BIOWF_CORK4
ID BIOWF_CORK4 Reviewed; 720 AA.
AC C4LK80;
DT 27-JUL-2011, integrated into UniProtKB/Swiss-Prot.
DT 07-JUL-2009, sequence version 1.
DT 03-AUG-2022, entry version 68.
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 Name=bioWF; OrderedLocusNames=ckrop_1506;
OS Corynebacterium kroppenstedtii (strain DSM 44385 / JCM 11950 / CIP 105744 /
OS CCUG 35717).
OC Bacteria; Actinobacteria; Corynebacteriales; Corynebacteriaceae;
OC Corynebacterium.
OX NCBI_TaxID=645127;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 44385 / JCM 11950 / CIP 105744 / CCUG 35717;
RX PubMed=18430482; DOI=10.1016/j.jbiotec.2008.03.004;
RA Tauch A., Schneider J., Szczepanowski R., Tilker A., Viehoever P.,
RA Gartemann K.-H., Arnold W., Blom J., Brinkrolf K., Brune I., Goetker S.,
RA Weisshaar B., Goesmann A., Droege M., Puehler A.;
RT "Ultrafast pyrosequencing of Corynebacterium kroppenstedtii DSM44385
RT revealed insights into the physiology of a lipophilic corynebacterium that
RT lacks mycolic acids.";
RL J. Biotechnol. 136:22-30(2008).
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; CP001620; ACR18235.1; -; Genomic_DNA.
DR AlphaFoldDB; C4LK80; -.
DR SMR; C4LK80; -.
DR STRING; 645127.ckrop_1506; -.
DR PRIDE; C4LK80; -.
DR EnsemblBacteria; ACR18235; ACR18235; ckrop_1506.
DR KEGG; ckp:ckrop_1506; -.
DR eggNOG; COG0156; Bacteria.
DR HOGENOM; CLU_028958_0_0_11; -.
DR OMA; RICLTAR; -.
DR UniPathway; UPA00078; -.
DR UniPathway; UPA00999; UER00351.
DR Proteomes; UP000001473; 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 Reference proteome; Transferase.
FT CHAIN 1..720
FT /note="Biotin biosynthesis bifunctional protein BioWF"
FT /id="PRO_0000412104"
FT REGION 1..39
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 9..24
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 25..39
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 314
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 401..402
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000250"
FT BINDING 439
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 488
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000250"
FT BINDING 513..516
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000250"
FT BINDING 564..567
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000250"
FT BINDING 684
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT MOD_RES 567
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000250"
SQ SEQUENCE 720 AA; 77612 MW; 08EC390FCF6CC4C1 CRC64;
MRFSIKMRAS ARVSSSPSTS DGSSGDHTES RDRADRHISG AERIVSASDI MQTVTELEHR
AWTHSNGQPD DVVVSVHRVD EDEITHIPAL TRETRHTHTV DDAHRTITEI LRDAGIRTAE
HALKALTRIR GMRGAMLLDA DTGERRDTKD IRGVRVTALD NDMATGADAA EEMSSSAATK
PYYCEALTLA SKVQYHPAVC AELCISDDPD YTTGYVSTSG RYVRIENIKP MGSPQGGRVF
LVRGTDDEIA DCINYLENTA VIVHGIPWPP QDNHSAHRDE PDAFGAIPAT DIATDLTTFA
EQSLTAWENK GLRRYPLEFS SAPMPRTTVA GSDTLLFSSS NYLGLSEHPD VIAAATEALK
HYGAGTGGSR LTTGNFTIHT STERTLAEFT GYDDAVLFGT GYQANGAALA TLATNIPEAP
STAPANTPGM TIFSDELNHA SLIDGIRMAT RGNAAVRIYP HKDTEHLENA LAQCASPRKL
IVSDGVFSMN GDIAPLPSIM RLARAHGSWV LIDDAHGTGT LGRTGRGIVE YWSDARRQDA
GADSSPGEEL PNDSDLQPDL LVVTASKALG SEGAAVCCST PVAEFLRNRA RGYVFSTSSA
PASVAATQVA VATILREPER VHRLQDNSLY LRNQLREHGI PLVDGTSNST PIIPIFIGDE
ADAVRISQGL SDRGFHVPGI RYPTVARGQA ILRVTTMATH TRDDLDHLVD ALRDLMPHSA
