ID A1KS75_NEIMF Unreviewed; 391 AA.
AC A1KS75;
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};
GN Name=pglC {ECO:0000313|EMBL:CAM09705.1};
GN OrderedLocusNames=NMC0397 {ECO:0000313|EMBL:CAM09705.1};
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:CAM09705.1, ECO:0000313|Proteomes:UP000002286};
RN [1] {ECO:0000313|EMBL:CAM09705.1, 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 -!- SIMILARITY: Belongs to the DegT/DnrJ/EryC1 family.
CC {ECO:0000256|RuleBase:RU004508}.
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; AM421808; CAM09705.1; -; Genomic_DNA.
DR AlphaFoldDB; A1KS75; -.
DR KEGG; nmc:NMC0397; -.
DR HOGENOM; CLU_033332_7_2_4; -.
DR Proteomes; UP000002286; Chromosome.
DR CDD; cd00616; AHBA_syn; 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; IPR000653; DegT/StrS_aminotransferase.
DR InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
DR PANTHER; PTHR30244:SF45; LIPOPOLYSACCHARIDE BIOSYNTHESIS PROTEIN RFBH; 1.
DR PANTHER; PTHR30244; TRANSAMINASE; 1.
DR Pfam; PF01041; DegT_DnrJ_EryC1; 1.
DR PIRSF; PIRSF000390; PLP_StrS; 1.
DR SUPFAM; SSF53383; PLP-dependent transferases; 1.
PE 3: Inferred from homology;
KW Pyridoxal phosphate {ECO:0000256|PIRSR:PIRSR000390-2,
KW ECO:0000256|RuleBase:RU004508}.
FT ACT_SITE 185
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000390-1"
FT MOD_RES 185
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR000390-2"
SQ SEQUENCE 391 AA; 43597 MW; 06D77523236D35E9 CRC64;
MLNTSLSPWP CFTQEEADAV SKVLLSNKVN YWTGNECREF EKEFAAFAGT RYAVALSNGT
LALDVALKAM GIGAGDDVIV TSRTFLASAS CIVNAGANPV FADVDLNSQN ISAETVKAVL
TPNTKAIIVV HLAGMPAEMD GIMALAKEHD LWVIEDCAQA HGAKYKGKSV GSIGHVGAWS
FCQDKIMTTG GEGGMVTTND KTLWEKMWSY KDHGKSYDAV YHREHAPGFR WLHESFGTNW
RMMEMQAVIG RIQLKRLPEW TARRQENAAK LAESLGKFAS IRLVEVADYI EHAQYKFYTF
VKPEHLKDGW MRDRIVNELN ARKVPCYQGS CSEVYLEKAF DNTPWRPKER LKNAVELGDT
SLMFLVHPTL TDGEIAFCKE HIEAVLTEAT R
//
