BIOF1_MYCTU
ID BIOF1_MYCTU Reviewed; 386 AA.
AC P9WQ87; L0TA03; O06621; P0A4X4;
DT 16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT 16-APR-2014, sequence version 1.
DT 03-AUG-2022, entry version 38.
DE RecName: Full=8-amino-7-oxononanoate synthase 1;
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;
GN Name=bioF1; OrderedLocusNames=Rv1569; ORFNames=MTCY336.34c;
OS Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv).
OC Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC Mycobacterium; Mycobacterium tuberculosis complex.
OX NCBI_TaxID=83332;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=9634230; DOI=10.1038/31159;
RA Cole S.T., Brosch R., Parkhill J., Garnier T., Churcher C.M., Harris D.E.,
RA Gordon S.V., Eiglmeier K., Gas S., Barry C.E. III, Tekaia F., Badcock K.,
RA Basham D., Brown D., Chillingworth T., Connor R., Davies R.M., Devlin K.,
RA Feltwell T., Gentles S., Hamlin N., Holroyd S., Hornsby T., Jagels K.,
RA Krogh A., McLean J., Moule S., Murphy L.D., Oliver S., Osborne J.,
RA Quail M.A., Rajandream M.A., Rogers J., Rutter S., Seeger K., Skelton S.,
RA Squares S., Squares R., Sulston J.E., Taylor K., Whitehead S.,
RA Barrell B.G.;
RT "Deciphering the biology of Mycobacterium tuberculosis from the complete
RT genome sequence.";
RL Nature 393:537-544(1998).
RN [2]
RP DISRUPTION PHENOTYPE.
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=14569030; DOI=10.1073/pnas.2134250100;
RA Sassetti C.M., Rubin E.J.;
RT "Genetic requirements for mycobacterial survival during infection.";
RL Proc. Natl. Acad. Sci. U.S.A. 100:12989-12994(2003).
RN [3]
RP FUNCTION AS A 8-AMINO-7-OXONONANOATE SYNTHASE, CATALYTIC ACTIVITY, MASS
RP SPECTROMETRY, BIOPHYSICOCHEMICAL PROPERTIES, SUBSTRATE SPECIFICITY,
RP ACTIVITY REGULATION, AND COFACTOR.
RX PubMed=16769720; DOI=10.1074/jbc.m604477200;
RA Bhor V.M., Dev S., Vasanthakumar G.R., Kumar P., Sinha S., Surolia A.;
RT "Broad substrate stereospecificity of the Mycobacterium tuberculosis 7-
RT keto-8-aminopelargonic acid synthase: Spectroscopic and kinetic studies.";
RL J. Biol. Chem. 281:25076-25088(2006).
RN [4]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=21969609; DOI=10.1074/mcp.m111.011627;
RA Kelkar D.S., Kumar D., Kumar P., Balakrishnan L., Muthusamy B., Yadav A.K.,
RA Shrivastava P., Marimuthu A., Anand S., Sundaram H., Kingsbury R.,
RA Harsha H.C., Nair B., Prasad T.S., Chauhan D.S., Katoch K., Katoch V.M.,
RA Kumar P., Chaerkady R., Ramachandran S., Dash D., Pandey A.;
RT "Proteogenomic analysis of Mycobacterium tuberculosis by high resolution
RT mass spectrometry.";
RL Mol. Cell. Proteomics 10:M111.011627-M111.011627(2011).
RN [5]
RP DISRUPTION PHENOTYPE.
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=20565114; DOI=10.1021/bi902097j;
RA Dey S., Lane J.M., Lee R.E., Rubin E.J., Sacchettini J.C.;
RT "Structural characterization of the Mycobacterium tuberculosis biotin
RT biosynthesis enzymes 7,8-diaminopelargonic acid synthase and dethiobiotin
RT synthetase.";
RL Biochemistry 49:6746-6760(2010).
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 (By similarity). Can also
CC use pimeloyl-CoA instead of pimeloyl-ACP as substrate. To a lesser
CC extent, can also utilize D-alanine instead of L-alanine as substrate.
