ID   BICOA_NEIMA             Reviewed;         592 AA.
AC   Q9JWI7; A1IPI6;
DT   09-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2000, sequence version 1.
DT   10-JUN-2026, entry version 123.
DE   RecName: Full=Bifunctional enzyme BirA/CoaX;
DE   Includes:
DE     RecName: Full=Biotin--[acetyl-CoA-carboxylase] synthetase;
DE              EC=6.3.4.15;
DE     AltName: Full=Biotin--protein ligase;
DE   Includes:
DE     RecName: Full=Type III pantothenate kinase;
DE              EC=2.7.1.33;
DE     AltName: Full=PanK-III;
DE     AltName: Full=Pantothenic acid kinase;
GN   Name=birA/coaX; OrderedLocusNames=NMA0357;
OS   Neisseria meningitidis serogroup A / serotype 4A (strain DSM 15465 /
OS   Z2491).
OC   Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria; Neisseriales;
OC   Neisseriaceae; Neisseria.
OX   NCBI_TaxID=122587;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 15465 / Z2491;
RX   PubMed=10761919; DOI=10.1038/35006655;
RA   Parkhill J., Achtman M., James K.D., Bentley S.D., Churcher C.M.,
RA   Klee S.R., Morelli G., Basham D., Brown D., Chillingworth T., Davies R.M.,
RA   Davis P., Devlin K., Feltwell T., Hamlin N., Holroyd S., Jagels K.,
RA   Leather S., Moule S., Mungall K.L., Quail M.A., Rajandream M.A.,
RA   Rutherford K.M., Simmonds M., Skelton J., Whitehead S., Spratt B.G.,
RA   Barrell B.G.;
RT   "Complete DNA sequence of a serogroup A strain of Neisseria meningitidis
RT   Z2491.";
RL   Nature 404:502-506(2000).
CC   -!- FUNCTION: Activates biotin to form biotinyl-5'-adenylate and transfers
CC       the biotin moiety to biotin-accepting proteins. {ECO:0000250}.
CC   -!- FUNCTION: Catalyzes the phosphorylation of pantothenate (Pan), the
CC       first step in CoA biosynthesis. {ECO:0000250}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=biotin + L-lysyl-[protein] + ATP = N(6)-biotinyl-L-lysyl-
CC         [protein] + AMP + diphosphate + H(+); Xref=Rhea:RHEA:11756,
CC         Rhea:RHEA-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   -!- CATALYTIC ACTIVITY:
CC       Reaction=(R)-pantothenate + ATP = (R)-4'-phosphopantothenate + ADP +
CC         H(+); Xref=Rhea:RHEA:16373, ChEBI:CHEBI:10986, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:29032, ChEBI:CHEBI:30616, ChEBI:CHEBI:456216;
CC         EC=2.7.1.33;
CC   -!- COFACTOR:
CC       Name=NH4(+); Xref=ChEBI:CHEBI:28938; Evidence={ECO:0000250};
CC       Name=K(+); Xref=ChEBI:CHEBI:29103; Evidence={ECO:0000250};
CC       Note=A monovalent cation. Ammonium or potassium. {ECO:0000250};
CC   -!- PATHWAY: Cofactor biosynthesis; coenzyme A biosynthesis; CoA from (R)-
CC       pantothenate: step 1/5.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}.
CC   -!- SIMILARITY: In the N-terminal section; belongs to the biotin--protein
CC       ligase family. {ECO:0000305}.
CC   -!- SIMILARITY: In the C-terminal section; belongs to the type III
CC       pantothenate kinase family. {ECO:0000305}.
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DR   EMBL; AL157959; CAM07655.1; -; Genomic_DNA.
DR   PIR; H82031; H82031.
DR   RefSeq; WP_002246520.1; NC_003116.1.
DR   AlphaFoldDB; Q9JWI7; -.
DR   SMR; Q9JWI7; -.
DR   EnsemblBacteria; CAM07655; CAM07655; NMA0357.
DR   GeneID; 93387002; -.
DR   KEGG; nma:NMA0357; -.
DR   HOGENOM; CLU_476347_0_0_4; -.
DR   UniPathway; UPA00241; UER00352.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0004077; F:biotin--[biotin carboxyl-carrier protein] ligase activity; IEA:UniProtKB-EC.
