxylase] ligase activity Inferred from mutant phenotype PubMed 6108218. Source: SGD biotin-[methylcrotonoyl-CoA-carboxylase] ligase activity Inferred from electronic annotation. Source: EC biotin-[methylmalonyl-CoA-carboxytransferase] ligase activity Inferred from electronic annotation. Source: EC biotin-[propionyl-CoA-carboxylase (ATP-hydrolyzing)] ligase activity Inferred from electronic annotation. Source: EC biotin-[pyruvate-carboxylase] ligase activity Inferred from direct assay PubMed 10551847. Source: SGD
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 690	690	Biotin--protein ligase		PRO_0000064981

Sequences

	Sequence		Length	Mass (Da)
	P48445 [UniParc]. Last modified February 1, 1996. Version 1. Checksum: ADA6BFE411C656AB	FASTA	690	76,363
	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

References

	« Hide 'large scale' referencesShow '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. , 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 96604 / S288c / FY1679.
[4]	Saccharomyces Genome Database Submitted (DEC-2009) to the EMBL/GenBank/DDBJ databases 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.
PIR	S64646.
RefSeq	NP_010140.1. NM_001180201.1.
3D structure databases
ProteinModelPortal	P48445.
ModBase	Search...
Protein-protein interaction databases
IntAct	P48445. 1 interaction.
MINT	MINT-2780539.
STRING	4932.YDL141W.
Proteomic databases
PaxDb	P48445.
PeptideAtlas	P48445.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblFungi	YDL141W; YDL141W; YDL141W.
GeneID	851414.
KEGG	sce:YDL141W.
Organism-specific databases
CYGD	YDL141w.
SGD	S000002300. BPL1.
Phylogenomic databases
eggNOG	COG0340.
GeneTree	ENSGT00390000002960.
HOGENOM	HOG000214585.
KO	K01942.
OMA	CAGGYYG.
OrthoDB	EOG4TF3TK.
Gene expression databases
Genevestigator	P48445.
GermOnline	YDL141W. Saccharomyces cerevisiae.
Family and domain databases
InterPro	IPR019197. Biotin-prot_ligase_N. IPR004408. Biotin_CoA_COase_ligase. IPR003142. BPL_C. IPR004143. BPL_LipA_LipB. [Graphical view]
PANTHER	PTHR12835. PTHR12835. 1 hit.
Pfam	PF02237. BPL_C. 1 hit. PF03099. BPL_LplA_LipB. 1 hit. PF09825. BPL_N. 1 hit. [Graphical view]
ProtoNet	Search...
Other
NextBio	968603.

Entry information

Entry name

BPL1_YEAST

Accession

Primary (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:	April 3, 2013
This is version 107 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Fungal Protein Annotation Program