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Database: UniProt
Entry: A0A0F5ZVC6_9GAMM
LinkDB: A0A0F5ZVC6_9GAMM
Original site: A0A0F5ZVC6_9GAMM 
ID   A0A0F5ZVC6_9GAMM        Unreviewed;       388 AA.
AC   A0A0F5ZVC6;
DT   24-JUN-2015, integrated into UniProtKB/TrEMBL.
DT   24-JUN-2015, sequence version 1.
DT   24-JAN-2024, entry version 42.
DE   RecName: Full=8-amino-7-ketopelargonate synthase {ECO:0000256|RuleBase:RU003693};
DE            EC=2.3.1.47 {ECO:0000256|RuleBase:RU003693};
GN   ORFNames=RN22_14765 {ECO:0000313|EMBL:KKD59701.1};
OS   Grimontia sp. AD028.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC   Grimontia.
OX   NCBI_TaxID=1581149 {ECO:0000313|EMBL:KKD59701.1, ECO:0000313|Proteomes:UP000033732};
RN   [1] {ECO:0000313|EMBL:KKD59701.1, ECO:0000313|Proteomes:UP000033732}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AD028 {ECO:0000313|EMBL:KKD59701.1,
RC   ECO:0000313|Proteomes:UP000033732};
RA   Adrian T.-G.-S., Chan K.-G.;
RT   "Genome sequencing of Grimontia sp. AD028.";
RL   Submitted (APR-2015) 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.
CC       {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:KKD59701.1}.
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DR   EMBL; LASY01000064; KKD59701.1; -; Genomic_DNA.
DR   RefSeq; WP_046305501.1; NZ_LASY01000064.1.
DR   AlphaFoldDB; A0A0F5ZVC6; -.
DR   PATRIC; fig|1581149.3.peg.3805; -.
DR   OrthoDB; 9807157at2; -.
DR   UniPathway; UPA00078; -.
DR   Proteomes; UP000033732; 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   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   Acyltransferase {ECO:0000313|EMBL:KKD59701.1};
KW   Biotin biosynthesis {ECO:0000256|ARBA:ARBA00022756};
KW   Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW   ECO:0000256|PIRSR:PIRSR604723-51};
KW   Transferase {ECO:0000256|RuleBase:RU003693, ECO:0000313|EMBL:KKD59701.1}.
FT   DOMAIN          46..379
FT                   /note="Aminotransferase class I/classII"
FT                   /evidence="ECO:0000259|Pfam:PF00155"
FT   MOD_RES         239
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR604723-51"
SQ   SEQUENCE   388 AA;  42109 MW;  861BD674588BC165 CRC64;
     MREQCQLQSR IEQRLEARRQ QRLHRQVAAF SHQDGLITDS GNRQFANFSG NDYLGLAQDA
     SLIKAWQEGL SLYGAGSTAS PLVTGFSKAH QFLEDQLCDW LGFDRAILFN SGFSANQAVI
     FSLLEKGDLL LQDKLNHASL MEAGMLSEAT MKRFPHNDVT KLGALLQKAD SPTLTVTEGV
     FSMDGDLSPL ADVKAQCEAH GSWLMVDDAH GCGILGKDGR GSCDHAGIKP DILIVTFGKA
     FGMMGAAVLC SESVHDYLTQ FARHYVYSTA MPPAQAHALT KAVEIISAQS WRREKLASLS
     ELYHSLLADV PEVIPTITPI KPVLLGGVER MQIAATSLKA SGFWTGAIRP PAVPANSSRL
     RITLSVNQSE SQVKELAATL SQILQEAS
//
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