GenomeNet

Database: UniProt
Entry: A0A1M3DBM3_9SPHN
LinkDB: A0A1M3DBM3_9SPHN
Original site: A0A1M3DBM3_9SPHN 
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}.
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; 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
//
DBGET integrated database retrieval system