BIOF_ALKOO
ID BIOF_ALKOO Reviewed; 395 AA.
AC A8MEX7;
DT 28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT 04-DEC-2007, sequence version 1.
DT 03-AUG-2022, entry version 80.
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=Clos_0909;
OS Alkaliphilus oremlandii (strain OhILAs) (Clostridium oremlandii (strain
OS OhILAs)).
OC Bacteria; Firmicutes; Clostridia; Eubacteriales; Clostridiaceae;
OC Alkaliphilus.
OX NCBI_TaxID=350688;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=OhILAs;
RA 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 Chain P., Malfatti S., Shin M., Vergez L., Schmutz J., Larimer F., Land M.,
RA Hauser L., Kyrpides N., Mikhailova N., Stolz J.F., Dawson A., Fisher E.,
RA Crable B., Perera E., Lisak J., Ranganathan M., Basu P., Richardson P.;
RT "Complete genome of Alkaliphilus oremlandii OhILAs.";
RL Submitted (OCT-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. {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; CP000853; ABW18456.1; -; Genomic_DNA.
DR RefSeq; WP_012158768.1; NC_009922.1.
DR AlphaFoldDB; A8MEX7; -.
DR SMR; A8MEX7; -.
DR STRING; 350688.Clos_0909; -.
DR EnsemblBacteria; ABW18456; ABW18456; Clos_0909.
DR KEGG; aoe:Clos_0909; -.
DR eggNOG; COG0156; Bacteria.
DR HOGENOM; CLU_015846_11_0_9; -.
DR OMA; MDTHGFG; -.
DR OrthoDB; 479874at2; -.
DR UniPathway; UPA00078; -.
DR Proteomes; UP000000269; 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_0000380893"
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; 43281 MW; B4D3D9D35CFAAD04 CRC64;
MSNVHELNFL KEKIQELKDQ GVYRQLPVLE GPNEAESILN GKKVINLSSN NYLGFANHPR
LKKAAIEAVE KYGVGSGAVR TIVGNMDIHE ILDKKLAEFK REEAVMSFQS GFNCNAGTIQ
AITEKGDLII SDELNHASII DGARLSRADK TIFKHADMNN LEEVLKANRD KYRNMLIITD
GVFSMDGDIA PLPDIVGLAE KYNAMTYVDD AHGSGVLGES GRGTVDHFGL HGRVDFTIGT
LSKAIGVVGG YVAGSATMRD WLSHRGRPLL FSTSLPPAAI AAITEAINML MTTTEYTDRL
WDNAKYFKAK MSQLGFNIGN SQTPITPVII GDEAKTMEFS RKLLENGVFV SAIVFPTVPK
GTGRLRCMVT AGHTKEQLDR AVETFKKVGE EMNLL
