BIOF_BACLD
ID BIOF_BACLD Reviewed; 379 AA.
AC Q65ML1; Q62Y04;
DT 28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT 25-OCT-2004, sequence version 1.
DT 03-AUG-2022, entry version 112.
DE RecName: Full=Putative 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=bioF; OrderedLocusNames=BLi00768, BL00954;
OS Bacillus licheniformis (strain ATCC 14580 / DSM 13 / JCM 2505 / CCUG 7422 /
OS NBRC 12200 / NCIMB 9375 / NCTC 10341 / NRRL NRS-1264 / Gibson 46).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX NCBI_TaxID=279010;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 14580 / DSM 13 / JCM 2505 / CCUG 7422 / NBRC 12200 / NCIMB 9375
RC / NCTC 10341 / NRRL NRS-1264 / Gibson 46;
RX PubMed=15383718; DOI=10.1159/000079829;
RA Veith B., Herzberg C., Steckel S., Feesche J., Maurer K.H., Ehrenreich P.,
RA Baeumer S., Henne A., Liesegang H., Merkl R., Ehrenreich A., Gottschalk G.;
RT "The complete genome sequence of Bacillus licheniformis DSM13, an organism
RT with great industrial potential.";
RL J. Mol. Microbiol. Biotechnol. 7:204-211(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 14580 / DSM 13 / JCM 2505 / CCUG 7422 / NBRC 12200 / NCIMB 9375
RC / NCTC 10341 / NRRL NRS-1264 / Gibson 46;
RX PubMed=15461803; DOI=10.1186/gb-2004-5-10-r77;
RA Rey M.W., Ramaiya P., Nelson B.A., Brody-Karpin S.D., Zaretsky E.J.,
RA Tang M., Lopez de Leon A., Xiang H., Gusti V., Clausen I.G., Olsen P.B.,
RA Rasmussen M.D., Andersen J.T., Joergensen P.L., Larsen T.S., Sorokin A.,
RA Bolotin A., Lapidus A., Galleron N., Ehrlich S.D., Berka R.M.;
RT "Complete genome sequence of the industrial bacterium Bacillus
RT licheniformis and comparisons with closely related Bacillus species.";
RL Genome Biol. 5:R77.1-R77.12(2004).
CC -!- FUNCTION: Catalyzes the decarboxylative condensation of pimeloyl-[acyl-
CC carrier protein] and L-alanine to produce 8-amino-7-oxononanoate (AON),
CC [acyl-carrier protein], and carbon dioxide. {ECO:0000250}.
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=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000250};
CC -!- PATHWAY: Cofactor biosynthesis; biotin biosynthesis.
CC -!- SUBUNIT: Homodimer. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the class-II pyridoxal-phosphate-dependent
CC aminotransferase family. BioF subfamily. {ECO:0000305}.
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DR EMBL; CP000002; AAU22354.1; -; Genomic_DNA.
DR EMBL; AE017333; AAU39703.1; -; Genomic_DNA.
DR RefSeq; WP_003179689.1; NC_006322.1.
DR AlphaFoldDB; Q65ML1; -.
DR SMR; Q65ML1; -.
DR STRING; 279010.BL00954; -.
DR PRIDE; Q65ML1; -.
DR EnsemblBacteria; AAU22354; AAU22354; BL00954.
DR GeneID; 66217093; -.
DR KEGG; bld:BLi00768; -.
DR KEGG; bli:BL00954; -.
DR eggNOG; COG0156; Bacteria.
DR HOGENOM; CLU_015846_11_3_9; -.
DR OMA; HYHASGI; -.
DR OrthoDB; 479874at2; -.
DR BioCyc; BLIC279010:BLI_RS03820-MON; -.
DR UniPathway; UPA00078; -.
DR Proteomes; UP000000606; Chromosome.
DR GO; GO:0008710; F:8-amino-7-oxononanoate synthase activity; IEA:UniProtKB-EC.
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; IPR001917; Aminotrans_II_pyridoxalP_BS.
DR InterPro; IPR004839; Aminotransferase_I/II.
DR InterPro; IPR004723; AONS_Archaea/Proteobacteria.
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 SUPFAM; SSF53383; SSF53383; 1.
DR TIGRFAMs; TIGR00858; bioF; 1.
DR PROSITE; PS00599; AA_TRANSFER_CLASS_2; 1.
PE 3: Inferred from homology;
KW Biotin biosynthesis; Pyridoxal phosphate; Reference proteome; Transferase.
FT CHAIN 1..379
FT /note="Putative 8-amino-7-oxononanoate synthase"
FT /id="PRO_0000380918"
FT BINDING 21
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 97..98
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000250"
FT BINDING 122
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 169
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000250"
FT BINDING 194..197
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000250"
FT BINDING 223..226
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000250"
FT BINDING 340
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT MOD_RES 226
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000250"
SQ SEQUENCE 379 AA; 41209 MW; C9CB203EA08F20AF CRC64;
MRIDEWLSSR LAKTKAAGLY RSLKLPQAER TNWASNDYLG LANDKRLIHA AETALRRFGA
GSTGSRLTSG NTAWHEKLER KIAGFKQTEA ALLFSSGYLA NVGVLSSLPE KGDVILSDQL
NHASIIDGCR LSKADTVVYR HKDMNDLEEK LRAAQSRARR FIVTDGVFSM DGTIAPLDEI
MLLAKQYRAF VIVDDAHATG VLGEAGRGTS EYFGVSPDVV IGTLSKAVGA EGGFVAGSKT
LIDFLLNHAR TFIFQTAVPP ASCAAACKAL DIIEDSRAKR RLLQSSVNTI KRSLVDIGFT
VNGEDTPIIP VMIGDPQKAV QFANGLKEKG IEAPAIRPPT VAEGESRIRL TVTAERRLKD
IEDLLEGFKL MGRELNLVK
