BPL1_SCHPO
ID BPL1_SCHPO Reviewed; 631 AA.
AC O14353;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 03-AUG-2022, entry version 123.
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; ORFNames=SPBC30D10.07c;
OS Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC Schizosaccharomycetes; Schizosaccharomycetales; Schizosaccharomycetaceae;
OC Schizosaccharomyces.
OX NCBI_TaxID=284812;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=972 / ATCC 24843;
RX PubMed=11859360; DOI=10.1038/nature724;
RA Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A.,
RA Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S.,
RA Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M.,
RA Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S.,
RA Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S.,
RA Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D.,
RA Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P.,
RA Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K.,
RA O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M.,
RA Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N.,
RA Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A.,
RA Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R.,
RA Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M.,
RA Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A.,
RA Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A.,
RA Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H.,
RA Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S.,
RA Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C.,
RA Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A.,
RA Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M.,
RA del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S.,
RA Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R.,
RA Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G.,
RA Nurse P.;
RT "The genome sequence of Schizosaccharomyces pombe.";
RL Nature 415:871-880(2002).
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 (By similarity). {ECO:0000250}.
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:0000250}.
CC -!- SIMILARITY: Belongs to the biotin--protein ligase family.
CC {ECO:0000305}.
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DR EMBL; CU329671; CAB10802.1; -; Genomic_DNA.
DR PIR; T40189; T40189.
DR RefSeq; NP_596278.1; NM_001022199.2.
DR AlphaFoldDB; O14353; -.
DR SMR; O14353; -.
DR STRING; 4896.SPBC30D10.07c.1; -.
DR SwissPalm; O14353; -.
DR MaxQB; O14353; -.
DR PaxDb; O14353; -.
DR PRIDE; O14353; -.
DR EnsemblFungi; SPBC30D10.07c.1; SPBC30D10.07c.1:pep; SPBC30D10.07c.
DR GeneID; 2540476; -.
DR KEGG; spo:SPBC30D10.07c; -.
DR PomBase; SPBC30D10.07c; bpl1.
DR VEuPathDB; FungiDB:SPBC30D10.07c; -.
DR eggNOG; KOG1536; Eukaryota.
DR HOGENOM; CLU_006150_1_1_1; -.
DR InParanoid; O14353; -.
DR OMA; DWLHMHQ; -.
DR PhylomeDB; O14353; -.
DR Reactome; R-SPO-196780; Biotin transport and metabolism.
DR PRO; PR:O14353; -.
DR Proteomes; UP000002485; Chromosome II.
DR GO; GO:0005737; C:cytoplasm; ISO:PomBase.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004077; F:biotin-[acetyl-CoA-carboxylase] ligase activity; IBA:GO_Central.
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:0051604; P:protein maturation; NAS:PomBase.
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 TIGRFAMs; TIGR00121; birA_ligase; 1.
DR PROSITE; PS51733; BPL_LPL_CATALYTIC; 1.
PE 3: Inferred from homology;
KW ATP-binding; Cytoplasm; Ligase; Multifunctional enzyme; Nucleotide-binding;
KW Reference proteome.
FT CHAIN 1..631
FT /note="Biotin--protein ligase"
FT /id="PRO_0000315970"
FT DOMAIN 341..553
FT /note="BPL/LPL catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01067"
SQ SEQUENCE 631 AA; 70632 MW; 37E08571359F5112 CRC64;
MNVLIYNGNG ASKICLLRTF QSLLPFVVPL YAMRFVDAST LEKEPWPAST ALLVMPGGRD
MGYCSSFNET IYRKITDFVK RGGAYLGLCA GGYFGSAVVD FRMPDSDLNV VGKRKLQFFP
GTCAGPTFPG FTYDSEDGAR RASIIVDGMQ SSPVHTHIYF NGGGSFLETE NYSNVKVVAR
YQETDFEKSA AIIYVKVGKG NVVLTGIHPE FSAEGSPILD KRDEKTRLEL LSYILKLLGL
KVPKDTSKCG QPTLTDQYLF PNNVETKRFI EKALTNKVKN QDEDTLYTFQ FSDISSEIPE
HQLANLDISA DLSDSDNEIV KIWYGDEEKI CKKAKPSFDL ELYAKLINGC RFGLPIIVAP
VIRSTQTLLD KNYRFLDSTN TGFTVLGNYQ TAGRGRGQNM WVSPYGTLAF SFIINVDAKN
FSTTPIALFQ YLMALAVVRG IREYAPGYEN IPAFIKWPND VYVRVDKGGI NFQGKQYMKL
SGIIVTSNYR KNVLHLVVGC GINVSNLGPT VSLNTLVDEW NKNSDNPRLE KFSFEKLLAS
VLNQFDRYHR LLLEEGFSLI LPEYYQYWLH SNQTVNLASG GKAIIQGITS DFGFLLAQLL
NENNEPTTKV VHLQPDGNSF DLMRNLITRK T
