BIOF_LYSSH
ID BIOF_LYSSH Reviewed; 389 AA.
AC P22806;
DT 01-AUG-1991, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1991, sequence version 1.
DT 03-AUG-2022, entry version 103.
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 AltName: Full=8-amino-7-ketopelargonate synthase;
GN Name=bioF;
OS Lysinibacillus sphaericus (Bacillus sphaericus).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Lysinibacillus.
OX NCBI_TaxID=1421;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 10208 / DSM 5019 / NBRC 3525 / NCIMB 11935 / NRS 966 / 1911;
RX PubMed=2110099; DOI=10.1016/0378-1119(90)90496-e;
RA Gloeckler R., Ohsawa I., Speck D., Ledoux C., Bernard S., Zinsius M.,
RA Villeval D., Kisou T., Kamogawa K., Lemoine Y.;
RT "Cloning and characterization of the Bacillus sphaericus genes controlling
RT the bioconversion of pimelate into dethiobiotin.";
RL Gene 87:63-70(1990).
RN [2]
RP PROTEIN SEQUENCE OF 1-14, FUNCTION AS A 8-AMINO-7-OXONONANOATE SYNTHASE,
RP BIOPHYSICOCHEMICAL PROPERTIES, COFACTOR, AND SUBUNIT.
RX PubMed=1575677; DOI=10.1042/bj2830327;
RA Ploux O., Marquet A.;
RT "The 8-amino-7-oxopelargonate synthase from Bacillus sphaericus.
RT Purification and preliminary characterization of the cloned enzyme
RT overproduced in Escherichia coli.";
RL Biochem. J. 283:327-331(1992).
RN [3]
RP FUNCTION, AND REACTION MECHANISM.
RX PubMed=8617279; DOI=10.1111/j.1432-1033.1996.00301.x;
RA Ploux O., Marquet A.;
RT "Mechanistic studies on the 8-amino-7-oxopelargonate synthase, a pyridoxal-
RT 5'-phosphate-dependent enzyme involved in biotin biosynthesis.";
RL Eur. J. Biochem. 236:301-308(1996).
RN [4]
RP CRYSTALLIZATION.
RX PubMed=15299653; DOI=10.1107/s0907444996001448;
RA Spinelli S., Ploux O., Marquet A., Anguille C., Jelsch C., Cambillau C.,
RA Martinez C.;
RT "Crystallization and preliminary X-ray study of the 8-amino-7-
RT oxopelargonate synthase from Bacillus sphaericus.";
RL Acta Crystallogr. D 52:866-868(1996).
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 (By similarity). Can also
CC use pimeloyl-CoA instead of pimeloyl-ACP as substrate. {ECO:0000250,
CC ECO:0000269|PubMed:1575677, ECO:0000269|PubMed:8617279}.
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:0000269|PubMed:1575677};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=1.0 uM for pimeloyl-CoA (at pH 7.0 and at 37 degrees Celsius)
CC {ECO:0000269|PubMed:1575677};
CC KM=3.0 mM for L-alanine (at pH 7.0 and at 37 degrees Celsius)
CC {ECO:0000269|PubMed:1575677};
CC -!- PATHWAY: Cofactor biosynthesis; biotin biosynthesis.
CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:1575677}.
CC -!- SIMILARITY: Belongs to the class-II pyridoxal-phosphate-dependent
CC aminotransferase family. BioF subfamily. {ECO:0000305}.
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DR EMBL; M29291; AAA22271.1; -; Genomic_DNA.
DR PIR; JQ0512; JQ0512.
DR RefSeq; WP_024362857.1; NZ_UFSZ01000001.1.
DR AlphaFoldDB; P22806; -.
DR SMR; P22806; -.
DR GeneID; 48278542; -.
DR BioCyc; MetaCyc:MON-14018; -.
DR SABIO-RK; P22806; -.
DR UniPathway; UPA00078; -.
DR GO; GO:0008710; F:8-amino-7-oxononanoate synthase activity; IEA:UniProtKB-EC.
DR GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR GO; GO:0009102; P:biotin biosynthetic process; IEA:UniProtKB-UniPathway.
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 1: Evidence at protein level;
KW Biotin biosynthesis; Direct protein sequencing; Pyridoxal phosphate;
KW Transferase.
FT CHAIN 1..389
FT /note="8-amino-7-oxononanoate synthase"
FT /id="PRO_0000163808"
FT BINDING 19
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 106..107
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000250"
FT BINDING 131
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 178
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000250"
FT BINDING 203..206
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000250"
FT BINDING 234..237
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000250"
FT BINDING 351
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT MOD_RES 237
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000250"
SQ SEQUENCE 389 AA; 42531 MW; 7808F3A1A57EB5F6 CRC64;
MNDRFRRELQ VIEEQGLTRK LRLFSTGNES EVVMNGKKFL LFSSNNYLGL ATDSRLKKKA
TEGISKYGTG AGGSRLTTGN FDIHEQLESE IADFKKTEAA IVFSSGYLAN VGVISSVMKA
GDTIFSDAWN HASIIDGCRL SKAKTIVYEH ADMVDLERKL RQSHGDGLKF IVTDGVFSMD
GDIAPLPKIV ELAKEYKAYI MIDDAHATGV LGNDGCGTAD YFGLKDEIDF TVGTLSKAIG
AEGGFVSTSS IAKNYLLNNA RSFIFQTALS PSAIEAAREG ISIIQNEPER RKQLLKNAQY
LRLKLEESGF VMKEGETPII SLIIGGSHEA MQFSAKLLDE GVFIPAIRPP TVPKGSSRLR
ITVMATHTIE QLDMVISKIK KIGKEMGIV
