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Database: UniProt
Entry: G8SFD1_ACTS5
LinkDB: G8SFD1_ACTS5
Original site: G8SFD1_ACTS5 
ID   G8SFD1_ACTS5            Unreviewed;       378 AA.
AC   G8SFD1;
DT   22-FEB-2012, integrated into UniProtKB/TrEMBL.
DT   22-FEB-2012, sequence version 1.
DT   27-MAR-2024, entry version 48.
DE   RecName: Full=8-amino-7-oxononanoate synthase {ECO:0000256|ARBA:ARBA00013187};
DE            EC=2.3.1.47 {ECO:0000256|ARBA:ARBA00013187};
DE   AltName: Full=7-keto-8-amino-pelargonic acid synthase {ECO:0000256|ARBA:ARBA00032610};
DE   AltName: Full=8-amino-7-ketopelargonate synthase {ECO:0000256|ARBA:ARBA00033381};
GN   Name=bioF {ECO:0000313|EMBL:AEV87922.1};
GN   OrderedLocusNames=ACPL_7042 {ECO:0000313|EMBL:AEV87922.1};
OS   Actinoplanes sp. (strain ATCC 31044 / CBS 674.73 / SE50/110).
OC   Bacteria; Actinomycetota; Actinomycetes; Micromonosporales;
OC   Micromonosporaceae; Actinoplanes.
OX   NCBI_TaxID=134676 {ECO:0000313|EMBL:AEV87922.1, ECO:0000313|Proteomes:UP000005440};
RN   [1] {ECO:0000313|Proteomes:UP000005440}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 31044 / CBS 674.73 / SE50/110
RC   {ECO:0000313|Proteomes:UP000005440};
RA   Schwientek P., Szczepanowski R., Kalinowski J., Klein A., Selber K.,
RA   Wehmeier U.F., Stoye J., Puehler A.;
RT   "The complete genome sequence of the acarbose producer Actinoplanes sp.
RT   SE50/110.";
RL   Submitted (DEC-2011) to the EMBL/GenBank/DDBJ databases.
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   -!- COFACTOR:
CC       Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC         Evidence={ECO:0000256|ARBA:ARBA00001933,
CC         ECO:0000256|RuleBase:RU003693};
CC   -!- PATHWAY: Cofactor biosynthesis; biotin biosynthesis.
CC       {ECO:0000256|ARBA:ARBA00004746}.
CC   -!- SUBUNIT: Homodimer. {ECO:0000256|ARBA:ARBA00011738}.
CC   -!- SIMILARITY: Belongs to the class-II pyridoxal-phosphate-dependent
CC       aminotransferase family. BioF subfamily.
CC       {ECO:0000256|ARBA:ARBA00010008}.
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DR   EMBL; CP003170; AEV87922.1; -; Genomic_DNA.
DR   RefSeq; WP_014693986.1; NZ_LT827010.1.
DR   AlphaFoldDB; G8SFD1; -.
DR   STRING; 134676.ACPL_7042; -.
DR   KEGG; ase:ACPL_7042; -.
DR   PATRIC; fig|134676.3.peg.6952; -.
DR   eggNOG; COG0156; Bacteria.
DR   HOGENOM; CLU_015846_11_2_11; -.
DR   OrthoDB; 9807157at2; -.
DR   Proteomes; UP000005440; 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-KW.
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; IPR015424; PyrdxlP-dep_Trfase.
DR   InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR   InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
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   Acyltransferase {ECO:0000313|EMBL:AEV87922.1};
KW   Biotin biosynthesis {ECO:0000256|ARBA:ARBA00022756};
KW   Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW   ECO:0000256|RuleBase:RU003693};
KW   Reference proteome {ECO:0000313|Proteomes:UP000005440};
KW   Transferase {ECO:0000313|EMBL:AEV87922.1}.
FT   DOMAIN          32..373
FT                   /note="Aminotransferase class I/classII"
FT                   /evidence="ECO:0000259|Pfam:PF00155"
SQ   SEQUENCE   378 AA;  38243 MW;  C707439E40CC3BC2 CRC64;
     MADWSESLDR LARDRAKAGL TRHLRPRPAD DDVVDLAGND YLGLSRHVAV TSAARSAIAA
     YGVGATGSRL VRGSTDAHTA LESGLAGWLG AEAALVFSSG YLANLAVVRA AAAVCDLVVS
     DAYNHASLID GCKISGRPVV VAPHNDPAAV AAILDAHPGR TAAVVTESVF SVDGDLAPLA
     ALHAVTTARG ALLIVDDAHA LGLLGPAGAG GVVAAGLAGQ PDVIVTATLS KSLGGAGGVV
     AGPARVIRHL IDTGRTFIYD TAPPPAVVAG VHAAIDLARA ADDRRATLTA RGQRLAARLR
     AAGYPVRDPA AGVLSVVAPG PEAALTWSDD CRDRGVAVGC FRPPSTPDGT SRLRLTLNAG
     IPEADFTRAL DVILECAP
//
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