BIOF_ACET2
ID BIOF_ACET2 Reviewed; 388 AA.
AC A3DBD5;
DT 28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT 20-MAR-2007, sequence version 1.
DT 03-AUG-2022, entry version 84.
DE RecName: Full=Putative 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 AltName: Full=8-amino-7-ketopelargonate synthase;
GN Name=bioF; OrderedLocusNames=Cthe_0022;
OS Acetivibrio thermocellus (strain ATCC 27405 / DSM 1237 / JCM 9322 / NBRC
OS 103400 / NCIMB 10682 / NRRL B-4536 / VPI 7372) (Clostridium thermocellum).
OC Bacteria; Firmicutes; Clostridia; Eubacteriales; Oscillospiraceae;
OC Acetivibrio.
OX NCBI_TaxID=203119;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 27405 / DSM 1237 / JCM 9322 / NBRC 103400 / NCIMB 10682 / NRRL
RC B-4536 / VPI 7372;
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA Chertkov O., Brettin T., Bruce D., Han C., Tapia R., Gilna P., Schmutz J.,
RA Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N., Wu J.H.D.,
RA Newcomb M., Richardson P.;
RT "Complete sequence of Clostridium thermocellum ATCC 27405.";
RL Submitted (FEB-2007) to the EMBL/GenBank/DDBJ databases.
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; CP000568; ABN51264.1; -; Genomic_DNA.
DR RefSeq; WP_003511929.1; NC_009012.1.
DR AlphaFoldDB; A3DBD5; -.
DR SMR; A3DBD5; -.
DR STRING; 203119.Cthe_0022; -.
DR PRIDE; A3DBD5; -.
DR EnsemblBacteria; ABN51264; ABN51264; Cthe_0022.
DR KEGG; cth:Cthe_0022; -.
DR eggNOG; COG0156; Bacteria.
DR HOGENOM; CLU_015846_11_0_9; -.
DR OMA; MDTHGFG; -.
DR OrthoDB; 479874at2; -.
DR UniPathway; UPA00078; -.
DR Proteomes; UP000002145; 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; IPR004723; AONS_Archaea/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.
DR PROSITE; PS00599; AA_TRANSFER_CLASS_2; 1.
PE 3: Inferred from homology;
KW Biotin biosynthesis; Pyridoxal phosphate; Reference proteome; Transferase.
FT CHAIN 1..388
FT /note="Putative 8-amino-7-oxononanoate synthase"
FT /id="PRO_0000380956"
FT BINDING 18
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 105..106
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000250"
FT BINDING 130
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 176
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000250"
FT BINDING 201..204
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 349
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT MOD_RES 235
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000250"
SQ SEQUENCE 388 AA; 42878 MW; 04A5C0E08725A902 CRC64;
MYDFQGALKD IKNKGLYREF RNVNAAQGPY TVIDGRKMLM MSSNNYLGLC DDIRLKRAAI
ESIRKFGVGA GGSRLTCGNF ELHRELEERL AKFKDVESCI VFGSGYAANI GAISGIADKN
WVIFCDRLNH ASIVDGIRLS GAKLVVYKHC DMEDLESKIV RYHTGKSLIV TDGVFSMDGD
VAPVDRIVKL AKKYNLMTMV DDAHATGILG EKGRGTSEYF GLKDAVDISM GTLSKAFGVE
GGFVAGKRKL VDFLRHKAKS FIYSTAPPPH NMAAALEALN IIETEPQARK ELAEKSVWLR
NRLIEKGFNV PKGVTPIIPL MVGDVNTAVE FSMLLYNEGI YIPAIRPPTV PKGTSRLRIS
IMASHSYEDM EFALKNLVRF GRKLGIIP
