ID BIOF_ACICJ Reviewed; 381 AA.
AC A5FZN8;
DT 28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT 12-JUN-2007, sequence version 1.
DT 27-MAR-2024, entry version 88.
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=Acry_1868;
OS Acidiphilium cryptum (strain JF-5).
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodospirillales;
OC Acetobacteraceae; Acidiphilium.
OX NCBI_TaxID=349163;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JF-5;
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA Sims D., Brettin T., Bruce D., Han C., Schmutz J., Larimer F., Land M.,
RA Hauser L., Kyrpides N., Kim E., Magnuson T., Richardson P.;
RT "Complete sequence of chromosome of Acidiphilium cryptum JF-5.";
RL Submitted (MAY-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: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; CP000697; ABQ31070.1; -; Genomic_DNA.
DR RefSeq; WP_012039683.1; NC_009484.1.
DR AlphaFoldDB; A5FZN8; -.
DR SMR; A5FZN8; -.
DR STRING; 349163.Acry_1868; -.
DR KEGG; acr:Acry_1868; -.
DR eggNOG; COG0156; Bacteria.
DR HOGENOM; CLU_015846_11_0_5; -.
DR UniPathway; UPA00078; -.
DR Proteomes; UP000000245; 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; 3.90.1150.10; Aspartate Aminotransferase, domain 1; 1.
DR Gene3D; 3.40.640.10; Type I PLP-dependent aspartate aminotransferase-like (Major domain); 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 NCBIfam; TIGR00858; bioF; 1.
DR PANTHER; PTHR13693:SF100; 8-AMINO-7-OXONONANOATE SYNTHASE; 1.
DR PANTHER; PTHR13693; CLASS II AMINOTRANSFERASE/8-AMINO-7-OXONONANOATE SYNTHASE; 1.
DR Pfam; PF00155; Aminotran_1_2; 1.
DR SUPFAM; SSF53383; PLP-dependent transferases; 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..381
FT /note="Putative 8-amino-7-oxononanoate synthase"
FT /id="PRO_0000380884"
FT BINDING 22
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 109..110
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000250"
FT BINDING 134
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 182
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000250"
FT BINDING 207..210
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000250"
FT BINDING 233..236
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000250"
FT BINDING 345
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT MOD_RES 236
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000250"
SQ SEQUENCE 381 AA; 40007 MW; 246E65ECBE315D05 CRC64;
MTTLDQFATD KLARLEAGAL RRRLRPTARA PGAVLERDGQ RLISFSCNDY LNLSTHPAVI
DAAIDAARRH GAGAGASRLV TGDHPLYCAL EARLAALKQT EDAVVFGSGF LANTGIIPAL
MAREDAIFVD ELAHACIWAG ARLSGAALHV FRHNDLAHLA ELLAAHRQAA RHAMVVTDGV
FSMDGDLAPV GEMLALAKAH DAWLMTDDAH GIGVINEGRG SAHGHDVPLQ MGTLSKAVGS
YGGYLCASHV VCELIRNRAR SFVYTTGLPP AVVGASIAAL DLIATDPAMC AAPLAHARRF
CAALGLPPAE SPIVPLLLGT AERALAAQAV LEAAGFLVAA IRPPTVPEGT ARLRFAFTAC
HAPDDIDRLA QLVHDRILVT A
//
