BIOF_MYCS2
ID BIOF_MYCS2 Reviewed; 382 AA.
AC A0QX65; I7G8Q0;
DT 28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT 09-JAN-2007, sequence version 1.
DT 03-AUG-2022, entry version 97.
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 Name=bioF; OrderedLocusNames=MSMEG_3189, MSMEI_3107;
OS Mycolicibacterium smegmatis (strain ATCC 700084 / mc(2)155) (Mycobacterium
OS smegmatis).
OC Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC Mycolicibacterium.
OX NCBI_TaxID=246196;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700084 / mc(2)155;
RA Fleischmann R.D., Dodson R.J., Haft D.H., Merkel J.S., Nelson W.C.,
RA Fraser C.M.;
RL Submitted (OCT-2006) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700084 / mc(2)155;
RX PubMed=17295914; DOI=10.1186/gb-2007-8-2-r20;
RA Deshayes C., Perrodou E., Gallien S., Euphrasie D., Schaeffer C.,
RA Van-Dorsselaer A., Poch O., Lecompte O., Reyrat J.-M.;
RT "Interrupted coding sequences in Mycobacterium smegmatis: authentic
RT mutations or sequencing errors?";
RL Genome Biol. 8:R20.1-R20.9(2007).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700084 / mc(2)155;
RX PubMed=18955433; DOI=10.1101/gr.081901.108;
RA Gallien S., Perrodou E., Carapito C., Deshayes C., Reyrat J.-M.,
RA Van Dorsselaer A., Poch O., Schaeffer C., Lecompte O.;
RT "Ortho-proteogenomics: multiple proteomes investigation through orthology
RT and a new MS-based protocol.";
RL Genome Res. 19:128-135(2009).
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:0000250}.
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 -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000250};
CC -!- PATHWAY: Cofactor biosynthesis; biotin biosynthesis.
CC -!- SUBUNIT: Homodimer. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the class-II pyridoxal-phosphate-dependent
CC aminotransferase family. BioF subfamily. {ECO:0000305}.
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DR EMBL; CP000480; ABK73253.1; -; Genomic_DNA.
DR EMBL; CP001663; AFP39571.1; -; Genomic_DNA.
DR RefSeq; WP_011728881.1; NZ_SIJM01000015.1.
DR RefSeq; YP_887503.1; NC_008596.1.
DR PDB; 3WY7; X-ray; 2.30 A; A/B/C/D=1-382.
DR PDB; 7S5M; X-ray; 2.25 A; A/B/C/D=2-382.
DR PDBsum; 3WY7; -.
DR PDBsum; 7S5M; -.
DR AlphaFoldDB; A0QX65; -.
DR SMR; A0QX65; -.
DR STRING; 246196.MSMEI_3107; -.
DR EnsemblBacteria; ABK73253; ABK73253; MSMEG_3189.
DR EnsemblBacteria; AFP39571; AFP39571; MSMEI_3107.
DR GeneID; 66734589; -.
DR KEGG; msg:MSMEI_3107; -.
DR KEGG; msm:MSMEG_3189; -.
DR PATRIC; fig|246196.19.peg.3151; -.
DR eggNOG; COG0156; Bacteria.
DR OMA; MDTHGFG; -.
DR OrthoDB; 479874at2; -.
DR BRENDA; 2.3.1.47; 3512.
DR UniPathway; UPA00078; -.
DR Proteomes; UP000000757; Chromosome.
DR Proteomes; UP000006158; Chromosome.
DR GO; GO:0008710; F:8-amino-7-oxononanoate synthase activity; IEA:UniProtKB-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.
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 3D-structure; Acyltransferase; Biotin biosynthesis; Pyridoxal phosphate;
KW Reference proteome; Transferase.
