BIOF_HAEDU
ID BIOF_HAEDU Reviewed; 387 AA.
AC Q7VL09;
DT 28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2003, sequence version 1.
DT 03-AUG-2022, entry version 107.
DE RecName: Full=8-amino-7-oxononanoate synthase {ECO:0000250|UniProtKB:P12998};
DE Short=AONS {ECO:0000250|UniProtKB:P12998};
DE EC=2.3.1.47 {ECO:0000250|UniProtKB:P12998};
DE AltName: Full=7-keto-8-amino-pelargonic acid synthase {ECO:0000250|UniProtKB:P12998};
DE Short=7-KAP synthase {ECO:0000250|UniProtKB:P12998};
DE Short=KAPA synthase {ECO:0000250|UniProtKB:P12998};
DE AltName: Full=8-amino-7-ketopelargonate synthase {ECO:0000250|UniProtKB:P12998};
GN Name=bioF {ECO:0000250|UniProtKB:P12998}; OrderedLocusNames=HD_1684;
OS Haemophilus ducreyi (strain 35000HP / ATCC 700724).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales;
OC Pasteurellaceae; Haemophilus.
OX NCBI_TaxID=233412;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=35000HP / ATCC 700724;
RA Munson R.S. Jr., Ray W.C., Mahairas G., Sabo P., Mungur R., Johnson L.,
RA Nguyen D., Wang J., Forst C., Hood L.;
RT "The complete genome sequence of Haemophilus ducreyi.";
RL Submitted (JUN-2003) 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.
CC {ECO:0000250|UniProtKB:P12998}.
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 Evidence={ECO:0000250|UniProtKB:P12998};
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000250|UniProtKB:P12998};
CC -!- PATHWAY: Cofactor biosynthesis; biotin biosynthesis.
CC {ECO:0000250|UniProtKB:P12998}.
CC -!- SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:P12998}.
CC -!- SIMILARITY: Belongs to the class-II pyridoxal-phosphate-dependent
CC aminotransferase family. BioF subfamily.
CC {ECO:0000250|UniProtKB:P12998}.
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DR EMBL; AE017143; AAP96450.1; -; Genomic_DNA.
DR RefSeq; WP_010945482.1; NC_002940.2.
DR AlphaFoldDB; Q7VL09; -.
DR SMR; Q7VL09; -.
DR STRING; 233412.HD_1684; -.
DR PRIDE; Q7VL09; -.
DR EnsemblBacteria; AAP96450; AAP96450; HD_1684.
DR KEGG; hdu:HD_1684; -.
DR eggNOG; COG0156; Bacteria.
DR HOGENOM; CLU_015846_11_2_6; -.
DR OMA; YPYFRPI; -.
DR UniPathway; UPA00078; -.
DR Proteomes; UP000001022; 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; 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 PROSITE; PS00599; AA_TRANSFER_CLASS_2; 1.
PE 3: Inferred from homology;
KW Acyltransferase; Biotin biosynthesis; Pyridoxal phosphate;
KW Reference proteome; Transferase.
FT CHAIN 1..387
FT /note="8-amino-7-oxononanoate synthase"
FT /id="PRO_0000381003"
FT BINDING 109..110
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000250|UniProtKB:P12998"
FT BINDING 134
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P12998"
FT BINDING 182
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000250|UniProtKB:P12998"
FT BINDING 214
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000250|UniProtKB:P12998"
FT BINDING 242
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000250|UniProtKB:P12998"
FT BINDING 359
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P12998"
FT MOD_RES 245
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000250|UniProtKB:P12998"
SQ SEQUENCE 387 AA; 43362 MW; B42AD05D0BDDC0D6 CRC64;
MSYFAEKLAE LAQVGLNRSL PEIEHQGKWI IAQNRKMLNF SSNDYLGLAS DTELQQTFLQ
NILQEAPLHQ WFSSSSSRLL TGNFPIYARL EQLLAQRFQR ETALLFNSGY HANIGILPAL
VDKHSLILAD KLVHASLIDG TRLAGCDFYR YQHNNLAHLT QLLEKHTGQY RRIIIVTESV
FSMDGDVAPL PQLVALKKAF SSQTEVMLYV DEAHAIGVYG ANGLGMAEFF DCIDDIDLLV
GTFGKALASM GAYLICDQLI KQYLVNTMRP LIFSTALAPI NVAWTHFLFE KLPQFQPKRA
HLARLSQQLK QAVELRNGDT LATQSCIVPF VVGENRQAVE KSQYLQQQGY YCLPIRPPTV
PKGTARIRFS LTADLTEAEL NGLIACL
