BIOF_AQUAE
ID BIOF_AQUAE Reviewed; 373 AA.
AC O66875;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1998, sequence version 1.
DT 03-AUG-2022, entry version 127.
DE RecName: Full=Putative 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 AltName: Full=8-amino-7-ketopelargonate synthase;
GN Name=bioF; OrderedLocusNames=aq_626;
OS Aquifex aeolicus (strain VF5).
OC Bacteria; Aquificae; Aquificales; Aquificaceae; Aquifex.
OX NCBI_TaxID=224324;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=VF5;
RX PubMed=9537320; DOI=10.1038/32831;
RA Deckert G., Warren P.V., Gaasterland T., Young W.G., Lenox A.L.,
RA Graham D.E., Overbeek R., Snead M.A., Keller M., Aujay M., Huber R.,
RA Feldman R.A., Short J.M., Olsen G.J., Swanson R.V.;
RT "The complete genome of the hyperthermophilic bacterium Aquifex aeolicus.";
RL Nature 392:353-358(1998).
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; AE000657; AAC06836.1; -; Genomic_DNA.
DR PIR; G70355; G70355.
DR RefSeq; NP_213435.1; NC_000918.1.
DR RefSeq; WP_010880373.1; NC_000918.1.
DR AlphaFoldDB; O66875; -.
DR SMR; O66875; -.
DR STRING; 224324.aq_626; -.
DR PRIDE; O66875; -.
DR EnsemblBacteria; AAC06836; AAC06836; aq_626.
DR KEGG; aae:aq_626; -.
DR PATRIC; fig|224324.8.peg.508; -.
DR eggNOG; COG0156; Bacteria.
DR HOGENOM; CLU_015846_11_0_0; -.
DR InParanoid; O66875; -.
DR OMA; GDHAIAP; -.
DR OrthoDB; 479874at2; -.
DR UniPathway; UPA00078; -.
DR Proteomes; UP000000798; Chromosome.
DR GO; GO:0008710; F:8-amino-7-oxononanoate synthase activity; IBA:GO_Central.
DR GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR GO; GO:0009102; P:biotin biosynthetic process; IBA:GO_Central.
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; 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 PROSITE; PS00599; AA_TRANSFER_CLASS_2; 1.
PE 3: Inferred from homology;
KW Biotin biosynthesis; Pyridoxal phosphate; Reference proteome; Transferase.
FT CHAIN 1..373
FT /note="Putative 8-amino-7-oxononanoate synthase"
FT /id="PRO_0000163807"
FT BINDING 18
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 93..94
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000250"
FT BINDING 118
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 166
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000250"
FT BINDING 191..194
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000250"
FT BINDING 220..223
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000250"
FT BINDING 337
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT MOD_RES 223
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000250"
SQ SEQUENCE 373 AA; 42532 MW; 536B34A5D5F84401 CRC64;
MRWIEEELKR IKEANLYRER ILLEGVKDFC SNDYLGLRKH PEVVEESIRV LKEAGLGSGA
SQLVSGYTKH HRELEEKLAE FKGTESCVLF GSGFLANVGT IPALVEEGDL VLSDELNHAS
IIDGVRLSKA QKRVFKHKDY EELEEFLKKN RKKFRRVLII TDTVFSMDGD VADLKRLTQI
CEEYDCMLYI DEAHTTGTIG KGGLDYFGIE HKEYIIVMGT LSKALGSYGA FVCGTKLLID
YLVNKARSLI FSTSLPPSVC AGAKKAIEII EENPKLIEFL RKKEKEILEI LEQFSLDYKY
YSTPIIPIMV YDEKETVRIK EELLKEGVFI QAIRYPTVPK GKARLRLTAS LNYTRKDLEF
LKNALEKVLK GRA