CC {ECO:0000250, ECO:0000269|PubMed:16769720}.
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:0000269|PubMed:16769720};
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000269|PubMed:16769720};
CC -!- ACTIVITY REGULATION: Inhibited by D-alanine and D-7-keto-8-amino-
CC pelargonic acid. {ECO:0000269|PubMed:16769720}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=1.5 uM for pimeloyl-CoA (at pH 7.7 and 25 degrees Celsius)
CC {ECO:0000269|PubMed:16769720};
CC KM=201.5 uM for D-alanine (at pH 7.7 and 25 degrees Celsius)
CC {ECO:0000269|PubMed:16769720};
CC KM=467.5 uM for L-alanine (at pH 7.7 and 25 degrees Celsius)
CC {ECO:0000269|PubMed:16769720};
CC Note=kcat is 0.007 sec(-1) and 0.0036 sec(-1) with L-alanine and D-
CC alanine as substrate, respectively, and pimeloyl-CoA as co-
CC substrate.;
CC -!- PATHWAY: Cofactor biosynthesis; biotin biosynthesis.
CC -!- SUBUNIT: Homodimer. {ECO:0000250}.
CC -!- MASS SPECTROMETRY: Mass=42248; Method=Electrospray;
CC Evidence={ECO:0000269|PubMed:16769720};
CC -!- DISRUPTION PHENOTYPE: Cells lacking this gene are shown to be highly
CC attenuated in a mouse tuberculosis model (PubMed:14569030). Essential
CC for growth even in liquid culture; growth does not occur on biotin-
CC containing medium after biotin deprivation (PubMed:20565114).
CC {ECO:0000269|PubMed:14569030, ECO:0000269|PubMed:20565114}.
CC -!- SIMILARITY: Belongs to the class-II pyridoxal-phosphate-dependent
CC aminotransferase family. BioF subfamily. {ECO:0000305}.
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DR EMBL; AL123456; CCP44333.1; -; Genomic_DNA.
DR PIR; C70540; C70540.
DR RefSeq; WP_003407805.1; NZ_NVQJ01000004.1.
DR RefSeq; YP_177822.1; NC_000962.3.
DR AlphaFoldDB; P9WQ87; -.
DR SMR; P9WQ87; -.
DR STRING; 83332.Rv1569; -.
DR PaxDb; P9WQ87; -.
DR DNASU; 886345; -.
DR GeneID; 886345; -.
DR KEGG; mtu:Rv1569; -.
DR TubercuList; Rv1569; -.
DR eggNOG; COG0156; Bacteria.
DR OMA; MDTHGFG; -.
DR PhylomeDB; P9WQ87; -.
DR UniPathway; UPA00078; -.
DR Proteomes; UP000001584; Chromosome.
DR GO; GO:0009274; C:peptidoglycan-based cell wall; HDA:MTBBASE.
DR GO; GO:0005886; C:plasma membrane; HDA:MTBBASE.
DR GO; GO:0008710; F:8-amino-7-oxononanoate synthase activity; IDA:MTBBASE.
DR GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR GO; GO:0009102; P:biotin biosynthetic process; IDA:MTBBASE.
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.
DR InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
DR Pfam; PF00155; Aminotran_1_2; 1.
DR SUPFAM; SSF53383; SSF53383; 1.
DR PROSITE; PS00599; AA_TRANSFER_CLASS_2; 1.
PE 1: Evidence at protein level;
KW Acyltransferase; Biotin biosynthesis; Pyridoxal phosphate;
KW Reference proteome; Transferase.
FT CHAIN 1..386
FT /note="8-amino-7-oxononanoate synthase 1"
FT /id="PRO_0000163818"
FT BINDING 31
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 109..110
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000250"
FT BINDING 134
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 180
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000250"
FT BINDING 205..208
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000250"
FT BINDING 236..239
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000250"
FT BINDING 349
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT MOD_RES 239
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000250"
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
