ID BIOF_MYCTF Reviewed; 386 AA.
AC A5WMQ5;
DT 01-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT 28-JUL-2009, sequence version 1.
DT 29-MAY-2013, entry version 34.
DE RecName: Full=8-amino-7-oxononanoate synthase;
DE Short=AONS;
DE EC=2.3.1.47;
DE AltName: Full=7-keto-8-amino-pelargonic acid synthase;
DE Short=7-KAP synthase;
DE Short=KAPA synthase;
DE AltName: Full=8-amino-7-ketopelargonate synthase;
DE AltName: Full=Alpha-oxoamine synthase;
GN OrderedLocusNames=TBFG_11601;
OS Mycobacterium tuberculosis (strain F11).
OC Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales;
OC Corynebacterineae; Mycobacteriaceae; Mycobacterium;
OC Mycobacterium tuberculosis complex.
OX NCBI_TaxID=336982;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=F11;
RA Birren B., Lander E., Galagan J., Devon K., Nusbaum C., Borowsky M.L.,
RA Grabherr M., Mauceli E., Brockman W., Young S., LaButti K.,
RA Pushparaj V., Sykes S., Baldwin J., Fitzgerald M., Bloom T.,
RA Zimmer A., Settipalli S., Shea T., Arachchi H., Macdonald P.,
RA Abouelleil A., Lui A., Priest M., Berlin A., Gearin G., Brown A.,
RA Aftuck L., Bessette D., Allen N., Lubonja R., Lokyitsang T.,
RA Matthews C., Dunbar C., Benamara M., Nguyen T., Negash T.,
RA DeCaprio D., Crawford M., Koehrsen M., Engels R., Montgomery P.,
RA Pearson M., Howarth C., Kodira C., Zeng Q., Yandava C., O'Leary S.,
RA Alvarado L., Victor T., Murray M.;
RT "The complete genome sequence of Mycobacterium tuberculosis F11.";
RL Submitted (APR-2007) to the EMBL/GenBank/DDBJ databases.
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 (By
CC similarity).
CC -!- CATALYTIC ACTIVITY: Pimeloyl-[acyl-carrier protein] + L-alanine =
CC 8-amino-7-oxononanoate + CO(2) + holo-[acyl-carrier protein].
CC -!- COFACTOR: Pyridoxal phosphate (By similarity).
CC -!- PATHWAY: Cofactor biosynthesis; biotin biosynthesis.
CC -!- SUBUNIT: Homodimer (By similarity).
CC -!- SIMILARITY: Belongs to the class-II pyridoxal-phosphate-dependent
CC aminotransferase family. BioF subfamily.
CC -----------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution-NoDerivs License
CC -----------------------------------------------------------------------
DR EMBL; CP000717; ABR05944.1; -; Genomic_DNA.
DR RefSeq; YP_001287546.1; NC_009565.1.
DR ProteinModelPortal; A5WMQ5; -.
DR SMR; A5WMQ5; 45-371.
DR STRING; 336982.TBFG_11601; -.
DR EnsemblBacteria; ABR05944; ABR05944; TBFG_11601.
DR GeneID; 5222279; -.
DR KEGG; mtf:TBFG_11601; -.
DR PATRIC; 18134198; VBIMycTub9078_1752.
DR eggNOG; COG0156; -.
DR HOGENOM; HOG000221021; -.
DR KO; K00652; -.
DR OMA; VCVESVY; -.
DR ProtClustDB; PRK05958; -.
DR BioCyc; MTUB336982:GH7I-1623-MONOMER; -.
DR UniPathway; UPA00078; -.
DR GO; GO:0008710; F:8-amino-7-oxononanoate synthase activity; IEA:EC.
DR GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR GO; GO:0009102; P:biotin biosynthetic process; IEA:UniProtKB-UniPathway.
DR Gene3D; 3.40.640.10; -; 1.
DR Gene3D; 3.90.1150.10; -; 1.
DR InterPro; IPR001917; Aminotrans_II_pyridoxalP_BS.
DR InterPro; IPR004839; Aminotransferase_I/II.
DR InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR InterPro; IPR015421; PyrdxlP-dep_Trfase_major_sub1.
DR InterPro; IPR015422; PyrdxlP-dep_Trfase_major_sub2.
DR Pfam; PF00155; Aminotran_1_2; 1.
DR SUPFAM; SSF53383; PyrdxlP-dep_Trfase_major; 1.
DR PROSITE; PS00599; AA_TRANSFER_CLASS_2; 1.
PE 3: Inferred from homology;
KW Acyltransferase; Biotin biosynthesis; Complete proteome;
KW Pyridoxal phosphate; Transferase.
FT CHAIN 1 386 8-amino-7-oxononanoate synthase.
FT /FTId=PRO_0000381044.
FT REGION 109 110 Pyridoxal phosphate binding (By
FT similarity).
FT REGION 205 208 Pyridoxal phosphate binding (By
FT similarity).
FT REGION 236 239 Pyridoxal phosphate binding (By
FT similarity).
FT BINDING 31 31 Substrate (By similarity).
FT BINDING 134 134 Substrate (By similarity).
FT BINDING 180 180 Pyridoxal phosphate (By similarity).
FT BINDING 349 349 Substrate (By similarity).
FT MOD_RES 239 239 N6-(pyridoxal phosphate)lysine (By
FT similarity).
SQ SEQUENCE 386 AA; 40028 MW; DE2C7D9B3300104F CRC64;
MKAATQARID DSPLAWLDAV QRQRHEAGLR RCLRPRPAVA TELDLASNDY LGLSRHPAVI
DGGVQALRIW GAGATGSRLV TGDTKLHQQF EAELAEFVGA AAGLLFSSGY TANLGAVVGL
SGPGSLLVSD ARSHASLVDA CRLSRARVVV TPHRDVDAVD AALRSRDEQR AVVVTDSVFS
ADGSLAPVRE LLEVCRRHGA LLLVDEAHGL GVRGGGRGLL YELGLAGAPD VVMTTTLSKA
LGSQGGVVLG PTPVRAHLID AARPFIFDTG LAPAAVGAAR AALRVLQAEP WRPQAVLNHA
GELARMCGVA AVPDSAMVSV ILGEPESAVA AAAACLDAGV KVGCFRPPTV PAGTSRLRLT
ARASLNAGEL ELARRVLTDV LAVARR
//
