BPL1_YEAST
ID BPL1_YEAST Reviewed; 690 AA.
AC P48445; D6VRK7;
DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1996, sequence version 1.
DT 03-AUG-2022, entry version 169.
DE RecName: Full=Biotin--protein ligase;
DE EC=6.3.4.-;
DE AltName: Full=Biotin apo-protein ligase;
DE Includes:
DE RecName: Full=Biotin--[methylmalonyl-CoA-carboxytransferase] ligase;
DE EC=6.3.4.9;
DE Includes:
DE RecName: Full=Biotin--[propionyl-CoA-carboxylase [ATP-hydrolyzing]] ligase;
DE EC=6.3.4.10;
DE AltName: Full=Holocarboxylase synthetase;
DE Short=HCS;
DE Includes:
DE RecName: Full=Biotin--[methylcrotonoyl-CoA-carboxylase] ligase;
DE EC=6.3.4.11;
DE Includes:
DE RecName: Full=Biotin--[acetyl-CoA-carboxylase] ligase;
DE EC=6.3.4.15;
GN Name=BPL1; Synonyms=ACC2; OrderedLocusNames=YDL141W; ORFNames=D2140;
OS Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX NCBI_TaxID=559292;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=7649444; DOI=10.1111/j.1574-6968.1995.tb07724.x;
RA Cronan J.E. Jr., Wallace J.C.;
RT "The gene encoding the biotin-apoprotein ligase of Saccharomyces
RT cerevisiae.";
RL FEMS Microbiol. Lett. 130:221-230(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 96604 / S288c / FY1679;
RX PubMed=8972577;
RX DOI=10.1002/(sici)1097-0061(199612)12:15<1549::aid-yea42>3.0.co;2-s;
RA Woelfl S., Haneman V., Saluz H.P.;
RT "Analysis of a 26,756 bp segment from the left arm of yeast chromosome
RT IV.";
RL Yeast 12:1549-1554(1996).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169867;
RA Jacq C., Alt-Moerbe J., Andre B., Arnold W., Bahr A., Ballesta J.P.G.,
RA Bargues M., Baron L., Becker A., Biteau N., Bloecker H., Blugeon C.,
RA Boskovic J., Brandt P., Brueckner M., Buitrago M.J., Coster F.,
RA Delaveau T., del Rey F., Dujon B., Eide L.G., Garcia-Cantalejo J.M.,
RA Goffeau A., Gomez-Peris A., Granotier C., Hanemann V., Hankeln T.,
RA Hoheisel J.D., Jaeger W., Jimenez A., Jonniaux J.-L., Kraemer C.,
RA Kuester H., Laamanen P., Legros Y., Louis E.J., Moeller-Rieker S.,
RA Monnet A., Moro M., Mueller-Auer S., Nussbaumer B., Paricio N., Paulin L.,
RA Perea J., Perez-Alonso M., Perez-Ortin J.E., Pohl T.M., Prydz H.,
RA Purnelle B., Rasmussen S.W., Remacha M.A., Revuelta J.L., Rieger M.,
RA Salom D., Saluz H.P., Saiz J.E., Saren A.-M., Schaefer M., Scharfe M.,
RA Schmidt E.R., Schneider C., Scholler P., Schwarz S., Soler-Mira A.,
RA Urrestarazu L.A., Verhasselt P., Vissers S., Voet M., Volckaert G.,
RA Wagner G., Wambutt R., Wedler E., Wedler H., Woelfl S., Harris D.E.,
RA Bowman S., Brown D., Churcher C.M., Connor R., Dedman K., Gentles S.,
RA Hamlin N., Hunt S., Jones L., McDonald S., Murphy L.D., Niblett D.,
RA Odell C., Oliver K., Rajandream M.A., Richards C., Shore L., Walsh S.V.,
RA Barrell B.G., Dietrich F.S., Mulligan J.T., Allen E., Araujo R., Aviles E.,
RA Berno A., Carpenter J., Chen E., Cherry J.M., Chung E., Duncan M.,
RA Hunicke-Smith S., Hyman R.W., Komp C., Lashkari D., Lew H., Lin D.,
RA Mosedale D., Nakahara K., Namath A., Oefner P., Oh C., Petel F.X.,
RA Roberts D., Schramm S., Schroeder M., Shogren T., Shroff N., Winant A.,
RA Yelton M.A., Botstein D., Davis R.W., Johnston M., Andrews S., Brinkman R.,
RA Cooper J., Ding H., Du Z., Favello A., Fulton L., Gattung S., Greco T.,
RA Hallsworth K., Hawkins J., Hillier L.W., Jier M., Johnson D., Johnston L.,
RA Kirsten J., Kucaba T., Langston Y., Latreille P., Le T., Mardis E.,
RA Menezes S., Miller N., Nhan M., Pauley A., Peluso D., Rifkin L., Riles L.,
RA Taich A., Trevaskis E., Vignati D., Wilcox L., Wohldman P., Vaudin M.,
RA Wilson R., Waterston R., Albermann K., Hani J., Heumann K., Kleine K.,
RA Mewes H.-W., Zollner A., Zaccaria P.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome IV.";
RL Nature 387:75-78(1997).
