ID   A1KUS2_NEIMF            Unreviewed;       404 AA.
AC   A1KUS2;
DT   06-FEB-2007, integrated into UniProtKB/TrEMBL.
DT   06-FEB-2007, sequence version 1.
DT   27-MAR-2024, entry version 85.
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=NMC1410 {ECO:0000313|EMBL:CAM10621.1};
OS   Neisseria meningitidis serogroup C / serotype 2a (strain ATCC 700532 / DSM
OS   15464 / FAM18).
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Neisseriales; Neisseriaceae;
OC   Neisseria.
OX   NCBI_TaxID=272831 {ECO:0000313|EMBL:CAM10621.1, ECO:0000313|Proteomes:UP000002286};
RN   [1] {ECO:0000313|EMBL:CAM10621.1, ECO:0000313|Proteomes:UP000002286}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700532 / DSM 15464 / FAM18
RC   {ECO:0000313|Proteomes:UP000002286};
RX   PubMed=17305430; DOI=10.1371/journal.pgen.0030023;
RA   Bentley S.D., Vernikos G.S., Snyder L.A.S., Churcher C., Arrowsmith C.,
RA   Chillingworth T., Cronin A., Davis P.H., Holroyd N.E., Jagels K.,
RA   Maddison M., Moule S., Rabbinowitsch E., Sharp S., Unwin L., Whitehead S.,
RA   Quail M.A., Achtman M., Barrell B., Saunders N.J., Parkhill J.;
RT   "Meningococcal genetic variation mechanisms viewed through comparative
RT   analysis of serogroup C strain FAM18.";
RL   PLoS Genet. 3:230-240(2007).
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; AM421808; CAM10621.1; -; Genomic_DNA.
DR   RefSeq; WP_002220612.1; NC_008767.1.
DR   AlphaFoldDB; A1KUS2; -.
DR   KEGG; nmc:NMC1410; -.
DR   HOGENOM; CLU_017584_4_2_4; -.
DR   Proteomes; UP000002286; 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:CAM10621.1};
KW   Transferase {ECO:0000313|EMBL:CAM10621.1}.
FT   DOMAIN          35..390
FT                   /note="Aminotransferase class I/classII"
FT                   /evidence="ECO:0000259|Pfam:PF00155"
SQ   SEQUENCE   404 AA;  45445 MW;  99EF0B47F1DF4A2D 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 EMYRIHDDMK FVYDLLVREK
     VLLVQGTGFN WIKPDHFRIV TLPYVHQIEE AMGRLARFLQ TYRQ
//