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Database: UniProt
Entry: S6BGQ0_9GAMM
LinkDB: S6BGQ0_9GAMM
Original site: S6BGQ0_9GAMM 
ID   S6BGQ0_9GAMM            Unreviewed;       228 AA.
AC   S6BGQ0;
DT   16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT   16-OCT-2013, sequence version 1.
DT   24-JAN-2024, entry version 38.
DE   RecName: Full=Pyridoxal phosphate homeostasis protein {ECO:0000256|HAMAP-Rule:MF_02087};
DE            Short=PLP homeostasis protein {ECO:0000256|HAMAP-Rule:MF_02087};
GN   ORFNames=EBS_0306 {ECO:0000313|EMBL:BAN68286.1};
OS   endosymbiont of unidentified scaly snail isolate Monju.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria.
OX   NCBI_TaxID=1248727 {ECO:0000313|EMBL:BAN68286.1, ECO:0000313|Proteomes:UP000015562};
RN   [1] {ECO:0000313|EMBL:BAN68286.1, ECO:0000313|Proteomes:UP000015562}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Monju {ECO:0000313|EMBL:BAN68286.1};
RX   PubMed=23924784; DOI=10.1038/ismej.2013.131;
RA   Nakagawa S., Shimamura S., Takaki Y., Suzuki Y., Murakami S., Watanabe T.,
RA   Fujiyoshi S., Mino S., Sawabe T., Maeda T., Makita H., Nemoto S.,
RA   Nishimura S., Watanabe H., Watsuji T., Takai K.;
RT   "Allying with armored snails: the complete genome of gammaproteobacterial
RT   endosymbiont.";
RL   ISME J. 8:40-51(2014).
CC   -!- FUNCTION: Pyridoxal 5'-phosphate (PLP)-binding protein, which is
CC       involved in PLP homeostasis. {ECO:0000256|HAMAP-Rule:MF_02087}.
CC   -!- COFACTOR:
CC       Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC         Evidence={ECO:0000256|PIRSR:PIRSR004848-1};
CC   -!- SIMILARITY: Belongs to the pyridoxal phosphate-binding protein
CC       YggS/PROSC family. {ECO:0000256|HAMAP-Rule:MF_02087,
CC       ECO:0000256|RuleBase:RU004514}.
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DR   EMBL; AP012978; BAN68286.1; -; Genomic_DNA.
DR   RefSeq; WP_043107006.1; NZ_AP012978.1.
DR   AlphaFoldDB; S6BGQ0; -.
DR   STRING; 1248727.EBS_0306; -.
DR   KEGG; enm:EBS_0306; -.
DR   HOGENOM; CLU_059988_0_1_6; -.
DR   OrthoDB; 9804072at2; -.
DR   Proteomes; UP000015562; Chromosome.
DR   GO; GO:0030170; F:pyridoxal phosphate binding; IEA:UniProtKB-UniRule.
DR   CDD; cd06824; PLPDE_III_Yggs_like; 1.
DR   Gene3D; 3.20.20.10; Alanine racemase; 1.
DR   HAMAP; MF_02087; PLP_homeostasis; 1.
DR   InterPro; IPR001608; Ala_racemase_N.
DR   InterPro; IPR029066; PLP-binding_barrel.
DR   InterPro; IPR011078; PyrdxlP_homeostasis.
DR   NCBIfam; TIGR00044; YggS family pyridoxal phosphate-dependent enzyme; 1.
DR   PANTHER; PTHR10146; PROLINE SYNTHETASE CO-TRANSCRIBED BACTERIAL HOMOLOG PROTEIN; 1.
DR   PANTHER; PTHR10146:SF14; PYRIDOXAL PHOSPHATE HOMEOSTASIS PROTEIN; 1.
DR   Pfam; PF01168; Ala_racemase_N; 1.
DR   PIRSF; PIRSF004848; YBL036c_PLPDEIII; 1.
DR   SUPFAM; SSF51419; PLP-binding barrel; 1.
PE   3: Inferred from homology;
KW   Pyridoxal phosphate {ECO:0000256|HAMAP-Rule:MF_02087,
KW   ECO:0000256|PIRSR:PIRSR004848-1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000015562}.
FT   DOMAIN          28..227
FT                   /note="Alanine racemase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF01168"
FT   MOD_RES         36
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02087,
FT                   ECO:0000256|PIRSR:PIRSR004848-1"
SQ   SEQUENCE   228 AA;  24700 MW;  B977B0332ACB6831 CRC64;
     MPTIAQALED VHRRIAQAAL AAGRNPPEIE LLAVSKTKPA TMIREAWSAG QQAFGENYLQ
     DALPKIQALA DLPVEWHYIG RIQSNKTRDI ARHFAWVHGL DRLKHARRLS DQRPEALPPL
     NCCIQVNLSG EASKGGVPAD ALEELALAVN ELPGLRLRGL MTMPDPASPR EAQAAVFRGL
     ADLRHQLEKQ AGLSLDTLSM GMSGDLELAI AAGSTLVRVG TDIFGARE
//
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