RN [4]
RP GENOME REANNOTATION.
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=24374639; DOI=10.1534/g3.113.008995;
RA Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
RA Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
RA Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.;
RT "The reference genome sequence of Saccharomyces cerevisiae: Then and now.";
RL G3 (Bethesda) 4:389-398(2014).
RN [5]
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX PubMed=14562095; DOI=10.1038/nature02026;
RA Huh W.-K., Falvo J.V., Gerke L.C., Carroll A.S., Howson R.W.,
RA Weissman J.S., O'Shea E.K.;
RT "Global analysis of protein localization in budding yeast.";
RL Nature 425:686-691(2003).
RN [6]
RP LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
RX PubMed=14562106; DOI=10.1038/nature02046;
RA Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N.,
RA O'Shea E.K., Weissman J.S.;
RT "Global analysis of protein expression in yeast.";
RL Nature 425:737-741(2003).
CC -!- FUNCTION: Post-translational modification of specific protein by
CC attachment of biotin. Acts on various carboxylases such as acetyl-CoA-
CC carboxylase, pyruvate carboxylase, propionyl CoA carboxylase, and 3-
CC methylcrotonyl CoA carboxylase.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=apo-[methylmalonyl-CoA:pyruvate carboxytransferase] + ATP +
CC biotin = AMP + diphosphate + H(+) + holo-[methylmalonyl-CoA:pyruvate
CC carboxytransferase]; Xref=Rhea:RHEA:23668, Rhea:RHEA-COMP:10508,
CC Rhea:RHEA-COMP:10509, ChEBI:CHEBI:15378, ChEBI:CHEBI:29969,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:57586,
CC ChEBI:CHEBI:83144, ChEBI:CHEBI:456215; EC=6.3.4.9;
CC -!- CATALYTIC ACTIVITY:
CC Reaction=apo-[propionyl-CoA:carbon-dioxide ligase (ADP-forming)] + ATP
CC + biotin = AMP + diphosphate + H(+) + holo-[propionyl-CoA:carbon-
CC dioxide ligase (ADP-forming)]; Xref=Rhea:RHEA:11204, Rhea:RHEA-
CC COMP:10511, Rhea:RHEA-COMP:10512, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:29969, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019,
CC ChEBI:CHEBI:57586, ChEBI:CHEBI:83144, ChEBI:CHEBI:456215;
CC EC=6.3.4.10;
CC -!- CATALYTIC ACTIVITY:
CC Reaction=apo-[3-methylcrotonoyl-CoA:carbon-dioxide ligase (ADP-
CC forming)] + ATP + biotin = AMP + diphosphate + H(+) + holo-[3-
CC methylcrotonoyl-CoA:carbon-dioxide ligase (ADP-forming)];
CC Xref=Rhea:RHEA:24376, Rhea:RHEA-COMP:10514, Rhea:RHEA-COMP:10515,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:29969, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:33019, ChEBI:CHEBI:57586, ChEBI:CHEBI:83144,
CC ChEBI:CHEBI:456215; EC=6.3.4.11;
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + biotin + L-lysyl-[protein] = AMP + diphosphate + H(+) +
CC N(6)-biotinyl-L-lysyl-[protein]; Xref=Rhea:RHEA:11756, Rhea:RHEA-
CC COMP:9752, Rhea:RHEA-COMP:10505, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:29969, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019,
CC ChEBI:CHEBI:57586, ChEBI:CHEBI:83144, ChEBI:CHEBI:456215;
CC EC=6.3.4.15;
CC -!- SUBUNIT: Monomer. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:14562095}.
CC -!- MISCELLANEOUS: Present with 1970 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the biotin--protein ligase family.
CC {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; U27182; AAC49057.1; -; Genomic_DNA.
DR EMBL; X96876; CAA65617.1; -; Genomic_DNA.
DR EMBL; Z74189; CAA98714.1; -; Genomic_DNA.
DR EMBL; BK006938; DAA11717.1; -; Genomic_DNA.
DR PIR; S64646; S64646.
DR RefSeq; NP_010140.1; NM_001180201.1.
DR AlphaFoldDB; P48445; -.
DR SMR; P48445; -.
DR BioGRID; 31920; 26.
DR IntAct; P48445; 1.
DR MINT; P48445; -.
DR STRING; 4932.YDL141W; -.
DR iPTMnet; P48445; -.
DR MaxQB; P48445; -.
DR PaxDb; P48445; -.
DR PRIDE; P48445; -.
