ID   BIOF_ALKMQ              Reviewed;         395 AA.
AC   A6TU88;
DT   28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT   21-AUG-2007, sequence version 1.
DT   03-AUG-2022, entry version 81.
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=Amet_3634;
OS   Alkaliphilus metalliredigens (strain QYMF).
OC   Bacteria; Firmicutes; Clostridia; Eubacteriales; Clostridiaceae;
OC   Alkaliphilus.
OX   NCBI_TaxID=293826;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=QYMF;
RX   PubMed=27811105; DOI=10.1128/genomea.01226-16;
RA   Hwang C., Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA   Glavina Del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA   Chertkov O., Brettin T., Bruce D., Han C., Schmutz J., Larimer F.,
RA   Land M.L., Hauser L., Kyrpides N., Mikhailova N., Ye Q., Zhou J.,
RA   Richardson P., Fields M.W.;
RT   "Complete genome sequence of Alkaliphilus metalliredigens strain QYMF, an
RT   alkaliphilic and metal-reducing bacterium isolated from borax-contaminated
RT   leachate ponds.";
RL   Genome Announc. 4:0-0(2016).
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; CP000724; ABR49756.1; -; Genomic_DNA.
DR   RefSeq; WP_012064716.1; NC_009633.1.
DR   AlphaFoldDB; A6TU88; -.
DR   SMR; A6TU88; -.
DR   STRING; 293826.Amet_3634; -.
DR   EnsemblBacteria; ABR49756; ABR49756; Amet_3634.
DR   KEGG; amt:Amet_3634; -.
DR   eggNOG; COG0156; Bacteria.
DR   HOGENOM; CLU_015846_11_0_9; -.
DR   OMA; MDTHGFG; -.
DR   OrthoDB; 479874at2; -.
DR   UniPathway; UPA00078; -.
DR   Proteomes; UP000001572; 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_0000380892"
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;  43258 MW;  BF2641F314F6CD6F CRC64;
     MNNVHELQFL KEKIQELKND GVYRKLPILE GPNEAEIMLN GKKVINLSSN NYLGFANHPQ
     IKKAAIDAVE KYGVGAGAVR TIVGNMDIHE ELERVLAEFK REEAVMVFQS GFNCNAGTIQ
     AVTEKGDLII SDQLNHASII DGARLSRADK TVFKHADMDN LEQVLKENQD KYRNKLIITD
     GVFSMDGDIA PLPDIVELAE KYGAMTYVDD AHGSGVLGEN GRGTVDHFGL HGRVDFTIGT
     LSKAIGVIGG YVAGSHTMKE WLSHRGRPLL FSTSLPPAAV GSIIEAVKLL MSTTEYTDRL
     WDNAKYFKEK ISQLGFDIGH SGTPITPVII GEEGKAMAFS KKLLENGVFV SGIIFPTVAK
     GTGRVRCMVT AGHTKEQLDR AVEVFKKVGQ EMDLL