BIOF_DESDA
ID BIOF_DESDA Reviewed; 384 AA.
AC B8J3V0;
DT 28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT 03-MAR-2009, sequence version 1.
DT 03-AUG-2022, entry version 68.
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=Ddes_0423;
OS Desulfovibrio desulfuricans (strain ATCC 27774 / DSM 6949 / MB).
OC Bacteria; Proteobacteria; Deltaproteobacteria; Desulfovibrionales;
OC Desulfovibrionaceae; Desulfovibrio.
OX NCBI_TaxID=525146;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 27774 / DSM 6949 / MB;
RG US DOE Joint Genome Institute;
RA Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Tice H., Bruce D.,
RA Goodwin L., Pitluck S., Sims D., Lu M., Kiss H., Meineke L., Brettin T.,
RA Detter J.C., Han C., Larimer F., Land M., Hauser L., Kyrpides N.,
RA Ovchinnikova G., Hazen T.C.;
RT "Complete sequence of Desulfovibrio desulfuricans subsp. desulfuricans str.
RT ATCC 27774.";
RL Submitted (JAN-2009) 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; CP001358; ACL48335.1; -; Genomic_DNA.
DR RefSeq; WP_012624065.1; NC_011883.1.
DR AlphaFoldDB; B8J3V0; -.
DR SMR; B8J3V0; -.
DR STRING; 525146.Ddes_0423; -.
DR EnsemblBacteria; ACL48335; ACL48335; Ddes_0423.
DR KEGG; dds:Ddes_0423; -.
DR eggNOG; COG0156; Bacteria.
DR HOGENOM; CLU_015846_11_0_7; -.
DR OMA; YPYFRPI; -.
DR OrthoDB; 479874at2; -.
DR UniPathway; UPA00078; -.
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; 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.
PE 3: Inferred from homology;
KW Biotin biosynthesis; Pyridoxal phosphate; Transferase.
FT CHAIN 1..384
FT /note="Putative 8-amino-7-oxononanoate synthase"
FT /id="PRO_0000380965"
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 233..236
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 236
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000250"
SQ SEQUENCE 384 AA; 40916 MW; CB2A19EAE2D50EFB CRC64;
MSDVAARLET IRAAHLYRRL RTLSTPQDRE VVIDGRRVLL FSSNSYLGLG INAHIRRSAV
RALEKFGTGA GGSRLVTGNM TPHMQLESAL AAFKGSESAL AFTSGYTANM GVISALCHKD
TVIFSDALNH ASIIDGCRLA RGRTVVYAHN DMDDLLEKIR QLRPRQGFII TDGVFSMDGD
LARLPELAHI ARSYGLTLMV DDAHATGVLG ATGRGTLEHF GLSHEDVPVV TGTLSKAIPS
EGGFVCGSEI LCELLRNTAR PFIFTTAPSP AAVAAATAGI GHIAAHPGLV RRLQDNVAYF
TGSLAEQGMH VPGQSPIIPI MAGEEEKAVR AAEALLALGV FAPCIRYPTV PRGQARLRLT
VMASHTRDDL DHAAVSLRKA LAGV
