ID   BIOF_PSEA7              Reviewed;         401 AA.
AC   A6UYW1;
DT   28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT   21-AUG-2007, sequence version 1.
DT   03-AUG-2022, entry version 83.
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}; OrderedLocusNames=PSPA7_0601;
OS   Pseudomonas aeruginosa (strain PA7).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=381754;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PA7;
RA   Dodson R.J., Harkins D., Paulsen I.T.;
RL   Submitted (JUN-2007) to the EMBL/GenBank/DDBJ databases.
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; CP000744; ABR81961.1; -; Genomic_DNA.
DR   RefSeq; WP_012074070.1; NC_009656.1.
DR   AlphaFoldDB; A6UYW1; -.
DR   SMR; A6UYW1; -.
DR   EnsemblBacteria; ABR81961; ABR81961; PSPA7_0601.
DR   KEGG; pap:PSPA7_0601; -.
DR   HOGENOM; CLU_015846_11_0_6; -.
DR   OMA; HYHASGI; -.
DR   OrthoDB; 479874at2; -.
DR   UniPathway; UPA00078; -.
DR   Proteomes; UP000001582; Chromosome.
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; IPR001917; Aminotrans_II_pyridoxalP_BS.
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.
DR   PROSITE; PS00599; AA_TRANSFER_CLASS_2; 1.
PE   3: Inferred from homology;
KW   Biotin biosynthesis; Pyridoxal phosphate; Transferase.
FT   CHAIN           1..401
FT                   /note="8-amino-7-oxononanoate synthase"
FT                   /id="PRO_0000381072"
FT   BINDING         19
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01693"
FT   BINDING         106..107
FT                   /ligand="pyridoxal 5'-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:597326"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01693"
FT   BINDING         131
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01693"
FT   BINDING         176
FT                   /ligand="pyridoxal 5'-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:597326"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01693"
FT   BINDING         204
FT                   /ligand="pyridoxal 5'-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:597326"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01693"
FT   BINDING         233
FT                   /ligand="pyridoxal 5'-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:597326"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01693"
FT   BINDING         350
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01693"
FT   MOD_RES         236
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01693"
SQ   SEQUENCE   401 AA;  42271 MW;  5F57B42ADB81D839 CRC64;
     MSFDLASRLA ARRAEDLYRQ RPLLQSAQGP DVVVDGQPLL AFCSNDYLGL ASHPEVIAAL
     RAGAERWGVG GGASHLVVGH SGPHHELELA LAEFTGRPRA LLFSTGYMAN LGAVTALVGK
     GDTVLEDRLN HASLLDAGLL SGARFSRYLH NDPASLAARL DKAEGNTLVV TDGVFSMDGN
     LADLPALAAV AQARGAWLMV DDAHGFGPLG AAGGGIVEHF GLGQEQVPVL IGTLGKGFGT
     AGAFVAGSEE LIETLVQYAR PYIYTTSQPP AVACATLKSL ELLRRESWRR EHLAALIARF
     RRGAEALGLT LMDSFTPIQP ILVGGSRQAV ALADMLRARG IMVGAIRPPT VPANSARLRV
     TLSAAHSEAQ VDRLLEALGE SWRQLSSSLL AEIEAEEGDD A