FT CHAIN 1..382
FT /note="8-amino-7-oxononanoate synthase"
FT /id="PRO_0000381039"
FT BINDING 26
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 104..105
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000250"
FT BINDING 129
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 175
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000250"
FT BINDING 200..203
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000250"
FT BINDING 232..235
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000250"
FT BINDING 345
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT MOD_RES 235
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000250"
FT HELIX 7..21
FT /evidence="ECO:0007829|PDB:7S5M"
FT STRAND 36..39
FT /evidence="ECO:0007829|PDB:7S5M"
FT HELIX 52..65
FT /evidence="ECO:0007829|PDB:7S5M"
FT TURN 73..76
FT /evidence="ECO:0007829|PDB:7S5M"
FT HELIX 80..93
FT /evidence="ECO:0007829|PDB:7S5M"
FT STRAND 96..103
FT /evidence="ECO:0007829|PDB:7S5M"
FT HELIX 104..115
FT /evidence="ECO:0007829|PDB:7S5M"
FT STRAND 120..125
FT /evidence="ECO:0007829|PDB:7S5M"
FT TURN 126..128
FT /evidence="ECO:0007829|PDB:3WY7"
FT HELIX 130..139
FT /evidence="ECO:0007829|PDB:7S5M"
FT STRAND 141..146
FT /evidence="ECO:0007829|PDB:7S5M"
FT HELIX 151..160
FT /evidence="ECO:0007829|PDB:7S5M"
FT STRAND 164..173
FT /evidence="ECO:0007829|PDB:7S5M"
FT TURN 175..177
FT /evidence="ECO:0007829|PDB:7S5M"
FT HELIX 183..193
FT /evidence="ECO:0007829|PDB:7S5M"
FT STRAND 196..200
FT /evidence="ECO:0007829|PDB:7S5M"
FT TURN 202..207
FT /evidence="ECO:0007829|PDB:7S5M"
FT HELIX 215..218
FT /evidence="ECO:0007829|PDB:7S5M"
FT STRAND 227..235
FT /evidence="ECO:0007829|PDB:7S5M"
FT STRAND 242..246
FT /evidence="ECO:0007829|PDB:7S5M"
FT HELIX 248..257
FT /evidence="ECO:0007829|PDB:7S5M"
FT HELIX 259..262
FT /evidence="ECO:0007829|PDB:7S5M"
FT HELIX 269..284
FT /evidence="ECO:0007829|PDB:7S5M"
FT HELIX 287..303
FT /evidence="ECO:0007829|PDB:7S5M"
FT STRAND 310..317
FT /evidence="ECO:0007829|PDB:7S5M"
FT HELIX 321..333
FT /evidence="ECO:0007829|PDB:7S5M"
FT STRAND 339..341
FT /evidence="ECO:0007829|PDB:7S5M"
FT TURN 343..345
FT /evidence="ECO:0007829|PDB:3WY7"
FT STRAND 352..356
FT /evidence="ECO:0007829|PDB:7S5M"
FT HELIX 363..380
FT /evidence="ECO:0007829|PDB:7S5M"
SQ SEQUENCE 382 AA; 39343 MW; A1605D7DF40D6111 CRC64;
MTRAGLSPLA WLADIEQRRR AEGLRRELRV RPPVAAELDL ASNDYLGLSQ HPDVLDGGVE
ALRTWGGGAG GSRLVTGNTE LHEAFEHQLA SFLGAESALV FSSGYTANLG ALVALSGPGS
LIVSDALSHA SLVDACRLSR ARVVVSPHRD VDAVDAALAA RTEERAVVVT ESVFSADGDL
APLRDLHAVC RRHGALLLVD EAHGLGVRGT RGQGLLHEVG LAGAPDIVMT TTLSKALGSQ
GGAVLGPEAV RAHLIDTARS FIFDTGLAPA AVGAASAALR VLDAEPQRAR AVLDRAAELA
TIAGVTEAPV SAVVSVILGD PEIAVGAAAA CLDRGVRVGC FRPPTVPAGT SRLRLAARAS
LTDDEMALAR QVLTDVLATA RA
