GenomeNet

Database: UniProt
Entry: K9B375_9STAP
LinkDB: K9B375_9STAP
Original site: K9B375_9STAP 
ID   K9B375_9STAP            Unreviewed;       373 AA.
AC   K9B375;
DT   06-FEB-2013, integrated into UniProtKB/TrEMBL.
DT   06-FEB-2013, sequence version 1.
DT   27-MAR-2024, entry version 29.
DE   RecName: Full=8-amino-7-oxononanoate synthase {ECO:0000256|ARBA:ARBA00013187};
DE            EC=2.3.1.47 {ECO:0000256|ARBA:ARBA00013187};
GN   ORFNames=C273_05972 {ECO:0000313|EMBL:EKU48230.1};
OS   Staphylococcus massiliensis S46.
OC   Bacteria; Bacillota; Bacilli; Bacillales; Staphylococcaceae;
OC   Staphylococcus.
OX   NCBI_TaxID=1229783 {ECO:0000313|EMBL:EKU48230.1, ECO:0000313|Proteomes:UP000009885};
RN   [1] {ECO:0000313|EMBL:EKU48230.1, ECO:0000313|Proteomes:UP000009885}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=S46 {ECO:0000313|EMBL:EKU48230.1,
RC   ECO:0000313|Proteomes:UP000009885};
RX   PubMed=23929469;
RA   Srivastav R., Singh A., Jangir P.K., Kumari C., Muduli S., Sharma R.;
RT   "Genome Sequence of Staphylococcus massiliensis Strain S46, Isolated from
RT   the Surface of Healthy Human Skin.";
RL   Genome Announc. 1:e00553-13(2013).
CC   -!- COFACTOR:
CC       Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC         Evidence={ECO:0000256|ARBA:ARBA00001933};
CC   -!- PATHWAY: Cofactor biosynthesis; biotin biosynthesis.
CC       {ECO:0000256|ARBA:ARBA00004746}.
CC   -!- SUBUNIT: Homodimer. {ECO:0000256|ARBA:ARBA00011738}.
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:EKU48230.1}.
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DR   EMBL; AMSQ01000007; EKU48230.1; -; Genomic_DNA.
DR   RefSeq; WP_009383365.1; NZ_AMSQ01000007.1.
DR   AlphaFoldDB; K9B375; -.
DR   STRING; 1229783.C273_05972; -.
DR   PATRIC; fig|1229783.3.peg.1209; -.
DR   eggNOG; COG0156; Bacteria.
DR   OrthoDB; 9807157at2; -.
DR   Proteomes; UP000009885; Unassembled WGS sequence.
DR   GO; GO:0003824; F:catalytic activity; IEA:UniProt.
DR   GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR   GO; GO:0009058; P:biosynthetic process; IEA:InterPro.
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; 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.
PE   4: Predicted;
KW   Reference proteome {ECO:0000313|Proteomes:UP000009885}.
FT   DOMAIN          37..366
FT                   /note="Aminotransferase class I/classII"
FT                   /evidence="ECO:0000259|Pfam:PF00155"
SQ   SEQUENCE   373 AA;  42460 MW;  C0180C00E1767B0F CRC64;
     MDFEASLQRI KDQGLYRELT SFNKVDQATI RTETDTYINF TSNDYLGLGQ CSRATDMDAT
     LKDVGMHYAS SRLVSGNTYL YEAIEHDMSA IFQFKHSLIT TSGYAANLAA FSIFRNEPHV
     MVFSDEKNHA SIIDGIKLNR LETVVYPHLD YNTLEDELAK YPHTTKIIVS DSIFSTNGDM
     VDIDQLKHLK DNYQDTYIIL DDAHGLGLNM FQSYDAVDIL TSSLSKALGA FGGLIMTRDT
     MMHDLIINKG RSFIYSGCLP NYNLIQLRHL LDIYQSETYR QSDLKALSSY FNRQYAALFK
     AEPFTLAPIK AIPVNDIENG FKVHAYLKAH GFLTSFFRYP TVETPMIRLS LTSMHTKSDI
     DNFLTTLSNF EER
//
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