DR EnsemblFungi; YDL141W_mRNA; YDL141W; YDL141W.
DR GeneID; 851414; -.
DR KEGG; sce:YDL141W; -.
DR SGD; S000002300; BPL1.
DR VEuPathDB; FungiDB:YDL141W; -.
DR eggNOG; KOG1536; Eukaryota.
DR GeneTree; ENSGT00390000002960; -.
DR HOGENOM; CLU_006150_1_1_1; -.
DR InParanoid; P48445; -.
DR OMA; DWLHMHQ; -.
DR BioCyc; YEAST:YDL141W-MON; -.
DR Reactome; R-SCE-196780; Biotin transport and metabolism.
DR PRO; PR:P48445; -.
DR Proteomes; UP000002311; Chromosome IV.
DR RNAct; P48445; protein.
DR GO; GO:0005737; C:cytoplasm; HDA:SGD.
DR GO; GO:0005634; C:nucleus; HDA:SGD.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004077; F:biotin-[acetyl-CoA-carboxylase] ligase activity; IMP:SGD.
DR GO; GO:0004078; F:biotin-[methylcrotonoyl-CoA-carboxylase] ligase activity; IEA:UniProtKB-EC.
DR GO; GO:0004079; F:biotin-[methylmalonyl-CoA-carboxytransferase] ligase activity; IEA:UniProtKB-EC.
DR GO; GO:0004080; F:biotin-[propionyl-CoA-carboxylase (ATP-hydrolyzing)] ligase activity; IEA:UniProtKB-EC.
DR GO; GO:0071734; F:biotin-[pyruvate-carboxylase] ligase activity; IDA:SGD.
DR GO; GO:0036211; P:protein modification process; IDA:SGD.
DR CDD; cd16442; BPL; 1.
DR Gene3D; 3.30.930.10; -; 1.
DR Gene3D; 3.40.50.880; -; 1.
DR InterPro; IPR045864; aa-tRNA-synth_II/BPL/LPL.
DR InterPro; IPR019197; Biotin-prot_ligase_N.
DR InterPro; IPR004408; Biotin_CoA_COase_ligase.
DR InterPro; IPR003142; BPL_C.
DR InterPro; IPR004143; BPL_LPL_catalytic.
DR InterPro; IPR029062; Class_I_gatase-like.
DR Pfam; PF02237; BPL_C; 1.
DR Pfam; PF03099; BPL_LplA_LipB; 1.
DR Pfam; PF09825; BPL_N; 1.
DR SUPFAM; SSF52317; SSF52317; 1.
DR SUPFAM; SSF55681; SSF55681; 1.
DR PROSITE; PS51733; BPL_LPL_CATALYTIC; 1.
PE 1: Evidence at protein level;
KW ATP-binding; Cytoplasm; Ligase; Multifunctional enzyme; Nucleotide-binding;
KW Reference proteome.
FT CHAIN 1..690
FT /note="Biotin--protein ligase"
FT /id="PRO_0000064981"
FT DOMAIN 378..606
FT /note="BPL/LPL catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01067"
SQ SEQUENCE 690 AA; 76363 MW; ADA6BFE411C656AB CRC64;
MNVLVYNGPG TTPGSVKHAV ESLRDFLEPY YAVSTVNVKV LQTEPWMSKT SAVVFPGGAD
LPYVQACQPI ISRLKHFVSK QGGVFIGFCA GGYFGTSRVE FAQGDPTMEV SGSRDLRFFP
GTSRGPAYNG FQYNSEAGAR AVKLNLPDGS QFSTYFNGGA VFVDADKFDN VEILATYAEH
PDVPSSDSGK GQSENPAAVV LCTVGRGKVL LTGPHPEFNV RFMRKSTDKH FLETVVENLK
AQEIMRLKFM RTVLTKTGLN CNNDFNYVRA PNLTPLFMAS APNKRNYLQE MENNLAHHGM
HANNVELCSE LNAETDSFQF YRGYRASYDA ASSSLLHKEP DEVPKTVIFP GVDEDIPPFQ
YTPNFDMKEY FKYLNVQNTI GSLLLYGEVV TSTSTILNNN KSLLSSIPES TLLHVGTIQV
SGRGRGGNTW INPKGVCAST AVVTMPLQSP VTNRNISVVF VQYLSMLAYC KAILSYAPGF
SDIPVRIKWP NDLYALSPTY YKRKNLKLVN TGFEHTKLPL GDIEPAYLKI SGLLVNTHFI
NNKYCLLLGC GINLTSDGPT TSLQTWIDIL NEERQQLHLD LLPAIKAEKL QALYMNNLEV
ILKQFINYGA AEILPSYYEL WLHSNQIVTL PDHGNTQAMI TGITEDYGLL IAKELVSGSS
TQFTGNVYNL QPDGNTFDIF KSLIAKKVQS
