BIOF_SALPB
ID BIOF_SALPB Reviewed; 385 AA.
AC A9MTI7;
DT 28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT 05-FEB-2008, 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=SPAB_02724;
OS Salmonella paratyphi B (strain ATCC BAA-1250 / SPB7).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Salmonella.
OX NCBI_TaxID=1016998;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-1250 / SPB7;
RG The Salmonella enterica serovar Paratyphi B Genome Sequencing Project;
RA McClelland M., Sanderson E.K., Porwollik S., Spieth J., Clifton W.S.,
RA Fulton R., Cordes M., Wollam A., Shah N., Pepin K., Bhonagiri V., Nash W.,
RA Johnson M., Thiruvilangam P., Wilson R.;
RL Submitted (NOV-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; CP000886; ABX68102.1; -; Genomic_DNA.
DR RefSeq; WP_000118944.1; NC_010102.1.
DR AlphaFoldDB; A9MTI7; -.
DR SMR; A9MTI7; -.
DR KEGG; spq:SPAB_02724; -.
DR PATRIC; fig|1016998.12.peg.2577; -.
DR HOGENOM; CLU_015846_11_2_6; -.
DR OMA; HYHASGI; -.
DR BioCyc; SENT1016998:SPAB_RS11065-MON; -.
DR UniPathway; UPA00078; -.
DR Proteomes; UP000008556; 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..385
FT /note="8-amino-7-oxononanoate synthase"
FT /id="PRO_0000381101"
FT BINDING 21
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01693"
FT BINDING 108..109
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01693"
FT BINDING 133
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01693"
FT BINDING 179
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01693"
FT BINDING 207
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 352
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 385 AA; 41912 MW; 1DD97878EABC3094 CRC64;
MSWQQRVDDA LTARRATDTL RRRYVVSQGA GRWLVANGRQ YLNFSSNDYL GLSQHPQIIR
AWQQAATRFG VGSGGSGHIS GYSVAHQALE EELAQWLGYP RALLFISGFA ANQAVITALM
KKNDRIVADR LSHASLLEAA NLSPAQLRRF IHNDTQHLSR LLQSPSVGQQ LVVTEGVYSM
DGDSAPLAEI QHIARRHHAW LLVDDAHGIG VTGDEGRGTC WLRGVKPELL VVTFGKGFGV
SGAAVLCSES VADYLLQFAR HLVYSTSMPP AQAQALSASL AVIRSDEGGE RREKLAALVQ
RFRAGVNASR FTLLNAHSAI QPLIVGDNSR ALRLAEALRQ QGCWATAIRP PTVPVGTARL
RLTLTQAHEA CDIDRLLEVL HGAGE
