BIOF_PARXL
ID BIOF_PARXL Reviewed; 394 AA.
AC Q146K3;
DT 28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT 22-AUG-2006, sequence version 1.
DT 03-AUG-2022, entry version 94.
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=Bxeno_A0198;
GN ORFNames=Bxe_A4264;
OS Paraburkholderia xenovorans (strain LB400).
OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Paraburkholderia.
OX NCBI_TaxID=266265;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LB400;
RX PubMed=17030797; DOI=10.1073/pnas.0606924103;
RA Chain P.S.G., Denef V.J., Konstantinidis K.T., Vergez L.M., Agullo L.,
RA Reyes V.L., Hauser L., Cordova M., Gomez L., Gonzalez M., Land M., Lao V.,
RA Larimer F., LiPuma J.J., Mahenthiralingam E., Malfatti S.A., Marx C.J.,
RA Parnell J.J., Ramette A., Richardson P., Seeger M., Smith D., Spilker T.,
RA Sul W.J., Tsoi T.V., Ulrich L.E., Zhulin I.B., Tiedje J.M.;
RT "Burkholderia xenovorans LB400 harbors a multi-replicon, 9.73-Mbp genome
RT shaped for versatility.";
RL Proc. Natl. Acad. Sci. U.S.A. 103:15280-15287(2006).
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; CP000270; ABE28736.1; -; Genomic_DNA.
DR RefSeq; WP_011486581.1; NZ_CP008760.1.
DR PDB; 5JAY; X-ray; 1.75 A; A/B=1-394.
DR PDBsum; 5JAY; -.
DR AlphaFoldDB; Q146K3; -.
DR SMR; Q146K3; -.
DR STRING; 266265.Bxe_A4264; -.
DR EnsemblBacteria; ABE28736; ABE28736; Bxe_A4264.
DR KEGG; bxb:DR64_1940; -.
DR KEGG; bxe:Bxe_A4264; -.
DR PATRIC; fig|266265.5.peg.209; -.
DR eggNOG; COG0156; Bacteria.
DR OMA; HYHASGI; -.
DR OrthoDB; 479874at2; -.
DR UniPathway; UPA00078; -.
DR Proteomes; UP000001817; 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_0000380947"
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 3..16
FT /evidence="ECO:0007829|PDB:5JAY"
FT STRAND 26..28
FT /evidence="ECO:0007829|PDB:5JAY"
FT STRAND 30..36
FT /evidence="ECO:0007829|PDB:5JAY"
FT STRAND 39..43
FT /evidence="ECO:0007829|PDB:5JAY"
FT HELIX 56..69
FT /evidence="ECO:0007829|PDB:5JAY"
FT HELIX 84..97
FT /evidence="ECO:0007829|PDB:5JAY"
FT STRAND 104..111
FT /evidence="ECO:0007829|PDB:5JAY"
FT HELIX 112..123
FT /evidence="ECO:0007829|PDB:5JAY"
FT STRAND 128..133
FT /evidence="ECO:0007829|PDB:5JAY"
FT HELIX 138..146
FT /evidence="ECO:0007829|PDB:5JAY"
FT STRAND 149..154
FT /evidence="ECO:0007829|PDB:5JAY"
FT HELIX 159..167
FT /evidence="ECO:0007829|PDB:5JAY"
FT STRAND 172..181
FT /evidence="ECO:0007829|PDB:5JAY"
FT TURN 183..185
FT /evidence="ECO:0007829|PDB:5JAY"
FT HELIX 191..200
FT /evidence="ECO:0007829|PDB:5JAY"
FT STRAND 204..208
FT /evidence="ECO:0007829|PDB:5JAY"
FT TURN 210..215
FT /evidence="ECO:0007829|PDB:5JAY"
FT HELIX 218..220
FT /evidence="ECO:0007829|PDB:5JAY"
FT HELIX 223..226
FT /evidence="ECO:0007829|PDB:5JAY"
FT STRAND 234..242
FT /evidence="ECO:0007829|PDB:5JAY"
FT STRAND 249..254
FT /evidence="ECO:0007829|PDB:5JAY"
FT HELIX 255..264
FT /evidence="ECO:0007829|PDB:5JAY"
FT HELIX 267..270
FT /evidence="ECO:0007829|PDB:5JAY"
FT HELIX 276..289
FT /evidence="ECO:0007829|PDB:5JAY"
FT HELIX 292..314
FT /evidence="ECO:0007829|PDB:5JAY"
FT STRAND 315..319
FT /evidence="ECO:0007829|PDB:5JAY"
FT STRAND 323..333
FT /evidence="ECO:0007829|PDB:5JAY"
FT HELIX 334..346
FT /evidence="ECO:0007829|PDB:5JAY"
FT STRAND 364..369
FT /evidence="ECO:0007829|PDB:5JAY"
FT HELIX 376..388
FT /evidence="ECO:0007829|PDB:5JAY"
SQ SEQUENCE 394 AA; 41282 MW; 615599B866AA47FC CRC64;
MHLLDTLAEG LKEIDARGLR RRRRTADTPC AAHMTVDGRA IIGFASNDYL GLAAHPQLIA
AIAEGAQRYG AGSGGSHLLG GHSRAHAQLE DDLAEFVGGF VENARALYFS TGYMANLATL
TALAGRGTTL FSDALNHASL IDGARLSRAD VQIYPHCDTD ALSAMLEASD ADVKVIVSDT
VFSMDGDIAP LPRLLELAEQ HGAWLIVDDA HGFGVLGPQG RGAIAQAALR SPNLISIGTL
GKAAGVSGAF VAAHETVIEW LVQRARPYIF TTASVPAAAH AVSASLRIIG GEEGDARRAH
LQQLIGRTRA MLKATPWLPV DSHTAVQPLI IGANDATLEI AATLDRAGLW VPAIRPPTVP
TGTSRLRISL SAAHSQADLD RLEAGLQQLG AKAA
