BIOF_THEP3
ID BIOF_THEP3 Reviewed; 395 AA.
AC B0KC20;
DT 28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT 18-MAR-2008, sequence version 1.
DT 03-AUG-2022, entry version 79.
DE RecName: Full=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 Short=KAPA synthase;
DE AltName: Full=8-amino-7-ketopelargonate synthase;
DE AltName: Full=Alpha-oxoamine synthase;
GN OrderedLocusNames=Teth39_0287;
OS Thermoanaerobacter pseudethanolicus (strain ATCC 33223 / 39E) (Clostridium
OS thermohydrosulfuricum).
OC Bacteria; Firmicutes; Clostridia; Thermoanaerobacterales;
OC Thermoanaerobacteraceae; Thermoanaerobacter.
OX NCBI_TaxID=340099;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 33223 / DSM 2355 / 39E;
RA Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E.,
RA Tice H., Pitluck S., Bruce D., Goodwin L., Saunders E., Brettin T.,
RA Detter J.C., Han C., Schmutz J., Larimer F., Land M., Hauser L.,
RA Kyrpides N., Lykidis A., Hemme C., Fields M.W., He Z., Zhou J.,
RA Richardson P.;
RT "Complete sequence of Thermoanaerobacter pseudethanolicus 39E.";
RL Submitted (JAN-2008) 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; CP000924; ABY93956.1; -; Genomic_DNA.
DR RefSeq; WP_003867784.1; NC_010321.1.
DR AlphaFoldDB; B0KC20; -.
DR SMR; B0KC20; -.
DR STRING; 340099.Teth39_0287; -.
DR PRIDE; B0KC20; -.
DR EnsemblBacteria; ABY93956; ABY93956; Teth39_0287.
DR KEGG; tpd:Teth39_0287; -.
DR eggNOG; COG0156; Bacteria.
DR HOGENOM; CLU_015846_11_0_9; -.
DR OMA; MDTHGFG; -.
DR UniPathway; UPA00078; -.
DR Proteomes; UP000002156; 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..395
FT /note="8-amino-7-oxononanoate synthase"
FT /id="PRO_0000381123"
FT BINDING 24
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 111..112
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000250"
FT BINDING 136
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 184
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000250"
FT BINDING 209..212
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000250"
FT BINDING 240..243
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000250"
FT BINDING 357
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT MOD_RES 243
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000250"
SQ SEQUENCE 395 AA; 43453 MW; 8521E0B700489F73 CRC64;
MSSIHDLDFI KEKLEELKKA GVYRKLTVLE SPSGPRSIID GKEVINLSSN NYLGLANHPR
LKKAAIEAIE KWGVGAGAVR TIIGNMTIHE ELERKLAEFK REEAVLTFQS GFTANMGVIQ
AVVDKGDVII SDELNHASII DGCRLSRADV VIYKHSDMED LERVLKEVKD KYRVKMIITD
GVFSMDGDIA KLPEIVKLAE KYSAITYVDD AHASGVLGES GRGSADHFNL HGRIDIQIGT
LSKAIGVVGG YVAGKRELIE WLNHRGRPFL FSTALPPAAV AASIEAINIL SESDALTRKL
WDNAKYFKEK LKSLGFDTGK SETPITPVII GEETKALEFS RKLFEEGVFA QGIVYPTVPK
NKARVRTIVT AAHTKEDLDA ALKAFEKVGK QLNII
