ID H8XRI2_FLAIG Unreviewed; 383 AA.
AC H8XRI2;
DT 16-MAY-2012, integrated into UniProtKB/TrEMBL.
DT 16-MAY-2012, sequence version 1.
DT 27-MAR-2024, entry version 43.
DE RecName: Full=8-amino-7-oxononanoate synthase {ECO:0000256|ARBA:ARBA00013187};
DE EC=2.3.1.47 {ECO:0000256|ARBA:ARBA00013187};
GN Name=bioF {ECO:0000313|EMBL:CCG54416.1};
GN OrderedLocusNames=KQS_12555 {ECO:0000313|EMBL:CCG54416.1};
OS Flavobacterium indicum (strain DSM 17447 / CIP 109464 / GPTSA100-9).
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC Flavobacteriaceae; Flavobacterium.
OX NCBI_TaxID=1094466 {ECO:0000313|EMBL:CCG54416.1, ECO:0000313|Proteomes:UP000007599};
RN [1] {ECO:0000313|EMBL:CCG54416.1, ECO:0000313|Proteomes:UP000007599}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 17447 / CIP 109464 / GPTSA100-9
RC {ECO:0000313|Proteomes:UP000007599};
RX PubMed=22582381; DOI=10.1128/JB.00420-12;
RA Barbier P., Houel A., Loux V., Poulain J., Bernardet J.F., Touchon M.,
RA Duchaud E.;
RT "Complete Genome Sequence of Flavobacterium indicum GPSTA100-9T, Isolated
RT from Warm Spring Water.";
RL J. Bacteriol. 194:3024-3025(2012).
RN [2] {ECO:0000313|Proteomes:UP000007599}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 17447 / CIP 109464 / GPTSA100-9
RC {ECO:0000313|Proteomes:UP000007599};
RA Barbier P., Houel A., Loux V., Poulain J., Bernardet J.-F., Touchon M.,
RA Duchaud E.;
RT "Complete genome sequence of Flavobacterium indicum GPTSA100-9T, isolated
RT from warm spring water.";
RL Submitted (MAR-2012) to the EMBL/GenBank/DDBJ databases.
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 -!- SIMILARITY: Belongs to the class-II pyridoxal-phosphate-dependent
CC aminotransferase family. {ECO:0000256|RuleBase:RU003693}.
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DR EMBL; HE774682; CCG54416.1; -; Genomic_DNA.
DR RefSeq; WP_014389534.1; NC_017025.1.
DR AlphaFoldDB; H8XRI2; -.
DR STRING; 1094466.KQS_12555; -.
DR KEGG; fin:KQS_12555; -.
DR PATRIC; fig|1094466.5.peg.2453; -.
DR eggNOG; COG0156; Bacteria.
DR HOGENOM; CLU_015846_11_2_10; -.
DR OrthoDB; 9807157at2; -.
DR Proteomes; UP000007599; 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:SF77; 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:CCG54416.1};
KW Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW ECO:0000256|RuleBase:RU003693};
KW Reference proteome {ECO:0000313|Proteomes:UP000007599};
KW Transferase {ECO:0000313|EMBL:CCG54416.1}.
FT DOMAIN 28..374
FT /note="Aminotransferase class I/classII"
FT /evidence="ECO:0000259|Pfam:PF00155"
SQ SEQUENCE 383 AA; 43403 MW; FD3B9A3C30ABBAFD CRC64;
MKFPKSLSEK LNLREETHAL RKLPIDTNGI DFSSNDYLGF AQNSDLFDRI HHFLVDQNIK
FNGATGSRLI SGNHHLYTIT EDFIAQFHES EAALLFNSGY DANIGFFSAV PQRNDIVLYD
ELCHASIRDG IQMGTAKSYK FQHNDYEDLE EKLKKYYALK TDNFSIYVVT ESVFSMDGDS
PNFESILNLC QQYKAYLVVD EAHALGVFGE KGEGLLQFQK LHKKVFARIM TFGKGLGCHG
AVILGSSELK SYLINFARSF IYTTGLSPHA VATILMAYKE LKHSHQIQLL KENVTYFNQQ
KQLFGLKPLF IYSKSAIHSA IIPGNEKVKN VALHIQNKGF EVKPILSPTV PEGQERLRIC
IHSYNTQEQI SQLLMVLTEA LLN
//
