BIOF_METPP
ID BIOF_METPP Reviewed; 396 AA.
AC A2SD53;
DT 28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT 06-MAR-2007, sequence version 1.
DT 03-AUG-2022, entry version 84.
DE RecName: Full=8-amino-7-oxononanoate synthase {ECO:0000255|HAMAP-Rule:MF_01693};
DE Short=AONS {ECO:0000255|HAMAP-Rule:MF_01693};
DE EC=2.3.1.47 {ECO:0000255|HAMAP-Rule:MF_01693};
DE AltName: Full=7-keto-8-amino-pelargonic acid synthase {ECO:0000255|HAMAP-Rule:MF_01693};
DE Short=7-KAP synthase {ECO:0000255|HAMAP-Rule:MF_01693};
DE Short=KAPA synthase {ECO:0000255|HAMAP-Rule:MF_01693};
DE AltName: Full=8-amino-7-ketopelargonate synthase {ECO:0000255|HAMAP-Rule:MF_01693};
GN Name=bioF {ECO:0000255|HAMAP-Rule:MF_01693}; OrderedLocusNames=Mpe_A0530;
OS Methylibium petroleiphilum (strain ATCC BAA-1232 / LMG 22953 / PM1).
OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales; Methylibium.
OX NCBI_TaxID=420662;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-1232 / LMG 22953 / PM1;
RX PubMed=17158667; DOI=10.1128/jb.01259-06;
RA Kane S.R., Chakicherla A.Y., Chain P.S.G., Schmidt R., Shin M.W.,
RA Legler T.C., Scow K.M., Larimer F.W., Lucas S.M., Richardson P.M.,
RA Hristova K.R.;
RT "Whole-genome analysis of the methyl tert-butyl ether-degrading beta-
RT proteobacterium Methylibium petroleiphilum PM1.";
RL J. Bacteriol. 189:1931-1945(2007).
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:0000255|HAMAP-
CC Rule:MF_01693}.
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; Evidence={ECO:0000255|HAMAP-
CC Rule:MF_01693};
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_01693};
CC -!- PATHWAY: Cofactor biosynthesis; biotin biosynthesis.
CC {ECO:0000255|HAMAP-Rule:MF_01693}.
CC -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_01693}.
CC -!- SIMILARITY: Belongs to the class-II pyridoxal-phosphate-dependent
CC aminotransferase family. BioF subfamily. {ECO:0000255|HAMAP-
CC Rule:MF_01693}.
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DR EMBL; CP000555; ABM93492.1; -; Genomic_DNA.
DR RefSeq; WP_011828130.1; NC_008825.1.
DR AlphaFoldDB; A2SD53; -.
DR SMR; A2SD53; -.
DR STRING; 420662.Mpe_A0530; -.
DR PRIDE; A2SD53; -.
DR EnsemblBacteria; ABM93492; ABM93492; Mpe_A0530.
DR KEGG; mpt:Mpe_A0530; -.
DR eggNOG; COG0156; Bacteria.
DR HOGENOM; CLU_015846_11_2_4; -.
DR OMA; HYHASGI; -.
DR OrthoDB; 479874at2; -.
DR UniPathway; UPA00078; -.
DR Proteomes; UP000000366; Chromosome.
DR GO; GO:0008710; F:8-amino-7-oxononanoate synthase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0030170; F:pyridoxal phosphate binding; IEA:UniProtKB-UniRule.
DR GO; GO:0009102; P:biotin biosynthetic process; IEA:UniProtKB-UniRule.
DR Gene3D; 3.40.640.10; -; 1.
DR Gene3D; 3.90.1150.10; -; 1.
DR HAMAP; MF_01693; BioF_aminotrans_2; 1.
DR InterPro; IPR004839; Aminotransferase_I/II.
DR InterPro; IPR004723; AONS_Archaea/Proteobacteria.
DR InterPro; IPR022834; AONS_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.
PE 3: Inferred from homology;
KW Biotin biosynthesis; Pyridoxal phosphate; Reference proteome; Transferase.
FT CHAIN 1..396
FT /note="8-amino-7-oxononanoate synthase"
FT /id="PRO_0000381027"
FT BINDING 23
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01693"
FT BINDING 110..111
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01693"
FT BINDING 135
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01693"
FT BINDING 182
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01693"
FT BINDING 210
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01693"
FT BINDING 242
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01693"
FT BINDING 359
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01693"
FT MOD_RES 245
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01693"
SQ SEQUENCE 396 AA; 41946 MW; 74E44B59A30CC3C2 CRC64;
MPPDIHDVFG SALAALDTQQ LRRHRRVVSA LDGAMVQADT QPRLAFAGND YLGLSQHPAL
IEAARQGAAR YGVGATASPL ICGHSPAHEA LEQELARFVG LPRALYFYAG YAANAGAIPA
LVERGDALIS DALNHACLID GARLSRADLT VYPHNDLAAL ERALVAARGA RRRLVVADAV
FSMDGDLAPL PEMLALCERH DAWLYVDDAH GFGVLGEGGR GSLSHWRVPT DAMSSRLIYM
ATLGKAAGVA GAFIAGAPAV IEWLVQKART FFFATGAPPM IAEALRASLQ VIESEGWRRE
RLLQLRTRLA CGLAALPWPA PASQSAIQPL LLGDNGTALR VMAALDAQGI WVPAIRPPTV
PDGTARLRIS MSAAHTPDDV DRLCAALLAA SARPPV
