BIOF_BURM1
ID BIOF_BURM1 Reviewed; 394 AA.
AC A9AE46;
DT 28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT 15-JAN-2008, sequence version 1.
DT 03-AUG-2022, entry version 90.
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};
GN OrderedLocusNames=Bmul_0373, BMULJ_02881;
OS Burkholderia multivorans (strain ATCC 17616 / 249).
OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Burkholderia; Burkholderia cepacia complex.
OX NCBI_TaxID=395019;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 17616 / 249;
RA Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E.,
RA Tice H., Pitluck S., Chain P., Malfatti S., Shin M., Vergez L., Schmutz J.,
RA Larimer F., Land M., Hauser L., Kyrpides N., Kim E., Tiedje J.,
RA Richardson P.;
RT "Complete sequence of chromosome 1 of Burkholderia multivorans ATCC
RT 17616.";
RL Submitted (OCT-2007) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 17616 / 249;
RA Ohtsubo Y., Yamashita A., Kurokawa K., Takami H., Yuhara S., Nishiyama E.,
RA Endo R., Miyazaki R., Ono A., Yano K., Ito M., Sota M., Yuji N.,
RA Hattori M., Tsuda M.;
RT "Complete genome sequence of Burkholderia multivorans ATCC 17616.";
RL Submitted (APR-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: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; CP000868; ABX14068.1; -; Genomic_DNA.
DR EMBL; AP009385; BAG44769.1; -; Genomic_DNA.
DR RefSeq; WP_012212612.1; NC_010804.1.
DR PDB; 5VNX; X-ray; 1.65 A; A/B/C=1-393.
DR PDBsum; 5VNX; -.
DR AlphaFoldDB; A9AE46; -.
DR SMR; A9AE46; -.
DR STRING; 395019.Bmul_0373; -.
DR PRIDE; A9AE46; -.
DR EnsemblBacteria; BAG44769; BAG44769; BMULJ_02881.
DR KEGG; bmj:BMULJ_02881; -.
DR KEGG; bmu:Bmul_0373; -.
DR eggNOG; COG0156; Bacteria.
DR HOGENOM; CLU_015846_11_2_4; -.
DR OMA; YPYFRPI; -.
DR UniPathway; UPA00078; -.
DR Proteomes; UP000008815; Chromosome 1.
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 1: Evidence at protein level;
KW 3D-structure; Biotin biosynthesis; Pyridoxal phosphate; Reference proteome;
KW Transferase.
FT CHAIN 1..394
FT /note="8-amino-7-oxononanoate synthase"
FT /id="PRO_0000380933"
FT BINDING 21
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01693"
FT BINDING 112..113
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01693"
FT BINDING 137
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01693"
FT BINDING 183
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01693"
FT BINDING 211
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01693"
FT BINDING 239
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01693"
FT BINDING 358
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01693"
FT MOD_RES 242
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01693"
FT HELIX 2..16
FT /evidence="ECO:0007829|PDB:5VNX"
FT STRAND 26..28
FT /evidence="ECO:0007829|PDB:5VNX"
FT STRAND 30..36
FT /evidence="ECO:0007829|PDB:5VNX"
FT STRAND 39..43
FT /evidence="ECO:0007829|PDB:5VNX"
FT HELIX 56..69
FT /evidence="ECO:0007829|PDB:5VNX"
FT TURN 77..80
FT /evidence="ECO:0007829|PDB:5VNX"
FT HELIX 84..97
FT /evidence="ECO:0007829|PDB:5VNX"
FT STRAND 102..110
FT /evidence="ECO:0007829|PDB:5VNX"
FT HELIX 112..123
FT /evidence="ECO:0007829|PDB:5VNX"
FT STRAND 129..133
FT /evidence="ECO:0007829|PDB:5VNX"
FT HELIX 138..146
FT /evidence="ECO:0007829|PDB:5VNX"
FT STRAND 147..154
FT /evidence="ECO:0007829|PDB:5VNX"
FT HELIX 159..168
FT /evidence="ECO:0007829|PDB:5VNX"
FT STRAND 172..181
FT /evidence="ECO:0007829|PDB:5VNX"
FT TURN 183..185
FT /evidence="ECO:0007829|PDB:5VNX"
FT HELIX 191..201
FT /evidence="ECO:0007829|PDB:5VNX"
FT STRAND 203..208
FT /evidence="ECO:0007829|PDB:5VNX"
FT TURN 210..215
FT /evidence="ECO:0007829|PDB:5VNX"
FT HELIX 218..220
FT /evidence="ECO:0007829|PDB:5VNX"
FT HELIX 223..227
FT /evidence="ECO:0007829|PDB:5VNX"
FT STRAND 234..239
FT /evidence="ECO:0007829|PDB:5VNX"
FT STRAND 249..254
FT /evidence="ECO:0007829|PDB:5VNX"
FT HELIX 255..264
FT /evidence="ECO:0007829|PDB:5VNX"
FT HELIX 266..269
FT /evidence="ECO:0007829|PDB:5VNX"
FT HELIX 276..290
FT /evidence="ECO:0007829|PDB:5VNX"
FT HELIX 292..312
FT /evidence="ECO:0007829|PDB:5VNX"
FT STRAND 315..319
FT /evidence="ECO:0007829|PDB:5VNX"
FT STRAND 324..333
FT /evidence="ECO:0007829|PDB:5VNX"
FT HELIX 334..345
FT /evidence="ECO:0007829|PDB:5VNX"
FT TURN 346..348
FT /evidence="ECO:0007829|PDB:5VNX"
FT STRAND 364..369
FT /evidence="ECO:0007829|PDB:5VNX"
FT HELIX 376..392
FT /evidence="ECO:0007829|PDB:5VNX"
SQ SEQUENCE 394 AA; 41199 MW; 6DCCEC8E62F8BABE CRC64;
MNLLDTLQRG LADLDAQGLR RVRRTADSAC DAHMTVNGRE IVGFASNDYL GLAAHPKLVA
AFAEGAQRYG SGSGGSHLLG GHSRAHAKLE DELAGFAGGF SDAPRALYFS TGYMANLAAV
TALAGKDATI FSDALNHASL IDGTRLSRAT VQVYPHADTA TLGALLEACT SQTKLIVTDT
VFSMDGDIAP LAELLALAER HGAWLVVDDA HGFGVLGPQG RGALAAAALR SPHLVYVGTL
GKAAGVAGAF VVAHETVIEW LIQRARSYIF TTAAPPAVAH AVSASLKVIA GDEGDARRAH
LAALIERTRA LLRRTRWQPV DSHTAVQPLV IGSNEATLAA MRALDAHGLW VPAIRPPTVP
AGTSRLRISL SAAHSFDDLA RLETALLRAS EEAA
