ID   C6S7T9_NEIML            Unreviewed;       404 AA.
AC   C6S7T9;
DT   22-SEP-2009, integrated into UniProtKB/TrEMBL.
DT   22-SEP-2009, sequence version 1.
DT   27-MAR-2024, entry version 65.
DE   RecName: Full=Putative 8-amino-7-oxononanoate synthase {ECO:0000256|ARBA:ARBA00021531};
DE            EC=2.6.1.2 {ECO:0000256|ARBA:ARBA00026106};
GN   OrderedLocusNames=NMO_1303 {ECO:0000313|EMBL:CBA06735.1};
OS   Neisseria meningitidis (strain alpha14).
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Neisseriales; Neisseriaceae;
OC   Neisseria.
OX   NCBI_TaxID=662598 {ECO:0000313|EMBL:CBA06735.1, ECO:0000313|Proteomes:UP000002054};
RN   [1] {ECO:0000313|EMBL:CBA06735.1, ECO:0000313|Proteomes:UP000002054}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=alpha14 {ECO:0000313|Proteomes:UP000002054};
RX   PubMed=18305155; DOI=10.1073/pnas.0800151105;
RA   Schoen C., Blom J., Claus H., Schramm-Glueck A., Brandt P., Mueller T.,
RA   Goesmann A., Joseph B., Konietzny S., Kurzai O., Schmitt C., Friedrich T.,
RA   Linke B., Vogel U., Frosch M.;
RT   "Whole-genome comparison of disease and carriage strains provides insights
RT   into virulence evolution in Neisseria meningitidis.";
RL   Proc. Natl. Acad. Sci. U.S.A. 105:3473-3478(2008).
CC   -!- COFACTOR:
CC       Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC         Evidence={ECO:0000256|ARBA:ARBA00001933};
CC   -!- SIMILARITY: Belongs to the class-I pyridoxal-phosphate-dependent
CC       aminotransferase family. {ECO:0000256|ARBA:ARBA00007441}.
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DR   EMBL; AM889136; CBA06735.1; -; Genomic_DNA.
DR   RefSeq; WP_002212951.1; NC_013016.1.
DR   AlphaFoldDB; C6S7T9; -.
DR   KEGG; nmi:NMO_1303; -.
DR   HOGENOM; CLU_017584_4_2_4; -.
DR   Proteomes; UP000002054; Chromosome.
DR   GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR   GO; GO:0008483; F:transaminase activity; IEA:UniProtKB-KW.
DR   GO; GO:0009058; P:biosynthetic process; IEA:InterPro.
DR   CDD; cd00609; AAT_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; 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; PTHR43488; GLUTAMATE-PYRUVATE AMINOTRANSFERASE ALAA; 1.
DR   PANTHER; PTHR43488:SF2; GLUTAMATE-PYRUVATE AMINOTRANSFERASE ALAA; 1.
DR   Pfam; PF00155; Aminotran_1_2; 1.
DR   SUPFAM; SSF53383; PLP-dependent transferases; 1.
PE   3: Inferred from homology;
KW   Aminotransferase {ECO:0000313|EMBL:CBA06735.1};
KW   Transferase {ECO:0000313|EMBL:CBA06735.1}.
FT   DOMAIN          35..390
FT                   /note="Aminotransferase class I/classII"
FT                   /evidence="ECO:0000259|Pfam:PF00155"
SQ   SEQUENCE   404 AA;  45464 MW;  99EF115DF1C5502D CRC64;
     MDKFPKSAKL DHVCYDIRGP VHKKALQLEE EGNKILKLNI GNPAPFGFEA PDEILVDVIR
     NLPTSQGYCD SKGLYSARKA IVHYYQTKGL RDITVDDVYI GNGVSELITM SMQALLNDGD
     EILIPAPDYP LWTAAATLAG GTVRHYLCDE ENGWFPNLAD MEAKITPKTK AIVVINPNNP
     TGAVYSREIL LEIAELARKH GLIIFADEIY DKILYDGAVH HHIAALAPDL LTVTFNGLSK
     SYRVAGFRQG WMVLNGPKHH AKGYIEGLDM LSSMRLCANT PMQHAIQTAL GGYQSINEFI
     LPGGRLLEQR NRAWELVSQI PGVSCVKPMG AMYMFPKIDT EMYRIRDDMK FVYDLLVREK
     VLLVQGTGFN WIKPDHFRIV TLPYVHQIEE AMGRLARFLQ TYRQ
//