BIOF_THEAB
ID BIOF_THEAB Reviewed; 391 AA.
AC B7ID58;
DT 28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT 10-FEB-2009, sequence version 1.
DT 03-AUG-2022, entry version 89.
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=THA_1494;
OS Thermosipho africanus (strain TCF52B).
OC Bacteria; Thermotogae; Thermotogales; Fervidobacteriaceae; Thermosipho.
OX NCBI_TaxID=484019;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=TCF52B;
RX PubMed=19124572; DOI=10.1128/jb.01448-08;
RA Nesboe C.L., Bapteste E., Curtis B., Dahle H., Lopez P., Macleod D.,
RA Dlutek M., Bowman S., Zhaxybayeva O., Birkeland N.-K., Doolittle W.F.;
RT "The genome of Thermosipho africanus TCF52B: lateral genetic connections to
RT the Firmicutes and Archaea.";
RL J. Bacteriol. 191:1974-1978(2009).
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; CP001185; ACJ75935.1; -; Genomic_DNA.
DR RefSeq; WP_004101993.1; NC_011653.1.
DR AlphaFoldDB; B7ID58; -.
DR SMR; B7ID58; -.
DR STRING; 484019.THA_1494; -.
DR EnsemblBacteria; ACJ75935; ACJ75935; THA_1494.
DR KEGG; taf:THA_1494; -.
DR eggNOG; COG0156; Bacteria.
DR HOGENOM; CLU_015846_11_0_0; -.
DR OMA; MDTHGFG; -.
DR OrthoDB; 479874at2; -.
DR UniPathway; UPA00078; -.
DR Proteomes; UP000002453; Chromosome.
DR GO; GO:0008710; F:8-amino-7-oxononanoate synthase activity; ISS:UniProtKB.
DR GO; GO:0008890; F:glycine C-acetyltransferase activity; ISS:UniProtKB.
DR GO; GO:0030170; F:pyridoxal phosphate binding; ISS:UniProtKB.
DR GO; GO:0009102; P:biotin biosynthetic process; ISS:UniProtKB.
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; IPR010962; AONS_Archaea/Firmicutes.
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 Pfam; PF00155; Aminotran_1_2; 1.
DR SUPFAM; SSF53383; SSF53383; 1.
DR TIGRFAMs; TIGR00858; bioF; 1.
DR TIGRFAMs; TIGR01825; gly_Cac_T_rel; 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..391
FT /note="8-amino-7-oxononanoate synthase"
FT /id="PRO_0000381120"
FT BINDING 108..109
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000250|UniProtKB:P12998"
FT BINDING 133
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P12998"
FT BINDING 180
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000250|UniProtKB:P12998"
FT BINDING 208
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000250|UniProtKB:P12998"
FT BINDING 236
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000250|UniProtKB:P12998"
FT BINDING 353
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P12998"
FT MOD_RES 239
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000250|UniProtKB:P12998"
SQ SEQUENCE 391 AA; 43479 MW; E03FB70499BC7BC1 CRC64;
MFDYSIFSKE LENLKEQGLY TYIKTLESPQ GAWLTINGKK VLNLCSNNYL GFANEERLKK
AAIEAIEKWG VGPGAVRTIA GTFSLHNELE KTLAEFKKVE ATIFLQSGFV ANQAVIPAIT
NEEDAILSDE LNHASIIDGV RLSKAKRYVW KHRDVKDLEE KLKEAKDARR KLIITDGVFS
MDGDLAPLPE IVELAEKYNA MVMVDDAHGE GVLGSHGRGI VDHFGLHGRV DIEIGTLSKA
FGVLGGYVAG KKELIDYLKQ KARPFLFSSP LSPADTAAAL EATKILQESD DRVKRLWDNA
KYFKEEMKKL GFDTGESETP ITPVMLYDAK LSTNFSKELF EEGIFAQSIG YPTVPKGKAR
IRVMISAVHT KEDLDFALEK FEKVGKKLGV I
