(data stored in ACNUC7421 zone)

SWISSPROT: 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   08-MAY-2019, entry version 81.
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=Bxeno_A0198; 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.,
RA   Lao V., Larimer F., LiPuma J.J., Mahenthiralingam E., Malfatti S.A.,
RA   Marx C.J., Parnell J.J., Ramette A., Richardson P., Seeger M.,
RA   Smith D., Spilker T., Sul W.J., Tsoi T.V., Ulrich L.E., Zhulin I.B.,
RA   Tiedje J.M.;
RT   "Burkholderia xenovorans LB400 harbors a multi-replicon, 9.73-Mbp
RT   genome shaped for versatility.";
RL   Proc. Natl. Acad. Sci. U.S.A. 103:15280-15287(2006).
CC   -!- FUNCTION: Catalyzes the decarboxylative condensation of pimeloyl-
CC       [acyl-carrier protein] and L-alanine to produce 8-amino-7-
CC       oxononanoate (AON), [acyl-carrier protein], and carbon dioxide.
CC       {ECO:0000255|HAMAP-Rule:MF_01693}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=H(+) + L-alanine + pimeloyl-[ACP] = 8-amino-7-
CC         oxononanoate + CO2 + holo-[ACP]; Xref=Rhea:RHEA:42288,
CC         Rhea:RHEA-COMP:9685, Rhea:RHEA-COMP:9955, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:16526, ChEBI:CHEBI:57532, ChEBI:CHEBI:57972,
CC         ChEBI:CHEBI:64479, ChEBI:CHEBI:78846; EC=2.3.1.47;
CC         Evidence={ECO:0000255|HAMAP-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}.
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   SMR; Q146K3; -.
DR   STRING; 266265.Bxe_A4264; -.
DR   EnsemblBacteria; ABE28736; ABE28736; Bxe_A4264.
DR   GeneID; 4003943; -.
DR   KEGG; bxb:DR64_1940; -.
DR   KEGG; bxe:Bxe_A4264; -.
DR   PATRIC; fig|266265.5.peg.209; -.
DR   eggNOG; ENOG4107EEK; Bacteria.
DR   eggNOG; COG0156; LUCA.
DR   HOGENOM; HOG000221021; -.
DR   KO; K00652; -.
DR   OMA; HYHASGI; -.
DR   OrthoDB; 479874at2; -.
DR   BioCyc; BXEN266265:BXE_RS00990-MONOMER; -.
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; IPR015422; PyrdxlP-dep_Trfase_dom1.
DR   InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR   Pfam; PF00155; Aminotran_1_2; 1.
DR   SUPFAM; SSF53383; SSF53383; 1.
DR   TIGRFAMs; TIGR00858; bioF; 1.
PE   1: Evidence at protein level;
DR   PRODOM; Q146K3.
DR   SWISS-2DPAGE; Q146K3.
KW   3D-structure; Biotin biosynthesis; Complete proteome;
KW   Pyridoxal phosphate; Reference proteome; Transferase.
FT   CHAIN         1    394       8-amino-7-oxononanoate synthase.
FT                                /FTId=PRO_0000380947.
FT   REGION      112    113       Pyridoxal phosphate binding.
FT                                {ECO:0000255|HAMAP-Rule:MF_01693}.
FT   BINDING      21     21       Substrate. {ECO:0000255|HAMAP-
FT                                Rule:MF_01693}.
FT   BINDING     137    137       Substrate. {ECO:0000255|HAMAP-
FT                                Rule:MF_01693}.
FT   BINDING     183    183       Pyridoxal phosphate. {ECO:0000255|HAMAP-
FT                                Rule:MF_01693}.
FT   BINDING     211    211       Pyridoxal phosphate. {ECO:0000255|HAMAP-
FT                                Rule:MF_01693}.
FT   BINDING     239    239       Pyridoxal phosphate. {ECO:0000255|HAMAP-
FT                                Rule:MF_01693}.
FT   BINDING     358    358       Substrate. {ECO:0000255|HAMAP-
FT                                Rule:MF_01693}.
FT   MOD_RES     242    242       N6-(pyridoxal phosphate)lysine.
FT                                {ECO:0000255|HAMAP-Rule:MF_01693}.
FT   HELIX         3     16       {ECO:0000244|PDB:5JAY}.
FT   STRAND       26     28       {ECO:0000244|PDB:5JAY}.
FT   STRAND       30     36       {ECO:0000244|PDB:5JAY}.
FT   STRAND       39     43       {ECO:0000244|PDB:5JAY}.
FT   HELIX        56     69       {ECO:0000244|PDB:5JAY}.
FT   HELIX        84     97       {ECO:0000244|PDB:5JAY}.
FT   STRAND      104    111       {ECO:0000244|PDB:5JAY}.
FT   HELIX       112    123       {ECO:0000244|PDB:5JAY}.
FT   STRAND      128    133       {ECO:0000244|PDB:5JAY}.
FT   HELIX       138    146       {ECO:0000244|PDB:5JAY}.
FT   STRAND      149    154       {ECO:0000244|PDB:5JAY}.
FT   HELIX       159    167       {ECO:0000244|PDB:5JAY}.
FT   STRAND      172    181       {ECO:0000244|PDB:5JAY}.
FT   TURN        183    185       {ECO:0000244|PDB:5JAY}.
FT   HELIX       191    200       {ECO:0000244|PDB:5JAY}.
FT   STRAND      204    208       {ECO:0000244|PDB:5JAY}.
FT   TURN        210    215       {ECO:0000244|PDB:5JAY}.
FT   HELIX       218    220       {ECO:0000244|PDB:5JAY}.
FT   HELIX       223    226       {ECO:0000244|PDB:5JAY}.
FT   STRAND      234    242       {ECO:0000244|PDB:5JAY}.
FT   STRAND      249    254       {ECO:0000244|PDB:5JAY}.
FT   HELIX       255    264       {ECO:0000244|PDB:5JAY}.
FT   HELIX       267    270       {ECO:0000244|PDB:5JAY}.
FT   HELIX       276    289       {ECO:0000244|PDB:5JAY}.
FT   HELIX       292    314       {ECO:0000244|PDB:5JAY}.
FT   STRAND      315    319       {ECO:0000244|PDB:5JAY}.
FT   STRAND      323    333       {ECO:0000244|PDB:5JAY}.
FT   HELIX       334    346       {ECO:0000244|PDB:5JAY}.
FT   STRAND      364    369       {ECO:0000244|PDB:5JAY}.
FT   HELIX       376    388       {ECO:0000244|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
//

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