ID A0A433N0M5_CHLFR Unreviewed; 391 AA.
AC A0A433N0M5;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 27-MAR-2024, entry version 21.
DE RecName: Full=8-amino-7-ketopelargonate synthase {ECO:0000256|RuleBase:RU003693};
DE EC=2.3.1.47 {ECO:0000256|RuleBase:RU003693};
GN Name=bioF {ECO:0000313|EMBL:RUR74471.1};
GN ORFNames=PCC6912_52460 {ECO:0000313|EMBL:RUR74471.1};
OS Chlorogloeopsis fritschii PCC 6912.
OC Bacteria; Cyanobacteriota; Cyanophyceae; Nostocales; Chlorogloeopsidaceae;
OC Chlorogloeopsis.
OX NCBI_TaxID=211165 {ECO:0000313|EMBL:RUR74471.1, ECO:0000313|Proteomes:UP000268857};
RN [1] {ECO:0000313|EMBL:RUR74471.1, ECO:0000313|Proteomes:UP000268857}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PCC 6912 {ECO:0000313|EMBL:RUR74471.1,
RC ECO:0000313|Proteomes:UP000268857};
RX PubMed=30590650;
RA Will S.E., Henke P., Boedeker C., Huang S., Brinkmann H., Rohde M.,
RA Jarek M., Friedl T., Seufert S., Schumacher M., Overmann J.,
RA Neumann-Schaal M., Petersen J.;
RT "Day and night: Metabolic profiles and evolutionary relationships of six
RT axenic non-marine cyanobacteria.";
RL Genome Biol. Evol. 0:0-0(2018).
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.
CC {ECO:0000256|ARBA:ARBA00002513, ECO:0000256|RuleBase:RU003693}.
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:0000256|ARBA:ARBA00034067,
CC ECO:0000256|RuleBase:RU003693};
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000256|ARBA:ARBA00001933,
CC ECO:0000256|PIRSR:PIRSR604723-51, ECO:0000256|RuleBase:RU003693};
CC -!- PATHWAY: Cofactor biosynthesis; biotin biosynthesis.
CC {ECO:0000256|ARBA:ARBA00004746, ECO:0000256|RuleBase:RU003693}.
CC -!- SUBUNIT: Homodimer. {ECO:0000256|ARBA:ARBA00011738,
CC ECO:0000256|RuleBase:RU003693}.
CC -!- SIMILARITY: Belongs to the class-II pyridoxal-phosphate-dependent
CC aminotransferase family. BioF subfamily.
CC {ECO:0000256|ARBA:ARBA00010008, ECO:0000256|RuleBase:RU003693}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:RUR74471.1}.
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DR EMBL; RSCJ01000029; RUR74471.1; -; Genomic_DNA.
DR RefSeq; WP_016878266.1; NZ_RSCJ01000029.1.
DR AlphaFoldDB; A0A433N0M5; -.
DR STRING; 211165.GCA_000317285_05455; -.
DR OrthoDB; 9807157at2; -.
DR UniPathway; UPA00078; -.
DR Proteomes; UP000268857; Unassembled WGS sequence.
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 CDD; cd06454; KBL_like; 1.
DR Gene3D; 3.90.1150.10; Aspartate Aminotransferase, domain 1; 1.
DR Gene3D; 3.40.640.10; Type I PLP-dependent aspartate aminotransferase-like (Major domain); 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 NCBIfam; TIGR00858; bioF; 1.
DR PANTHER; PTHR13693:SF100; 8-AMINO-7-OXONONANOATE SYNTHASE; 1.
DR PANTHER; PTHR13693; CLASS II AMINOTRANSFERASE/8-AMINO-7-OXONONANOATE SYNTHASE; 1.
DR Pfam; PF00155; Aminotran_1_2; 1.
DR SUPFAM; SSF53383; PLP-dependent transferases; 1.
DR PROSITE; PS00599; AA_TRANSFER_CLASS_2; 1.
PE 3: Inferred from homology;
KW Biotin biosynthesis {ECO:0000256|ARBA:ARBA00022756};
KW Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW ECO:0000256|PIRSR:PIRSR604723-51};
KW Reference proteome {ECO:0000313|Proteomes:UP000268857};
KW Transferase {ECO:0000256|RuleBase:RU003693}.
FT DOMAIN 42..384
FT /note="Aminotransferase class I/classII"
FT /evidence="ECO:0000259|Pfam:PF00155"
FT MOD_RES 242
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR604723-51"
SQ SEQUENCE 391 AA; 42447 MW; EF17FE66133787CB CRC64;
MAVDPYAWIE QSLATIHRAD WYRSVQTING DPGATVLLEG REVINFASND YLGLAGDWRL
IAAATAAIQE YGTGSTGSRL LSGHRKLHCE LEEAIASLKQ TEDALVFSSG YLANLGTITA
LVGKRDLILA DQYNHSSLKN GAILSGATII EFPHCDVCAL KSELQRVRQN YRRCLIVTDS
VFSMDGDLCP LPALLELAEE FSCMLLVDEA HATGVLGKTG AGCVEHFGCT GRQLIQIGTM
SKALGSLGGY VAANATLIDF LRNRASTWIY TTALSPADAA AALAAIHVVQ QEPQRHTQLW
QNVAQLKELM QKYLPNQRLL PSESPILCLQ LPSAADALKV GQYLKSAGIF APAIRPPTVP
TSRIRISVMA THEAAHIEKL IQSLHSWFEK L
//
