BICOA_NEIMB
ID BICOA_NEIMB Reviewed; 592 AA.
AC Q9JXF1;
DT 09-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 109.
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=NMB2075;
OS Neisseria meningitidis serogroup B (strain MC58).
OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; Neisseriaceae;
OC Neisseria.
OX NCBI_TaxID=122586;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MC58;
RX PubMed=10710307; DOI=10.1126/science.287.5459.1809;
RA Tettelin H., Saunders N.J., Heidelberg J.F., Jeffries A.C., Nelson K.E.,
RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., Nelson W.C.,
RA Gwinn M.L., DeBoy R.T., Peterson J.D., Hickey E.K., Haft D.H.,
RA Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., Mason T.M.,
RA Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., Cotton M.D.,
RA Utterback T.R., Khouri H.M., Qin H., Vamathevan J.J., Gill J., Scarlato V.,
RA Masignani V., Pizza M., Grandi G., Sun L., Smith H.O., Fraser C.M.,
RA Moxon E.R., Rappuoli R., Venter J.C.;
RT "Complete genome sequence of Neisseria meningitidis serogroup B strain
RT MC58.";
RL Science 287:1809-1815(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}.
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; AE002098; AAF42394.1; -; Genomic_DNA.
DR PIR; B81009; B81009.
DR RefSeq; NP_275065.1; NC_003112.2.
DR RefSeq; WP_002225711.1; NC_003112.2.
DR AlphaFoldDB; Q9JXF1; -.
DR SMR; Q9JXF1; -.
DR STRING; 122586.NMB2075; -.
DR PaxDb; Q9JXF1; -.
DR EnsemblBacteria; AAF42394; AAF42394; NMB2075.
DR KEGG; nme:NMB2075; -.
DR PATRIC; fig|122586.8.peg.2655; -.
DR HOGENOM; CLU_476347_0_0_4; -.
DR OMA; RPAGKRY; -.
DR UniPathway; UPA00241; UER00352.
DR Proteomes; UP000000425; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0004077; F:biotin-[acetyl-CoA-carboxylase] ligase activity; IBA:GO_Central.
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; Reference proteome;
KW Transferase.
FT CHAIN 1..592
FT /note="Bifunctional enzyme BirA/CoaX"
FT /id="PRO_0000270884"
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; 64701 MW; 9E27421DA2B41DE3 CRC64;
MTVLKLSHWR VLAELADGLP QHVSQLARMA DMKPQQLNGF WQQMPAHIRG LLRQHDGYWR
LVRPLAVFDA EGLRELGERS GFQTALKHEC ASSNDEILEL ARIAPDKAHK TICVTHLQSK
GRGRQGRKWS HRLGECLMFS FGWVFDRPQY ELGSLSPVAA VACRRALSRL GLDVQIKWPN
DLVVGRDKLG GILIETVRTG GKTVAVVGIG INFVLPKEVE NAASVQSLFQ TASRRGNADA
AVLLETLLVE LDAVLLQYAR DGFAPFVAEY QAANRDHGKA VLLLRDGETV FEGTVKGVDG
QGVLHLETAE GKQTVVSGEI SLRSDDRPVS VPKRRDSERF LLLDGGNSRL KWAWVENGTF
ATVGSAPYRD LSPLGAEWAE KADGNVRIVG CAVCGEFKKA QVQEQLARKI EWLPSSAQAL
GIRNHYRHPE EHGSDRWFNA LGSRRFSRNA CVVVSCGTAV TVDALTDDGH YLGGTIMPGF
HLMKESLAVR TANLNRHAGK RYPFPTTTGN AVASGMMDAV CGSVMMMHGR LKEKTGAGKP
VDVIITGGGA AKVAEALPPA FLAENTVRVA DNLVIYGLLN MIAAEGREYE HI
