BICOA_NEIG1
ID BICOA_NEIG1 Reviewed; 592 AA.
AC Q5F5C8;
DT 09-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT 15-MAR-2005, sequence version 1.
DT 03-AUG-2022, entry version 102.
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=NGO2001;
OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090).
OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; Neisseriaceae;
OC Neisseria.
OX NCBI_TaxID=242231;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700825 / FA 1090;
RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F.,
RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C.,
RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S.,
RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.;
RT "The complete genome sequence of Neisseria gonorrhoeae.";
RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases.
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; AE004969; AAW90609.1; -; Genomic_DNA.
DR RefSeq; WP_010951380.1; NC_002946.2.
DR RefSeq; YP_209021.1; NC_002946.2.
DR AlphaFoldDB; Q5F5C8; -.
DR SMR; Q5F5C8; -.
DR STRING; 242231.NGO_2001; -.
DR EnsemblBacteria; AAW90609; AAW90609; NGO_2001.
DR KEGG; ngo:NGO_2001; -.
DR PATRIC; fig|242231.10.peg.2413; -.
DR HOGENOM; CLU_476347_0_0_4; -.
DR OMA; RPAGKRY; -.
DR UniPathway; UPA00241; UER00352.
DR Proteomes; UP000000535; 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; Reference proteome;
KW Transferase.
FT CHAIN 1..592
FT /note="Bifunctional enzyme BirA/CoaX"
FT /id="PRO_0000270882"
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; 64167 MW; 1FEA35BF638D2BF6 CRC64;
MTVLKPSHWR VLAELADGLP QHVSQLAREA DMKPQQLNGF WQQMPAHIRG LLRQHDGYWR
LVRPLAVFDA EGLRDLGERS GFQTALKHEC ASSNDEILEL ARIAPDKAHK TICVTHLQSK
GRGRQGRKWS HRLGECLMFS FGWAFDRPQY ELGSLSPVAA LACRRALGCL GLETQIKWPN
DLVVGRDKLG GILIETVRAG GKTVAVVGIG INFVLPKEVE NAASVQSLFQ TASRRGNADA
AVLLETLLAE LGAVLEQYAE EGFAPFLNEY ETANRDHGKA VLLLRDGETV CEGTVKGVDG
RGVLHLETAE GEQTVVSGEI SLRPDNRSVS VPKRPDSERF LLLEGGNSRL KWAWVENGTF
ATVGSAPYRD LSPLGAEWAE KADGNVRIVG CAVCGESKKA QVKEQLARKI EWLPSSAQAL
GIRNHYRHPE EHGSDRWFNA LGSRRFSRNA CVVVSCGTAV TVDALTDDGH YLGGTIMPGF
HLMKESLAVR TANLNRPAGK RYPFPTTTGN AVASGMMDAV CGSIMMMHGR LKEKNGAGKP
VDVIITGGGA AKVAEALPPA FLAENTVRVA DNLVIHGLLN LIAAEGGESE HA
