ID A0A066RT89_9GAMM Unreviewed; 398 AA.
AC A0A066RT89;
DT 03-SEP-2014, integrated into UniProtKB/TrEMBL.
DT 03-SEP-2014, sequence version 1.
DT 24-JAN-2024, entry version 45.
DE RecName: Full=8-amino-7-oxononanoate synthase {ECO:0000256|HAMAP-Rule:MF_01693};
DE Short=AONS {ECO:0000256|HAMAP-Rule:MF_01693};
DE EC=2.3.1.47 {ECO:0000256|HAMAP-Rule:MF_01693};
DE AltName: Full=7-keto-8-amino-pelargonic acid synthase {ECO:0000256|HAMAP-Rule:MF_01693};
DE Short=7-KAP synthase {ECO:0000256|HAMAP-Rule:MF_01693};
DE Short=KAPA synthase {ECO:0000256|HAMAP-Rule:MF_01693};
DE AltName: Full=8-amino-7-ketopelargonate synthase {ECO:0000256|HAMAP-Rule:MF_01693};
GN Name=bioF {ECO:0000256|HAMAP-Rule:MF_01693};
GN ORFNames=EA58_07445 {ECO:0000313|EMBL:KDM92316.1};
OS Photobacterium galatheae.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC Photobacterium.
OX NCBI_TaxID=1654360 {ECO:0000313|EMBL:KDM92316.1, ECO:0000313|Proteomes:UP000027192};
RN [1] {ECO:0000313|EMBL:KDM92316.1, ECO:0000313|Proteomes:UP000027192}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=S2753 {ECO:0000313|EMBL:KDM92316.1,
RC ECO:0000313|Proteomes:UP000027192};
RA Machado H.R., Gram L.;
RT "Draft genome sequence of Photobacterium halotolerans S2753: a solonamide,
RT ngercheumicin and holomycin producer.";
RL Submitted (APR-2014) 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:0000256|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;
CC Evidence={ECO:0000256|ARBA:ARBA00034067, ECO:0000256|HAMAP-
CC Rule:MF_01693};
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000256|ARBA:ARBA00001933,
CC ECO:0000256|HAMAP-Rule:MF_01693, ECO:0000256|PIRSR:PIRSR604723-51};
CC -!- PATHWAY: Cofactor biosynthesis; biotin biosynthesis.
CC {ECO:0000256|ARBA:ARBA00004746, ECO:0000256|HAMAP-Rule:MF_01693}.
CC -!- SUBUNIT: Homodimer. {ECO:0000256|ARBA:ARBA00011738, ECO:0000256|HAMAP-
CC Rule:MF_01693}.
CC -!- SIMILARITY: Belongs to the class-II pyridoxal-phosphate-dependent
CC aminotransferase family. BioF subfamily.
CC {ECO:0000256|ARBA:ARBA00010008, ECO:0000256|HAMAP-Rule:MF_01693}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KDM92316.1}.
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DR EMBL; JMIB01000010; KDM92316.1; -; Genomic_DNA.
DR RefSeq; WP_036750761.1; NZ_JMIB01000010.1.
DR AlphaFoldDB; A0A066RT89; -.
DR STRING; 1654360.EA58_07445; -.
DR OrthoDB; 9807157at2; -.
DR UniPathway; UPA00078; -.
DR Proteomes; UP000027192; Unassembled WGS sequence.
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 CDD; cd06454; KBL_like; 1.
DR Gene3D; 3.90.1150.10; Aspartate Aminotransferase, domain 1; 1.
DR Gene3D; 3.40.640.10; Type I PLP-dependent aspartate aminotransferase-like (Major domain); 1.
DR HAMAP; MF_01693; BioF_aminotrans_2; 1.
DR InterPro; IPR001917; Aminotrans_II_pyridoxalP_BS.
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 NCBIfam; TIGR00858; bioF; 1.
DR PANTHER; PTHR13693:SF100; 8-AMINO-7-OXONONANOATE SYNTHASE; 1.
DR PANTHER; PTHR13693; CLASS II AMINOTRANSFERASE/8-AMINO-7-OXONONANOATE SYNTHASE; 1.
DR Pfam; PF00155; Aminotran_1_2; 1.
DR SUPFAM; SSF53383; PLP-dependent transferases; 1.
DR PROSITE; PS00599; AA_TRANSFER_CLASS_2; 1.
PE 3: Inferred from homology;
KW Acyltransferase {ECO:0000313|EMBL:KDM92316.1};
KW Biotin biosynthesis {ECO:0000256|ARBA:ARBA00022756, ECO:0000256|HAMAP-
KW Rule:MF_01693};
KW Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898, ECO:0000256|HAMAP-
KW Rule:MF_01693};
KW Transferase {ECO:0000256|HAMAP-Rule:MF_01693, ECO:0000313|EMBL:KDM92316.1}.
FT DOMAIN 43..380
FT /note="Aminotransferase class I/classII"
FT /evidence="ECO:0000259|Pfam:PF00155"
FT BINDING 21
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01693"
FT BINDING 109..110
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01693"
FT BINDING 134
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01693"
FT BINDING 182
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01693"
FT BINDING 210
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01693"
FT BINDING 236
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01693"
FT BINDING 352
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01693"
FT MOD_RES 239
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01693,
FT ECO:0000256|PIRSR:PIRSR604723-51"
SQ SEQUENCE 398 AA; 43302 MW; 64934E38C17C93AC CRC64;
MPLKHRIAQA LNQREAQGLY RRRKTLTRQA SSVRQANQTQ PSLNFSSNDY LGLAQDPTLI
AAWQQGLSKY GAGSGASPLV TGHHTPHQSL EARLAEWLGF ERALLFSTGF SANQAVLFAL
LEKGDLLIQD KLNHASLMEA GMLSPAIMRR FAHNDADALH KLLSQNTDEN MARLVVTEGV
FSMDGDQAPL ADIAARCHTS QSWLMVDDAH GCGILGDEGR GSCHQAGIRP DILIVTFGKA
FGMQGAAVLC SQDVAEYLIQ FARHYVYSTA MPPAQAYALC TACDLVQAGD WRREKLLTLG
TILEETLLPE VGLVSTATPI KPVLLGESER ALTLSALLSE KGFWVSAIRP PTVPVHQARL
RITLTASHSE AHVRELANHL NASFEEVQDA ANPSEQPD
//
