BICOA_NEIMA
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 03-AUG-2022, entry version 110.
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; Proteobacteria; Betaproteobacteria; Neisseriales; Neisseriaceae;
OC 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=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 -!- 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 KEGG; nma:NMA0357; -.
DR HOGENOM; CLU_476347_0_0_4; -.
DR OMA; RPAGKRY; -.
DR BioCyc; NMEN122587:NMA_RS01825-MON; -.
DR UniPathway; UPA00241; UER00352.
DR Proteomes; UP000000626; Chromosome.
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-[acetyl-CoA-carboxylase] 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 GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR CDD; cd16442; BPL; 1.
DR Gene3D; 3.30.930.10; -; 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 Pfam; PF02237; BPL_C; 1.
DR Pfam; PF03099; BPL_LplA_LipB; 1.
DR Pfam; PF03309; Pan_kinase; 1.
DR SUPFAM; SSF50037; SSF50037; 1.
DR SUPFAM; SSF53067; SSF53067; 2.
DR SUPFAM; SSF55681; SSF55681; 1.
DR TIGRFAMs; TIGR00671; baf; 1.
DR TIGRFAMs; TIGR00121; birA_ligase; 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
