ID A0A0J8VG52_9GAMM Unreviewed; 383 AA.
AC A0A0J8VG52;
DT 14-OCT-2015, integrated into UniProtKB/TrEMBL.
DT 14-OCT-2015, sequence version 1.
DT 24-JAN-2024, entry version 41.
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 ECO:0000313|EMBL:PSW27018.1};
GN ORFNames=C9I94_03295 {ECO:0000313|EMBL:PSW27018.1};
OS Photobacterium swingsii.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC Photobacterium.
OX NCBI_TaxID=680026 {ECO:0000313|EMBL:PSW27018.1, ECO:0000313|Proteomes:UP000240481};
RN [1] {ECO:0000313|EMBL:PSW27018.1, ECO:0000313|Proteomes:UP000240481}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 24669 {ECO:0000313|EMBL:PSW27018.1,
RC ECO:0000313|Proteomes:UP000240481};
RA Butler K.;
RT "Whole genome sequencing of Histamine producing bacteria.";
RL Submitted (JAN-2018) 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:PSW27018.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; PYLZ01000001; PSW27018.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0J8VG52; -.
DR STRING; 680026.AB733_01395; -.
DR OrthoDB; 9807157at2; -.
DR UniPathway; UPA00078; -.
DR Proteomes; UP000240481; 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 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}; Transferase {ECO:0000256|HAMAP-Rule:MF_01693}.
FT DOMAIN 41..377
FT /note="Aminotransferase class I/classII"
FT /evidence="ECO:0000259|Pfam:PF00155"
FT BINDING 22
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01693"
FT BINDING 108..109
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01693"
FT BINDING 133
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01693"
FT BINDING 179
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01693"
FT BINDING 207
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01693"
FT BINDING 233
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01693"
FT BINDING 349
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01693"
FT MOD_RES 236
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01693,
FT ECO:0000256|PIRSR:PIRSR604723-51"
SQ SEQUENCE 383 AA; 42247 MW; 2B2D704004897488 CRC64;
MSRFNEHITQ ALAERHQQGL YRQRVCLERT AQHVNHQGKS LLNFSSNDYL GLAQDPQLLQ
AWQQGLQRFG AGSGASPLVT GFNQPHQQLE QQLAEWLGYD RALLFNSGFS ANQAVLFTLL
NKAHILLQDK LNHASLIEAG MLSPASMKRF KHNDAAHLQR LLCQQVDQTS LVVTEGVFSM
DGDLAPLTDI SNLTQAADAW LMVDDAHGCG VLGEKGRGSC DLAKIKADIL VVTFGKAFGL
QGAAVLCSEE TAEYLVQFAR HFIYSTAMPP AQAYALSQAC ELIQQGDWRR EKLAHLSHEF
EQALDSAIKF INTPSPIKPL LVGCSEKAMQ LSHAINQRGC WVSAIRPPTV PANSARLRIT
LTASHSIEDV KYLATTINEV MYD
//