DR   GO; GO:0004594; F:pantothenate kinase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0015937; P:coenzyme A biosynthetic process; IEA:UniProtKB-UniRule.
DR   CDD; cd24015; ASKHA_NBD_PanK-III; 1.
DR   CDD; cd16442; BPL; 1.
DR   Gene3D; 2.30.30.100; -; 1.
DR   Gene3D; 3.30.420.40; -; 2.
DR   Gene3D; 3.30.930.10; Bira Bifunctional Protein, Domain 2; 1.
DR   HAMAP; MF_01274; Pantothen_kinase_3; 1.
DR   InterPro; IPR045864; aa-tRNA-synth_II/BPL/LPL.
DR   InterPro; IPR043129; ATPase_NBD.
DR   InterPro; IPR004408; Biotin_CoA_COase_ligase.
DR   InterPro; IPR003142; BPL_C.
DR   InterPro; IPR004143; BPL_LPL_catalytic.
DR   InterPro; IPR008988; Transcriptional_repressor_C.
DR   InterPro; IPR004619; Type_III_PanK.
DR   NCBIfam; TIGR00671; baf; 1.
DR   NCBIfam; TIGR00121; birA_ligase; 1.
DR   NCBIfam; NF009862; PRK13325.1; 1.
DR   PANTHER; PTHR12835; BIOTIN PROTEIN LIGASE; 1.
DR   PANTHER; PTHR12835:SF5; BIOTIN--PROTEIN LIGASE; 1.
DR   Pfam; PF02237; BPL_C; 1.
DR   Pfam; PF03099; BPL_LplA_LipB; 1.
DR   Pfam; PF03309; Pan_kinase; 1.
DR   SUPFAM; SSF53067; Actin-like ATPase domain; 2.
DR   SUPFAM; SSF50037; C-terminal domain of transcriptional repressors; 1.
DR   SUPFAM; SSF55681; Class II aaRS and biotin synthetases; 1.
DR   PROSITE; PS51733; BPL_LPL_CATALYTIC; 1.
PE   3: Inferred from homology;
KW   ATP-binding; Biotin; Coenzyme A biosynthesis; Cytoplasm; Kinase; Ligase;
KW   Multifunctional enzyme; Nucleotide-binding; Potassium; Transferase.
FT   CHAIN           1..592
FT                   /note="Bifunctional enzyme BirA/CoaX"
FT                   /id="PRO_0000270883"
FT   DOMAIN          83..259
FT                   /note="BPL/LPL catalytic"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01067"
FT   REGION          1..329
FT                   /note="Biotin--protein ligase"
FT   REGION          336..592
FT                   /note="Type III pantothenate kinase"
FT   ACT_SITE        435
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255"
FT   BINDING         344..351
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250"
FT   BINDING         426
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         433..436
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         458
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255"
FT   BINDING         508
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   592 AA;  64469 MW;  7ED2E0CD3B31C630 CRC64;
     MTVLKPSHWR VLAELADGLP QHVSQLARMA DMKPQQLNGF WQQMPAHIRG LLRQHDGYWR
     LVRPLAVFDA EGLRELGERS GFQTALKHEC ASSNDEILEL ARIAPDKAHK TICVTHLQSK
     GRGRQGRKWS HRLGECLMFS FGWVFDRPQY ELGSLSPVAA VACRRALSRL GLKTQIKWPN
     DLVVGRDKLG GILIETVRTG GKTVAVVGIG INFVLPKEVE NAASVQSLFQ TASRRGNADA
     AVLLETLLAE LDAVLLQYAR DGFAPFVAEY QAANRDHGKA VLLLRDGETV FEGTVKGVDG
     QGVLHLETAE GKQTVVSGEI SLRSDDRPVS VPKRRDSERF LLLDGGNSRL KWAWVENGTF
     ATVGSAPYRD LSPLGAEWAE KVDGNVRIVG CAVCGEFKKA QVQEQLARKI EWLPSSAQAL
     GIRNHYRHPE EHGSDRWFNA LGSRRFSRNA CVVVSCGTAV TVDALTDDGH YLGGTIMPGF
     HLMKESLAVR TANLNRHAGK RYPFPTTTGN AVASGMMDAV CGSVMMMHGR LKEKTGAGKP
     VDVIITGGGA AKVAEALPPA FLAENTVRVA DNLVIHGLLN LIAAEGGESE HT
//