BIOF_THEM4
ID BIOF_THEM4 Reviewed; 391 AA.
AC A6LMP4;
DT 28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT 24-JUL-2007, sequence version 1.
DT 03-AUG-2022, entry version 96.
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=Tmel_1346;
OS Thermosipho melanesiensis (strain DSM 12029 / CIP 104789 / BI429).
OC Bacteria; Thermotogae; Thermotogales; Fervidobacteriaceae; Thermosipho.
OX NCBI_TaxID=391009;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 12029 / CIP 104789 / BI429;
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E.,
RA Tice H., Pitluck S., Chertkov O., Brettin T., Bruce D., Detter J.C.,
RA Han C., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N.,
RA Mikhailova N., Nelson K., Gogarten J.P., Noll K., Richardson P.;
RT "Complete sequence of Thermosipho melanesiensis BI429.";
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.
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; CP000716; ABR31195.1; -; Genomic_DNA.
DR RefSeq; WP_012057554.1; NC_009616.1.
DR AlphaFoldDB; A6LMP4; -.
DR SMR; A6LMP4; -.
DR STRING; 391009.Tmel_1346; -.
DR EnsemblBacteria; ABR31195; ABR31195; Tmel_1346.
DR KEGG; tme:Tmel_1346; -.
DR eggNOG; COG0156; Bacteria.
DR HOGENOM; CLU_015846_11_0_0; -.
DR OMA; MDTHGFG; -.
DR UniPathway; UPA00078; -.
DR Proteomes; UP000001110; 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; Transferase.
FT CHAIN 1..391
FT /note="8-amino-7-oxononanoate synthase"
FT /id="PRO_0000381122"
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; 43502 MW; 9125A9B0EF2ADB2E CRC64;
MFDYSIFAKE IDELKNQGLY TYIRTLESPQ GAWLVIDGKK VLNLCSNNYL GFANEERLKN
AAKQAVEKWG VGPGAVRTIA GTFSLHNELE ETLAKFKKVE ATIFLQSGFV ANQAVIPAIT
NEEDAILSDE LNHASIIDGV RLSKAKRFVW KHRDIKDLEE KLKEAKDARR KLIITDGVFS
MDGDLAPLPE IVELAEKYNA MVMVDDAHGE GVLGSHGRGI VDHFGLHGRV DIEIGTLSKA
FGVLGGYIAG KKELIDYLKQ KARPFLFSSP LSPADTAAAL EATKILQESD ERVKRLWDNA
KYFKEEMKKL GFDTGESETP ITPVMLYDAK LSTQFSKELF EEGIFAQSIG YPTVPKGKAR
IRVMISAVHT KEDLDFALEK FEKVGKKLGV I
