BIOF_BURP0
ID BIOF_BURP0 Reviewed; 394 AA.
AC A3NQS3;
DT 28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT 03-APR-2007, sequence version 1.
DT 03-AUG-2022, entry version 77.
DE RecName: Full=8-amino-7-oxononanoate synthase {ECO:0000255|HAMAP-Rule:MF_01693};
DE Short=AONS {ECO:0000255|HAMAP-Rule:MF_01693};
DE EC=2.3.1.47 {ECO:0000255|HAMAP-Rule:MF_01693};
DE AltName: Full=7-keto-8-amino-pelargonic acid synthase {ECO:0000255|HAMAP-Rule:MF_01693};
DE Short=7-KAP synthase {ECO:0000255|HAMAP-Rule:MF_01693};
DE Short=KAPA synthase {ECO:0000255|HAMAP-Rule:MF_01693};
DE AltName: Full=8-amino-7-ketopelargonate synthase {ECO:0000255|HAMAP-Rule:MF_01693};
GN Name=bioF {ECO:0000255|HAMAP-Rule:MF_01693};
GN OrderedLocusNames=BURPS1106A_0411;
OS Burkholderia pseudomallei (strain 1106a).
OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Burkholderia; pseudomallei group.
OX NCBI_TaxID=357348;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=1106a;
RX PubMed=20333227; DOI=10.1093/gbe/evq003;
RA Losada L., Ronning C.M., DeShazer D., Woods D., Fedorova N., Kim H.S.,
RA Shabalina S.A., Pearson T.R., Brinkac L., Tan P., Nandi T., Crabtree J.,
RA Badger J., Beckstrom-Sternberg S., Saqib M., Schutzer S.E., Keim P.,
RA Nierman W.C.;
RT "Continuing evolution of Burkholderia mallei through genome reduction and
RT large-scale rearrangements.";
RL Genome Biol. Evol. 2:102-116(2010).
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:0000255|HAMAP-
CC Rule:MF_01693}.
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; Evidence={ECO:0000255|HAMAP-
CC Rule:MF_01693};
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_01693};
CC -!- PATHWAY: Cofactor biosynthesis; biotin biosynthesis.
CC {ECO:0000255|HAMAP-Rule:MF_01693}.
CC -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_01693}.
CC -!- SIMILARITY: Belongs to the class-II pyridoxal-phosphate-dependent
CC aminotransferase family. BioF subfamily. {ECO:0000255|HAMAP-
CC Rule:MF_01693}.
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DR EMBL; CP000572; ABN90185.1; -; Genomic_DNA.
DR RefSeq; WP_004189736.1; NC_009076.1.
DR AlphaFoldDB; A3NQS3; -.
DR SMR; A3NQS3; -.
DR EnsemblBacteria; ABN90185; ABN90185; BURPS1106A_0411.
DR GeneID; 56594628; -.
DR KEGG; bpl:BURPS1106A_0411; -.
DR HOGENOM; CLU_015846_11_2_4; -.
DR OMA; YPYFRPI; -.
DR UniPathway; UPA00078; -.
DR Proteomes; UP000006738; Chromosome I.
DR GO; GO:0008710; F:8-amino-7-oxononanoate synthase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0030170; F:pyridoxal phosphate binding; IEA:UniProtKB-UniRule.
DR GO; GO:0009102; P:biotin biosynthetic process; IEA:UniProtKB-UniRule.
DR Gene3D; 3.40.640.10; -; 1.
DR Gene3D; 3.90.1150.10; -; 1.
DR HAMAP; MF_01693; BioF_aminotrans_2; 1.
DR InterPro; IPR004839; Aminotransferase_I/II.
DR InterPro; IPR004723; AONS_Archaea/Proteobacteria.
DR InterPro; IPR022834; AONS_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.
PE 3: Inferred from homology;
KW Biotin biosynthesis; Pyridoxal phosphate; Transferase.
FT CHAIN 1..394
FT /note="8-amino-7-oxononanoate synthase"
FT /id="PRO_0000380938"
FT BINDING 21
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01693"
FT BINDING 112..113
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01693"
FT BINDING 137
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01693"
FT BINDING 183
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01693"
FT BINDING 211
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01693"
FT BINDING 239
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01693"
FT BINDING 358
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01693"
FT MOD_RES 242
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01693"
SQ SEQUENCE 394 AA; 40699 MW; 6F13182EA9D2A68D CRC64;
MNPLATLEQG LADIDAQGLR RCRRVADTAC GAHMTVDGRA IIGFASNDYL GLAAHPRLVE
AFAEGARRYG SGSGGSHLLG GHSRAHATLE DELAAFSGGF SDAPRALYFS TGYMANLAAL
TALAGRGATI FSDALNHASL IDGARLSRAN VQIYPHGDAD ALDARLRACD APTKLIVSDT
VFSMDGDVAP LARLVALAET HGAWLVVDDA HGFGVLGPQG RGALAAHGLR SPNLVYVGTL
GKAAGVAGAF VVAHETVIEW LVQRARSYIF TTAAPPSVAC AVSASLAVIA SDEGDARRAH
LGALIKRTRA ILRATHWQPV DSHTAVQPLV IGSNEATLAA MAALDAQGLW VPAIRPPTVP
AGTSRLRISL SAAHSFDDLA RLEAALVTPI GAAA
