BIOWF_CUTAK
ID BIOWF_CUTAK Reviewed; 653 AA.
AC Q6A6M4;
DT 27-JUL-2011, integrated into UniProtKB/Swiss-Prot.
DT 13-SEP-2004, sequence version 1.
DT 03-AUG-2022, entry version 100.
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=PPA1866;
OS Cutibacterium acnes (strain DSM 16379 / KPA171202) (Propionibacterium
OS acnes).
OC Bacteria; Actinobacteria; Propionibacteriales; Propionibacteriaceae;
OC Cutibacterium.
OX NCBI_TaxID=267747;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 16379 / KPA171202;
RX PubMed=15286373; DOI=10.1126/science.1100330;
RA Brueggemann H., Henne A., Hoster F., Liesegang H., Wiezer A.,
RA Strittmatter A., Hujer S., Duerre P., Gottschalk G.;
RT "The complete genome sequence of Propionibacterium acnes, a commensal of
RT human skin.";
RL Science 305:671-673(2004).
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; AE017283; AAT83589.1; -; Genomic_DNA.
DR AlphaFoldDB; Q6A6M4; -.
DR SMR; Q6A6M4; -.
DR STRING; 267747.PPA1866; -.
DR EnsemblBacteria; AAT83589; AAT83589; PPA1866.
DR KEGG; pac:PPA1866; -.
DR eggNOG; COG0156; Bacteria.
DR HOGENOM; CLU_028958_0_0_11; -.
DR OMA; RICLTAR; -.
DR UniPathway; UPA00078; -.
DR UniPathway; UPA00999; UER00351.
DR Proteomes; UP000000603; Chromosome.
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..653
FT /note="Biotin biosynthesis bifunctional protein BioWF"
FT /id="PRO_0000412105"
FT BINDING 278
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 365..366
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000250"
FT BINDING 390
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 436
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000250"
FT BINDING 461..464
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000250"
FT BINDING 492..495
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000250"
FT MOD_RES 495
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000250"
SQ SEQUENCE 653 AA; 69153 MW; 75729FE28BFFBAF6 CRC64;
MLSQNPTTVA WWSVRMRATG TLDDEPYHVS GAESLVAPGM IEQTVAGLTQ RALAPGHTVK
ARQVRVSLDQ LDVEPTIIPA LPTELKECPD PVAARQYFVD VLSRFVPHPA EALRVLTEGP
TMRGAAMVEA GTDRRLEADP LRGVRVTKFG DLTESAPGAS LAHKKHHHEA VLLASKVAAA
PGVLAEFCIS DDPHYTRGYV CVDGVYTTVT NVKADGDPNG GRVILVDTAR ADPTTITTWL
ENHPVLIGPA TASSQKATSW HGHLCGRLNA WRAAGLERRP RTFCSAQDPD AVTTDGPALL
FSSSDYLGLS TEPKVQQAMN NTVRRLGSSS GGSRLTTGTS VAHHQAEHEI AAWLGYPQAV
FMASGYQANI ATIQLLADPH VTVISDAENH ASLIDGCRLA RARTVVVPHA DLDAIDTALD
CVTTDRALVL TEGVYSMGGD VAPVGELVEI AHRHGALVVV DDAHGIGTVG PTGRGATEEL
PASQRPDVLL GTASKALGVE GGFACVDETL ATLMRNCARG YVFSSAPSPV VAAGVAAAVE
YLRTDTRRVC SLQANVAQAR LLLAEADLIP PSAAHDRGPI IRIPVGPESR AVAAQEELAR
RGLMVGAIRY PAVARGDAIL RICLTARHTD EHIRILVTSL REVLDGALSD APR
