BIOF_THEPX
ID BIOF_THEPX Reviewed; 395 AA.
AC B0K590;
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 {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=Teth514_0779;
OS Thermoanaerobacter sp. (strain X514).
OC Bacteria; Firmicutes; Clostridia; Thermoanaerobacterales;
OC Thermoanaerobacteraceae; Thermoanaerobacter;
OC unclassified Thermoanaerobacter.
OX NCBI_TaxID=399726;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=X514;
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., 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., Kim E., Hemme C., Fields M.W., He Z., Zhou J., Richardson P.;
RT "Complete sequence of Thermoanaerobacter sp. X514.";
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.
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; CP000923; ABY92083.1; -; Genomic_DNA.
DR RefSeq; WP_009052998.1; NC_010320.1.
DR AlphaFoldDB; B0K590; -.
DR SMR; B0K590; -.
DR EnsemblBacteria; ABY92083; ABY92083; Teth514_0779.
DR KEGG; tex:Teth514_0779; -.
DR HOGENOM; CLU_015846_11_0_9; -.
DR OMA; MDTHGFG; -.
DR UniPathway; UPA00078; -.
DR Proteomes; UP000002155; 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..395
FT /note="8-amino-7-oxononanoate synthase"
FT /id="PRO_0000381124"
FT BINDING 111..112
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000250|UniProtKB:P12998"
FT BINDING 136
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P12998"
FT BINDING 184
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000250|UniProtKB:P12998"
FT BINDING 212
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000250|UniProtKB:P12998"
FT BINDING 240
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000250|UniProtKB:P12998"
FT BINDING 357
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P12998"
FT MOD_RES 243
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000250|UniProtKB:P12998"
SQ SEQUENCE 395 AA; 43452 MW; 4FFA02692FAACC36 CRC64;
MSSIHDLDFI KEKLEELKKA GVYRKLTVLE SPSGPRSIID GKKVINLSSN 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
