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Database: UniProt
Entry: M1NP15_9CORY
LinkDB: M1NP15_9CORY
Original site: M1NP15_9CORY 
ID   M1NP15_9CORY            Unreviewed;       254 AA.
AC   M1NP15;
DT   01-MAY-2013, integrated into UniProtKB/TrEMBL.
DT   01-MAY-2013, sequence version 1.
DT   24-JAN-2024, entry version 48.
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=A605_01165 {ECO:0000313|EMBL:AGF71247.1};
OS   Corynebacterium halotolerans YIM 70093 = DSM 44683.
OC   Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales;
OC   Corynebacteriaceae; Corynebacterium.
OX   NCBI_TaxID=1121362 {ECO:0000313|EMBL:AGF71247.1, ECO:0000313|Proteomes:UP000011723};
RN   [1] {ECO:0000313|EMBL:AGF71247.1, ECO:0000313|Proteomes:UP000011723}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=YIM 70093 {ECO:0000313|EMBL:AGF71247.1};
RX   PubMed=23408721;
RA   Ruckert C., Albersmeier A., Al-Dilaimi A., Niehaus K., Szczepanowski R.,
RA   Kalinowski J.;
RT   "Genome sequence of the halotolerant bacterium Corynebacterium halotolerans
RT   type strain YIM 70093(T) (= DSM 44683(T)).";
RL   Stand. Genomic Sci. 7:284-293(2012).
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; CP003697; AGF71247.1; -; Genomic_DNA.
DR   RefSeq; WP_015399671.1; NZ_JIAJ01000002.1.
DR   AlphaFoldDB; M1NP15; -.
DR   STRING; 1121362.A605_01165; -.
DR   KEGG; chn:A605_01165; -.
DR   PATRIC; fig|1121362.3.peg.225; -.
DR   eggNOG; COG0325; Bacteria.
DR   HOGENOM; CLU_059988_1_0_11; -.
DR   OrthoDB; 9804072at2; -.
DR   Proteomes; UP000011723; Chromosome.
DR   GO; GO:0030170; F:pyridoxal phosphate binding; IEA:UniProtKB-UniRule.
DR   CDD; cd00635; PLPDE_III_YBL036c_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:UP000011723}.
FT   DOMAIN          16..238
FT                   /note="Alanine racemase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF01168"
FT   MOD_RES         45
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02087,
FT                   ECO:0000256|PIRSR:PIRSR004848-1"
SQ   SEQUENCE   254 AA;  28330 MW;  C75E13A00195464B CRC64;
     MSDFPFPETV EEFRIAREAV EERIADAARR AGRDPGEVRL LPVSKTWPAE RLRLAIAAGM
     TTLGENRIQE LSAKARELAD TGVRWCVIGH LQRNKARDCA AWADEFHALD SVRVGAALQR
     RLEAVDRHLD VFIQVNTSLE PQKHGLAADE VAGVLAGLAD FDRLRVRGLM TLAEFSRDET
     VVRPCFARLR ELRERLIPGL PDGMNLDELS MGMSGDFEWA IEEGATTVRV GQAIFGARAT
     KDSEYWPGQG RENH
//
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