ID A0A167XQH9_9FLAO Unreviewed; 379 AA.
AC A0A167XQH9;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 27-MAR-2024, entry version 22.
DE RecName: Full=8-amino-7-oxononanoate synthase {ECO:0000256|ARBA:ARBA00013187};
DE EC=2.3.1.47 {ECO:0000256|ARBA:ARBA00013187};
GN ORFNames=FBFR_07860 {ECO:0000313|EMBL:OAB28594.1};
OS Flavobacterium fryxellicola.
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC Flavobacteriaceae; Flavobacterium.
OX NCBI_TaxID=249352 {ECO:0000313|EMBL:OAB28594.1, ECO:0000313|Proteomes:UP000077164};
RN [1] {ECO:0000313|EMBL:OAB28594.1, ECO:0000313|Proteomes:UP000077164}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 16209 {ECO:0000313|EMBL:OAB28594.1,
RC ECO:0000313|Proteomes:UP000077164};
RA Shin S.-K., Yi H.;
RT "Draft genome sequence of Flavobacterium fryxellicola DSM 16209.";
RL Submitted (MAR-2016) 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}.
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:OAB28594.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; LVJE01000011; OAB28594.1; -; Genomic_DNA.
DR RefSeq; WP_066079325.1; NZ_LVJE01000011.1.
DR AlphaFoldDB; A0A167XQH9; -.
DR STRING; 249352.SAMN05444395_101284; -.
DR OrthoDB; 9807157at2; -.
DR Proteomes; UP000077164; Unassembled WGS sequence.
DR GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR GO; GO:0016740; F:transferase activity; 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 Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW ECO:0000256|RuleBase:RU003693}.
FT DOMAIN 29..371
FT /note="Aminotransferase class I/classII"
FT /evidence="ECO:0000259|Pfam:PF00155"
SQ SEQUENCE 379 AA; 42421 MW; C9AB93B7F30D3B1E CRC64;
MKQFPKNLFD KLAIRKQNNA LRQLPLPATL IDFASNDYLG FSKSEIIFNE THQYLIKNKT
IQNGATGSRL LSGNHKLYQE TEGFIATFHQ AETALIFNSG YDANIGFFGS IPQKGDLIVY
DELCHASIRD GIQLSNAKAY KFNHNDCEDL EKLIVRNPNT TIYIVTESVF SMDGDCPNLQ
ELVSVSTKHK CYLVVDEAHA LGVFGSSGEG FVQMLGLQDH VFARIMTFGK GLGCHGAAIL
GSVELRDYLV NFARSFIYTT GLSPHSVATI LIAYQFLEKE KKNIEILREN IIHFNQEKNM
LGLKPLFVRS KSAIQSAIIP GNEKVKVIAS QLQQEGFDVK AILSPTVPEG QERLRICLHS
YNSTEEISEV LRLLTTFVF
//
