ID   BIRA_PARDE              Reviewed;         240 AA.
AC   P29906;
DT   01-APR-1993, integrated into UniProtKB/Swiss-Prot.
DT   01-APR-1993, sequence version 1.
DT   03-AUG-2022, entry version 82.
DE   RecName: Full=Biotin--[acetyl-CoA-carboxylase] ligase;
DE            EC=6.3.4.15;
DE   AltName: Full=Biotin--protein ligase;
DE   AltName: Full=Biotin-[acetyl-CoA carboxylase] synthetase;
GN   Name=birA;
OS   Paracoccus denitrificans.
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales;
OC   Rhodobacteraceae; Paracoccus.
OX   NCBI_TaxID=266;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 13543 / NRRL B-3784 / NRC 449;
RX   PubMed=8422400; DOI=10.1021/bi00054a030;
RA   Xu X., Matsuno-Yagi A., Yagi T.;
RT   "DNA sequencing of the seven remaining structural genes of the gene cluster
RT   encoding the energy-transducing NADH-quinone oxidoreductase of Paracoccus
RT   denitrificans.";
RL   Biochemistry 32:968-981(1993).
CC   -!- FUNCTION: Activates biotin to form biotinyl-5'-adenylate and transfers
CC       the biotin moiety to biotin-accepting proteins. {ECO:0000250}.
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   -!- SIMILARITY: Belongs to the biotin--protein ligase family.
CC       {ECO:0000305}.
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DR   EMBL; L02354; AAA25601.1; -; Genomic_DNA.
DR   PIR; B47751; B47751.
DR   AlphaFoldDB; P29906; -.
DR   SMR; P29906; -.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0004077; F:biotin-[acetyl-CoA-carboxylase] ligase activity; IEA:UniProtKB-EC.
DR   CDD; cd16442; BPL; 1.
DR   Gene3D; 3.30.930.10; -; 1.
DR   InterPro; IPR045864; aa-tRNA-synth_II/BPL/LPL.
DR   InterPro; IPR004408; Biotin_CoA_COase_ligase.
DR   InterPro; IPR003142; BPL_C.
DR   InterPro; IPR004143; BPL_LPL_catalytic.
DR   Pfam; PF02237; BPL_C; 1.
DR   Pfam; PF03099; BPL_LplA_LipB; 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; Biotin; Ligase; Nucleotide-binding.
FT   CHAIN           1..240
FT                   /note="Biotin--[acetyl-CoA-carboxylase] ligase"
FT                   /id="PRO_0000064934"
FT   DOMAIN          1..176
FT                   /note="BPL/LPL catalytic"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01067"
FT   BINDING         7..9
FT                   /ligand="biotin"
FT                   /ligand_id="ChEBI:CHEBI:57586"
FT                   /evidence="ECO:0000250"
FT   BINDING         30
FT                   /ligand="biotin"
FT                   /ligand_id="ChEBI:CHEBI:57586"
FT                   /evidence="ECO:0000250"
FT   BINDING         34..36
FT                   /ligand="biotin"
FT                   /ligand_id="ChEBI:CHEBI:57586"
FT                   /evidence="ECO:0000250"
FT   BINDING         102
FT                   /ligand="biotin"
FT                   /ligand_id="ChEBI:CHEBI:57586"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   240 AA;  24407 MW;  9FD9184ACC1221D8 CRC64;
     MLARTDSTNA EALKLAPGLS GSAWVLAREQ FAGRGRRGRE WVMPAGNFAG TLVLRPQGGA
     LAAAQLSFVA ALALYDALGL ACGPAARLAI KWPNDVLLNG GKVAGILLES SGSGPGVQAV
     AVGIGVNLAG APDAGAVEPG ATPPVSVQGE TGHAVDPEEF LDLLAPAFAR WQAQLDTYGF
     APIRNAWLAR AARLGEPIIA RTGTAESHGI FEGIDDSGAL ILRGPAGRQV IPAAEVFFGG