ID A0A1M3DBM3_9SPHN Unreviewed; 419 AA.
AC A0A1M3DBM3;
DT 15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT 15-MAR-2017, sequence version 1.
DT 24-JAN-2024, entry version 16.
DE SubName: Full=8-amino-7-oxononanoate synthase {ECO:0000313|EMBL:OJV31862.1};
GN ORFNames=BGO24_15505 {ECO:0000313|EMBL:OJV31862.1};
OS Sphingomonas sp. 67-36.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC Sphingomonadaceae; Sphingomonas.
OX NCBI_TaxID=1895849 {ECO:0000313|EMBL:OJV31862.1, ECO:0000313|Proteomes:UP000183964};
RN [1] {ECO:0000313|EMBL:OJV31862.1, ECO:0000313|Proteomes:UP000183964}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=67-36 {ECO:0000313|EMBL:OJV31862.1};
RA Kantor R.S., Huddy R.J., Iyer R., Thomas B.C., Brown C.T., Anantharaman K.,
RA Tringe S., Hettich R.L., Harrison S.T., Banfield J.F.;
RT "Genome-resolved meta-omics ties microbial dynamics to process performance
RT in biotechnology for thiocyanate degradation.";
RL Submitted (SEP-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 -!- 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:OJV31862.1}.
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DR EMBL; MKSU01000015; OJV31862.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1M3DBM3; -.
DR STRING; 1895849.BGO24_15505; -.
DR Proteomes; UP000183964; 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:0009058; P:biosynthetic process; IEA:InterPro.
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; IPR015424; PyrdxlP-dep_Trfase.
DR InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
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 66..406
FT /note="Aminotransferase class I/classII"
FT /evidence="ECO:0000259|Pfam:PF00155"
SQ SEQUENCE 419 AA; 45083 MW; 0E4CD3D751B9D456 CRC64;
MSDSGQQSDL PPAATPAPAE RDLFDKFAPL IAEREALLSS GLRDPFGIVM EEVKSPTVAV
IKGRETILLG TYNYMGMTFD PDVIAAGKQA FDRFGTGTNG SRALNGTFHD HMEVEQALRE
FYGMSGAIVF STGYQANLGV ISAIAGKGEY IILDADSHAS IYDGCAMGNA EVVRFRHNSV
EDLDKRLGRL PREPGKLVVL EGVYSMLGDV APLREMVAVA KKHGAMVLVD EAHSMGFFGP
NGRGVYEEQG LEDQVDFVIG TFSKSVGTVG GFCVSNHPKF EILRFVCRPY IFTASLPPAV
MASAAVSIRK LMHAHNKRAH LWENTRALHG GLKALGFRLP TDEPQSAVVA VLLDDQDQAV
AMWHALLEAG LYVNVARPPA TPAGTFLLRC SVCAEHTSEQ IARVIAMFEA AGRATGAIA
//