BIOWF_CUTAS
ID BIOWF_CUTAS Reviewed; 668 AA.
AC D4H9Y2;
DT 27-JUL-2011, integrated into UniProtKB/Swiss-Prot.
DT 18-MAY-2010, sequence version 1.
DT 03-AUG-2022, entry version 59.
DE RecName: Full=Biotin biosynthesis bifunctional protein BioWF;
DE Includes:
DE RecName: Full=6-carboxyhexanoate--CoA ligase;
DE EC=6.2.1.14;
DE AltName: Full=Pimeloyl-CoA synthase;
DE Includes:
DE RecName: Full=8-amino-7-oxononanoate synthase;
DE Short=AONS;
DE EC=2.3.1.47;
DE AltName: Full=7-keto-8-amino-pelargonic acid synthase;
DE Short=7-KAP synthase;
DE AltName: Full=8-amino-7-ketopelargonate synthase;
GN OrderedLocusNames=HMPREF0675_4919;
OS Cutibacterium acnes (strain SK137) (Propionibacterium acnes).
OC Bacteria; Actinobacteria; Propionibacteriales; Propionibacteriaceae;
OC Cutibacterium.
OX NCBI_TaxID=553199;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SK137;
RA Harkins D.M., Madupu R., Durkin A.S., Torralba M., Methe B., Sutton G.G.,
RA Nelson K.E.;
RT "The complete genome of Propionibacterium acnes SK137.";
RL Submitted (MAR-2010) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Catalyzes both the decarboxylative condensation of pimeloyl-
CC [acyl-carrier protein] and L-alanine to produce 8-amino-7-oxononanoate
CC (AON), [acyl-carrier protein], and carbon dioxide, and the
CC transformation of pimelate into pimeloyl-CoA with concomitant
CC hydrolysis of ATP to AMP. {ECO:0000250}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + CoA + heptanedioate = 6-carboxyhexanoyl-CoA + AMP +
CC diphosphate; Xref=Rhea:RHEA:14781, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:33019, ChEBI:CHEBI:36165, ChEBI:CHEBI:57287,
CC ChEBI:CHEBI:57360, ChEBI:CHEBI:456215; EC=6.2.1.14;
CC -!- CATALYTIC ACTIVITY:
CC Reaction=6-carboxyhexanoyl-[ACP] + H(+) + L-alanine = (8S)-8-amino-7-
CC oxononanoate + CO2 + holo-[ACP]; Xref=Rhea:RHEA:42288, Rhea:RHEA-
CC COMP:9685, Rhea:RHEA-COMP:9955, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526,
CC ChEBI:CHEBI:57972, ChEBI:CHEBI:64479, ChEBI:CHEBI:78846,
CC ChEBI:CHEBI:149468; EC=2.3.1.47;
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000250};
CC -!- PATHWAY: Metabolic intermediate metabolism; pimeloyl-CoA biosynthesis;
CC pimeloyl-CoA from pimelate: step 1/1.
CC -!- PATHWAY: Cofactor biosynthesis; biotin biosynthesis.
CC -!- SUBUNIT: Homodimer. {ECO:0000250}.
CC -!- SIMILARITY: In the N-terminal section; belongs to the BioW family.
CC {ECO:0000305}.
CC -!- SIMILARITY: In the C-terminal section; belongs to the class-II
CC pyridoxal-phosphate-dependent aminotransferase family. BioF subfamily.
CC {ECO:0000305}.
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DR EMBL; CP001977; ADD99092.1; -; Genomic_DNA.
DR AlphaFoldDB; D4H9Y2; -.
DR SMR; D4H9Y2; -.
DR EnsemblBacteria; ADD99092; ADD99092; HMPREF0675_4919.
DR KEGG; pak:HMPREF0675_4919; -.
DR HOGENOM; CLU_028958_0_0_11; -.
DR OMA; RICLTAR; -.
DR UniPathway; UPA00078; -.
DR UniPathway; UPA00999; UER00351.
DR GO; GO:0042410; F:6-carboxyhexanoate-CoA ligase activity; IEA:UniProtKB-EC.
DR GO; GO:0008710; F:8-amino-7-oxononanoate synthase activity; IEA:UniProtKB-EC.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR GO; GO:0009102; P:biotin biosynthetic process; IEA:UniProtKB-UniPathway.
DR Gene3D; 3.40.640.10; -; 1.
DR Gene3D; 3.90.1150.10; -; 1.
DR InterPro; IPR004839; Aminotransferase_I/II.
DR InterPro; IPR005499; BioW.
DR InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
DR Pfam; PF00155; Aminotran_1_2; 1.
DR Pfam; PF03744; BioW; 1.
DR SUPFAM; SSF53383; SSF53383; 1.
PE 3: Inferred from homology;
KW ATP-binding; Biotin biosynthesis; Ligase; Magnesium;
KW Multifunctional enzyme; Nucleotide-binding; Pyridoxal phosphate;
KW Transferase.
FT CHAIN 1..668
FT /note="Biotin biosynthesis bifunctional protein BioWF"
FT /id="PRO_0000412106"
FT BINDING 293
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 380..381
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000250"
FT BINDING 405
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 451
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000250"
FT BINDING 476..479
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000250"
FT BINDING 507..510
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000250"
FT MOD_RES 510
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000250"
SQ SEQUENCE 668 AA; 70822 MW; 80E7AF2CB014E185 CRC64;
MVFNCYPVAN AEESPMSSQN PTTVAWWSVR MRATGTLDDE PYHVSGAESL VAPGMIEQTV
AGLTQRALAP GHTVKARQVR VSLDQLDVEP TIIPALPTEL KECPDPVAAR QYFVDVLSRF
VPHPAEALRV LTEGPTMRGA AMVEAGTDRR LEADPLRGVR VTKFGDLTES APGASLAHKK
HHHEAVLLAS KVAAAPGVLA EFCISDDPHY TRGYVCVDGV YTTVTNVKAD GDPNGGRVIL
VDTARADPTT ITTWLENHPV LIGPATASSQ KATSWHGHLC GRLNAWRAAG LERRPRTFCS
AQDPDAVTTD GPALLFSSSD YLGLSTEPKV QQAMNNTVRR LGSSSGGSRL TTGTSVAHHQ
AEHEIAAWLG YPQAVFMASG YQANIATIQL LADPHVTVIS DAENHASLID GCRLARARTV
VVPHADLDVI DTALDCVTTD RALVLTEGVY SMGGDVAPVG ELVEIAHRHG ALVVVDDAHG
IGTVGPTGRG ATEELPASQR PDVLLGTASK ALGVEGGFAC LDETLATLMR NCARGYVFSS
APSPVVAAGV AAAVEYLRTD TRRVCSLQAN VAQARLLLAE ADLIPPSAAH DRGPIIRIPV
GPESRAVAAQ EELARRGLMV GAIRYPAVAR GDAILRICLT ARHTDEHIRI LVTSLREVLD
GALSDAPR
